|
Name |
Accession |
Description |
Interval |
E-value |
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
848-1928 |
0e+00 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 1486.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 848 TRQEEEMQAKEDELQKTKERQQKAESELKELEQKHSQLTEEKNLLQEQLQAETELYAEAEEMRVRLAAKKQELEEILHEM 927
Cdd:pfam01576 1 TRQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 928 EARLEEEEDRSQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDDILVMDDQNNKLSKERKLLEER 1007
Cdd:pfam01576 81 ESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1008 ISDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLDGEASDLHEQIAELQAQIAELKMQLAK 1087
Cdd:pfam01576 161 ISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1088 KEEELQAALGRLDDEMAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALKTELEDTLDSTATQQE 1167
Cdd:pfam01576 241 KEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1168 LRAKREQEVTMLKKALDEETRSHESQVQEMRQKHTQVVEELTEQLEQFKRAKANLDKNKQALEKENAELAGELRVLSQAK 1247
Cdd:pfam01576 321 LRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1248 QEVEHKKKKLEVQLQELQSKYSDGEKVRAELNDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLGSQLQDTQELLQEE 1327
Cdd:pfam01576 401 QDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1328 TRQKLNVSTKLRQLEDERNSLQEQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFASTVELLEEGKKKFQKEIESLTQQ 1407
Cdd:pfam01576 481 TRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQ 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1408 YEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQKKFDQLLAEEKNISSKYADERDRAEAEAREKETKALS 1487
Cdd:pfam01576 561 LEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALS 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1488 LARALEEALEAKEELERTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEV 1567
Cdd:pfam01576 641 LARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEV 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1568 NMQALKVQFERDLQARDEQNEEKRRQLQRQLHEYETELEDERKQRALAVAAKKKLEGDLKDLELQADSAIKGREEAIKQL 1647
Cdd:pfam01576 721 NMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQL 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1648 RKLQAQMKDFQRELEDARASRDEIFATAKENEKKAKSLEADLMQLQEDLAAAERARKQADLEKDELAEELASSVSGRNAL 1727
Cdd:pfam01576 801 KKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSAL 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1728 QDEKRRLEARIAQLEEELEEEQGNTEAMSERVRKATQQAEQLSNELATERSAAQKNENARQQLERQNKELRSKLQEMEGA 1807
Cdd:pfam01576 881 QDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGT 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1808 VKSKFKSTIAALEAKIAQLEEQVEQEAREKQATAKALKQKDKKLKEALLQVEDERKMAEQYKEQAEKGNLRVKQLKRQLE 1887
Cdd:pfam01576 961 VKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLE 1040
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|.
gi 156120901 1888 EAEEESQRINANRRKLQRELDEATESNEAMGREVTALKSKL 1928
Cdd:pfam01576 1041 EAEEEASRANAARRKLQRELDDATESNESMNREVSTLKSKL 1081
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
99-771 |
0e+00 |
|
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin heavy chain 11 (also called SMMHC, SMHC). The gene product is a subunit of a hexameric protein that consists of two heavy chain subunits and two pairs of non-identical light chain subunits. It functions as a major contractile protein, converting chemical energy into mechanical energy through the hydrolysis of ATP. The gene encoding a human ortholog of rat NUDE1 is transcribed from the reverse strand of this gene, and its 3' end overlaps with that of the latter. Inversion of the MYH11 locus is one of the most frequent chromosomal aberrations found in acute myeloid leukemia. Alternative splicing generates isoforms that are differentially expressed, with ratios changing during muscle cell maturation. Mutations in MYH11 have been described in individuals with thoracic aortic aneurysms leading to acute aortic dissections with patent ductus arteriosus. MYH11 mutations are also thought to contribute to human colorectal cancer and are also associated with Peutz-Jeghers syndrome. The mutations found in human intestinal neoplasia result in unregulated proteins with constitutive motor activity, similar to the mutant myh11 zebrafish. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276885 [Multi-domain] Cd Length: 673 Bit Score: 1317.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKQLPIYSEKIIEMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 178
Cdd:cd14921 1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 179 ESGAGKTENTKKVIQYLAMVASSHKGKKDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVVASSHKGKKDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 259 ANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRNDLLLEGFNNYTFLSNGFVPIPAAQDDEMFNETVEAMAIMGF 338
Cdd:cd14921 161 ANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDDEMFQETLEAMSIMGF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 339 TEEEQLSILRVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQAD 418
Cdd:cd14921 241 SEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQAD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 419 FAVEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEE 498
Cdd:cd14921 321 FAIEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 499 YQREGIEWNFIDFGLDLQPCIELIERPTNPPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQKPKQLKDKTEFSII 578
Cdd:cd14921 401 YQREGIEWNFIDFGLDLQPCIELIERPNNPPGVLALLDEECWFPKATDKSFVEKLCTEQGNHPKFQKPKQLKDKTEFSII 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 579 HYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFMADLWKDVDRIVGLDQMAKMTESSLPSASKTKKGMFRTVGQLYK 658
Cdd:cd14921 481 HYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVGLDQMAKMTESSLPSASKTKKGMFRTVGQLYK 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 659 EQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANAIPK 738
Cdd:cd14921 561 EQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANAIPK 640
|
650 660 670
....*....|....*....|....*....|...
gi 156120901 739 GFMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd14921 641 GFMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
99-771 |
0e+00 |
|
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. Thus, myosin II has two heads. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276951 [Multi-domain] Cd Length: 662 Bit Score: 1317.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKQLPIYSEKIIEMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 178
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 179 ESGAGKTENTKKVIQYLAMVASSHKGKKDTSIT-GELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 257
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASSKKKKESGKKkGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTGKIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 258 GANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRNDLLLEGFNNYT-FLSNGFVPIPAAQDDEMFNETVEAMAIM 336
Cdd:cd01377 161 GADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYfFLSQGELTIDGVDDAEEFKLTDEAFDIL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 337 GFTEEEQLSILRVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQ 416
Cdd:cd01377 241 GFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKGQNKEQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 417 ADFAVEALAKATYERLFRWILTRVNKALDKThRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQ 496
Cdd:cd01377 321 VVFSVGALAKALYERLFLWLVKRINKTLDTK-SKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMFVLEQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 497 EEYQREGIEWNFIDFGLDLQPCIELIERPtnPPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPK-FQKPKQLKDKTEF 575
Cdd:cd01377 400 EEYKKEGIEWTFIDFGLDLQPTIDLIEKP--NMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKnFKKPKPKKSEAHF 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 576 SIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFMADLWKDVDRivgldqmakmtESSLPSASKTKKGMFRTVGQ 655
Cdd:cd01377 478 ILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEE-----------SGGGGGKKKKKGGSFRTVSQ 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 656 LYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANA 735
Cdd:cd01377 547 LHKEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNA 626
|
650 660 670
....*....|....*....|....*....|....*.
gi 156120901 736 IPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd01377 627 IPKGFDDGKAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
99-771 |
0e+00 |
|
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy chain 10 (also called NMMHCB). Mutations in this gene have been associated with May-Hegglin anomaly and developmental defects in brain and heart. Multiple transcript variants encoding different isoforms have been found for this gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276952 [Multi-domain] Cd Length: 673 Bit Score: 1297.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKQLPIYSEKIIEMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 178
Cdd:cd14920 1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 179 ESGAGKTENTKKVIQYLAMVASSHKGKKDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd14920 81 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 259 ANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRNDLLLEGFNNYTFLSNGFVPIPAAQDDEMFNETVEAMAIMGF 338
Cdd:cd14920 161 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMHIMGF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 339 TEEEQLSILRVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQAD 418
Cdd:cd14920 241 SHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQAD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 419 FAVEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEE 498
Cdd:cd14920 321 FAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 499 YQREGIEWNFIDFGLDLQPCIELIERPTNPPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQKPKQLKDKTEFSII 578
Cdd:cd14920 401 YQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKDKADFCII 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 579 HYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFMADLWKDVDRIVGLDQMAKMTESSLPSASKTKKGMFRTVGQLYK 658
Cdd:cd14920 481 HYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTETAFGSAYKTKKGMFRTVGQLYK 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 659 EQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANAIPK 738
Cdd:cd14920 561 ESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPK 640
|
650 660 670
....*....|....*....|....*....|...
gi 156120901 739 GFMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd14920 641 GFMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
99-771 |
0e+00 |
|
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain 18. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276895 [Multi-domain] Cd Length: 676 Bit Score: 1198.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKQLPIYSEKIIEMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 178
Cdd:cd14932 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 179 ESGAGKTENTKKVIQYLAMVASSHKGKKDTSIT----GELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTG 254
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVASSFKTKKDQSSIalshGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 255 YIVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRNDLLLEGFNNYTFLSNGFVPIPAAQDDEMFNETVEAMA 334
Cdd:cd14932 161 YIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNVTIPGQQDKELFAETMEAFR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 335 IMGFTEEEQLSILRVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTK 414
Cdd:cd14932 241 IMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQKAQTQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 415 EQADFAVEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFIL 494
Cdd:cd14932 321 EQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 495 EQEEYQREGIEWNFIDFGLDLQPCIELIERPTNPPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQKPKQLKDKTE 574
Cdd:cd14932 401 EQEEYQREGIEWSFIDFGLDLQPCIELIEKPNGPPGILALLDEECWFPKATDKSFVEKVVQEQGNNPKFQKPKKLKDDAD 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 575 FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFMADLWKDVDRIVGLDQMAKMTEsSLPSASKTKKGMFRTVG 654
Cdd:cd14932 481 FCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVDRIVGLDKVAGMGE-SLHGAFKTRKGMFRTVG 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 655 QLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAAN 734
Cdd:cd14932 560 QLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 639
|
650 660 670
....*....|....*....|....*....|....*..
gi 156120901 735 AIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd14932 640 AIPKGFMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
99-771 |
0e+00 |
|
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy chain 9 (also called NMMHCA, NMHC-II-A, MHA, FTNS, EPSTS, and DFNA17). Myosin is a hexameric protein composed of a pair of myosin heavy chains (MYH) and two pairs of nonidentical light chains. The encoded protein is a myosin IIA heavy chain that contains an IQ domain and a myosin head-like domain which is involved in several important functions, including cytokinesis, cell motility and maintenance of cell shape. Defects in this gene have been associated with non-syndromic sensorineural deafness autosomal dominant type 17, Epstein syndrome, Alport syndrome with macrothrombocytopenia, Sebastian syndrome, Fechtner syndrome and macrothrombocytopenia with progressive sensorineural deafness. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276883 [Multi-domain] Cd Length: 670 Bit Score: 1156.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKQLPIYSEKIIEMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 178
Cdd:cd14919 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 179 ESGAGKTENTKKVIQYLAMVASSHKGKKDTsitGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHVASSHKSKKDQ---GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 259 ANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRNDLLLEGFNNYTFLSNGFVPIPAAQDDEMFNETVEAMAIMGF 338
Cdd:cd14919 158 ANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 339 TEEEQLSILRVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQAD 418
Cdd:cd14919 238 PEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQAD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 419 FAVEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEE 498
Cdd:cd14919 318 FAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 499 YQREGIEWNFIDFGLDLQPCIELIERPTNPPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQKPKQLKDKTEFSII 578
Cdd:cd14919 398 YQREGIEWNFIDFGLDLQPCIDLIEKPAGPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKQLKDKADFCII 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 579 HYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFMADLWKDVDRIVGLDQMAKMTESSLPSASKTKKGMFRTVGQLYK 658
Cdd:cd14919 478 HYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGMSETALPGAFKTRKGMFRTVGQLYK 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 659 EQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANAIPK 738
Cdd:cd14919 558 EQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPK 637
|
650 660 670
....*....|....*....|....*....|...
gi 156120901 739 GFMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd14919 638 GFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
99-771 |
0e+00 |
|
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain 19. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276899 [Multi-domain] Cd Length: 675 Bit Score: 1135.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKQLPIYSEKIIEMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 178
Cdd:cd15896 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 179 ESGAGKTENTKKVIQYLAMVASSHKGKKDTS----ITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTG 254
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVASSHKTKKDQNslalSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 255 YIVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRNDLLLEGFNNYTFLSNGFVPIPAAQDDEMFNETVEAMA 334
Cdd:cd15896 161 YIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYNNYRFLSNGNVTIPGQQDKDLFTETMEAFR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 335 IMGFTEEEQLSILRVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTK 414
Cdd:cd15896 241 IMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQKAQTQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 415 EQADFAVEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFIL 494
Cdd:cd15896 321 EQAEFAVEALAKATYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 495 EQEEYQREGIEWNFIDFGLDLQPCIELIERPTNPPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQKPKQLKDKTE 574
Cdd:cd15896 401 EQEEYQREGIEWSFIDFGLDLQPCIDLIEKPASPPGILALLDEECWFPKATDKSFVEKVLQEQGTHPKFFKPKKLKDEAD 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 575 FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFMADLWKDVDRIVGLDQMAKMTEssLPSASKTKKGMFRTVG 654
Cdd:cd15896 481 FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVDRIVGLDKVSGMSE--MPGAFKTRKGMFRTVG 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 655 QLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAAN 734
Cdd:cd15896 559 QLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 638
|
650 660 670
....*....|....*....|....*....|....*..
gi 156120901 735 AIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd15896 639 AIPKGFMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
99-771 |
0e+00 |
|
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle myosin heavy chain 2 (also called MYH2A, MYHSA2, MyHC-IIa, MYHas8, MyHC-2A) in insects and mollusks. This gene encodes a member of the class II or conventional myosin heavy chains, and functions in skeletal muscle contraction. Mutations in this gene results in inclusion body myopathy-3 and familial congenital myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276876 [Multi-domain] Cd Length: 674 Bit Score: 1130.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKQLPIYSEKIIEMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 178
Cdd:cd14911 1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 179 ESGAGKTENTKKVIQYLAMVASS---------HKGKKDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 249
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVAASkpkgsgavpHPAVNPAVLIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 250 FDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRNDLLLEGFNNYTFLSNGFVPIPAAQDDEMFNET 329
Cdd:cd14911 161 FDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVPGVDDYAEFQAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 330 VEAMAIMGFTEEEQLSILRVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQ 409
Cdd:cd14911 241 VKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFVT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 410 KAQTKEQADFAVEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNH 489
Cdd:cd14911 321 KAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 490 TMFILEQEEYQREGIEWNFIDFGLDLQPCIELIERPTnppGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQKpKQL 569
Cdd:cd14911 401 TMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPG---GIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMK-TDF 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 570 KDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFMADLWKDVDrIVGLDQMAkMTESSLpsASKTKKGM 649
Cdd:cd14911 477 RGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAE-IVGMAQQA-LTDTQF--GARTRKGM 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 650 FRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 729
Cdd:cd14911 553 FRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYE 632
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 156120901 730 ILAANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd14911 633 LLTPNVIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
87-771 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 1125.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 87 VEDMAELTCLNEASVLHNLRERYFSGLIYTYSGLFCVVVNPYKQLPIYSEKIIEMYKGKKRHEMPPHIYAIADTAYRSML 166
Cdd:pfam00063 1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 167 QDREDQSILCTGESGAGKTENTKKVIQYLAMVASSHKGKKdtsiTGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFI 246
Cdd:pfam00063 81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAGN----VGRLEEQILQSNPILEAFGNAKTVRNNNSSRFGKYI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 247 RINFDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRNDLLLEGFNNYTFLSN-GFVPIPAAQDDEM 325
Cdd:pfam00063 157 EIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYLSQsGCYTIDGIDDSEE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 326 FNETVEAMAIMGFTEEEQLSILRVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGR 405
Cdd:pfam00063 237 FKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCKRRIKTGR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 406 DVVQKAQTKEQADFAVEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQ 485
Cdd:pfam00063 317 ETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTIEKASFIGVLDIYGFEIFEKNSFEQLCINYVNEKLQQ 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 486 LFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIELIERPtnPPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQK 565
Cdd:pfam00063 397 FFNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEKK--PLGILSLLDEECLFPKATDQTFLDKLYSTFSKHPHFQK 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 566 PKQlKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFMADLWKDVDRIVgldqMAKMTESSLPSASKT 645
Cdd:pfam00063 474 PRL-QGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAE----SAAANESGKSTPKRT 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 646 KKGMFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFR 725
Cdd:pfam00063 549 KKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQEFV 628
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 156120901 726 QRYEILAANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:pfam00063 629 QRYRILAPKTWPKWKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
99-771 |
0e+00 |
|
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy chain 14 (also called FLJ13881, KIAA2034, MHC16, MYH17). Its members include mammals, chickens, and turtles. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Some of the data used for this classification were produced by the CyMoBase team at the Max-Planck-Institute for Biophysical Chemistry. The sequence names are composed of the species abbreviation followed by the protein abbreviation and optional protein classifier and variant designations.
Pssm-ID: 276893 [Multi-domain] Cd Length: 670 Bit Score: 1083.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKQLPIYSEKIIEMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 178
Cdd:cd14930 1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 179 ESGAGKTENTKKVIQYLAMVASSHKGKKDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 259 ANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRNDLLLEGFNNYTFLSNGFVPIPAaQDDEMFNETVEAMAIMGF 338
Cdd:cd14930 161 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPG-QERELFQETLESLRVLGF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 339 TEEEQLSILRVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQAD 418
Cdd:cd14930 240 SHEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQAD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 419 FAVEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEE 498
Cdd:cd14930 320 FALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 499 YQREGIEWNFIDFGLDLQPCIELIERPTNPPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQKPKQLKDKTEFSII 578
Cdd:cd14930 400 YQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRHLRDQADFSVL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 579 HYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFMADLWKDVDRIVGLDQMAKMTESslPSASKTKKGMFRTVGQLYK 658
Cdd:cd14930 480 HYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDG--PPGGRPRRGMFRTVGQLYK 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 659 EQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANAIPK 738
Cdd:cd14930 558 ESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPK 637
|
650 660 670
....*....|....*....|....*....|...
gi 156120901 739 GFMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd14930 638 GFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
80-783 |
0e+00 |
|
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical interaction between myosin and actin. The core of the myosin structure is similar in fold to that of kinesin.
Pssm-ID: 214580 [Multi-domain] Cd Length: 677 Bit Score: 1005.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 80 NPPKFSKVEDMAELTCLNEASVLHNLRERYFSGLIYTYSGLFCVVVNPYKQLPIYSEKIIEMYKGKKRHEMPPHIYAIAD 159
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 160 TAYRSMLQDREDQSILCTGESGAGKTENTKKVIQYLAMVASSHKGKkdtsitGELEKQLLQANPILEAFGNAKTVKNDNS 239
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNTEV------GSVEDQILESNPILEAFGNAKTLRNNNS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 240 SRFGKFIRINFDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRNDLLLEGFNNYTFLSNGFVPIPA 319
Cdd:smart00242 155 SRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSPEDYRYLNQGGCLTVD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 320 AQDD-EMFNETVEAMAIMGFTEEEQLSILRVVSSVLQLGNIVFKKERNTDQASMPDNT-AAQKVCHLMGINVTDFTRSIL 397
Cdd:smart00242 235 GIDDaEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAASTVKDKeELSNAAELLGVDPEELEKALT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 398 TPRIKVGRDVVQKAQTKEQADFAVEALAKATYERLFRWILTRVNKALDKTHRQgASFLGILDIAGFEIFEVNSFEQLCIN 477
Cdd:smart00242 315 KRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGS-TYFIGVLDIYGFEIFEVNSFEQLCIN 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 478 YTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIELIERPtnPPGVLALLDEECWFPKATDKSFVEKLCTEQ 557
Cdd:smart00242 394 YANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIEKK--PPGILSLLDEECRFPKGTDQTFLEKLNQHH 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 558 GSHPKFQKPKQlKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFMADLWKDVdrivgldqmakmtes 637
Cdd:smart00242 471 KKHPHFSKPKK-KGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSG--------------- 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 638 slpSASKTKKGMFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPN 717
Cdd:smart00242 535 ---VSNAGSKKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPY 611
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156120901 718 RIVFQEFRQRYEILAANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFRTGVLAHLEEERD 783
Cdd:smart00242 612 RLPFDEFLQRYRVLLPDTWPPWGGDAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELRE 677
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
36-1462 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 890.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 36 VWVPSEKQGFEAASIKEEKGDEVIVEL---VENGKKVTVGKDDIQ--KMNPPKFSKVEDMAELTCLNEASVLHNLRERYF 110
Cdd:COG5022 12 CWIPDEEKGWIWAEIIKEAFNKGKVTEegkKEDGESVSVKKKVLGndRIKLPKFDGVDDLTELSYLNEPAVLHNLEKRYN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 111 SGLIYTYSGLFCVVVNPYKQLPIYSEKIIEMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGESGAGKTENTKK 190
Cdd:COG5022 92 NGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTENAKR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 191 VIQYLAMVASSHkgkkdTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGANIETYLLEKSR 270
Cdd:COG5022 172 IMQYLASVTSSS-----TVEISSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETYLLEKSR 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 271 AIRQARDERTFHIFYYLIAGAKEKMRNDLLLEGFNNYTFLSNGFVP-IPAAQDDEMFNETVEAMAIMGFTEEEQLSILRV 349
Cdd:COG5022 247 VVHQNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLSQGGCDkIDGIDDAKEFKITLDALKTIGIDEEEQDQIFKI 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 350 VSSVLQLGNIVFKKERNtDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQADFAVEALAKATY 429
Cdd:COG5022 327 LAAILHIGNIEFKEDRN-GAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALAIRDSLAKALY 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 430 ERLFRWILTRVNKALDKTHRQGaSFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFI 509
Cdd:COG5022 406 SNLFDWIVDRINKSLDHSAAAS-NFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKEGIEWSFI 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 510 DFgLDLQPCIELIERpTNPPGVLALLDEECWFPKATDKSFVEKLCT--EQGSHPKFQKPKQLKDKteFSIIHYAGKVDYN 587
Cdd:COG5022 485 DY-FDNQPCIDLIEK-KNPLGILSLLDEECVMPHATDESFTSKLAQrlNKNSNPKFKKSRFRDNK--FVVKHYAGDVEYD 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 588 ASAWLTKNMDPLNDNVTSLLNASSDKFMADLWKDVDRIVgldqmakmtesslpsasktKKGMFRTVGQLYKEQLGKLMTT 667
Cdd:COG5022 561 VEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDEENIE-------------------SKGRFPTLGSRFKESLNSLMST 621
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 668 LRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANA----IPKGFMDG 743
Cdd:COG5022 622 LNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSKswtgEYTWKEDT 701
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 744 KQACILMIKALELDPNLYRIGQSKIFFRTGVLAHLEEERDLKITDVIMAFQAMCRGYLARKAFAKRQQQLTAMKVIQRNC 823
Cdd:COG5022 702 KNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKKIQVIQHGF 781
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 824 AAYLKLRNWQWWRLFTKVKPLLQVTRQEEEMQAKED---ELQKTKERQQKAESELKeleqkhsqltEEKNLLQEQLQAET 900
Cdd:COG5022 782 RLRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLAciiKLQKTIKREKKLRETEE----------VEFSLKAEVLIQKF 851
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 901 ELYAEAEEMRVRLaakkqELEEILHEMEARLEEEEDRSQQLQAERKKMAQqmldleeqleeeeAARQKLQLEKVTAEAKI 980
Cdd:COG5022 852 GRSLKAKKRFSLL-----KKETIYLQSAQRVELAERQLQELKIDVKSISS-------------LKLVNLELESEIIELKK 913
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 981 KKLEDDILVMDDQNNKLSKERKLLEER--ISDLTTNLAEEEEKAKNLTKLKNKHESmISELEVRLKKEE-------KSRQ 1051
Cdd:COG5022 914 SLSSDLIENLEFKTELIARLKKLLNNIdlEEGPSIEYVKLPELNKLHEVESKLKET-SEEYEDLLKKSTilvregnKANS 992
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1052 ELEKLKRKLDG---EASDLHEQIAEL---QAQIAELKmQLAKKEEELQAALGRLDDEMAQKNNALKKIRELEGHISDLQe 1125
Cdd:COG5022 993 ELKNFKKELAElskQYGALQESTKQLkelPVEVAELQ-SASKIISSESTELSILKPLQKLKGLLLLENNQLQARYKALK- 1070
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1126 dldseraARNKAEKQKRDLGEELEA----LKTELEDTLDSTATQQELRAKREQEVTMLKKALDEETRSHES--QVQEMRQ 1199
Cdd:COG5022 1071 -------LRRENSLLDDKQLYQLEStenlLKTINVKDLEVTNRNLVKPANVLQFIVAQMIKLNLLQEISKFlsQLVNTLE 1143
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1200 KHTQVVEELTEQLEQFKRAKAN--------LDKNKQALEKENAELAgELRVLSQAkqEVEHKKKKLEVQLQELQSKYSDG 1271
Cdd:COG5022 1144 PVFQKLSVLQLELDGLFWEANLealpspppFAALSEKRLYQSALYD-EKSKLSSS--EVNDLKNELIALFSKIFSGWPRG 1220
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1272 EKVRaELNDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLGSQLQDTQELLQEETRQKLNVSTKLRQLEDERNSLQEQ 1351
Cdd:COG5022 1221 DKLK-KLISEGWVPTEYSTSLKGFNNLNKKFDTPASMSNEKLLSLLNSIDNLLSSYKLEEEVLPATINSLLQYINVGLFN 1299
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1352 L------DEEMEAKQNLERHISTL-----NIQLSDSKKKLQDFASTVELLEEGKKKFQKEIESLTQQYEEKAAAYDKLEK 1420
Cdd:COG5022 1300 AlrtkasSLRWKSATEVNYNSEELddwcrEFEISDVDEELEELIQAVKVLQLLKDDLNKLDELLDACYSLNPAEIQNLKS 1379
|
1450 1460 1470 1480 1490
....*....|....*....|....*....|....*....|....*....|.
gi 156120901 1421 TKNRLQQE-------LDDLVVDLDNQRQLVSNLEKK--QKKFDQLLAEEKN 1462
Cdd:COG5022 1380 RYDPADKEnnlpkeiLKKIEALLIKQELQLSLEGKDetEVHLSEIFSEEKS 1430
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
99-771 |
0e+00 |
|
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276950 [Multi-domain] Cd Length: 633 Bit Score: 884.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKQLPIYSEKIIEMYKGKKRH-EMPPHIYAIADTAYRSMLQDREDQSILCT 177
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 178 GESGAGKTENTKKVIQYLAMVASSHKGKKDTSiTGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 257
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAALSGSGSSKSSSS-ASSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPTGRLV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 258 GANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRNDLLLEGFNNYTFL-----SNGFVPIPAAQDDEMFNETVEA 332
Cdd:cd00124 160 GASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYYYLndylnSSGCDRIDGVDDAEEFQELLDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 333 MAIMGFTEEEQLSILRVVSSVLQLGNIVFKKERNT--DQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQK 410
Cdd:cd00124 240 LDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDedSSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGETITK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 411 AQTKEQADFAVEALAKATYERLFRWILTRVNKALDKTHRQ-GASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNH 489
Cdd:cd00124 320 PLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAeSTSFIGILDIFGFENFEVNSFEQLCINYANEKLQQFFNQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 490 TMFILEQEEYQREGIEWNFIDFgLDLQPCIELIERPtnPPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQKPKQl 569
Cdd:cd00124 400 HVFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEGK--PLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFFSKKR- 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 570 KDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDkfmadlwkdvdrivgldqmakmtesslpsasktkkgm 649
Cdd:cd00124 476 KAKLEFGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSGSQ------------------------------------- 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 650 frtvgqlYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 729
Cdd:cd00124 519 -------FRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYR 591
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 156120901 730 ILAANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd00124 592 ILAPGATEKASDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
99-771 |
0e+00 |
|
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta myosin heavy chain 7b (also called KIAA1512, dJ756N5.1, MYH14, MHC14). MYH7B is a slow-twitch myosin. Mutations in this gene result in one form of autosomal dominant hearing impairment. Multiple transcript variants encoding different isoforms have been found for this gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276953 [Multi-domain] Cd Length: 676 Bit Score: 786.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKQLPIYSEKIIEMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 178
Cdd:cd14927 1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 179 ESGAGKTENTKKVIQYLAMVASSHKGKKD------TSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDV 252
Cdd:cd14927 81 ESGAGKTVNTKRVIQYFAIVAALGDGPGKkaqflaTKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 253 TGYIVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRnDLLLEGFN--NYTFLSNGFVPIPAAQDDEMFNETV 330
Cdd:cd14927 161 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQ-DMLLVSMNpyDYHFCSQGVTTVDNMDDGEELMATD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 331 EAMAIMGFTEEEQLSILRVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQK 410
Cdd:cd14927 240 HAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYVTK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 411 AQTKEQADFAVEALAKATYERLFRWILTRVNKALD-KTHRQgaSFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNH 489
Cdd:cd14927 320 GQSVEQVVYAVGALAKATYDRMFKWLVSRINQTLDtKLPRQ--FFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNH 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 490 TMFILEQEEYQREGIEWNFIDFGLDLQPCIELIERPTnppGVLALLDEECWFPKATDKSFVEKLCTEQ-GSHPKFQKP-- 566
Cdd:cd14927 398 HMFILEQEEYKREGIEWVFIDFGLDLQACIDLIEKPL---GILSILEEECMFPKASDASFKAKLYDNHlGKSPNFQKPrp 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 567 -KQLKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFMADLWKDVdriVGLDQMAKmtESSLPSASKT 645
Cdd:cd14927 475 dKKRKYEAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYENY---VGSDSTED--PKSGVKEKRK 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 646 KKGMFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFR 725
Cdd:cd14927 550 KAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFK 629
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 156120901 726 QRYEILAANAIPK-GFMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd14927 630 QRYRILNPSAIPDdKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
100-771 |
0e+00 |
|
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle myosin heavy chain 3 (MYHC-EMB, MYHSE1, HEMHC, SMHCE) in tetrapods including mammals, lizards, and frogs. This gene is a member of the MYH family and encodes a protein with an IQ domain and a myosin head-like domain. Mutations in this gene have been associated with two congenital contracture (arthrogryposis) syndromes, Freeman-Sheldon syndrome and Sheldon-Hall syndrome. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276878 [Multi-domain] Cd Length: 668 Bit Score: 769.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 100 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKQLPIYSEKIIEMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGE 179
Cdd:cd14913 2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 180 SGAGKTENTKKVIQYLAMVASSH--KGKKDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 257
Cdd:cd14913 82 SGAGKTVNTKRVIQYFATIAATGdlAKKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 258 GANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRnDLLLEGFN--NYTFLSNGFVPIPAAQDDEMFNETVEAMAI 335
Cdd:cd14913 162 SADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELI-ELLLITTNpyDYPFISQGEILVASIDDAEELLATDSAIDI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 336 MGFTEEEQLSILRVVSSVLQLGNIVFKKERNTDQASmPDNT-AAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTK 414
Cdd:cd14913 241 LGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 415 EQADFAVEALAKATYERLFRWILTRVNKALD-KTHRQgaSFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFI 493
Cdd:cd14913 320 DQVHHAVNALSKSVYEKLFLWMVTRINQQLDtKLPRQ--HFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFV 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 494 LEQEEYQREGIEWNFIDFGLDLQPCIELIERPTnppGVLALLDEECWFPKATDKSFVEKLCTEQ-GSHPKFQKPKQLKDK 572
Cdd:cd14913 398 LEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYDQHlGKSNNFQKPKVVKGR 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 573 TE--FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFMADLWKDVDRIVGldqmakmtESSLPSASKTKKGMF 650
Cdd:cd14913 475 AEahFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFATADA--------DSGKKKVAKKKGSSF 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 651 RTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 730
Cdd:cd14913 547 QTVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRV 626
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 156120901 731 LAANAIPKG-FMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd14913 627 LNASAIPEGqFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
99-771 |
0e+00 |
|
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle myosin heavy chain 1 (also called MYHSA1, MYHa, MyHC-2X/D, MGC133384) in insects and crustaceans. Myh1 is a type I skeletal muscle myosin that in Humans is encoded by the MYH1 gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276874 Cd Length: 666 Bit Score: 756.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKQLPIYSEKIIEMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 178
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 179 ESGAGKTENTKKVIQYLAMVASSHKGKKDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGASKKTDEAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 259 ANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRNDLLL-EGFNNYTFLSNGFVPIPAAQDDEMFNETVEAMAIMG 337
Cdd:cd14909 161 ADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLsDNIYDYYIVSQGKVTVPNVDDGEEFSLTDQAFDILG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 338 FTEEEQLSILRVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQA 417
Cdd:cd14909 241 FTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNVQQV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 418 DFAVEALAKATYERLFRWILTRVNKALDkTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQE 497
Cdd:cd14909 321 TNSIGALCKGVFDRLFKWLVKKCNETLD-TQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLEQE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 498 EYQREGIEWNFIDFGLDLQPCIELIERPTnppGVLALLDEECWFPKATDKSFVEKLCTEQ-GSHPKFQKPKQLK---DKT 573
Cdd:cd14909 400 EYKREGIDWAFIDFGMDLLACIDLIEKPM---GILSILEEESMFPKATDQTFSEKLTNTHlGKSAPFQKPKPPKpgqQAA 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 574 EFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFMADLWKDVDRIVGLDQMAKmtesslpSASKTKKGMFRTV 653
Cdd:cd14909 477 HFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAGQSGGGEQAK-------GGRGKKGGGFATV 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 654 GQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAA 733
Cdd:cd14909 550 SSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNP 629
|
650 660 670
....*....|....*....|....*....|....*...
gi 156120901 734 NAIpKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd14909 630 AGI-QGEEDPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
99-771 |
0e+00 |
|
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 pseudogene (also called MHC20, MYH16, and myh5), encoding a sarcomeric myosin heavy chain expressed in nonhuman primate masticatory muscles, is inactivated in humans. This cd contains Myh16 in mammals. MYH16 has intermediate fibres between that of slow type 1 and fast 2B fibres, but exert more force than any other fibre type examined. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Some of the data used for this classification were produced by the CyMoBase team at the Max-Planck-Institute for Biophysical Chemistry. The sequence names are composed of the species abbreviation followed by the protein abbreviation and optional protein classifier and variant designations.
Pssm-ID: 276896 [Multi-domain] Cd Length: 659 Bit Score: 740.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKQLPIYSEKIIEMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 178
Cdd:cd14934 1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 179 ESGAGKTENTKKVIQYLAMVASShkGKKDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd14934 81 ESGAGKTENTKKVIQYFANIGGT--GKQSSDGKGSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKLAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 259 ANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRNDLLL-EGFNNYTFLSNGFVPIPAAQDDEMFNETVEAMAIMG 337
Cdd:cd14934 159 ADIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLLvPNPKEYHWVSQGVTVVDNMDDGEELQITDVAFDVLG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 338 FTEEEQLSILRVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQA 417
Cdd:cd14934 239 FSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQKGQNMEQC 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 418 DFAVEALAKATYERLFRWILTRVNKALDkTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQE 497
Cdd:cd14934 319 NNSIGALGKAVYDKMFKWLVVRINKTLD-TKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFVLEQE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 498 EYQREGIEWNFIDFGLDLQPCIELIERPTnppGVLALLDEECWFPKATDKSFVEKLCTEQ-GSHPKFQKPKQLKDK---T 573
Cdd:cd14934 398 EYKREGIEWVFIDFGLDLQACIDLLEKPM---GIFSILEEQCVFPKATDATFKAALYDNHlGKSSNFLKPKGGKGKgpeA 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 574 EFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSdkfmadlwkdvdriVGLDQMAKMTESSLPSASKTKKGM-FRT 652
Cdd:cd14934 475 HFELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSS--------------LGLLALLFKEEEAPAGSKKQKRGSsFMT 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 653 VGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILA 732
Cdd:cd14934 541 VSNFYREQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLN 620
|
650 660 670
....*....|....*....|....*....|....*....
gi 156120901 733 ANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd14934 621 PNVIPQGFVDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
100-771 |
0e+00 |
|
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins that transport a variety of intracellular cargo processively along actin filaments, such as melanosomes, synaptic vesicles, vacuoles, and mRNA. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. It also contains a IQ domain and a globular DIL domain. Myosin V is a class of actin-based motor proteins involved in cytoplasmic vesicle transport and anchorage, spindle-pole alignment and mRNA translocation. The protein encoded by this gene is abundant in melanocytes and nerve cells. Mutations in this gene cause Griscelli syndrome type-1 (GS1), Griscelli syndrome type-3 (GS3) and neuroectodermal melanolysosomal disease, or Elejalde disease. Multiple alternatively spliced transcript variants encoding different isoforms have been reported, but the full-length nature of some variants has not been determined. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Note that the Dictyostelium myoVs are not contained in this child group. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276831 [Multi-domain] Cd Length: 629 Bit Score: 713.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 100 SVLHNLRERYFSG-LIYTYSGLFCVVVNPYKQLPIYSEKIIEMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 178
Cdd:cd01380 2 AVLHNLKVRFCQRnAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 179 ESGAGKTENTKKVIQYLAMVASSHKGKkdTSItgelEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd01380 82 ESGAGKTVSAKYAMRYFATVGGSSSGE--TQV----EEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYRIIG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 259 ANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRNDLLLEGFNNYTFLSNGFVP-IPAAQDDEMFNETVEAMAIMG 337
Cdd:cd01380 156 ANMRTYLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNQGGSPvIDGVDDAAEFEETRKALTLLG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 338 FTEEEQLSILRVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQA 417
Cdd:cd01380 236 ISEEEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPLTLQQA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 418 DFAVEALAKATYERLFRWILTRVNKALDKTHRQGA-SFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQ 496
Cdd:cd01380 316 IVARDALAKHIYAQLFDWIVDRINKALASPVKEKQhSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHVFKLEQ 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 497 EEYQREGIEWNFIDFgLDLQPCIELIErptNPPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPK--FQKPKQlkDKTE 574
Cdd:cd01380 396 EEYVKEEIEWSFIDF-YDNQPCIDLIE---GKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKPNkhFKKPRF--SNTA 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 575 FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNassdkfmadlwkdvdrivgldqmakmtesslpsASKTKKgmfRTVG 654
Cdd:cd01380 470 FIVKHFADDVEYQVEGFLEKNRDTVSEEHLNVLK---------------------------------ASKNRK---KTVG 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 655 QLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILaan 734
Cdd:cd01380 514 SQFRDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVL--- 590
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 156120901 735 aIPKGF---MDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd01380 591 -LPSKEwlrDDKKKTCENILENLILDPDKYQFGKTKIFFR 629
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
99-771 |
0e+00 |
|
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy chain 15 in mammals (also called KIAA1000) . MYH15 is a slow-twitch myosin. Myh15 is a ventricular myosin heavy chain. Myh15 is absent in embryonic and fetal muscles and is found in orbital layer of extraocular muscles at birth. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276892 [Multi-domain] Cd Length: 662 Bit Score: 713.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKQLPIYSEKIIEMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 178
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 179 ESGAGKTENTKKVIQYLAMVASSHKGKKDTsitGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAMIESKKKL---GALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 259 ANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEkMRNDLLL-EGFNNYTFLSNGFVPIPAAQDDEMFNETVEAMAIMG 337
Cdd:cd14929 158 ADIDIYLLEKSRVIFQQPGERNYHIFYQILSGKKE-LRDLLLVsANPSDFHFCSCGAVAVESLDDAEELLATEQAMDILG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 338 FTEEEQLSILRVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQA 417
Cdd:cd14929 237 FLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTRSQNIEQV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 418 DFAVEALAKATYERLFRWILTRVNKALD-KTHRQgaSFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQ 496
Cdd:cd14929 317 TYAVGALSKSIYERMFKWLVARINRVLDaKLSRQ--FFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMFVLEQ 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 497 EEYQREGIEWNFIDFGLDLQPCIELIERPTnppGVLALLDEECWFPKATDKSFVEKLCTEQ-GSHPKFQKPKQLKDKTE- 574
Cdd:cd14929 395 EEYRKEGIDWVSIDFGLDLQACIDLIEKPM---GIFSILEEECMFPKATDLTFKTKLFDNHfGKSVHFQKPKPDKKKFEa 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 575 -FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFMADLW-KDVdrivgldqmakMTESSLPSASKT-KKGM-F 650
Cdd:cd14929 472 hFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFeNYI-----------STDSAIQFGEKKrKKGAsF 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 651 RTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 730
Cdd:cd14929 541 QTVASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCI 620
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 156120901 731 LAANAIPKG-FMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd14929 621 LNPRTFPKSkFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
100-771 |
0e+00 |
|
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I cardiac muscle myosin heavy chain 7 (also called CMH1, MPD1, and CMD1S). Muscle myosin is a hexameric protein containing 2 heavy chain subunits, 2 alkali light chain subunits, and 2 regulatory light chain subunits. It is expressed predominantly in normal human ventrical and in skeletal muscle tissues rich in slow-twitch type I muscle fibers. Changes in the relative abundance of this protein and the alpha (or fast) heavy subunit of cardiac myosin correlate with the contractile velocity of cardiac muscle. Its expression is also altered during thyroid hormone depletion and hemodynamic overloading. Mutations in this gene are associated with familial hypertrophic cardiomyopathy, myosin storage myopathy, dilated cardiomyopathy, and Laing early-onset distal myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276881 [Multi-domain] Cd Length: 668 Bit Score: 698.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 100 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKQLPIYSEKIIEMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGE 179
Cdd:cd14917 2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 180 SGAGKTENTKKVIQYLAMVAS-SHKGKKDTSI-TGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 257
Cdd:cd14917 82 SGAGKTVNTKRVIQYFAVIAAiGDRSKKDQTPgKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 258 GANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRNDLLLEgfNN---YTFLSNGFVPIPAAQDDEMFNETVEAMA 334
Cdd:cd14917 162 SADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLIT--NNpydYAFISQGETTVASIDDAEELMATDNAFD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 335 IMGFTEEEQLSILRVVSSVLQLGNIVFKKERNTDQASmPDNT-AAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQT 413
Cdd:cd14917 240 VLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAE-PDGTeEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 414 KEQADFAVEALAKATYERLFRWILTRVNKALDkTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFI 493
Cdd:cd14917 319 VQQVIYATGALAKAVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFV 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 494 LEQEEYQREGIEWNFIDFGLDLQPCIELIERPTnppGVLALLDEECWFPKATDKSFVEKLCTEQ-GSHPKFQKPKQLKDK 572
Cdd:cd14917 398 LEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKATDMTFKAKLFDNHlGKSNNFQKPRNIKGK 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 573 TE--FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFMADLWKDVdriVGLDQMAKmtesslPSASKTKKG-M 649
Cdd:cd14917 475 PEahFSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFANY---AGADAPIE------KGKGKAKKGsS 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 650 FRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 729
Cdd:cd14917 546 FQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYR 625
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 156120901 730 ILAANAIPKG-FMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd14917 626 ILNPAAIPEGqFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
101-771 |
0e+00 |
|
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle myosin heavy chain 8 (also called MyHC-peri, MyHC-pn). Myosin is a hexameric protein composed of a pair of myosin heavy chains (MYH) and two pairs of nonidentical light chains. A mutation in this gene results in trismus-pseudocamptodactyly syndrome. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276882 [Multi-domain] Cd Length: 668 Bit Score: 696.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 101 VLHNLRERYFSGLIYTYSGLFCVVVNPYKQLPIYSEKIIEMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGES 180
Cdd:cd14918 3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 181 GAGKTENTKKVIQYLAMVASSHKGKKDTS--ITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd14918 83 GAGKTVNTKRVIQYFATIAVTGEKKKEESgkMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLAS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 259 ANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRNDLLL-EGFNNYTFLSNGFVPIPAAQDDEMFNETVEAMAIMG 337
Cdd:cd14918 163 ADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLItTNPYDYAFVSQGEITVPSIDDQEELMATDSAIDILG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 338 FTEEEQLSILRVVSSVLQLGNIVFKKERNTDQASmPDNT-AAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQ 416
Cdd:cd14918 243 FTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVQQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 417 ADFAVEALAKATYERLFRWILTRVNKALDkTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQ 496
Cdd:cd14918 322 VYNAVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 497 EEYQREGIEWNFIDFGLDLQPCIELIERPTnppGVLALLDEECWFPKATDKSFVEKLCTEQ-GSHPKFQKPKQLKDKTE- 574
Cdd:cd14918 401 EEYKKEGIEWTFIDFGMDLAACIELIEKPL---GIFSILEEECMFPKATDTSFKNKLYDQHlGKSANFQKPKVVKGKAEa 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 575 -FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFMADLWKDVdrivgldqMAKMTESSLPSASKTKKGMFRTV 653
Cdd:cd14918 478 hFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTY--------ASAEADSGAKKGAKKKGSSFQTV 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 654 GQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAA 733
Cdd:cd14918 550 SALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNA 629
|
650 660 670
....*....|....*....|....*....|....*....
gi 156120901 734 NAIPKG-FMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd14918 630 SAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
100-771 |
0e+00 |
|
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle myosin heavy chain 1 (also called MYHSA1, MYHa, MyHC-2X/D, MGC133384) in mammals. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276875 [Multi-domain] Cd Length: 671 Bit Score: 687.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 100 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKQLPIYSEKIIEMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGE 179
Cdd:cd14910 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 180 SGAGKTENTKKVIQYLAMVASSHKGKKDT----SITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGY 255
Cdd:cd14910 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEatsgKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 256 IVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRNDLLL-EGFNNYTFLSNGFVPIPAAQDDEMFNETVEAMA 334
Cdd:cd14910 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLItTNPYDYAFVSQGEITVPSIDDQEELMATDSAIE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 335 IMGFTEEEQLSILRVVSSVLQLGNIVFKKERNTDQASmPDNT-AAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQT 413
Cdd:cd14910 242 ILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 414 KEQADFAVEALAKATYERLFRWILTRVNKALDkTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFI 493
Cdd:cd14910 321 VQQVYNAVGALAKAVYDKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 494 LEQEEYQREGIEWNFIDFGLDLQPCIELIERPTnppGVLALLDEECWFPKATDKSFVEKLCTEQ-GSHPKFQKPKQLKDK 572
Cdd:cd14910 400 LEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQKPKPAKGK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 573 TE--FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFMADLWKDVdrivgldQMAKMTESSLPSASKTKKGMF 650
Cdd:cd14910 477 VEahFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGA-------AAAEAEEGGGKKGGKKKGSSF 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 651 RTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 730
Cdd:cd14910 550 QTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKV 629
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 156120901 731 LAANAIPKG-FMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd14910 630 LNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
100-771 |
0e+00 |
|
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac muscle myosin heavy chain 6. Cardiac muscle myosin is a hexamer consisting of two heavy chain subunits, two light chain subunits, and two regulatory subunits. This gene encodes the alpha heavy chain subunit of cardiac myosin. Mutations in this gene cause familial hypertrophic cardiomyopathy and atrial septal defect. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276880 [Multi-domain] Cd Length: 670 Bit Score: 686.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 100 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKQLPIYSEKIIEMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGE 179
Cdd:cd14916 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 180 SGAGKTENTKKVIQYLAMVAS-SHKGKKD--TSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYI 256
Cdd:cd14916 82 SGAGKTVNTKRVIQYFASIAAiGDRSKKEnpNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 257 VGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRNDLLLEgfNN---YTFLSNGFVPIPAAQDDEMFNETVEAM 333
Cdd:cd14916 162 ASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVT--NNpydYAFVSQGEVSVASIDDSEELLATDSAF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 334 AIMGFTEEEQLSILRVVSSVLQLGNIVFKKERNTDQASmPDNTA-AQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQ 412
Cdd:cd14916 240 DVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAE-PDGTEdADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 413 TKEQADFAVEALAKATYERLFRWILTRVNKALDkTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMF 492
Cdd:cd14916 319 SVQQVYYSIGALAKSVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 493 ILEQEEYQREGIEWNFIDFGLDLQPCIELIERPTnppGVLALLDEECWFPKATDKSFVEKLCTEQ-GSHPKFQKPKQLKD 571
Cdd:cd14916 398 VLEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKASDMTFKAKLYDNHlGKSNNFQKPRNVKG 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 572 KTE--FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFMADLWKDVdrivgldQMAKMTESSLPSASKTKKGM 649
Cdd:cd14916 475 KQEahFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTY-------ASADTGDSGKGKGGKKKGSS 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 650 FRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 729
Cdd:cd14916 548 FQTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYR 627
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 156120901 730 ILAANAIPKG-FMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd14916 628 ILNPAAIPEGqFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
100-771 |
0e+00 |
|
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin heavy chain 13 (also called MyHC-eo) in mammals, chicken, and green anole. Myh13 is a myosin whose expression is restricted primarily to the extrinsic eye muscles which are specialized for function in eye movement. Class II myosins, also called conventional myosins, are the myosin type responsible for producing muscle contraction in muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276887 [Multi-domain] Cd Length: 671 Bit Score: 684.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 100 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKQLPIYSEKIIEMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGE 179
Cdd:cd14923 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 180 SGAGKTENTKKVIQYLAMVASSHKGKKD---TSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYI 256
Cdd:cd14923 82 SGAGKTVNTKRVIQYFATIAVTGDKKKEqqpGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 257 VGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRnDLLLEGFN--NYTFLSNGFVPIPAAQDDEMFNETVEAMA 334
Cdd:cd14923 162 ASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELI-DLLLISTNpfDFPFVSQGEVTVASIDDSEELLATDNAID 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 335 IMGFTEEEQLSILRVVSSVLQLGNIVFKKERNTDQASmPDNT-AAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQT 413
Cdd:cd14923 241 ILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 414 KEQADFAVEALAKATYERLFRWILTRVNKALDkTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFI 493
Cdd:cd14923 320 VQQVTNSVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 494 LEQEEYQREGIEWNFIDFGLDLQPCIELIERPTnppGVLALLDEECWFPKATDKSFVEKLCTEQ-GSHPKFQKPKQLKDK 572
Cdd:cd14923 399 LEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYDQHlGKSNNFQKPKPAKGK 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 573 TE--FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFMADLWKDVDRIVGLDQMAKmtesslPSASKTKKGMF 650
Cdd:cd14923 476 AEahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYAGAEAGDSGGS------KKGGKKKGSSF 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 651 RTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 730
Cdd:cd14923 550 QTVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRI 629
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 156120901 731 LAANAIPKG-FMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd14923 630 LNASAIPEGqFIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
100-771 |
0e+00 |
|
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle myosin heavy chain 2 (also called MYH2A, MYHSA2, MyHC-IIa, MYHas8, MyHC-2A) in mammals. Mutations in this gene results in inclusion body myopathy-3 and familial congenital myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276877 [Multi-domain] Cd Length: 673 Bit Score: 681.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 100 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKQLPIYSEKIIEMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGE 179
Cdd:cd14912 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 180 SGAGKTENTKKVIQYLAMVASSHKGKKDT----SITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGY 255
Cdd:cd14912 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEitsgKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 256 IVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRNDLLL-EGFNNYTFLSNGFVPIPAAQDDEMFNETVEAMA 334
Cdd:cd14912 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLItTNPYDYPFVSQGEISVASIDDQEELMATDSAID 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 335 IMGFTEEEQLSILRVVSSVLQLGNIVFKKERNTDQASmPDNT-AAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQT 413
Cdd:cd14912 242 ILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAE-PDGTeVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 414 KEQADFAVEALAKATYERLFRWILTRVNKALDkTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFI 493
Cdd:cd14912 321 VEQVTNAVGALAKAVYEKMFLWMVARINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 494 LEQEEYQREGIEWNFIDFGLDLQPCIELIERPTnppGVLALLDEECWFPKATDKSFVEKLCTEQ-GSHPKFQKPKQLKDK 572
Cdd:cd14912 400 LEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSANFQKPKVVKGK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 573 TE--FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFMADLWKDVDRIVGldqmaKMTESSLPSASKTKKGMF 650
Cdd:cd14912 477 AEahFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSGAQTAEG-----ASAGGGAKKGGKKKGSSF 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 651 RTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 730
Cdd:cd14912 552 QTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKV 631
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 156120901 731 LAANAIPKG-FMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd14912 632 LNASAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
100-771 |
0e+00 |
|
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin heavy chain 4 (also called MYH2B, MyHC-2B, MyHC-IIb). Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276879 [Multi-domain] Cd Length: 671 Bit Score: 674.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 100 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKQLPIYSEKIIEMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGE 179
Cdd:cd14915 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 180 SGAGKTENTKKVIQYLAMVASSHKGKKDTSITGE----LEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGY 255
Cdd:cd14915 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEAASGKmqgtLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 256 IVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRnDLLLEGFNNYTF--LSNGFVPIPAAQDDEMFNETVEAM 333
Cdd:cd14915 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELI-EMLLITTNPYDFafVSQGEITVPSIDDQEELMATDSAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 334 AIMGFTEEEQLSILRVVSSVLQLGNIVFKKERNTDQASmPDNT-AAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQ 412
Cdd:cd14915 241 DILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 413 TKEQADFAVEALAKATYERLFRWILTRVNKALDkTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMF 492
Cdd:cd14915 320 TVQQVYNSVGALAKAIYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 493 ILEQEEYQREGIEWNFIDFGLDLQPCIELIERPTnppGVLALLDEECWFPKATDKSFVEKLCTEQ-GSHPKFQKPKQLKD 571
Cdd:cd14915 399 VLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQKPKPAKG 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 572 KTE--FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFMADLWKDvdrivglDQMAKMTESSLPSASKTKKGM 649
Cdd:cd14915 476 KAEahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFSG-------GQTAEAEGGGGKKGGKKKGSS 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 650 FRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 729
Cdd:cd14915 549 FQTVSALFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYK 628
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 156120901 730 ILAANAIPKG-FMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd14915 629 VLNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
100-771 |
0e+00 |
|
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ motifs such as found in class V, VIII, XI, and XIII myosins. These myosins are defined by two tandem MyTH4 and FERM domains. The apicomplexan, but not diatom myosins contain 4-6 WD40 repeats near the end of the C-terminal tail which suggests a possible function of these myosins in signal transduction and transcriptional regulation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276849 [Multi-domain] Cd Length: 661 Bit Score: 657.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 100 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKQLPIYSEKIIEMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGE 179
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 180 SGAGKTENTKKVIQYLAMVASSHKgkkdtsitgELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGA 259
Cdd:cd14883 82 SGAGKTETTKLILQYLCAVTNNHS---------WVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGHIKGA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 260 NIETYLLEKSRAIRQARDERTFHIFYYLIAGAKE--KMRNDLLLEGFNNYTFLS-NGFVPIPAAQDDEMFNETVEAMAIM 336
Cdd:cd14883 153 IIQDYLLEQSRITFQAPGERNYHVFYQLLAGAKHskELKEKLKLGEPEDYHYLNqSGCIRIDNINDKKDFDHLRLAMNVL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 337 GFTEEEQLSILRVVSSVLQLGNIVFKK-ERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKE 415
Cdd:cd14883 233 GIPEEMQEGIFSVLSAILHLGNLTFEDiDGETGALTVEDKEILKIVAKLLGVDPDKLKKALTIRQINVRGNVTEIPLKVQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 416 QADFAVEALAKATYERLFRWILTRVNKALDK---THRqgasFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMF 492
Cdd:cd14883 313 EARDNRDAMAKALYSRTFAWLVNHINSCTNPgqkNSR----FIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHYVF 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 493 ILEQEEYQREGIEWNFIDFGlDLQPCIELIERPtnPPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQKPKQLKDK 572
Cdd:cd14883 389 KLEQEEYEKEGINWSHIVFT-DNQECLDLIEKP--PLGILKLLDEECRFPKGTDLTYLEKLHAAHEKHPYYEKPDRRRWK 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 573 TEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFMADLWKDVD--RIVGLDQMAKMTESSlpsaSKTKKGMf 650
Cdd:cd14883 466 TEFGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFTYPDllALTGLSISLGGDTTS----RGTSKGK- 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 651 RTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 730
Cdd:cd14883 541 PTVGDTFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLC 620
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 156120901 731 LAANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd14883 621 LDPRARSADHKETCGAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
100-771 |
0e+00 |
|
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated with endocytosis, cytokinesis, cell-to-cell coupling and gating at plasmodesmata. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. It also contains IQ domains Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276834 Cd Length: 647 Bit Score: 651.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 100 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKQLPIYSEKIIEMYKgkKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGE 179
Cdd:cd01383 2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYR--QKLLDSPHVYAVADTAYREMMRDEINQSIIISGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 180 SGAGKTENTKKVIQYLAMVASSHKGkkdtsitgeLEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGA 259
Cdd:cd01383 80 SGAGKTETAKIAMQYLAALGGGSSG---------IENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKICGA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 260 NIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRNDLLLEGFNNYTFLS-NGFVPIPAAQDDEMFNETVEAMAIMGF 338
Cdd:cd01383 151 KIQTYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKSASEYKYLNqSNCLTIDGVDDAKKFHELKEALDTVGI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 339 TEEEQLSILRVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQAD 418
Cdd:cd01383 231 SKEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKLTLQQAI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 419 FAVEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEE 498
Cdd:cd01383 311 DARDALAKAIYASLFDWLVEQINKSLEVGKRRTGRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLFKLEQEE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 499 YQREGIEWNFIDFgLDLQPCIELIERptNPPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQKpkqlKDKTEFSII 578
Cdd:cd01383 391 YELDGIDWTKVDF-EDNQECLDLIEK--KPLGLISLLDEESNFPKATDLTFANKLKQHLKSNSCFKG----ERGGAFTIR 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 579 HYAGKVDYNASAWLTKNMDPLNDNVTSLLnASSDKFMADLWKdvdrIVGLDQMAKMTESSLPSASKTKKgmfRTVGQLYK 658
Cdd:cd01383 464 HYAGEVTYDTSGFLEKNRDLLHSDLIQLL-SSCSCQLPQLFA----SKMLDASRKALPLTKASGSDSQK---QSVATKFK 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 659 EQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANAIpK 738
Cdd:cd01383 536 GQLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLPEDV-S 614
|
650 660 670
....*....|....*....|....*....|...
gi 156120901 739 GFMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd01383 615 ASQDPLSTSVAILQQFNILPEMYQVGYTKLFFR 647
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
100-771 |
0e+00 |
|
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, and class I myosins have been implicated in phagocytosis and vesicle transport. Myosin I, an unconventional myosin, does not form dimers. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. There are 5 myosin subclasses with subclasses c/h, d/g, and a/b have an IQ domain and a TH1 domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276829 Cd Length: 652 Bit Score: 646.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 100 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKQLPIYSEKIIEMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGE 179
Cdd:cd01378 2 AINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 180 SGAGKTENTKKVIQYLAMVASSHkgkkDTSItGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGA 259
Cdd:cd01378 82 SGAGKTEASKRIMQYIAAVSGGS----ESEV-ERVKDMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEPVGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 260 NIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRNDLLLEGFNNYTFLSNGFVPIPAAQDDEM-FNETVEAMAIMGF 338
Cdd:cd01378 157 HITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGCFDVDGIDDAAdFKEVLNAMKVIGF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 339 TEEEQLSILRVVSSVLQLGNIVFKKERNtDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVG---RDVVQKAQTKE 415
Cdd:cd01378 237 TEEEQDSIFRILAAILHLGNIQFAEDEE-GNAAISDTSVLDFVAYLLGVDPDQLEKALTHRTIETGgggRSVYEVPLNVE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 416 QADFAVEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILE 495
Cdd:cd01378 316 QAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKKKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFIELTLKAE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 496 QEEYQREGIEWNFIDFgLDLQPCIELIERptNPPGVLALLDEECWFP-KATDKSFVEKLCTEQGSHPKFQKPKQLKD--K 572
Cdd:cd01378 396 QEEYVREGIEWTPIKY-FNNKIICDLIEE--KPPGIFAILDDACLTAgDATDQTFLQKLNQLFSNHPHFECPSGHFElrR 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 573 TEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFMADLWKDVDrivgldqmakmtesslpsaSKTKKGMFRT 652
Cdd:cd01378 473 GEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEGV-------------------DLDSKKRPPT 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 653 VGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILA 732
Cdd:cd01378 534 AGTKFKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYKLLS 613
|
650 660 670
....*....|....*....|....*....|....*....
gi 156120901 733 ANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd01378 614 PKTWPAWDGTWQGGVESILKDLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
99-771 |
0e+00 |
|
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle transport. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle.
Pssm-ID: 276835 Cd Length: 647 Bit Score: 618.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKQLP-IYSEKIIEMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCT 177
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 178 GESGAGKTENTKKVIQYLAmvassHKGKKDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 257
Cdd:cd01384 81 GESGAGKTETTKMLMQYLA-----YMGGRAVTEGRSVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAGRIS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 258 GANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRNDLLLEGFNNYTFL--SNGFvPIPAAQDDEMFNETVEAMAI 335
Cdd:cd01384 156 GAAIRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKDPKQFHYLnqSKCF-ELDGVDDAEEYRATRRAMDV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 336 MGFTEEEQLSILRVVSSVLQLGNIVFKKERNTDQASMPD---NTAAQKVCHLMGINVTDFTRSiLTPRIKVGRD-VVQKA 411
Cdd:cd01384 235 VGISEEEQDAIFRVVAAILHLGNIEFSKGEEDDSSVPKDeksEFHLKAAAELLMCDEKALEDA-LCKRVIVTPDgIITKP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 412 QTKEQADFAVEALAKATYERLFRWILTRVNKALDKTHRQgASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTM 491
Cdd:cd01384 314 LDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNS-KRLIGVLDIYGFESFKTNSFEQFCINLANEKLQQHFNQHV 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 492 FILEQEEYQREGIEWNFIDFgLDLQPCIELIERptNPPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQKPKqlKD 571
Cdd:cd01384 393 FKMEQEEYTKEEIDWSYIEF-VDNQDVLDLIEK--KPGGIIALLDEACMFPRSTHETFAQKLYQTLKDHKRFSKPK--LS 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 572 KTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFMADLWKDVDRivgldqmakmtesslpsaSKTKKGM-F 650
Cdd:cd01384 468 RTDFTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLFPPLPR------------------EGTSSSSkF 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 651 RTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 730
Cdd:cd01384 530 SSIGSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGL 609
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 156120901 731 LAANAiPKGFMDGKQACILMIKALELDPnlYRIGQSKIFFR 771
Cdd:cd01384 610 LAPEV-LKGSDDEKAACKKILEKAGLKG--YQIGKTKVFLR 647
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
99-771 |
0e+00 |
|
class VII myosin, motor domain; These monomeric myosins have been associated with functions in sensory systems such as vision and hearing. Mammalian myosin VII has a tail with 2 MyTH4 domains, 2 FERM domains, and a SH3 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276832 Cd Length: 648 Bit Score: 607.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKQLPIYSEKIIEMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 178
Cdd:cd01381 1 AGILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 179 ESGAGKTENTKKVIQYLAMVASSHkgkkdTSItgelEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd01381 81 ESGAGKTESTKLILQYLAAISGQH-----SWI----EQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIEG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 259 ANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRNDLLLEGFNNYTFLSNG-FVPIPAAQDDEMFNETVEAMAIMG 337
Cdd:cd01381 152 AKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDASDYYYLTQGnCLTCEGRDDAAEFADIRSAMKVLM 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 338 FTEEEQLSILRVVSSVLQLGNIVFKK--ERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKE 415
Cdd:cd01381 232 FTDEEIWDIFKLLAAILHLGNIKFEAtvVDNLDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSPLSAE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 416 QADFAVEALAKATYERLFRWILTRVNKALDKTHRQGASFL--GILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFI 493
Cdd:cd01381 312 QALDVRDAFVKGIYGRLFIWIVNKINSAIYKPRGTDSSRTsiGVLDIFGFENFEVNSFEQLCINFANENLQQFFVRHIFK 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 494 LEQEEYQREGIEWNFIDFgLDLQPCIELI-ERPTNppgVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQKPKQLKDk 572
Cdd:cd01381 392 LEQEEYDKEGINWQHIEF-VDNQDVLDLIaLKPMN---IMSLIDEESKFPKGTDQTMLEKLHSTHGNNKNYLKPKSDLN- 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 573 TEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFMADLWkDVDRIVGLDqmakmtesslpSASKTKkgmfrT 652
Cdd:cd01381 467 TSFGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLF-NEDISMGSE-----------TRKKSP-----T 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 653 VGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILA 732
Cdd:cd01381 530 LSSQFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVLV 609
|
650 660 670
....*....|....*....|....*....|....*....
gi 156120901 733 ANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd01381 610 PGIPPAHKTDCRAATRKICCAVLGGDADYQLGKTKIFLK 648
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
99-771 |
0e+00 |
|
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the minus-end of actin filaments, in contrast to most other myosins which moves towards the plus-end of actin filaments. It is thought that myosin VI, unlike plus-end directed myosins, does not use a pure lever arm mechanism, but instead steps with a mechanism analogous to the kinesin neck-linker uncoupling model. It has been implicated in a myriad of functions including: the transport of cytoplasmic organelles, maintenance of normal Golgi morphology, endocytosis, secretion, cell migration, border cell migration during development, and in cancer metastasis playing roles in deafness and retinal development among others. While how this is accomplished is largely unknown there are several interacting proteins that have been identified such as disabled homolog 2 (DAB2), GIPC1, synapse-associated protein 97 (SAP97; also known as DLG1) and optineurin, which have been found to target myosin VI to different cellular compartments. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the minus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276833 Cd Length: 649 Bit Score: 595.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKQLP-IYSEKIIEMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCT 177
Cdd:cd01382 1 ATLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 178 GESGAGKTENTKKVIQYLAMVASSHkgkkdtsiTGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 257
Cdd:cd01382 81 GESGAGKTESTKYILRYLTESWGSG--------AGPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 258 GANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRNDLLLegfnnytflsngfvpIPAAQDDEMFNETVEAMAIMG 337
Cdd:cd01382 153 GGFVSHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLLK---------------DPLLDDVGDFIRMDKAMKKIG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 338 FTEEEQLSILRVVSSVLQLGNIVFKKERNT-------DQASMPDNTAAQKvchLMGINVTDF-----TRSILTPRIKVGR 405
Cdd:cd01382 218 LSDEEKLDIFRVVAAVLHLGNIEFEENGSDsgggcnvKPKSEQSLEYAAE---LLGLDQDELrvsltTRVMQTTRGGAKG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 406 DVVQKAQTKEQADFAVEALAKATYERLFRWILTRVNKALdkTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQ 485
Cdd:cd01382 295 TVIKVPLKVEEANNARDALAKAIYSKLFDHIVNRINQCI--PFETSSYFIGVLDIAGFEYFEVNSFEQFCINYCNEKLQQ 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 486 LFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIELIERPTNppGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQK 565
Cdd:cd01382 373 FFNERILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEAKLV--GILDLLDEESKLPKPSDQHFTSAVHQKHKNHFRLSI 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 566 P--------KQLKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFMADLWkdvdrivgldqmAKMTES 637
Cdd:cd01382 450 PrksklkihRNLRDDEGFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLF------------ESSTNN 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 638 SLPSASKTKKGMFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPN 717
Cdd:cd01382 518 NKDSKQKAGKLSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPS 597
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 156120901 718 RIVFQEFRQRYEILAANAIPKgfMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd01382 598 RTSFHDLYNMYKKYLPPKLAR--LDPRLFCKALFKALGLNENDFKFGLTKVFFR 649
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
99-771 |
0e+00 |
|
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or C-terminal to their motor domain and a tail with a MyTH4 domain followed by a SH3 domain in some instances. The monomeric Acanthamoebas were the first identified members of this group and have been joined by Stramenopiles. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276839 Cd Length: 644 Bit Score: 570.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKQLPIYSEKIIEMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 178
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 179 ESGAGKTENTKKVIQYLAMVASShkgkkdtsiTGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd14872 81 ESGAGKTEATKQCLSFFAEVAGS---------TNGVEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRICG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 259 ANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRNDLLLEGFNNYTFLSnGFVPIPAAQDDEMFNETVEAMAIMGF 338
Cdd:cd14872 152 ASTENYLLEKSRVVYQIKGERNFHIFYQLLASPDPASRGGWGSSAAYGYLSLS-GCIEVEGVDDVADFEEVVLAMEQLGF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 339 TEEEQLSILRVVSSVLQLGNIVFKKERNTDQAS---MPDNTAAQKVCHLMGINVTDFTRSILTPRIKV-GRDVVQKAQTK 414
Cdd:cd14872 231 DDADINNVMSLIAAILKLGNIEFASGGGKSLVSgstVANRDVLKEVATLLGVDAATLEEALTSRLMEIkGCDPTRIPLTP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 415 EQADFAVEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFIL 494
Cdd:cd14872 311 AQATDACDALAKAAYSRLFDWLVKKINESMRPQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEKLQQHFNQYTFKL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 495 EQEEYQREGIEWNFIDFgLDLQPCIELIERptNPPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQKPKQLKDKTE 574
Cdd:cd14872 391 EEALYQSEGVKFEHIDF-IDNQPVLDLIEK--KQPGLMLALDDQVKIPKGSDATFMIAANQTHAAKSTFVYAEVRTSRTE 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 575 FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFmadlwkdvdrivgldqMAKMTESSLPSaSKTKKGmfrTVG 654
Cdd:cd14872 468 FIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKL----------------IAVLFPPSEGD-QKTSKV---TLG 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 655 QLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAAn 734
Cdd:cd14872 528 GQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKRYRFLVK- 606
|
650 660 670
....*....|....*....|....*....|....*...
gi 156120901 735 AIPKGFM-DGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd14872 607 TIAKRVGpDDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
99-771 |
2.39e-178 |
|
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have very long tail domains consisting of three IQ motifs, short coiled-coil regions, up to 18 CBS domains, a PB1 domain, and a carboxy-terminal transmembrane domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276855 [Multi-domain] Cd Length: 662 Bit Score: 556.70 E-value: 2.39e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKQLP-IYSEKIIEMYKGKKRHEMPPHIYAIADTAYRSMLQ----DREDQS 173
Cdd:cd14890 1 ASLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQsgvlDPSNQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 174 ILCTGESGAGKTENTKKVIQYLAMVASSHKGKKDTSIT----------GELEKQLLQANPILEAFGNAKTVKNDNSSRFG 243
Cdd:cd14890 81 IIISGESGAGKTEATKIIMQYLARITSGFAQGASGEGEaaseaieqtlGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 244 KFIRINFDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRNDLLLEGFNNYTFLSNGFVPIPAAQDD 323
Cdd:cd14890 161 KFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPVEYFYLRGECSSIPSCDDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 324 EMFNETVEAMAIMGFTEEEQLSILRVVSSVLQLGNIVFKKERNTDQASmpDNTAAQ---KVCHLMGINVTDFTRSILTPR 400
Cdd:cd14890 241 KAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTVLE--DATTLQslkLAAELLGVNEDALEKALLTRQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 401 IKVGRDVVQKAQTKEQADFAVEALAKATYERLFRWILTRVNKALDKTHRQgASFLGILDIAGFEIFEVNSFEQLCINYTN 480
Cdd:cd14890 319 LFVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDK-WGFIGVLDIYGFEKFEWNTFEQLCINYAN 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 481 EKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIELIE-RPTNPPGVLALLDeECWFPKAT--DKSFVEKL---- 553
Cdd:cd14890 398 EKLQRHFNQHMFEVEQVEYSNEGIDWQYITFN-DNQACLELIEgKVNGKPGIFITLD-DCWRFKGEeaNKKFVSQLhasf 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 554 ---------CTEQGSHPKFQKPKQLKDKtEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSdkfmadlwkdvdr 624
Cdd:cd14890 476 grksgsggtRRGSSQHPHFVHPKFDADK-QFGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSR------------- 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 625 ivgldqmakmteSSLPSASktkkgmfrtVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGV 704
Cdd:cd14890 542 ------------RSIREVS---------VGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGM 600
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156120901 705 LEGIRICRQGFPNRIVFQEFRQRYEILAANAipkgfMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd14890 601 MEAIQIRQQGFALREEHDSFFYDFQVLLPTA-----ENIEQLVAVLSKMLGLGKADWQIGSSKIFLK 662
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
99-771 |
2.21e-172 |
|
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, myosin XV appears to be expressed in sensory tissue and play a role in hearing. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to the head domain are 2 MyTH4 domain, a FERM domain, and a SH3 domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276838 [Multi-domain] Cd Length: 657 Bit Score: 540.50 E-value: 2.21e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKQLPIYSEKIIEMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 178
Cdd:cd01387 1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 179 ESGAGKTENTKKVIQYLAMVASShkgkKDTSITgeleKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDvTGYIVG 258
Cdd:cd01387 81 ESGSGKTEATKLIMQYLAAVNQR----RNNLVT----EQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFFE-GGVIVG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 259 ANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRNDLLLEGFNNYTFLSNG-FVPIPAAQDDEMFNETVEAMAIMG 337
Cdd:cd01387 152 AITSQYLLEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQEAEKYFYLNQGgNCEIAGKSDADDFRRLLAAMQVLG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 338 FTEEEQLSILRVVSSVLQLGNIVFKKERNTDQ---ASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTK 414
Cdd:cd01387 232 FSSEEQDSIFRILASVLHLGNVYFHKRQLRHGqegVSVGSDAEIQWVAHLLQISPEGLQKALTFKVTETRRERIFTPLTI 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 415 EQADFAVEALAKATYERLFRWILTRVN----KALDKTHRqgasfLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHT 490
Cdd:cd01387 312 DQALDARDAIAKALYALLFSWLVTRVNaivySGTQDTLS-----IAILDIFGFEDLSENSFEQLCINYANENLQYYFNKH 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 491 MFILEQEEYQREGIEWNFIDFgLDLQPCIELIERptNPPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQKPKQlk 570
Cdd:cd01387 387 VFKLEQEEYIREQIDWTEIAF-ADNQPVINLISK--KPVGILHILDDECNFPQATDHSFLEKCHYHHALNELYSKPRM-- 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 571 DKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFMADLWKdvdrivgldQMAKMTESSLPSASK----TK 646
Cdd:cd01387 462 PLPEFTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFS---------SHRAQTDKAPPRLGKgrfvTM 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 647 KGMFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQ 726
Cdd:cd01387 533 KPRTPTVAARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFID 612
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 156120901 727 RYEILAANAIPKGfMDGKQACILMIKALELDP-NLYRIGQSKIFFR 771
Cdd:cd01387 613 RYRCLVALKLPRP-APGDMCVSLLSRLCTVTPkDMYRLGATKVFLR 657
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
99-771 |
5.43e-171 |
|
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain followed by a GlcAT-I (Beta1,3-glucuronyltransferase I) domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276862 [Multi-domain] Cd Length: 635 Bit Score: 535.81 E-value: 5.43e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKQLPIYSEKIIEMYKGKK-RHEMPPHIYAIADTAYRSMLQDREDQSILCT 177
Cdd:cd14897 1 NTIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 178 GESGAGKTENTKKVIQYLAMVASShkgkkdtsITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 257
Cdd:cd14897 81 GESGAGKTESTKYMIKHLMKLSPS--------DDSDLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQLL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 258 GANIETYLLEKSRAIRQARDERTFHIFYYLIAGA-KEKMRNdLLLEGFNNYTFLSNGFVPIPAAQDDE-------MFNET 329
Cdd:cd14897 153 GAKIDDYLLEKSRVVHRGNGEKNFHIFYALFAGMsRDRLLY-YFLEDPDCHRILRDDNRNRPVFNDSEeleyyrqMFHDL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 330 VEAMAIMGFTEEEQLSILRVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQ 409
Cdd:cd14897 232 TNIMKLIGFSEEDISVIFTILAAILHLTNIVFIPDEDTDGVTVADEYPLHAVAKLLGIDEVELTEALISNVNTIRGERIQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 410 KAQTKEQADFAVEALAKATYERLFRWILTRVNKAL----DKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQ 485
Cdd:cd14897 312 SWKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLwpdkDFQIMTRGPSIGILDMSGFENFKINSFDQLCINLSNERLQQ 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 486 LFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIELIERptNPPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQK 565
Cdd:cd14897 392 YFNDYVFPRERSEYEIEGIEWRDIEYH-DNDDVLELFFK--KPLGILPLLDEESTFPQSTDSSLVQKLNKYCGESPRYVA 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 566 PKqlKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFMADLWKdvdrivgldqmakmtesslpsaskt 645
Cdd:cd14897 469 SP--GNRVAFGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLFT------------------------- 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 646 kkgmfrtvgQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFR 725
Cdd:cd14897 522 ---------SYFKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYEDFV 592
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 156120901 726 QRYEILAANAiPKGFMDGKQACILMIKALELDPnlYRIGQSKIFFR 771
Cdd:cd14897 593 KRYKEICDFS-NKVRSDDLGKCQKILKTAGIKG--YQFGKTKVFLK 635
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
99-771 |
6.34e-170 |
|
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276868 [Multi-domain] Cd Length: 658 Bit Score: 533.97 E-value: 6.34e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKQLP-IYSEKIIEMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCT 177
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 178 GESGAGKTENTKKVIQYLAMVASshkGKKDTSItgeleKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 257
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIAG---GLNDSTI-----KKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKNGTLV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 258 GANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRNDLLLEGFNNYTFlSNGFVPIPAAQDDEMFNETVEAMAIMG 337
Cdd:cd14903 153 GAKCRTYLLEKTRVISHERPERNYHIFYQLLASPDVEERLFLDSANECAYTG-ANKTIKIEGMSDRKHFARTKEALSLIG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 338 FTEEEQLSILRVVSSVLQLGNIVFKKERNTDQASM--PDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKE 415
Cdd:cd14903 232 VSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSAiaPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDVYTVPLKKD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 416 QADFAVEALAKATYERLFRWILTRVNKALDKTHRQgASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILE 495
Cdd:cd14903 312 QAEDCRDALAKAIYSNVFDWLVATINASLGNDAKM-ANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFTQDVFKTV 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 496 QEEYQREGIEWNFIDFgLDLQPCIELIERPTnppGVLALLDEECWFPKATDKSFVEKLcteQGSHPKFQK----PKqlKD 571
Cdd:cd14903 391 QIEYEEEGIRWAHIDF-ADNQDVLAVIEDRL---GIISLLNDEVMRPKGNEESFVSKL---SSIHKDEQDviefPR--TS 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 572 KTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFMADLWKDvdrIVGLDQMAKMTESSLPSASKTKKGMFR 651
Cdd:cd14903 462 RTQFTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKE---KVESPAAASTSLARGARRRRGGALTTT 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 652 TVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 731
Cdd:cd14903 539 TVGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWLF 618
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 156120901 732 AANAiPKGFMDGKQACILMIKALELD-PNLYRIGQSKIFFR 771
Cdd:cd14903 619 LPEG-RNTDVPVAERCEALMKKLKLEsPEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
99-732 |
1.45e-169 |
|
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276853 [Multi-domain] Cd Length: 667 Bit Score: 533.12 E-value: 1.45e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKQLP-IYSEKIIEMYKgKKRHEMPPHIYAIADTAYRSMLQDREDQSILCT 177
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 178 GESGAGKTENTKKVIQYLAMVASSHKGKKDTsitgeLEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVT---- 253
Cdd:cd14888 80 GESGAGKTESTKYVMKFLACAGSEDIKKRSL-----VEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFSKLkskr 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 254 -----GYIVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRNDLLLEGFNNYTFLSNGFVP------------ 316
Cdd:cd14888 155 msgdrGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAREAKNTGLSYEENDEKLAKGADAKPisidmssfephl 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 317 ------------IPAAQDDEMFNETVEAMAIMGFTEEEQLSILRVVSSVLQLGNIVFKKERNTDQASMPDNTAAQ---KV 381
Cdd:cd14888 235 kfryltksscheLPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFENNEACSEGAVVSASCTDdleKV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 382 CHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQADFAVEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIA 461
Cdd:cd14888 315 ASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGYSKDNSLLFCGVLDIF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 462 GFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIELIErpTNPPGVLALLDEECWF 541
Cdd:cd14888 395 GFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVDLLQ--EKPLGIFCMLDEECFV 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 542 PKATDKSFVEKLCTEQGSHPKFQKPKqlKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFMADLWKD 621
Cdd:cd14888 472 PGGKDQGLCNKLCQKHKGHKRFDVVK--TDPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKNPFISNLFSA 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 622 -VDRIVGldqmakmtesslpsaSKTKKGMFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLR 700
Cdd:cd14888 550 yLRRGTD---------------GNTKKKKFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQLK 614
|
650 660 670
....*....|....*....|....*....|..
gi 156120901 701 CNGVLEGIRICRQGFPNRIVFQEFRQRYEILA 732
Cdd:cd14888 615 YGGVLQAVQVSRAGYPVRLSHAEFYNDYRILL 646
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
99-771 |
2.40e-169 |
|
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play a role in signalling. It has a N-terminal RA domain, an IQ domain, a C1_1 domain, and a RhoGAP domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276836 [Multi-domain] Cd Length: 690 Bit Score: 533.49 E-value: 2.40e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKQLPIYSEKIIEMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 178
Cdd:cd01385 1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 179 ESGAGKTENTKKVIQYLamVASSHKGKKDTsitgeLEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd01385 81 ESGSGKTESTNFLLHHL--TALSQKGYGSG-----VEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 259 ANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRNDLLLEGFNNYTFLsNGFVPIPAAQDDEM--FNETVEAMAIM 336
Cdd:cd01385 154 AVVEKYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHYL-NQSDCYTLEGEDEKyeFERLKQAMEMV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 337 GFTEEEQLSILRVVSSVLQLGNIVFKKER-NTDQASMPDNTAAQK-VCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTK 414
Cdd:cd01385 233 GFLPETQRQIFSVLSAVLHLGNIEYKKKAyHRDESVTVGNPEVLDiISELLRVKEETLLEALTTKKTVTVGETLILPYKL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 415 EQADFAVEALAKATYERLFRWILTRVNKAL----DKTHRQGASfLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHT 490
Cdd:cd01385 313 PEAIATRDAMAKCLYSALFDWIVLRINHALlnkkDLEEAKGLS-IGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQH 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 491 MFILEQEEYQREGIEWNFIDFgLDLQPCIELIERptNPPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQKPkQLK 570
Cdd:cd01385 392 IFKLEQEEYKKEGISWHNIEY-TDNTGCLQLISK--KPTGLLCLLDEESNFPGATNQTLLAKFKQQHKDNKYYEKP-QVM 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 571 DkTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFMADLwkdvdriVGLD---------------QMAKMT 635
Cdd:cd01385 468 E-PAFIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVREL-------IGIDpvavfrwavlraffrAMAAFR 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 636 ESSLPSASKT-------------------KKGMFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVL 696
Cdd:cd01385 540 EAGRRRAQRTaghsltlhdrttksllhlhKKKKPPSVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVL 619
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 156120901 697 EQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILaanaIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd01385 620 RQLRYTGMLETVRIRRSGYSVRYTFQEFITQFQVL----LPKGLISSKEDIKDFLEKLNLDRDNYQIGKTKVFLK 690
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
99-769 |
1.22e-168 |
|
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276866 [Multi-domain] Cd Length: 655 Bit Score: 530.13 E-value: 1.22e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKQLPIYSEKIIEMY------KGKKRHEMPPHIYAIADTAYRSMLQDRE-- 170
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 171 --DQSILCTGESGAGKTENTKKVIQYLAMVASSHKGKKDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 248
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLASVSSATTHGQNATERENVRDRVLESNPILEAFGNARTNRNNNSSRFGKFIRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 249 NFDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRNDLLLEGFNNYTFL--SNGFVPIPAAQDDEMF 326
Cdd:cd14901 161 GFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYLnsSQCYDRRDGVDDSVQY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 327 NETVEAMAIMGFTEEEQLSILRVVSSVLQLGNIVF-KKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGR 405
Cdd:cd14901 241 AKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFvKKDGEGGTFSMSSLANVRAACDLLGLDMDVLEKTLCTREIRAGG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 406 DVVQKAQTKEQADFAVEALAKATYERLFRWILTRVNKALDKTHRQGAS-FLGILDIAGFEIFEVNSFEQLCINYTNEKLQ 484
Cdd:cd14901 321 EYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSESTGASrFIGIVDIFGFEIFATNSLEQLCINFANEKLQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 485 QLFNHTMFILEQEEYQREGIEWNFIDFgldlqP----CIELIERptNPPGVLALLDEECWFPKATDKSFVEKLCTEQGSH 560
Cdd:cd14901 401 QLFGKFVFEMEQDEYVAEAIPWTFVEY-----PnndaCVAMFEA--RPTGLFSLLDEQCLLPRGNDEKLANKYYDLLAKH 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 561 PKFQKPKQLKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFmadlwkdvdrivgldqmakmtessLP 640
Cdd:cd14901 474 ASFSVSKLQQGKRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAF------------------------LS 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 641 SasktkkgmfrTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIV 720
Cdd:cd14901 530 S----------TVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFP 599
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 156120901 721 FQEFRQRYEILAANAIPKGFMDGKQACILMIKA------LELDPNLYrIGQSKIF 769
Cdd:cd14901 600 HDAFVHTYSCLAPDGASDTWKVNELAERLMSQLqhselnIEHLPPFQ-VGKTKVF 653
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
100-771 |
1.10e-167 |
|
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process in insects and in hearing in mammals. Myosin III, an unconventional myosin, does not form dimers. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. They are characterized by an N-terminal protein kinase domain and several IQ domains. Some members also contain WW, SH2, PH, and Y-phosphatase domains. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276830 [Multi-domain] Cd Length: 633 Bit Score: 526.84 E-value: 1.10e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 100 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKQLPIYSEKIIEMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGE 179
Cdd:cd01379 2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 180 SGAGKTENTKKVIQYLAMVasshkGKKDTsitGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGA 259
Cdd:cd01379 82 SGAGKTESANLLVQQLTVL-----GKANN---RTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAVTGA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 260 NIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRND---LLLEGFNNYTFLSNGFVPIPAAQDD--EMFNETVEAMA 334
Cdd:cd01379 154 RISEYLLEKSRVVHQAIGERNFHIFYYIYAGLAEDKKLAkykLPENKPPRYLQNDGLTVQDIVNNSGnrEKFEEIEQCFK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 335 IMGFTEEEQLSILRVVSSVLQLGNIVFK---KERNTDQASM-PDNTAAQKVCHLMGINVTDFtRSILTPRIKVGR-DVVQ 409
Cdd:cd01379 234 VIGFTKEEVDSVYSILAAILHIGDIEFTeveSNHQTDKSSRiSNPEALNNVAKLLGIEADEL-QEALTSHSVVTRgETII 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 410 KAQTKEQADFAVEALAKATYERLFRWILTRVNKAL--DKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLF 487
Cdd:cd01379 313 RNNTVEEATDARDAMAKALYGRLFSWIVNRINSLLkpDRSASDEPLSIGILDIFGFENFQKNSFEQLCINIANEQIQYYF 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 488 NHTMFILEQEEYQREGIEWNFIDFGlDLQPCIE-LIERPTnppGVLALLDEECWFPKATDKSFVEKLCTEQGSHPkFQKP 566
Cdd:cd01379 393 NQHIFAWEQQEYLNEGIDVDLIEYE-DNRPLLDmFLQKPM---GLLALLDEESRFPKATDQTLVEKFHNNIKSKY-YWRP 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 567 KqlKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKfmadlwkdvdrivgldqMAKMTESSlpsasktk 646
Cdd:cd01379 468 K--SNALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENP-----------------LVRQTVAT-------- 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 647 kgMFRtvgqlY--KEQLGKLMTtlrnTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEF 724
Cdd:cd01379 521 --YFR-----YslMDLLSKMVV----GQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRILFADF 589
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 156120901 725 RQRYEILA--ANAIPKGfmdGKQACILMIKALELDPnlYRIGQSKIFFR 771
Cdd:cd01379 590 LKRYYFLAfkWNEEVVA---NRENCRLILERLKLDN--WALGKTKVFLK 633
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
99-771 |
4.36e-167 |
|
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a monomer. In mammalian cells, the motor is found to localize to filopodia. Myosin X walks towards the barbed ends of filaments and is thought to walk on bundles of actin, rather than single filaments, a unique behavior. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to the head domain are a variable number of IQ domains, 2 PH domains, a MyTH4 domain, and a FERM domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276840 [Multi-domain] Cd Length: 651 Bit Score: 525.90 E-value: 4.36e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKQLP-IYSEKIIEMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCT 177
Cdd:cd14873 1 GSIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 178 GESGAGKTENTKKVIQYLAMVASSHKGKKDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 257
Cdd:cd14873 81 GESGAGKTESTKLILKFLSVISQQSLELSLKEKTSCVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 258 GANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRNDLLLEGFNNYTFLS-NGFVPIPAAQDDEMFNETVEAMAIM 336
Cdd:cd14873 161 GGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTPENYHYLNqSGCVEDKTISDQESFREVITAMEVM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 337 GFTEEEQLSILRVVSSVLQLGNIVFKkerNTDQASMPDNTAAQKVCHLMGINVTDFTrSILTPRIKVGR-DVVQKAQTKE 415
Cdd:cd14873 241 QFSKEEVREVSRLLAGILHLGNIEFI---TAGGAQVSFKTALGRSAELLGLDPTQLT-DALTQRSMFLRgEEILTPLNVQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 416 QADFAVEALAKATYERLFRWILTRVNKALDKthRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILE 495
Cdd:cd14873 317 QAVDSRDSLAMALYARCFEWVIKKINSRIKG--KEDFKSIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKHIFSLE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 496 QEEYQREGIEWNFIDFgLDLQPCIELIERPTnppGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQKPKQlkDKTEF 575
Cdd:cd14873 395 QLEYSREGLVWEDIDW-IDNGECLDLIEKKL---GLLALINEESHFPQATDSTLLEKLHSQHANNHFYVKPRV--AVNNF 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 576 SIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFMADLWKDVDrivgldqmAKMTESSLPSASKTKKgmfRTVGQ 655
Cdd:cd14873 469 GVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEHVS--------SRNNQDTLKCGSKHRR---PTVSS 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 656 LYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANA 735
Cdd:cd14873 538 QFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMRNL 617
|
650 660 670
....*....|....*....|....*....|....*.
gi 156120901 736 IPKGFMDGKqaCILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd14873 618 ALPEDVRGK--CTSLLQLYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
99-771 |
1.73e-162 |
|
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of 17 IQ motifs and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276857 [Multi-domain] Cd Length: 656 Bit Score: 513.54 E-value: 1.73e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKQLPIYSEKIIEMYKGKKRHEM---PPHIYAIADTAYRSMLQDR----ED 171
Cdd:cd14892 1 APLLDVLRRRYERDAIYTFTADILISINPYKSIPLLYDVPGFDSQRKEEATAsspPPHVFSIAERAYRAMKGVGkgqgTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 172 QSILCTGESGAGKTENTKKVIQYLA----MVASSHKGKKDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIR 247
Cdd:cd14892 81 QSIVVSGESGAGKTEASKYIMKYLAtaskLAKGASTSKGAANAHESIEECVLLSNLILEAFGNAKTIRNDNSSRFGKYIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 248 INFDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRNDLLLEGFNNYTFLSNG-FVPIPAAQDDEMF 326
Cdd:cd14892 161 IHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAESFLFLNQGnCVEVDGVDDATEF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 327 NETVEAMAIMGFTEEEQLSILRVVSSVLQLGNIVFkkERNTDQ----ASMPDNTAAQKVCHLMGINVTDFTRSILTPRIK 402
Cdd:cd14892 241 KQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRF--EENADDedvfAQSADGVNVAKAAGLLGVDAAELMFKLVTQTTS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 403 VGR-DVVQKAQTKEQADFAVEALAKATYERLFRWILTRVNKALDKTHRQ---------GASFLGILDIAGFEIFEVNSFE 472
Cdd:cd14892 319 TARgSVLEIKLTAREAKNALDALCKYLYGELFDWLISRINACHKQQTSGvtggaasptFSPFIGILDIFGFEIMPTNSFE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 473 QLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIELIERPtnPPGVLALLDEECWFP-KATDKSFVE 551
Cdd:cd14892 399 QLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQ-DNQDCLDLIQKK--PLGLLPLLEEQMLLKrKTTDKQLLT 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 552 KL-CTEQGSHPKFQKPKQLKDktEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDkfmadlwkdvdrivgldq 630
Cdd:cd14892 476 IYhQTHLDKHPHYAKPRFECD--EFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSSSK------------------ 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 631 makmtesslpsasktkkgmFRTvgqlykeQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRI 710
Cdd:cd14892 536 -------------------FRT-------QLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVRI 589
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156120901 711 CRQGFPNRIVFQEFRQRYEILAAN-AIPKGFMDGKQACILMIKALE-----LDPNLYRIGQSKIFFR 771
Cdd:cd14892 590 RREGFPIRRQFEEFYEKFWPLARNkAGVAASPDACDATTARKKCEEivaraLERENFQLGRTKVFLR 656
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
101-771 |
3.73e-151 |
|
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The tail regions of these class-XXVIII myosins consist of an IQ motif, a short coiled-coil region, and an SH2 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276854 Cd Length: 659 Bit Score: 482.48 E-value: 3.73e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 101 VLHNLRERYFSGLIYTYSGLFCVVVNPYKQLPIYSEKIIEMYKGKKRHEMPPHIYAIADTAYRSML----QDREDQSILC 176
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 177 TGESGAGKTENTKKVIQYLAMVASSHKgkkdtsitgELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDvTGYI 256
Cdd:cd14889 83 SGESGAGKTESTKLLLRQIMELCRGNS---------QLEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRFR-NGHV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 257 VGANIETYLLEKSRAIRQARDERTFHIFYYLIAG--AKEKMRNDLLLEGFnnYTFLSNGFvpipaAQDDEM------FNE 328
Cdd:cd14889 153 KGAKINEYLLEKSRVVHQDGGEENFHIFYYMFAGisAEDRENYGLLDPGK--YRYLNNGA-----GCKREVqywkkkYDE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 329 TVEAMAIMGFTEEEQLSILRVVSSVLQLGNIVFkkERNTDQASMPDNTA---AQKVCHLMGINVTDFTRSiLTPRIKVGR 405
Cdd:cd14889 226 VCNAMDMVGFTEQEEVDMFTILAGILSLGNITF--EMDDDEALKVENDSngwLKAAAGQFGVSEEDLLKT-LTCTVTFTR 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 406 -DVVQKAQTKEQADFAVEALAKATYERLFRWILTRVNKALDKTHRQG--ASFLGILDIAGFEIFEVNSFEQLCINYTNEK 482
Cdd:cd14889 303 gEQIQRHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLLAPKDDSSveLREIGILDIFGFENFAVNRFEQACINLANEQ 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 483 LQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIELIErpTNPPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPK 562
Cdd:cd14889 383 LQYFFNHHIFLMEQKEYKKEGIDWKEITY-KDNKPILDLFL--NKPIGILSLLDEQSHFPQATDESFVDKLNIHFKGNSY 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 563 FQKPKQLKDKteFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFMADLWK-DVDRIVGLDQMAKMTESSLPS 641
Cdd:cd14889 460 YGKSRSKSPK--FTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFTaTRSRTGTLMPRAKLPQAGSDN 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 642 ASKTKKgmfRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVF 721
Cdd:cd14889 538 FNSTRK---QSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFSWRPSF 614
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 156120901 722 QEFRQRYEILAANAIPKGfmdGKQACILMIKALELDPnlYRIGQSKIFFR 771
Cdd:cd14889 615 AEFAERYKILLCEPALPG---TKQSCLRILKATKLVG--WKCGKTRLFFK 659
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
99-734 |
2.59e-147 |
|
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276872 [Multi-domain] Cd Length: 669 Bit Score: 472.21 E-value: 2.59e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKQLP-IYSEKIIEMYKGKKRH--------EMPPHIYAIADTAYRSMLQDR 169
Cdd:cd14907 1 AELLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEQIIQngeyfdikKEPPHIYAIAALAFKQLFENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 170 EDQSILCTGESGAGKTENTKKVIQYLAMVaSSHKGKKDTSITGE------------LEKQLLQANPILEAFGNAKTVKND 237
Cdd:cd14907 81 KKQAIVISGESGAGKTENAKYAMKFLTQL-SQQEQNSEEVLTLTssiratskstksIEQKILSCNPILEAFGNAKTVRND 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 238 NSSRFGKFIRINFD-VTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRNDLLLEG---FNNYTFLS-N 312
Cdd:cd14907 160 NSSRFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLKNqlsGDRYDYLKkS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 313 GFVPIPAAQDDEMFNETVEAMAIMGFTEEEQLSILRVVSSVLQLGNIVFKKERNTDQA--SMPDNTAAQKVCHLMGINVT 390
Cdd:cd14907 240 NCYEVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDSTLDDNSpcCVKNKETLQIIAKLLGIDEE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 391 DFTRSILTPRIKVGRDVVQKAQTKEQADFAVEALAKATYERLFRWILTRVNKAL------DKTHRQGASF-LGILDIAGF 463
Cdd:cd14907 320 ELKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpkdekDQQLFQNKYLsIGLLDIFGF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 464 EIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIE--WNFIDFgLDLQPCIELIERPtnPPGVLALLDEECWF 541
Cdd:cd14907 400 EVFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEdyLNQLSY-TDNQDVIDLLDKP--PIGIFNLLDDSCKL 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 542 PKATDKSFVEKLCTEQGSHPKFQKPKQLKDKTeFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFMADLWkd 621
Cdd:cd14907 477 ATGTDEKLLNKIKKQHKNNSKLIFPNKINKDT-FTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIF-- 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 622 vdriVGLDQMAKMTESSLPSASKTKKgmfrTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRC 701
Cdd:cd14907 554 ----SGEDGSQQQNQSKQKKSQKKDK----FLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRY 625
|
650 660 670
....*....|....*....|....*....|...
gi 156120901 702 NGVLEGIRICRQGFPNRIVFQEFRQRYEILAAN 734
Cdd:cd14907 626 LGVLESIRVRKQGYPYRKSYEDFYKQYSLLKKN 658
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
99-771 |
1.14e-142 |
|
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal SH3-like domain, two IQ motifs, a coiled-coil region and a PX domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276856 Cd Length: 645 Bit Score: 458.74 E-value: 1.14e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 99 ASVLHNLRERyfSGLI----YTYSGLFCVVVNPYKQLPiysEKIIEMYKGKKRHEMPPHIYAIADTAYRSMLQDRE---D 171
Cdd:cd14891 1 AGILHNLEER--SKLDnqrpYTFMANVLIAVNPLRRLP---EPDKSDYINTPLDPCPPHPYAIAEMAYQQMCLGSGrmqN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 172 QSILCTGESGAGKTENTKKVIQYLAM--VASSHKGKKDTSI--------TGELEKQLLQANPILEAFGNAKTVKNDNSSR 241
Cdd:cd14891 76 QSIVISGESGAGKTETSKIILRFLTTraVGGKKASGQDIEQsskkrklsVTSLDERLMDTNPILESFGNAKTLRNHNSSR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 242 FGKFIRINFDVTGY-IVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRNDLLLEGFNNYTFLS-NGFVPIPA 319
Cdd:cd14891 156 FGKFMKLQFTKDKFkLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSPEDFIYLNqSGCVSDDN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 320 AQDDEMFNETVEAMAIMGFTEEEQLSILRVVSSVLQLGNIVFKK----ERNTDQASMPDNTAAQKVCHLMGINVTDFTRS 395
Cdd:cd14891 236 IDDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEedtsEGEAEIASESDKEALATAAELLGVDEEALEKV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 396 ILTPRIkVGRDVVQKAQ-TKEQADFAVEALAKATYERLFRWILTRVNKALDKtHRQGASFLGILDIAGFEIFE-VNSFEQ 473
Cdd:cd14891 316 ITQREI-VTRGETFTIKrNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGH-DPDPLPYIGVLDIFGFESFEtKNDFEQ 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 474 LCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIELIErpTNPPGVLALLDEECWFPKATDKSFVEKL 553
Cdd:cd14891 394 LLINYANEALQATFNQQVFIAEQELYKSEGIDVGVITWP-DNRECLDLIA--SKPNGILPLLDNEARNPNPSDAKLNETL 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 554 CTEQGSHPKFQKPKQlKDKTE-FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLnASSDKFmadlwkdvdrivgLDQMA 632
Cdd:cd14891 471 HKTHKRHPCFPRPHP-KDMREmFIVKHYAGTVSYTIGSFIDKNNDIIPEDFEDLL-ASSAKF-------------SDQMQ 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 633 kmtesslpsasktkkgmfrtvgqlykeqlgKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICR 712
Cdd:cd14891 536 ------------------------------ELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVLK 585
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 713 QGFPNRIVFQEFRQRYEILAANAIPKGFMDGKQACILMIK-ALELDPNLYRIGQSKIFFR 771
Cdd:cd14891 586 VGLPTRVTYAELVDVYKPVLPPSVTRLFAENDRTLTQAILwAFRVPSDAYRLGRTRVFFR 645
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
100-737 |
3.88e-140 |
|
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276865 Cd Length: 627 Bit Score: 450.91 E-value: 3.88e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 100 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKQLP-IYSEKIIEMY-----------KGKKRHEMPPHIYAIADTAYRSM-- 165
Cdd:cd14900 2 TILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssstRNKGSDPMPPHIYQVAGEAYKAMml 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 166 --LQDREDQSILCTGESGAGKTENTKKVIQYLAMV------ASSHKGKKDTSITGelekQLLQANPILEAFGNAKTVKND 237
Cdd:cd14900 82 glNGVMSDQSILVSGESGSGKTESTKFLMEYLAQAgdnnlaASVSMGKSTSGIAA----KVLQTNILLESFGNARTLRND 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 238 NSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEkmrndlllegfnnytflsngfvpi 317
Cdd:cd14900 158 NSSRFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASE------------------------ 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 318 pAAQDDEMFNETVEAMAIMGFTEEEQLSILRVVSSVLQLGNIVFKKERNTD-QASMPDNTAAQKV------CHLMGINVT 390
Cdd:cd14900 214 -AARKRDMYRRVMDAMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDrLGQLKSDLAPSSIwsrdaaATLLSVDAT 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 391 DFTRSILTPRIKVGRDVVQKAQTKEQADFAVEALAKATYERLFRWILTRVNKALD----KTHRQGASFLGILDIAGFEIF 466
Cdd:cd14900 293 KLEKALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLKmddsSKSHGGLHFIGILDIFGFEVF 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 467 EVNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIELI-ERPTnppGVLALLDEECWFPKAT 545
Cdd:cd14900 373 PKNSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFC-DNQDCVNLIsQRPT---GILSLIDEECVMPKGS 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 546 DKSFVEKLCTEQGSHPKFQKPKQLKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVtsllnassdkfmadlwkdVDri 625
Cdd:cd14900 449 DTTLASKLYRACGSHPRFSASRIQRARGLFTIVHYAGHVEYSTDGFLEKNKDVLHQEA------------------VD-- 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 626 vgldqmakmtesslpsasktkkgMFRTVGQlYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVL 705
Cdd:cd14900 509 -----------------------LFVYGLQ-FKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVM 564
|
650 660 670
....*....|....*....|....*....|..
gi 156120901 706 EGIRICRQGFPNRIVFQEFRQRYEILAANAIP 737
Cdd:cd14900 565 EAVRVARAGFPIRLLHDEFVARYFSLARAKNR 596
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
99-728 |
4.41e-137 |
|
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276867 [Multi-domain] Cd Length: 716 Bit Score: 445.49 E-value: 4.41e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKQLP-IYSEKIIEMYK--------GKKRHEMPPHIYAIADTAYRSMLQ-D 168
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLKpE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 169 REDQSILCTGESGAGKTENTKKVIQYLAMV-ASSHKGKKDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIR 247
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLTSVgRDQSSTEQEGSDAVEIGKRILQTNPILESFGNAQTIRNDNSSRFGKFIK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 248 INFDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRNDLLLEGFNNYTFLSN---GFVPIPAAQDD- 323
Cdd:cd14902 161 IQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKGGKYELLNSygpSFARKRAVADKy 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 324 -EMFNETVEAMAIMGFTEEEQLSILRVVSSVLQLGNIVFKKE-RNTDQASMPDNTAAQ--KVCHLMGINVTDFTRSILTP 399
Cdd:cd14902 241 aQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAEnGQEDATAVTAASRFHlaKCAELMGVDVDKLETLLSSR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 400 RIKVGRDVVQKAQTKEQADFAVEALAKATYERLFRWILTRVNKALD--------KTHRQGASFLGILDIAGFEIFEVNSF 471
Cdd:cd14902 321 EIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINyfdsavsiSDEDEELATIGILDIFGFESLNRNGF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 472 EQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIELIERPTNppGVLALLDEECWFPKATDKSFVE 551
Cdd:cd14902 401 EQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYP-SNAACLALFDDKSN--GLFSLLDQECLMPKGSNQALST 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 552 KLCTEQGShpkfqkpkqlkdKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDkfmadlwkDVDRIVGLDQM 631
Cdd:cd14902 478 KFYRYHGG------------LGQFVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSN--------EVVVAIGADEN 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 632 AKMTESSLPSASKTKKGMFRT--VGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIR 709
Cdd:cd14902 538 RDSPGADNGAAGRRRYSMLRApsVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLEAVR 617
|
650
....*....|....*....
gi 156120901 710 ICRQGFPNRIVFQEFRQRY 728
Cdd:cd14902 618 IARHGYSVRLAHASFIELF 636
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
99-771 |
9.66e-136 |
|
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276869 Cd Length: 653 Bit Score: 439.38 E-value: 9.66e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKQLP-IYSEKIIEMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCT 177
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 178 GESGAGKTENTKKVIQYLAMVASshkGKKDTSITgelekQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 257
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVAG---GRKDKTIA-----KVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRGKLI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 258 GANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRNDLLLEGFNNYTFL--SNGFVPIPAAQDDEMFNETVEAMAI 335
Cdd:cd14904 153 GAKCETYLLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQYLgdSLAQMQIPGLDDAKLFASTQKSLSL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 336 MGFTEEEQLSILRVVSSVLQLGNIVFkKERNTDQASMPDNTAAQKVCHLMGINVTDF-----TRSILT--PRIKVGRDVV 408
Cdd:cd14904 233 IGLDNDAQRTLFKILSGVLHLGEVMF-DKSDENGSRISNGSQLSQVAKMLGLPTTRIeealcNRSVVTrnESVTVPLAPV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 409 QKAQTKeqadfavEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFN 488
Cdd:cd14904 312 EAEENR-------DALAKAIYSKLFDWMVVKINAAISTDDDRIKGQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFT 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 489 HTMFILEQEEYQREGIEWNFIDFGlDLQPCIELIErptNPPGVLALLDEECWFPKATDKSFVEKLCT---EQGSHPKFQK 565
Cdd:cd14904 385 TDVFKTVEEEYIREGLQWDHIEYQ-DNQGIVEVID---GKMGIIALMNDHLRQPRGTEEALVNKIRTnhqTKKDNESIDF 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 566 PKQlkDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFMADLWKDVDrivgldqmakMTESSLPSASKT 645
Cdd:cd14904 461 PKV--KRTQFIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFGSSE----------APSETKEGKSGK 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 646 KKGMFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFR 725
Cdd:cd14904 529 GTKAPKSLGSQFKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELA 608
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 156120901 726 QRYEILAANAIPKGfmDGKQACILMIKAL-ELDPNLYRIGQSKIFFR 771
Cdd:cd14904 609 TRYAIMFPPSMHSK--DVRRTCSVFMTAIgRKSPLEYQIGKSLIYFK 653
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
100-771 |
1.33e-135 |
|
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short coiled-coil region, 5 tandem ANK repeats, and a carboxy-terminal FYVE domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276860 [Multi-domain] Cd Length: 704 Bit Score: 440.93 E-value: 1.33e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 100 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKQLPiysekiiEMYKGKKRHE-------MPPHIYAIADTAYRSMLQ----- 167
Cdd:cd14895 2 AFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIP-------GLYDLHKYREempgwtaLPPHVFSIAEGAYRSLRRrlhep 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 168 --DREDQSILCTGESGAGKTENTKKVIQYLAMVASSHKGKKDTS----ITGElekQLLQANPILEAFGNAKTVKNDNSSR 241
Cdd:cd14895 75 gaSKKNQTILVSGESGAGKTETTKFIMNYLAESSKHTTATSSSKrrraISGS---ELLSANPILESFGNARTLRNDNSSR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 242 FGKFIRINF-----DVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRNDLLLEGFNNYTF--LSNG- 313
Cdd:cd14895 152 FGKFVRMFFeghelDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQLELLSAQEFqyISGGq 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 314 -FVPIPAAQDDEMFNETVEAMAIMGFTEEEQLSILRVVSSVLQLGNIVFKKERntDQASMPDNTAAQKVCHLMGINVTDF 392
Cdd:cd14895 232 cYQRNDGVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASS--EDEGEEDNGAASAPCRLASASPSSL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 393 T-------------------RSILTPR-IKVGRDVVQKAQTKEQADFAVEALAKATYERLFRWILTRVNKAL-------- 444
Cdd:cd14895 310 TvqqhldivsklfavdqdelVSALTTRkISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASpqrqfaln 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 445 --DKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDlQPCIELI 522
Cdd:cd14895 390 pnKAANKDTTPCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDN-SVCLEML 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 523 ERptNPPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQKPKQLKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDN 602
Cdd:cd14895 469 EQ--RPSGIFSLLDEECVVPKGSDAGFARKLYQRLQEHSNFSASRTDQADVAFQIHHYAGAVRYQAEGFCEKNKDQPNAE 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 603 VTSLLNASSDKFMADLWKDVDRIVGldqmAKMTESSLPSASKTKKGMFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPN 682
Cdd:cd14895 547 LFSVLGKTSDAHLRELFEFFKASES----AELSLGQPKLRRRSSVLSSVGIGSQFKQQLASLLDVVQQTQTHYIRCIKPN 622
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 683 HEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANAIPKGFMDGKQACILMIKALELdpnlyr 762
Cdd:cd14895 623 DESASDQFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLVAAKNASDATASALIETLKVDHAEL------ 696
|
....*....
gi 156120901 763 iGQSKIFFR 771
Cdd:cd14895 697 -GKTRVFLR 704
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
99-771 |
5.27e-135 |
|
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain which is commonly found in proteins establishing molecular complexes. The motor domain itself does not exhibit ATPase activity, suggesting that it functions as an actin tether protein. It also has two IQ domains that probably bind light chains or related calmodulins and a C-terminal tail with two sections of coiled-coil domains, which are thought to mediate homodimerization. The function of these myosins are largely unknown. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276837 [Multi-domain] Cd Length: 689 Bit Score: 438.67 E-value: 5.27e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKQLPIYSEKIIEMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 178
Cdd:cd01386 1 SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 179 ESGAGKTENTKKVIQYLAMVASSHKGKkdtsITGElekQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd01386 81 RSGSGKTTNCRHILEYLVTAAGSVGGV----LSVE---KLNAALTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQLAS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 259 ANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRNDLLLEGFNNytflSNGFVPIPAAQDDEM------FNETVEA 332
Cdd:cd01386 154 ASIQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLAE----SNSFGIVPLQKPEDKqkaaaaFSKLQAA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 333 MAIMGFTEEEQLSILRVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSI------------LTPR 400
Cdd:cd01386 230 MKTLGISEEEQRAIWSILAAIYHLGAAGATKAASAGRKQFARPEWAQRAAYLLGCTLEELSSAIfkhhlsggpqqsTTSS 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 401 IKVGRDVVQKAQTKEQADFAVEALAKATYERLFRWILTRVNKALDKTHRQGASFLgILDIAGFEifevN----------S 470
Cdd:cd01386 310 GQESPARSSSGGPKLTGVEALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSSIT-IVDTPGFQ----NpahsgsqrgaT 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 471 FEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIELIERP------------TNPPGVLALLDEE 538
Cdd:cd01386 385 FEDLCHNYAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQApqqalvrsdlrdEDRRGLLWLLDEE 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 539 CWFPKATDKSFVEKLCTEQG--SHPKFQKPKQLKDKT-EFSIIHYAGK--VDYNASAWLTK-NMDPLNDNVTSLLNASSD 612
Cdd:cd01386 465 ALYPGSSDDTFLERLFSHYGdkEGGKGHSLLRRSEGPlQFVLGHLLGTnpVEYDVSGWLKAaKENPSAQNATQLLQESQK 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 613 KFmadlwkdvdrivgldqmakmtesslpsASKTKKGMFRTVgqlyKEQLGKLMTTLRNTTPNFVRCIIPNH--EKRSGK- 689
Cdd:cd01386 545 ET---------------------------AAVKRKSPCLQI----KFQVDALIDTLRRTGLHFVHCLLPQHnaGKDERSt 593
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 690 ---------LDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANAIPKGF-----MDGKQACILMIKALE 755
Cdd:cd01386 594 sspaagdelLDVPLLRSQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPLTKKLGlnsevADERKAVEELLEELD 673
|
730
....*....|....*.
gi 156120901 756 LDPNLYRIGQSKIFFR 771
Cdd:cd01386 674 LEKSSYRIGLSQVFFR 689
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
99-771 |
1.76e-134 |
|
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 domains, a single FERM domain, and an SH3 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276861 [Multi-domain] Cd Length: 644 Bit Score: 435.75 E-value: 1.76e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKQLPIYSEKIIEMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 178
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 179 ESGAGKTENTKKVIQYLAMVASSHkgkkdtsiTGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDvTGYIVG 258
Cdd:cd14896 81 HSGSGKTEAAKKIVQFLSSLYQDQ--------TEDRLRQPEDVLPILESFGHAKTILNANASRFGQVLRLHLQ-HGVIVG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 259 ANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRNDLLLEGFNNYTFLSNGFV-PIPAAQDDEMFNETVEAMAIMG 337
Cdd:cd14896 152 ASVSHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQGPETYYYLNQGGAcRLQGKEDAQDFEGLLKALQGLG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 338 FTEEEQLSILRVVSSVLQLGNIVFKKERNTDQ--ASMPDNTAAQKVCHLMGINvTDFTRSILTPRIKV-GRDVVQKAQTK 414
Cdd:cd14896 232 LCAEELTAIWAVLAAILQLGNICFSSSERESQevAAVSSWAEIHTAARLLQVP-PERLEGAVTHRVTEtPYGRVSRPLPV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 415 EQADFAVEALAKATYERLFRWILTRVNKALDKTHRQGA-SFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFI 493
Cdd:cd14896 311 EGAIDARDALAKTLYSRLFTWLLKRINAWLAPPGEAESdATIGVVDAYGFEALRVNGLEQLCINLASERLQLFSSQTLLA 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 494 LEQEEYQREGIEWNFIDfGLDLQPCIELIErpTNPPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQKPKQlkDKT 573
Cdd:cd14896 391 QEEEECQRELLPWVPIP-QPPRESCLDLLV--DQPHSLLSILDDQTWLSQATDHTFLQKCHYHHGDHPSYAKPQL--PLP 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 574 EFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFMADLWKDVDRIVGLDQMAKmtesslpsasktkkgmfrTV 653
Cdd:cd14896 466 VFTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQEAEPQYGLGQGKP------------------TL 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 654 GQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAA 733
Cdd:cd14896 528 ASRFQQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGALGS 607
|
650 660 670
....*....|....*....|....*....|....*...
gi 156120901 734 NAIPkGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd14896 608 ERQE-ALSDRERCGAILSQVLGAESPLYHLGATKVLLK 644
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
64-814 |
8.60e-133 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 437.15 E-value: 8.60e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 64 ENGKKVTVGKDDIQKMNPP-KFSKVEDMAELTCLNEASVLHNLRERYFSGLIYTYSGLFCVVVNPYKQLPIYSEKIIEMY 142
Cdd:PTZ00014 74 PTNSTFEVKPEHAFNANSQiDPMTYGDIGLLPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRY 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 143 KGKKRHE-MPPHIYAIADTAYRSMLQDREDQSILCTGESGAGKTENTKKVIQYLAmvaSSHKGKKDTSItgelEKQLLQA 221
Cdd:PTZ00014 154 RDAKDSDkLPPHVFTTARRALENLHGVKKSQTIIVSGESGAGKTEATKQIMRYFA---SSKSGNMDLKI----QNAIMAA 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 222 NPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRNDLLL 301
Cdd:PTZ00014 227 NPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKL 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 302 EGFNNYTFLSNGFVPIPAAQDDEMFNETVEAMAIMGFTEEEQLSILRVVSSVLQLGNIVF--KKERNTDQASM--PDNTA 377
Cdd:PTZ00014 307 KSLEEYKYINPKCLDVPGIDDVKDFEEVMESFDSMGLSESQIEDIFSILSGVLLLGNVEIegKEEGGLTDAAAisDESLE 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 378 A-QKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQADFAVEALAKATYERLFRWILTRVNKALDKThrQG-ASFL 455
Cdd:PTZ00014 387 VfNEACELLFLDYESLKKELTVKVTYAGNQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPP--GGfKVFI 464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 456 GILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIELIERPTNppGVLALL 535
Cdd:PTZ00014 465 GMLDIFGFEVFKNNSLEQLFINITNEMLQKNFVDIVFERESKLYKDEGISTEELEY-TSNESVIDLLCGKGK--SVLSIL 541
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 536 DEECWFPKATDKSFVEKLCTEQGSHPKFQKPKQLKDKtEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFM 615
Cdd:PTZ00014 542 EDQCLAPGGTDEKFVSSCNTNLKNNPKYKPAKVDSNK-NFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLV 620
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 616 ADLWKDVdrivgldqmaKMTEsslpsaSKTKKGMFrtVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLV 695
Cdd:PTZ00014 621 RDLFEGV----------EVEK------GKLAKGQL--IGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKV 682
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 696 LEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFF-RTGV 774
Cdd:PTZ00014 683 LIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKYLDLAVSNDSSLDPKEKAEKLLERSGLPKDSYAIGKTMVFLkKDAA 762
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 156120901 775 --LAHLEEERDLKITDVIMAFQAMCRGYLARKAFAKRQQQLT 814
Cdd:PTZ00014 763 keLTQIQREKLAAWEPLVSVLEALILKIKKKRKVRKNIKSLV 804
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
99-757 |
2.05e-132 |
|
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not much is known about this myosin class. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276873 [Multi-domain] Cd Length: 682 Bit Score: 431.25 E-value: 2.05e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKQLPIYSEKIIEMYK--GKKRHE-------MPPHIYAIADTAYRSMLQD- 168
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSQgiespqaLGPHVFAIADRSYRQMMSEi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 169 REDQSILCTGESGAGKTENTKKVIQYLAMVASSHKGKKDTSitGELEK-----QLLQANPILEAFGNAKTVKNDNSSRFG 243
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLTTLGNGEEGAPNEG--EELGKlsimdRVLQSNPILEAFGNARTLRNDNSSRFG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 244 KFIRINFDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRN--------DLLLEGFNNYTFLSNGFV 315
Cdd:cd14908 159 KFIELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEEEHEkyefhdgiTGGLQLPNEFHYTGQGGA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 316 P-IPAAQDDEMFNETVEAMAIMGFTEEEQLSILRVVSSVLQLGNIVFKKERNtDQASMPDNTAAQK----VCHLMGINVT 390
Cdd:cd14908 239 PdLREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEE-DGAAEIAEEGNEKclarVAKLLGVDVD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 391 DFTRSILTPRIKVGRDVVQKAQTKEQADFAVEALAKATYERLFRWILTRVNKALDKTHRQGA-SFLGILDIAGFEIFEVN 469
Cdd:cd14908 318 KLLRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSINWENDKDIrSSVGVLDIFGFECFAHN 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 470 SFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIELIERPtnPPGVLALLDEECWFP-KATDKS 548
Cdd:cd14908 398 SFEQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQAK--KKGILTMLDDECRLGiRGSDAN 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 549 FVEKL--------CTEQGSHPKFQKPKQLKDKTEFSIIHYAGKVDYNA-SAWLTKNMDPLndnvtsllnassdkfmadlw 619
Cdd:cd14908 475 YASRLyetylpekNQTHSENTRFEATSIQKTKLIFAVRHFAGQVQYTVeTTFCEKNKDEI-------------------- 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 620 kdvdrivgldqmakmtesslpsaSKTKKGMFRTvGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQL 699
Cdd:cd14908 535 -----------------------PLTADSLFES-GQQFKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQL 590
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 156120901 700 RCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAAnAIPK----GFMDGKQACILMIKALELD 757
Cdd:cd14908 591 RYGGVLEAVRVARSGYPVRLPHKDFFKRYRMLLP-LIPEvvlsWSMERLDPQKLCVKKMCKD 651
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
99-769 |
3.91e-128 |
|
class XIV myosin, motor domain; These myosins localize to plasma membranes of the intracellular parasites and may be involved in the cell invasion process. Their known functions include: transporting phagosomes to the nucleus and perturbing the developmentally regulated elimination of the macronucleus during conjugation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to their motor domain these myosins have a MyTH4-FERM protein domain combination. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276843 Cd Length: 649 Bit Score: 417.85 E-value: 3.91e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKQLPIYSEKIIEMYKGKKRH-EMPPHIYAIADTAYRSMLQDREDQSILCT 177
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDAPDLtKLPPHVFYTARRALENLHGVNKSQTIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 178 GESGAGKTENTKKVIQYLAmvaSSHKGKKDTSItgelEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 257
Cdd:cd14876 81 GESGAGKTEATKQIMRYFA---SAKSGNMDLRI----QTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVASEGGIR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 258 GANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRNDLLLEGFNNYTFLSNGFVPIPAAQDDEMFNETVEAMAIMG 337
Cdd:cd14876 154 YGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLGLKEYKFLNPKCLDVPGIDDVADFEEVLESLKSMG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 338 FTEEEQLSILRVVSSVLQLGNIVFKKErntDQASMPDntAA----------QKVCHLMGINVTDFTRSILTPRIKVGRDV 407
Cdd:cd14876 234 LTEEQIDTVFSIVSGVLLLGNVKITGK---TEQGVDD--AAaisneslevfKEACSLLFLDPEALKRELTVKVTKAGGQE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 408 VQKAQTKEQADFAVEALAKATYERLFRWILTRVNKALDKTHRQGAsFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLF 487
Cdd:cd14876 309 IEGRWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIEPPGGFKN-FMGMLDIFGFEVFKNNSLEQLFINITNEMLQKNF 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 488 NHTMFILEQEEYQREGI---EWNFIDfgldlqpCIELIERPTNPPG-VLALLDEECWFPKATDKSFVEKLCTEQGSHPKF 563
Cdd:cd14876 388 IDIVFERESKLYKDEGIptaELEYTS-------NAEVIDVLCGKGKsVLSILEDQCLAPGGSDEKFVSACVSKLKSNGKF 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 564 qKPKQLKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFMADLWKDVdrivgldqmaKMTesslpsAS 643
Cdd:cd14876 461 -KPAKVDSNINFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEGV----------VVE------KG 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 644 KTKKGMFrtVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQE 723
Cdd:cd14876 524 KIAKGSL--IGSQFLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEE 601
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 156120901 724 FRQRYEILAANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIF 769
Cdd:cd14876 602 FLYQFKFLDLGIANDKSLDPKVAALKLLESSGLSEDEYAIGKTMVF 647
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
99-732 |
2.09e-117 |
|
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor for mitochondrial movement in vertebrate cells. It contains a variable number of IQ domains. Human myo19 contains a motor domain, three IQ motifs, and a short tail. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276846 [Multi-domain] Cd Length: 658 Bit Score: 387.67 E-value: 2.09e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKQLP-IYSEKIIEMYKGKKR-HEMPPHIYAIADTAYRSMLQDRE--DQSI 174
Cdd:cd14880 1 ETVLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQpQKLKPHIFTVGEQTYRNVKSLIEpvNQSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 175 LCTGESGAGKTENTKKVIQYLAMVASSHKGKKDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTG 254
Cdd:cd14880 81 VVSGESGAGKTWTSRCLMKFYAVVAASPTSWESHKIAERIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQLNRAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 255 YIVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRNDLLLEGFNNYTFLSNGfvpiPAAQDDEMFNETVEAMA 334
Cdd:cd14880 161 QMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAAFSWLPNP----ERNLEEDCFEVTREAML 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 335 IMGFTEEEQLSILRVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKV---CHLMGINVTDFTRSILTPRIKVGRD--VVQ 409
Cdd:cd14880 237 HLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPCQPMDDTKESVrtsALLLKLPEDHLLETLQIRTIRAGKQqqVFK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 410 KAQTKEQADFAVEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNH 489
Cdd:cd14880 317 KPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSICADTDSWTTFIGLLDVYGFESFPENSLEQLCINYANEKLQQHFVA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 490 TMFILEQEEYQREGIEWNFIDFGlDLQPCIELIErpTNPPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQKPKQL 569
Cdd:cd14880 397 HYLRAQQEEYAVEGLEWSFINYQ-DNQTCLDLIE--GSPISICSLINEECRLNRPSSAAQLQTRIESALAGNPCLGHNKL 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 570 KDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFMADLWKDVDRivgldqmakmtESSLPSASKTKKGM 649
Cdd:cd14880 474 SREPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPANPE-----------EKTQEEPSGQSRAP 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 650 FRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 729
Cdd:cd14880 543 VLTVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQNFVERYK 622
|
...
gi 156120901 730 ILA 732
Cdd:cd14880 623 LLR 625
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
99-767 |
1.07e-116 |
|
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds Dictyostelium and Polysphondylium. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276871 [Multi-domain] Cd Length: 715 Bit Score: 387.80 E-value: 1.07e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKQLP-IYSEKIIEMYKGKKR-HEMPPHIYAIADTAYRSMLQDREDQSILC 176
Cdd:cd14906 1 AIILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 177 TGESGAGKTENTKKVIQYLaMVASSHKGKKDTSITG---ELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVT 253
Cdd:cd14906 81 SGESGSGKTEASKTILQYL-INTSSSNQQQNNNNNNnnnSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFRSS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 254 GYIV-GANIETYLLEKSR-AIRQARDERTFHIFYYLIAGAKEKMR-----------------NDLLLEGFNNYTFLSNGF 314
Cdd:cd14906 160 DGKIdGASIETYLLEKSRiSHRPDNINLSYHIFYYLVYGASKDERskwglnndpskyryldaRDDVISSFKSQSSNKNSN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 315 VPiPAAQDDEMFNETVEAMAIMGFTEEEQLSILRVVSSVLQLGNIVFKKERNTDQAS--MPDNTAA-QKVCHLMGINVTD 391
Cdd:cd14906 240 HN-NKTESIESFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSDFSKYAyqKDKVTASlESVSKLLGYIESV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 392 FTRSILTPRIKVG---------RDVVQKAQTKEqadfaveALAKATYERLFRWILTRVNKALDK----------THRQGA 452
Cdd:cd14906 319 FKQALLNRNLKAGgrgsvycrpMEVAQSEQTRD-------ALSKSLYVRLFKYIVEKINRKFNQntqsndlaggSNKKNN 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 453 SFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIELIERPTNppGVL 532
Cdd:cd14906 392 LFIGVLDIFGFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELIEKKSD--GIL 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 533 ALLDEECWFPKATDKSFVEKlCTEQgSHPKFQKPKQLKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSD 612
Cdd:cd14906 469 SLLDDECIMPKGSEQSLLEK-YNKQ-YHNTNQYYQRTLAKGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSN 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 613 KFMADLWkdvdrivgldqmaKMTESSLPSASKTKKGMFRTVGQlYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDA 692
Cdd:cd14906 547 FLKKSLF-------------QQQITSTTNTTKKQTQSNTVSGQ-FLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNN 612
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 156120901 693 FLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANAIPKGFMDGKQACILMIKALELDPNLYRIGQSK 767
Cdd:cd14906 613 VHVLSQLRNVGVLNTIKVRKMGYSYRRDFNQFFSRYKCIVDMYNRKNNNNPKLASQLILQNIQSKLKTMGISNNK 687
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
99-771 |
1.85e-111 |
|
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain binding domain, and a C-terminal GPA/Q-rich domain. There is little known about the function of this myosin class. Two of the earliest members identified in this class are green alga Acetabularia cliftonii, Aclmyo1 and Aclmyo2. They are striking with their short tail of Aclmyo1 of 18 residues and the maximum of 7 IQ motifs in Aclmyo2. It is thought that these myosins are involved in organelle transport and tip growth. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276842 [Multi-domain] Cd Length: 664 Bit Score: 371.06 E-value: 1.85e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 99 ASVLHNLRERyFSGLIYTYS--GLFCVVVNPYKQLPIYSEKIIEMY-KGKKRHEMPPHIYAIADTAYRSM-LQDREDQSI 174
Cdd:cd14875 1 ATLLHCIKER-FEKLHQQYSlmGEMVLSVNPFRLMPFNSEEERKKYlALPDPRLLPPHIWQVAHKAFNAIfVQGLGNQSV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 175 LCTGESGAGKTENTKKVIQYLAMVASSHKGK-KDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD-V 252
Cdd:cd14875 80 VISGESGSGKTENAKMLIAYLGQLSYMHSSNtSQRSIADKIDENLKWSNPVMESFGNARTVRNDNSSRFGKYIKLYFDpT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 253 TGYIVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRNDL----------LLEGFNnyTFLSNGfVPIPAAQD 322
Cdd:cd14875 160 SGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELgglktaqdykCLNGGN--TFVRRG-VDGKTLDD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 323 DEMFNETVEAMAIMGFTEEEQLSILRVVSSVLQLGNIVFKKERNtDQASMPDNTAAQKVCHLMGINVTDFTRSILtprIK 402
Cdd:cd14875 237 AHEFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQN-DKAQIADETPFLTACRLLQLDPAKLRECFL---VK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 403 VGRDVVQKAQTKEQADFAVEALAKATYERLFRWILTRVNKALD-KTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNE 481
Cdd:cd14875 313 SKTSLVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNASITpQGDCSGCKYIGLLDIFGFENFTRNSFEQLCINYANE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 482 KLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIELIERPTNppGVLALLDEECWFPKATDKSFVEKLCTE-QGSH 560
Cdd:cd14875 393 SLQNHYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNMFDQKRT--GIFSMLDEECNFKGGTTERFTTNLWDQwANKS 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 561 PKFQKPKQLKDKTeFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFMADLWkdvdrivgldqmakmteSSLP 640
Cdd:cd14875 470 PYFVLPKSTIPNQ-FGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTLL-----------------STEK 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 641 SASKTKKgmfrTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIV 720
Cdd:cd14875 532 GLARRKQ----TVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRRP 607
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 156120901 721 FQEF-RQRYEILAANAIpKGFMDGK--QACILMIKALE-----LDPNlYRIGQSKIFFR 771
Cdd:cd14875 608 IEQFcRYFYLIMPRSTA-SLFKQEKysEAAKDFLAYYQrlygwAKPN-YAVGKTKVFLR 664
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
99-771 |
6.63e-109 |
|
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell adhesion and filopodia formation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276851 Cd Length: 650 Bit Score: 363.05 E-value: 6.63e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKQLP-IYSEKIIEMYKGKKRH-----EMPPHIYAIADTAYRSMLQDREDQ 172
Cdd:cd14886 1 AVVIDILRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 173 SILCTGESGAGKTENTKKVIQYLAMVASSHkgkkdtsiTGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDV 252
Cdd:cd14886 81 SCIVSGESGAGKTETAKQLMNFFAYGHSTS--------STDVQSLILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 253 TGYIVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRNDLLLEGFNNYTFLSNG-FVPIPAAQDDEMFNETVE 331
Cdd:cd14886 153 DGGLKGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLESYNFLNASkCYDAPGIDDQKEFAPVRS 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 332 AMAIMgFTEEEQLSILRVVSSVLQLGNIVFKKERN--TDQASMPDNTAA-QKVCHLMGINVTDFTRSILTPRIKVGRDVV 408
Cdd:cd14886 233 QLEKL-FSKNEIDSFYKCISGILLAGNIEFSEEGDmgVINAAKISNDEDfGKMCELLGIESSKAAQAIITKVVVINNETI 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 409 QKAQTKEQADFAVEALAKATYERLFRWILTRVNKALdKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFN 488
Cdd:cd14886 312 ISPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEII-QFDADARPWIGILDIYGFEFFERNTYEQLLINYANERLQQYFI 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 489 HTMFILEQEEYQREGIEWNFIDFGlDLQPCIELIERPTNppGVLALLDEECWFPKATDKSFVEKlCTEQGSHPKF--QKP 566
Cdd:cd14886 391 NQVFKSEIQEYEIEGIDHSMITFT-DNSNVLAVFDKPNL--SIFSFLEEQCLIQTGSSEKFTSS-CKSKIKNNSFipGKG 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 567 KQLKdkteFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSdkfmadlwkdvdrivglDQMAKMTESSLPSASKTK 646
Cdd:cd14886 467 SQCN----FTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGST-----------------NPIVNKAFSDIPNEDGNM 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 647 KGMFrtVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQ 726
Cdd:cd14886 526 KGKF--LGSTFQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFFH 603
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 156120901 727 RYEILA--ANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd14886 604 RNKILIshNSSSQNAGEDLVEAVKSILENLGIPCSDYRIGKTKVFLR 650
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
99-728 |
3.32e-108 |
|
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276864 [Multi-domain] Cd Length: 717 Bit Score: 363.26 E-value: 3.32e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKQLP-IYSEKIIEMY----------KGKKRHEMPPHIYAIADTAYRSMLQ 167
Cdd:cd14899 1 ASILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYaydhnsqfgdRVTSTDPREPHLFAVARAAYIDIVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 168 DREDQSILCTGESGAGKTENTKKVIQYLAMVASSHKGKKDTSITGE---------LEKQLLQANPILEAFGNAKTVKNDN 238
Cdd:cd14899 81 NGRSQSILISGESGAGKTEATKIIMTYFAVHCGTGNNNLTNSESISppaspsrttIEEQVLQSNPILEAFGNARTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 239 SSRFGKFIRINF-DVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYLIAG-----AKEKMRNDLLLEGFNNYTFLSN 312
Cdd:cd14899 161 SSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSAdnncvSKEQKQVLALSGGPQSFRLLNQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 313 GFVPI--PAAQDDEMFNETVEAMAIMGFTEEEQLSILRVVSSVLQLGNIVF-----KKERNT--DQASMPDNTAA----- 378
Cdd:cd14899 241 SLCSKrrDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFeqiphKGDDTVfaDEARVMSSTTGafdhf 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 379 QKVCHLMGINvTDFTRSILTPR--------IKVGRDVVQKAQTKEqadfaveALAKATYERLFRWILTRVNKAL------ 444
Cdd:cd14899 321 TKAAELLGVS-TEALDHALTKRwlhasnetLVVGVDVAHARNTRN-------ALTMECYRLLFEWLVARVNNKLqrqasa 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 445 --------DKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQ 516
Cdd:cd14899 393 pwgadesdVDDEEDATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFP-NNR 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 517 PCIELIERptNPPGVLALLDEECWFPKATDKSFVEKLCTE---QGSHPKFQKPKQLKDKTEFSIIHYAGKVDYNASAWLT 593
Cdd:cd14899 472 ACLELFEH--RPIGIFSLTDQECVFPQGTDRALVAKYYLEfekKNSHPHFRSAPLIQRTTQFVVAHYAGCVTYTIDGFLA 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 594 KNMDPLNDNVTSLLNASSDKFMADLWK-DVDRIVGLDQMAKMTESSLPSASKTKKGMFrTVGQLYKEQLGKLMTTLRNTT 672
Cdd:cd14899 550 KNKDSFCESAAQLLAGSSNPLIQALAAgSNDEDANGDSELDGFGGRTRRRAKSAIAAV-SVGTQFKIQLNELLSTVRATT 628
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 156120901 673 PNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 728
Cdd:cd14899 629 PRYVRCIKPNDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRY 684
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
99-771 |
7.03e-98 |
|
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the other myosins that have a MyTH4 domain such as class III, VII, IX, X , XV, XVI, XVII, XX, XXII, XXV, and XXXIV. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276852 Cd Length: 725 Bit Score: 333.54 E-value: 7.03e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 99 ASVLHNLRERYFS--------GLIYTYSGLFCVVVNPYKQLPIYSEKIIEMYKGKKRHEMPPHIYAIADTAYRSMLQDRE 170
Cdd:cd14887 1 PNLLENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 171 DQSILCTGESGAGKTENTKKVIQYLAMVASSHKGKKDTSitgeLEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 250
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTYLAAVSDRRHGADSQG----LEARLLQSGPVLEAFGNAHTVLNANSSRFGKMLLLHF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 251 DVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRNDLLL-EGFNNYTFLsngfvpipaaqddemfNET 329
Cdd:cd14887 157 TGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAVAAATQKSSAgEGDPESTDL----------------RRI 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 330 VEAMAIMGFTEEEQLSILRVVSSVLQLGNIVFKKERNTDQASMPDNTA--------AQKVCHLM-------GINVTDFTR 394
Cdd:cd14887 221 TAAMKTVGIGGGEQADIFKLLAAILHLGNVEFTTDQEPETSKKRKLTSvsvgceetAADRSHSSevkclssGLKVTEASR 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 395 SILTPRIK------------------VGRDV--VQKAQTKEQADFAVEALAKATYERLFRWILTRVNKALDKTHR----- 449
Cdd:cd14887 301 KHLKTVARllglppgvegeemlrlalVSRSVreTRSFFDLDGAAAARDAACKNLYSRAFDAVVARINAGLQRSAKpsesd 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 450 --------QGASFLGILDIAGFEIFE---VNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFI--DFGLDLQ 516
Cdd:cd14887 381 sdedtpstTGTQTIGILDLFGFEDLRnhsKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGVFQNQDcsAFPFSFP 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 517 PCIELIERPTN----------------------PPGVLALLDEECWFPKATDKSFVEKLCTEQGS-------HPKFQKPK 567
Cdd:cd14887 461 LASTLTSSPSStspfsptpsfrsssafatspslPSSLSSLSSSLSSSPPVWEGRDNSDLFYEKLNkniinsaKYKNITPA 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 568 QLKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSdkfmadlwkDVDRIVGLDQmakmteSSLPSASKTKK 647
Cdd:cd14887 541 LSRENLEFTVSHFACDVTYDARDFCRANREATSDELERLFLACS---------TYTRLVGSKK------NSGVRAISSRR 605
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 648 gmfRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQR 727
Cdd:cd14887 606 ---STLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVELWRR 682
|
730 740 750 760
....*....|....*....|....*....|....*....|....
gi 156120901 728 YEILAANAIpKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd14887 683 YETKLPMAL-REALTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
96-770 |
1.17e-95 |
|
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase uses its motor domain to tether its vesicular cargo to peripheral actin. It works in opposition to dynein, contributing to the retention of Mcs1 vesicles at the site of cell growth and increasing vesicle fusion necessary for polarized growth. Class 17 myosins consist of a N-terminal myosin motor domain with Cyt-b5, chitin synthase 2, and a DEK_C domains at it C-terminus. The chitin synthase region contains several transmembrane domains by which myosin 17 is thought to bind secretory vesicles. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276845 [Multi-domain] Cd Length: 647 Bit Score: 324.50 E-value: 1.17e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 96 LNEASVLHNLRERYFSGLIYTY---SGLfcVVVNPYKQLPIYSE----KIIEMYKG---KKRHEMPPHIYAIADTAYRSM 165
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRlgsSAL--VAVNPYKYLSSNSDaslgEYGSEYYDttsGSKEPLPPHAYDLAARAYLRM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 166 LQDREDQSILCTGESGAGKTENTKKVI-QYLAMVASSHKGKKdtsitgeLEKQLLQANPILEAFGNAKTVKNDNSSRFGK 244
Cdd:cd14879 79 RRRSEDQAVVFLGETGSGKSESRRLLLrQLLRLSSHSKKGTK-------LSSQISAAEFVLDSFGNAKTLTNPNASRFGR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 245 FIRINFDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRNDLLLEGFNNYTFL--SNGF--VPIPAA 320
Cdd:cd14879 152 YTELQFNERGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPSDYALLasYGCHplPLGPGS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 321 QDDEMFNETVEAMAIMGFTEEEQLSILRVVSSVLQLGNIVF--KKERNTDQASMpDNTAA-QKVCHLMGINVTDFtRSIL 397
Cdd:cd14879 232 DDAEGFQELKTALKTLGFKRKHVAQICQLLAAILHLGNLEFtyDHEGGEESAVV-KNTDVlDIVAAFLGVSPEDL-ETSL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 398 TPRIK-VGRDVV----QKAQTKEQADfaveALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIF---EVN 469
Cdd:cd14879 310 TYKTKlVRKELCtvflDPEGAAAQRD----ELARTLYSLLFAWVVETINQKLCAPEDDFATFISLLDFPGFQNRsstGGN 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 470 SFEQLCINYTNEKLQ-----QLFNHTMFILEQEEYQREGIEWNfidfglDLQPCIELIERPTNppGVLALLDEEC-WFPK 543
Cdd:cd14879 386 SLDQFCVNFANERLHnyvlrSFFERKAEELEAEGVSVPATSYF------DNSDCVRLLRGKPG--GLLGILDDQTrRMPK 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 544 ATDKSFVEKLCTEQGSHPKFQKPKQLKDKTE---FSIIHYAGKVDYNASAWLTKNMDPLndnvtsllnaSSDkFMAdlwk 620
Cdd:cd14879 458 KTDEQMLEALRKRFGNHSSFIAVGNFATRSGsasFTVNHYAGEVTYSVEGFLERNGDVL----------SPD-FVN---- 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 621 dvdrivgldqmakmtesslpsasktkkgMFRTVGQLyKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLR 700
Cdd:cd14879 523 ----------------------------LLRGATQL-NAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQIR 573
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 701 CNGVLEGIRICRQGFPNRIVFQEFRQRYEILAAnaipkgFMDGKQACILMIKALELDPNLYRIGQSKIFF 770
Cdd:cd14879 574 SLGLPELAARLRVEYVVSLEHAEFCERYKSTLR------GSAAERIRQCARANGWWEGRDYVLGNTKVFL 637
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
100-735 |
4.62e-95 |
|
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276863 Cd Length: 578 Bit Score: 320.31 E-value: 4.62e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 100 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKQlpIYSEKIIEMYKGKKRHeMPPHIYAIADTAYRSMLQdREDQSILCTGE 179
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYET--IYGAGAMKAYLKNYSH-VEPHVYDVAEASVQDLLV-HGNQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 180 SGAGKTENTKKVIQYLAmvasshkgkKDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDvtGYIVGA 259
Cdd:cd14898 78 SGSGKTENAKLVIKYLV---------ERTASTTSIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKFD--GKITGA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 260 NIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRNDLLlegfNNYTFLSNGFVPIPAAQDDEMFNETVEAMAIMGFT 339
Cdd:cd14898 147 KFETYLLEKSRVTHHEKGERNFHIFYQFCASKRLNIKNDFI----DTSSTAGNKESIVQLSEKYKMTCSAMKSLGIANFK 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 340 EEEQLSIlrvvsSVLQLGNIVFKKERNTDQASmpdNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQADF 419
Cdd:cd14898 223 SIEDCLL-----GILYLGSIQFVNDGILKLQR---NESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIEVFNTLKQART 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 420 AVEALAKATYERLFRWILTRVNKALDKThrqGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEEY 499
Cdd:cd14898 295 IRNSMARLLYSNVFNYITASINNCLEGS---GERSISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMFRAKQGMY 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 500 QREGIEWNFIDFgLDLQPCIELIERPTnppGVLALLDEECWFPKATDKSFVEKLcteqgsHPKFQKPKQLKDKTEFSIIH 579
Cdd:cd14898 372 KEEGIEWPDVEF-FDNNQCIRDFEKPC---GLMDLISEESFNAWGNVKNLLVKI------KKYLNGFINTKARDKIKVSH 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 580 YAGKVDYNASAWLTKNMDplndnvtsllnassdkfmadlwKDVDRIVGLDQMAkmTESSLPSASKtkkgmfrtvgqLYKE 659
Cdd:cd14898 442 YAGDVEYDLRDFLDKNRE----------------------KGQLLIFKNLLIN--DEGSKEDLVK-----------YFKD 486
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156120901 660 QLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANA 735
Cdd:cd14898 487 SMNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRILGITL 562
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
99-771 |
2.23e-93 |
|
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal tyrosine-phosphorylated phosphoinositide-3-kinase adapter 3/NYAP3. Myo16 is thought to play a regulatory role in cell cycle progression and has been recently implicated in Schizophrenia. Class XVI myosins are characterized by an N-terminal ankyrin repeat domain and some with chitin synthase domains that arose independently from the ones in the class XVII fungal myosins. They bind protein phosphatase 1 catalytic subunits 1alpha/PPP1CA and 1gamma/PPP1CC. Human Myo16 interacts with ACOT9, ARHGAP26 and PIK3R2 and with components of the WAVE1 complex, CYFIP1 and NCKAP1. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276844 [Multi-domain] Cd Length: 656 Bit Score: 318.30 E-value: 2.23e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKQLPIYSEKIIEMY---KGKKRHEMPPHIYAIADTAYRSMLQDREDQSIL 175
Cdd:cd14878 1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYlssSGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 176 CTGESGAGKTENTKKVIQYLAMVASSHKGKKDTSITgelekqllQANPILEAFGNAKTVKNDNSSRFGKFIRINF-DVTG 254
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLTCRASSSRTTFDSRFK--------HVNCILEAFGHAKTTLNDLSSCFIKYFELQFcERKK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 255 YIVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRNDLLLEGFNNYTFLSNGFVP-IPAA---QDDEMFNETV 330
Cdd:cd14878 153 HLTGARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTMREdVSTAersLNREKLAVLK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 331 EAMAIMGFTEEEQLSILRVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINvTDFTRSILTPRIKVGR-DVVQ 409
Cdd:cd14878 233 QALNVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVS-TDELASALTTDIQYFKgDMII 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 410 KAQTKEQADFAVEALAKATYERLFRWILTRVNKAL---DKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQL 486
Cdd:cd14878 312 RRHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLqsqDEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHY 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 487 FNHTMFILEQEEYQREGIewnfidfgldlqpCIELIERPTN-----------PPGVLALLDEECWFPKATDKSFVEKLCT 555
Cdd:cd14878 392 INEVLFLQEQTECVQEGV-------------TMETAYSPGNqtgvldfffqkPSGFLSLLDEESQMIWSVEPNLPKKLQS 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 556 --EQGSHPKFQKPKQ-------LKDK-TEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFMADLWKdvdri 625
Cdd:cd14878 459 llESSNTNAVYSPMKdgngnvaLKDQgTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQ----- 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 626 vgldqmAKMTesslpsasktkkgmfrTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVL 705
Cdd:cd14878 534 ------SKLV----------------TIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVL 591
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156120901 706 EGIRICRQGFPNRIVFQEFRQRYEILAANAI-PKGFMDGKQACILMIKALELDPnlYRIGQSKIFFR 771
Cdd:cd14878 592 EMVKIFRYGYPVRLSFSDFLSRYKPLADTLLgEKKKQSAEERCRLVLQQCKLQG--WQMGVRKVFLK 656
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
99-771 |
1.02e-88 |
|
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a coiled-coil region in their C-terminal tail. The function of the class XXIV myosins remain elusive. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276897 Cd Length: 637 Bit Score: 303.86 E-value: 1.02e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKQLPIYsekiIEMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 178
Cdd:cd14937 1 AEVLNMLALRYKKNYIYTIAEPMLISINPYQVIDVD----INEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 179 ESGAGKTENTKKVIQ-YLAMVasshkgKKDTSITgeleKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 257
Cdd:cd14937 77 ESGSGKTEASKLVIKyYLSGV------KEDNEIS----NTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 258 GANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRNDLLLEGFNNYTFLSNGFVPIPAAQDDEMFNETVEAMAIMG 337
Cdd:cd14937 147 SSSIEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSENEYKYIVNKNVVIPEIDDAKDFGNLMISFDKMN 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 338 FTEEEQlSILRVVSSVLQLGNIVFK---KERNTDQASMPDNT--AAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQ 412
Cdd:cd14937 227 MHDMKD-DLFLTLSGLLLLGNVEYQeieKGGKTNCSELDKNNleLVNEISNLLGINYENLKDCLVFTEKTIANQKIEIPL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 413 TKEQADFAVEALAKATYERLFRWILTRVNKALDkTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMF 492
Cdd:cd14937 306 SVEESVSICKSISKDLYNKIFSYITKRINNFLN-NNKELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIHSIYLYIVY 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 493 ILEQEEYQREGIEWNFIDFGLDlQPCIELIERPTNppgVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQKPKqlKDK 572
Cdd:cd14937 385 EKETELYKAEDILIESVKYTTN-ESIIDLLRGKTS---IISILEDSCLGPVKNDESIVSVYTNKFSKHEKYASTK--KDI 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 573 TE-FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFMADLWKDVDrivgldqmakMTESslpsasktkKGMFR 651
Cdd:cd14937 459 NKnFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDVE----------VSES---------LGRKN 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 652 TVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRIcRQGFPNRIVFQEFRQRYEIL 731
Cdd:cd14937 520 LITFKYLKNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNI-SFFFQYKYTFDVFLSYFEYL 598
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 156120901 732 AANAIPKGFMDGKQACILMIKAlELDPNLYRIGQSKIFFR 771
Cdd:cd14937 599 DYSTSKDSSLTDKEKVSMILQN-TVDPDLYKVGKTMVFLK 637
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
99-723 |
5.98e-79 |
|
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 IQ motifs and a single MyTH4 domain in its C-terminal tail. The lack of a FERM domain here is odd since MyTH4 domains are usually found alongside FERM domains where they bind to microtubules. At any rate these Class XXIII myosins are still proposed to function in the apicomplexan microtubule cytoskeleton. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276850 [Multi-domain] Cd Length: 685 Bit Score: 276.79 E-value: 5.98e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKQLP-IYSEKIIEMYKGKKRHE-------MPPHIYAIADTAYRSMLQDRE 170
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSaasaapfPKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 171 DQSILCTGESGAGKTENTKKVIQYLamvassHKGKKDTSITgELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 250
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYF------HYIQTDSQMT-ERIDKLIYINNILESMSNATTIKNNNSSRCGRINLLIF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 251 D---------VTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYLIAG-AKEKMRNDLLLEGFNNYTFL---------- 310
Cdd:cd14884 154 EeventqknmFNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGlSDEDLARRNLVRNCGVYGLLnpdeshqkrs 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 311 ----------SNGFVPIPAAQDDEMFNETVEAMAIMGFTEEEQLSILRVVSSVLQLGNIVFKKerntdqasmpdntaaqk 380
Cdd:cd14884 234 vkgtlrlgsdSLDPSEEEKAKDEKNFVALLHGLHYIKYDERQINEFFDIIAGILHLGNRAYKA----------------- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 381 VCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQADFAVEALAKATYERLFRWILTRVNKALDKTHRQGA-------- 452
Cdd:cd14884 297 AAECLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNVLKCKEKDEsdnediys 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 453 ---SFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIELIERptnpp 529
Cdd:cd14884 377 ineAIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDVAP-SYSDTLIFIAK----- 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 530 gVLALLDE-----ECWFPKATDKSF-----------VEKLCTEQGSHPKFQK---PKQLKDKTEFSIIHYAGKVDYNASA 590
Cdd:cd14884 451 -IFRRLDDitklkNQGQKKTDDHFFryllnnerqqqLEGKVSYGFVLNHDADgtaKKQNIKKNIFFIRHYAGLVTYRINN 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 591 WLTKNMDPLNDNVTSLLNASSDKFMADlwkdvdrivgldqmakmtesslpSASKTKKGMFRTVGQLYKEQLGKLMTTLRN 670
Cdd:cd14884 530 WIDKNSDKIETSIETLISCSSNRFLRE-----------------------ANNGGNKGNFLSVSKKYIKELDNLFTQLQS 586
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 156120901 671 TTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQE 723
Cdd:cd14884 587 TDMYYIRCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIPKKE 639
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
100-758 |
3.00e-78 |
|
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such members as Drosophila, Daphnia, and mosquitoes. These myosins contain a single IQ motif in the neck region. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276847 [Multi-domain] Cd Length: 633 Bit Score: 273.14 E-value: 3.00e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 100 SVLHNLRERYFSGLIYTYSGLFCVVVNPYkqlpiysekiieMYKGKKRH-------EMPPHIYAIADTAYRSMLQDREDQ 172
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPY------------RDVGNPLTltstrssPLAPQLLKVVQEAVRQQSETGYPQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 173 SILCTGESGAGKTENTKKVIQYLAMVASshkGKKDTsitgELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFdV 252
Cdd:cd14881 70 AIILSGTSGSGKTYASMLLLRQLFDVAG---GGPET----DAFKHLAAAFTVLRSLGSAKTATNSESSRIGHFIEVQV-T 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 253 TGYIVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRNDLLLEGFN--NYTFLSNGFVPIPAAQDDEMFNETV 330
Cdd:cd14881 142 DGALYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDGYSpaNLRYLSHGDTRQNEAEDAARFQAWK 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 331 EAMAIMG--FTEeeqlsILRVVSSVLQLGNIVFKkERNTDQASMPDNTAAQKVCHLMGINVTDFTRSiLTPRIK-VGRDV 407
Cdd:cd14881 222 ACLGILGipFLD-----VVRVLAAVLLLGNVQFI-DGGGLEVDVKGETELKSVAALLGVSGAALFRG-LTTRTHnARGQL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 408 VQKAQTKEQADFAVEALAKATYERLFRWILTRVN--KALDKTHRQGAS--FLGILDIAGFEIFEVNSFEQLCINYTNEKL 483
Cdd:cd14881 295 VKSVCDANMSNMTRDALAKALYCRTVATIVRRANslKRLGSTLGTHATdgFIGILDMFGFEDPKPSQLEHLCINLCAETM 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 484 QQLFNHTMFILEQEEYQREGIEWNF-IDFgLDLQPCIELIErpTNPPGVLALLDEECwFPKATDKSFVEKLCTEQGSHPK 562
Cdd:cd14881 375 QHFYNTHIFKSSIESCRDEGIQCEVeVDY-VDNVPCIDLIS--SLRTGLLSMLDVEC-SPRGTAESYVAKIKVQHRQNPR 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 563 FQKPKQlKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFmadlwkdvdrivgldqmakmtesslpsa 642
Cdd:cd14881 451 LFEAKP-QDDRMFGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYKQNCNF---------------------------- 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 643 sktkkgMFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQ 722
Cdd:cd14881 502 ------GFATHTQDFHTRLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAGGYPHRMRFK 575
|
650 660 670
....*....|....*....|....*....|....*...
gi 156120901 723 EFRQRYEILAANAIPKGFMDGKQAC--ILMIKALELDP 758
Cdd:cd14881 576 AFNARYRLLAPFRLLRRVEEKALEDcaLILQFLEAQPP 613
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
99-731 |
1.46e-72 |
|
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They are found predominately in nematodes. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276841 [Multi-domain] Cd Length: 628 Bit Score: 256.34 E-value: 1.46e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKQLPIYSEKIIEMYkgkkrhemppHIYAIADTAYRSMLQDRED-QSILCT 177
Cdd:cd14874 1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 178 GESGAGKTENTKKVIQYLAmvaSSHKGKKDTsitgeleKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDvTGYIV 257
Cdd:cd14874 71 GESGSGKSYNAFQVFKYLT---SQPKSKVTT-------KHSSAIESVFKSFGCAKTLKNDEATRFGCSIDLLYK-RNVLT 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 258 GANIE-TYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRNDLLLEGFNNYTFLSNGFVPIPAAQDDEMFNETVEAMAIM 336
Cdd:cd14874 140 GLNLKyTVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGLQKFFYINQGNSTENIQSDVNHFKHLEDALHVL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 337 GFTEEEQLSILRVVSSVLQLGNIVFKKERNTD---QASMPDNTAAQK-VCHLMGINVTDFTrSILTPRIKVGRDVvqkaq 412
Cdd:cd14874 220 GFSDDHCISIYKIISTILHIGNIYFRTKRNPNveqDVVEIGNMSEVKwVAFLLEVDFDQLV-NFLLPKSEDGTTI----- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 413 TKEQADFAVEALAKATYERLFRWILTRVNKALDKTHRQGAsfLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMF 492
Cdd:cd14874 294 DLNAALDNRDSFAMLIYEELFKWVLNRIGLHLKCPLHTGV--ISILDHYGFEKYNNNGVEEFLINSVNERIENLFVKHSF 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 493 ILEQEEYQREGIEWNF-IDFGLDLQPCIELIERptNPPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQKPKQlKD 571
Cdd:cd14874 372 HDQLVDYAKDGISVDYkVPNSIENGKTVELLFK--KPYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRSSYGKARN-KE 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 572 KTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFMADLWKdvdrivgldqmakmtesslpSASKTKKGMFR 651
Cdd:cd14874 449 RLEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFE--------------------SYSSNTSDMIV 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 652 TVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 731
Cdd:cd14874 509 SQAQFILRGAQEIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYRCL 588
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
100-724 |
2.13e-72 |
|
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV class. Members here include cellular slime mold Polysphondylium and soil-living amoeba Dictyostelium. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276870 Cd Length: 673 Bit Score: 257.33 E-value: 2.13e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 100 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKQLP-IYSEKIIEMYKgkKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 178
Cdd:cd14905 2 TLINIIQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNYN--QRRGLPPHLFALAAKAISDMQDFRRDQLIFIGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 179 ESGAGKTENTKKVIQYLAMVasshkgkkDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd14905 80 ESGSGKSENTKIIIQYLLTT--------DLSRSKYLRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 259 ANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRNDLLLEGFNNYTFLSN-GFVPIPAAQDDEMFNETVEAMAIMG 337
Cdd:cd14905 152 AKLYSYFLDENRVTYQNKGERNFHIFYQFLKGITDEEKAAYQLGDINSYHYLNQgGSISVESIDDNRVFDRLKMSFVFFD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 338 FTEEEQLSILRVVSSVLQLGNIVFKKERNtdQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAqtkeqa 417
Cdd:cd14905 232 FPSEKIDLIFKTLSFIIILGNVTFFQKNG--KTEVKDRTLIESLSHNITFDSTKLENILISDRSMPVNEAVENR------ 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 418 dfavEALAKATYERLFRWILTRVNKALDKThrQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQE 497
Cdd:cd14905 304 ----DSLARSLYSALFHWIIDFLNSKLKPT--QYSHTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVLKQEQR 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 498 EYQREGIEW-NFIDFGlDLQPCIELIERptnppgVLALLDEECWFPKATDKSFVEKLCTEQGSHPKF-QKPKQlkdkteF 575
Cdd:cd14905 378 EYQTERIPWmTPISFK-DNEESVEMMEK------IINLLDQESKNINSSDQIFLEKLQNFLSRHHLFgKKPNK------F 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 576 SIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFM--ADLWKDVDRIVG-LDQMAKMTESSLPSASKTKKGMFrT 652
Cdd:cd14905 445 GIEHYFGQFYYDVRGFIIKNRDEILQRTNVLHKNSITKYLfsRDGVFNINATVAeLNQMFDAKNTAKKSPLSIVKVLL-S 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 653 VGQLYKEQL-----------------------GKLMTTLRNTTP---------NFVRCIIPNHEKRSGKLDAFLVLEQLR 700
Cdd:cd14905 524 CGSNNPNNVnnpnnnsgggggggnsgggsgsgGSTYTTYSSTNKainnsncdfHFIRCIKPNSKKTHLTFDVKSVNEQIK 603
|
650 660
....*....|....*....|....*...
gi 156120901 701 CNGVLEGIRICRQGFP----NRIVFQEF 724
Cdd:cd14905 604 SLCLLETTRIQRFGYTihynNKIFFDRF 631
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
100-771 |
3.23e-71 |
|
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class XXI myosins do not group with them. Myo21, unlike other myosin proteins, contains UBA-like protein domains and has no structural or functional relationship with the myosins present in other organisms possessing cilia or flagella. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. They have diverse tails with IQ, WW, PX, and Tub domains. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276848 Cd Length: 642 Bit Score: 252.74 E-value: 3.23e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 100 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKQLPIYSEKIIEMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGE 179
Cdd:cd14882 2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 180 SGAGKTENTKKVIQYLAMVAsshKGKKDTSitgeleKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGA 259
Cdd:cd14882 82 SYSGKTTNARLLIKHLCYLG---DGNRGAT------GRVESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMSGA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 260 NIETYLLEKSRAIRQARDERTFHIFYYLIAG--AKEKMRnDLLLEGFNNYTFL----SNGFVPIPAAQDD-----EMFNE 328
Cdd:cd14882 153 IFWMYQLEKLRVSTTDGNQSNFHIFYYFYDFieAQNRLK-EYNLKAGRNYRYLrippEVPPSKLKYRRDDpegnvERYKE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 329 TVEAMAIMGFTEEEQLSILRVVSSVLQLGNIVFKKerNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVV 408
Cdd:cd14882 232 FEEILKDLDFNEEQLETVRKVLAAILNLGEIRFRQ--NGGYAELENTEIASRVAELLRLDEKKFMWALTNYCLIKGGSAE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 409 QKAQTKEQADFAVEALAKATYERLFRWILTRVNKALDKTHrqgaSFLG------ILDIAGFEIFEVNSFEQLCINYTNEK 482
Cdd:cd14882 310 RRKHTTEEARDARDVLASTLYSRLVDWIINRINMKMSFPR----AVFGdkysisIHDMFGFECFHRNRLEQLMVNTLNEQ 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 483 LQQLFNHTMFI---LEQEEYQREGIEWNFIDFGLDLQPCIelierpTNPPGVLALLDEECwfPKATDKSFVekLCTEQGS 559
Cdd:cd14882 386 MQYHYNQRIFIsemLEMEEEDIPTINLRFYDNKTAVDQLM------TKPDGLFYIIDDAS--RSCQDQNYI--MDRIKEK 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 560 HPKFQKPKQlkdKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFMADLWKDvdrivglDQMAKMtessl 639
Cdd:cd14882 456 HSQFVKKHS---AHEFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTN-------SQVRNM----- 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 640 psasktkkgmfRTVGQLYKEQLGKLMTTLRNTTPN----FVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGF 715
Cdd:cd14882 521 -----------RTLAATFRATSLELLKMLSIGANSggthFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGF 589
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 156120901 716 PNRIVFQEFRQRYEILAANAIPKGFMDgKQACILMIKALELDPnlYRIGQSKIFFR 771
Cdd:cd14882 590 SYRIPFQEFLRRYQFLAFDFDETVEMT-KDNCRLLLIRLKMEG--WAIGKTKVFLK 642
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
102-729 |
5.33e-69 |
|
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but possess tandem MyTH4 and FERM domains. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276858 Cd Length: 741 Bit Score: 248.73 E-value: 5.33e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 102 LHNLRERYFSGLIYTYSGLFCVVVNPYKQLPIY----------SEKIIEMYKGKKRHEMPPHIYAIADTAYRSMLQDRED 171
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYtpdhmqaynkSREQTPLYEKDTVNDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 172 QSILCTGESGAGKTENTKKVIQYLAMVASS----HKGKKDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIR 247
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQYLCEIGDEteprPDSEGASGVLHPIGQQILHAFTILEAFGNAATRQNRNSSRFAKMIS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 248 INFDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKE--KMRNDLLL-EGFNNYTFLSNGFVPIPA-AQDD 323
Cdd:cd14893 164 VEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQHdpTLRDSLEMnKCVNEFVMLKQADPLATNfALDA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 324 EMFNETVEAMAIMGFTEEEQLSILRVVSSVLQLGNIVF-------KKERNTDQASMPDNTA------AQ--KVCHLMGIN 388
Cdd:cd14893 244 RDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFvpdpeggKSVGGANSTTVSDAQScalkdpAQilLAAKLLEVE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 389 --VTD---FTRSILTpriKVGRDVVQ--KAQTKEQADFAVEALAKATYERLFRWILTRVNKAL----DKTHRQG----AS 453
Cdd:cd14893 324 pvVLDnyfRTRQFFS---KDGNKTVSslKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILggifDRYEKSNivinSQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 454 FLGILDIAGFEIFE--VNSFEQLCINYTNEKLQQLF-NHTMFI----LEQEEYQREG--IEWNFIDFGLDLQPCIELIER 524
Cdd:cd14893 401 GVHVLDMVGFENLTpsQNSFDQLCFNYWSEKVHHFYvQNTLAInfsfLEDESQQVENrlTVNSNVDITSEQEKCLQLFED 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 525 PtnPPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQKPKQLKDKTE------------FSIIHYAGKVDYNASAWL 592
Cdd:cd14893 481 K--PFGIFDLLTENCKVRLPNDEDFVNKLFSGNEAVGGLSRPNMGADTTNeylapskdwrllFIVQHHCGKVTYNGKGLS 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 593 TKNMDPLNDNVTSLLNASSDKfmadlwkdVDRIVGLDQM--------AKMTESSLPSASKTKKGMFR----------TVG 654
Cdd:cd14893 559 SKNMLSISSTCAAIMQSSKNA--------VLHAVGAAQMaaassekaAKQTEERGSTSSKFRKSASSaresknitdsAAT 630
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 156120901 655 QLYKeQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 729
Cdd:cd14893 631 DVYN-QADALLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRYK 704
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
121-255 |
2.40e-63 |
|
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.
Pssm-ID: 276814 [Multi-domain] Cd Length: 170 Bit Score: 213.36 E-value: 2.40e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 121 FCVVVNPYKQLPIYSE-KIIEMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGESGAGKTENTKKVIQYLAMVA 199
Cdd:cd01363 1 VLVRVNPFKELPIYRDsKIIVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 156120901 200 SSHKGKKD-------TSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGY 255
Cdd:cd01363 81 FNGINKGEtegwvylTEITVTLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEILLDIAGF 143
|
|
| MYSc_Myo24B |
cd14938 |
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
100-769 |
2.01e-56 |
|
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a coiled-coil region in their C-terminal tail. The functions of these myosins remain elusive. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276898 [Multi-domain] Cd Length: 713 Bit Score: 210.46 E-value: 2.01e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 100 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKQLPIYSEKIIEMYK-GKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 178
Cdd:cd14938 2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKcIDCIEDLSLNEYHVVHNALKNLNELKRNQSIIISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 179 ESGAGKTENTKKVIQYLAMVASSHKGKKDTSITGELEKQ---------------LLQANPILEAFGNAKTVKNDNSSRFG 243
Cdd:cd14938 82 ESGSGKSEIAKNIINFIAYQVKGSRRLPTNLNDQEEDNIhneentdyqfnmsemLKHVNVVMEAFGNAKTVKNNNSSRFS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 244 KFIRINFDvTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRNDLLLEGFNNYTFLSNGFVPIPAAQDD 323
Cdd:cd14938 162 KFCTIHIE-NEEIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIENYSMLNNEKGFEKFSDYS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 324 EMFNETVEAMAIMGFTEEEQLSILRVVSSVLQLGNI-----VFKKE---------------------RNTDQASMPDNTA 377
Cdd:cd14938 241 GKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNTeivkaFRKKSllmgknqcgqninyetilselENSEDIGLDENVK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 378 AQKV-CHLMGINVTDFTRSILTPRIkVGRDVVQKAQTKEQADFAVEALAKATYERLFRWILTRVNKALDKTHR--QGASF 454
Cdd:cd14938 321 NLLLaCKLLSFDIETFVKYFTTNYI-FNDSILIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEKCTQLQNinINTNY 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 455 LGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIELIERPTNppGVLAL 534
Cdd:cd14938 400 INVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLYNLLVGPTE--GSLFS 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 535 LDEECWFPKATDKSFVEKLCTEQGSH-PKFQKPKQLK-DKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSD 612
Cdd:cd14938 478 LLENVSTKTIFDKSNLHSSIIRKFSRnSKYIKKDDITgNKKTFVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQSEN 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 613 KFMADLWKDVDRIVGLDQMAKMTESSLPSASKTKKGMFRTVGQ----LYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRS- 687
Cdd:cd14938 558 EYMRQFCMFYNYDNSGNIVEEKRRYSIQSALKLFKRRYDTKNQmavsLLRNNLTELEKLQETTFCHFIVCMKPNESKREl 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 688 GKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAAnaipkgfmDGKQACILMIKALELDPNLYRIGQSK 767
Cdd:cd14938 638 CSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIKNE--------DLKEKVEALIKSYQISNYEWMIGNNM 709
|
..
gi 156120901 768 IF 769
Cdd:cd14938 710 IF 711
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1104-1919 |
1.28e-33 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 142.12 E-value: 1.28e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1104 AQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRdLGEELEALKTELEDTLDSTATQQELRAKREQEvtmlkkal 1183
Cdd:TIGR02168 172 ERRKETERKLERTRENLDRLEDILNELERQLKSLERQAE-KAERYKELKAELRELELALLVLRLEELREELE-------- 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1184 deETRSHESQVQEMRQKHTQVVEELTEQLEQFKRAKANLDKNKQALEKENAELAGELRVLSQAKQEVEHKKKKLEVQLQE 1263
Cdd:TIGR02168 243 --ELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1264 LQSKYSDGEKVRAELNDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLGSQLQDTQELLQEETRQKLNVSTKLRQLED 1343
Cdd:TIGR02168 321 LEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNN 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1344 ERNSLQEQLDEEMEAKQNLERHISTLNIQLSDSKKKL--QDFASTVELLEEGKKKF---QKEIESLTQQYEEKAAAYDKL 1418
Cdd:TIGR02168 401 EIERLEARLERLEDRRERLQQEIEELLKKLEEAELKElqAELEELEEELEELQEELerlEEALEELREELEEAEQALDAA 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1419 EKTKNRLQQELDDLVVDLDNQRQL---VSNLEKKQKKFDQ---LLAEEKNISSKY-----ADERDRAEAEAREKETKAL- 1486
Cdd:TIGR02168 481 ERELAQLQARLDSLERLQENLEGFsegVKALLKNQSGLSGilgVLSELISVDEGYeaaieAALGGRLQAVVVENLNAAKk 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1487 ---SLARALEEALEAKEELERTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDAKL 1563
Cdd:TIGR02168 561 aiaFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKK 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1564 ------------------------RLEVNMQALKVQFE-RDLQARDEQNEEKRRQLQRQLHEYETELEDERKQRALAVAA 1618
Cdd:TIGR02168 641 lrpgyrivtldgdlvrpggvitggSAKTNSSILERRREiEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKE 720
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1619 KKKLEGDLKDLELQADSAIKGREEAIKQLRKLQAQMKDFQRELEDARASRDEIFATAKENEKKAKSLEADLMQLQEDLAA 1698
Cdd:TIGR02168 721 LEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKA 800
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1699 AERARKQADLEKDELAEELASSVSGRNALQDEKRRLEARIaqleeelEEEQGNTEAMSERVRKATQQAEQLSNELATERS 1778
Cdd:TIGR02168 801 LREALDELRAELTLLNEEAANLRERLESLERRIAATERRL-------EDLEEQIEELSEDIESLAAEIEELEELIEELES 873
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1779 AAQKNENARQQLERQNKELRSKLQEMEgavkskfkSTIAALEAKIAQLEEQVeQEAREKQATAKALKQKDKKLKEALLQv 1858
Cdd:TIGR02168 874 ELEALLNERASLEEALALLRSELEELS--------EELRELESKRSELRREL-EELREKLAQLELRLEGLEVRIDNLQE- 943
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 156120901 1859 ederKMAEQYKeqaekgnlrvkqlkRQLEEAEEESQRINANRRKLQRELDEATESNEAMGR 1919
Cdd:TIGR02168 944 ----RLSEEYS--------------LTLEEAEALENKIEDDEEEARRRLKRLENKIKELGP 986
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
996-1832 |
1.43e-33 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 142.12 E-value: 1.43e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 996 KLSKERKLLEERISDLTTNLAEEE----EKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLDGEASDLHEQI 1071
Cdd:TIGR02168 169 KYKERRKETERKLERTRENLDRLEdilnELERQLKSLERQAEKAERYKELKAELRELELALLVLRLEELREELEELQEEL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1072 AELQAQIAELKMQLAKKE---EELQAALGRLDDEMAQKNNALKKIRELeghISDLQEDLDSERAARNKAEKQKRDLGEEL 1148
Cdd:TIGR02168 249 KEAEEELEELTAELQELEeklEELRLEVSELEEEIEELQKELYALANE---ISRLEQQKQILRERLANLERQLEELEAQL 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1149 EALKTELEDTLDSTATQQELRAKREQEVTMLKKALDEEtrshESQVQEMRQKhtqvVEELTEQLEQFKRAKANLDKNKQA 1228
Cdd:TIGR02168 326 EELESKLDELAEELAELEEKLEELKEELESLEAELEEL----EAELEELESR----LEELEEQLETLRSKVAQLELQIAS 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1229 LEKENAELAGEL----RVLSQAKQEVE-HKKKKLEVQLQELQSKYSDGEKVRAELNDKVHKLQNEVESVTGMLNEAEGKA 1303
Cdd:TIGR02168 398 LNNEIERLEARLerleDRRERLQQEIEeLLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQAL 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1304 IKLAKDVASLGSQ---LQDTQELLQEETRQKLNVSTKLRQLEDERNSLQEQLdeemEAKQNLERHISTLniqLSDSkkkL 1380
Cdd:TIGR02168 478 DAAERELAQLQARldsLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELI----SVDEGYEAAIEAA---LGGR---L 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1381 QDfastveLLEEGKKKFQKEIESLTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQKKFDQLLAee 1460
Cdd:TIGR02168 548 QA------VVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALS-- 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1461 kNISSKYADERDRAEAEAREKETKALSLA------RALEEALEAKEELERTNKML--KAEMEDLVsskddvgKNVHELEK 1532
Cdd:TIGR02168 620 -YLLGGVLVVDDLDNALELAKKLRPGYRIvtldgdLVRPGGVITGGSAKTNSSILerRREIEELE-------EKIEELEE 691
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1533 SKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKVQFERdLQARDEQNEEKRRQLQRQLHEYETELEDERKQR 1612
Cdd:TIGR02168 692 KIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLAR-LEAEVEQLEERIAQLSKELTELEAEIEELEERL 770
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1613 ALAVAAKKKLEGDLKDLELQADSAIKGREEAIKQLRKLQAQMKDFQRELEDARASRDEIFATAKENEKKAKSLEADLMQL 1692
Cdd:TIGR02168 771 EEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEEL 850
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1693 QEDLAAAERARKQADLEKDELAEELassvsgrNALQDEKRRLEARIAQLEEELEEEQGNTEAMSERVRKATQQAEQLSNE 1772
Cdd:TIGR02168 851 SEDIESLAAEIEELEELIEELESEL-------EALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREK 923
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1773 LATERSAAQKNENARQQLERQNKELRSKLQEMEGAVKSKFKSTIAALEAKIAQLEEQVEQ 1832
Cdd:TIGR02168 924 LAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKE 983
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
863-1677 |
4.73e-32 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 137.11 E-value: 4.73e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 863 KTKERQQKAESELKELEQKHSQLTEEKNLLQEQLQaetELYAEAEEMrVRLAAKKQELEEI-LHEMEARLEEEEDRSQQL 941
Cdd:TIGR02168 169 KYKERRKETERKLERTRENLDRLEDILNELERQLK---SLERQAEKA-ERYKELKAELRELeLALLVLRLEELREELEEL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 942 QAERKKMAQQmldleeqleeeeaaRQKLQLEKVTAEAKIKKLEDDILVMDDQNNKLSKERKLLEERISDLTTNLAEEEEK 1021
Cdd:TIGR02168 245 QEELKEAEEE--------------LEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRER 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1022 AKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLDGEASDLHEQIAELQAQIAELKMQLAKKEEELQAALGRLDD 1101
Cdd:TIGR02168 311 LANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQ 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1102 EMAQKNNALKKIRELEGHISDLQ---EDLDSERAARNKA--EKQKRDLGEELEALKTELEDTLDSTATQQELRAKREQEV 1176
Cdd:TIGR02168 391 LELQIASLNNEIERLEARLERLEdrrERLQQEIEELLKKleEAELKELQAELEELEEELEELQEELERLEEALEELREEL 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1177 TMLKKALDEEtrshESQVQEMRQKHTqVVEELTEQLEQFKRAKANLDKNKQALE------------KENAELAGELrVLS 1244
Cdd:TIGR02168 471 EEAEQALDAA----ERELAQLQARLD-SLERLQENLEGFSEGVKALLKNQSGLSgilgvlselisvDEGYEAAIEA-ALG 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1245 QAKQEVEHKKKKLEVQLQELQSKYSDGEKVRAELNDKVHK--------LQNEVESVTGMLNEAEGKAIKLAKDVASLGSQ 1316
Cdd:TIGR02168 545 GRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTeiqgndreILKNIEGFLGVAKDLVKFDPKLRKALSYLLGG 624
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1317 ------LQDTQELLQEETRQKLNVS---------------------------TKLRQLEDERNSLQEQLDEEMEAKQNLE 1363
Cdd:TIGR02168 625 vlvvddLDNALELAKKLRPGYRIVTldgdlvrpggvitggsaktnssilerrREIEELEEKIEELEEKIAELEKALAELR 704
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1364 RHISTLNIQLSDSKKKLQDFASTVELLEEGKKKFQKEIESLTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLV 1443
Cdd:TIGR02168 705 KELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEI 784
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1444 SNLEKKQKKF-DQLLAEEKNISSKYADERDRAEAEAREKETKALSLARALEEALEAKEELERTNKM------LKAEMEDL 1516
Cdd:TIGR02168 785 EELEAQIEQLkEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELsediesLAAEIEEL 864
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1517 VSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKVQFErDLQARDEQNEEKRRQLQR 1596
Cdd:TIGR02168 865 EELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLA-QLELRLEGLEVRIDNLQE 943
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1597 QLHE-YETELEDERKQRALAVAAKKKLEGDLKDLELQADS-------AIKGREEAIKQLRKLQAQMKDFQRELEDARASR 1668
Cdd:TIGR02168 944 RLSEeYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKElgpvnlaAIEEYEELKERYDFLTAQKEDLTEAKETLEEAI 1023
|
....*....
gi 156120901 1669 DEIFATAKE 1677
Cdd:TIGR02168 1024 EEIDREARE 1032
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1207-1933 |
4.27e-29 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 127.48 E-value: 4.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1207 ELTEQLEQFKRAKANLDKNKQALEKEnaELAGELRVLSQAKQEVEHKKKKLEVQLQELQSKYSDGEKVRAELNDKVHKLQ 1286
Cdd:TIGR02168 210 EKAERYKELKAELRELELALLVLRLE--ELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1287 NEVESVTGMLNEAEGKAIKLAKDVASLGSQLQDTQELLQEETRQKLNVSTKLRQLEDERNSLQEQLDEEMEAKQNLERHI 1366
Cdd:TIGR02168 288 KELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAEL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1367 STLNIQLSDSKKKLQDFASTVELLEEGKKKFQKEIESLtqqyeekaaaydklEKTKNRLQQELDDLvvdLDNQRQLVSNL 1446
Cdd:TIGR02168 368 EELESRLEELEEQLETLRSKVAQLELQIASLNNEIERL--------------EARLERLEDRRERL---QQEIEELLKKL 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1447 EKKQKKFDQLLAEEKNISSKYADERDRAEAEAREKETKALSLARALEEALEAKEELERTnkmLKAEMEDLVSSKDDVGKN 1526
Cdd:TIGR02168 431 EEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQA---RLDSLERLQENLEGFSEG 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1527 VHELEKSKRALETQMEEMKTQLEELEDELQATEDAklrLEVNMQALKV---QFERDLQARDEQNEEKRRQLQRQLHEYET 1603
Cdd:TIGR02168 508 VKALLKNQSGLSGILGVLSELISVDEGYEAAIEAA---LGGRLQAVVVenlNAAKKAIAFLKQNELGRVTFLPLDSIKGT 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1604 ELEDERKQRALAVAAKKKLEGDLKDLELQADSAIKGR----------EEAIKQLRKLQAQMKDFQRELEDARAS------ 1667
Cdd:TIGR02168 585 EIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLlggvlvvddlDNALELAKKLRPGYRIVTLDGDLVRPGgvitgg 664
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1668 RDEIFATAKENEKKAKSLEADLMQLQEDLAAAERARKQADLEKDELAEELASsvsgrnaLQDEKRRLEARIAQLEEELEE 1747
Cdd:TIGR02168 665 SAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQ-------LRKELEELSRQISALRKDLAR 737
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1748 EQGNTEAMSERVRKATQQAEQLSNELATERSAAQKNENARQQLERQNKELRSKLQEMEGAVKSkFKSTIAALEAKIAQLE 1827
Cdd:TIGR02168 738 LEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKA-LREALDELRAELTLLN 816
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1828 EQVEQEAREKQATAKALKQKDKKLKEALLQVEDERKMAEQYKEQAEKGNLRVKQLKRQLEEAEEESQRINANRRKLQREL 1907
Cdd:TIGR02168 817 EEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSEL 896
|
730 740
....*....|....*....|....*.
gi 156120901 1908 DEATESNEAMGREVTALKSKLRRGNE 1933
Cdd:TIGR02168 897 EELSEELRELESKRSELRRELEELRE 922
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
829-1623 |
2.83e-28 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 124.78 E-value: 2.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 829 LRNWQWWRLftkvkpLLQVTRQEEEMQAKEDELQKTKERQQKAESELKELEQKHSQLTEEKNLLQEQLQ-AETELYAeae 907
Cdd:TIGR02168 222 LRELELALL------VLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEeLQKELYA--- 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 908 emrvrLAAKKQELEEilhemearleeeedRSQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDDI 987
Cdd:TIGR02168 293 -----LANEISRLEQ--------------QKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 988 LVMDDQNNKLSKERKLLEERISDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLDGEASDL 1067
Cdd:TIGR02168 354 ESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1068 heQIAELQAQIAELKMQLAKKEEEL---QAALGRLDDEMAQKNNALKKIRELEGHIS-------DLQEDLDSERAARNKA 1137
Cdd:TIGR02168 434 --ELKELQAELEELEEELEELQEELerlEEALEELREELEEAEQALDAAERELAQLQarldsleRLQENLEGFSEGVKAL 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1138 EKQKRDLG-------------EELE-ALKTELEDTLDSTATQQELRAKREQEvtMLKKAldEETRSHESQVQEMRQKHTQ 1203
Cdd:TIGR02168 512 LKNQSGLSgilgvlselisvdEGYEaAIEAALGGRLQAVVVENLNAAKKAIA--FLKQN--ELGRVTFLPLDSIKGTEIQ 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1204 VVE-ELTEQLEQFKRAKANLDKNKQALEKENAELAGELRVLSQAKQEVEhkkkklevQLQELQSKYS----DGEKVR--- 1275
Cdd:TIGR02168 588 GNDrEILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALE--------LAKKLRPGYRivtlDGDLVRpgg 659
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1276 ------AELNDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLGSQLQDtqelLQEETRQKLnvsTKLRQLEDERNSLQ 1349
Cdd:TIGR02168 660 vitggsAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEE----LEEELEQLR---KELEELSRQISALR 732
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1350 EQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFASTVELLEEGKKKFQKEIESLTQQYEEKAAAYDKLEKTKNRLQQEL 1429
Cdd:TIGR02168 733 KDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAEL 812
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1430 DDLVVDLDNQRQLVSNLEKKQKKFDQLLAEEKNISSKYADERDRAEAEAREKETKALSLARALEEALEAKEELERTNKML 1509
Cdd:TIGR02168 813 TLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALL 892
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1510 KAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQ-----ATEDAKLRLEVnMQALKVQFERDLQARD 1584
Cdd:TIGR02168 893 RSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDnlqerLSEEYSLTLEE-AEALENKIEDDEEEAR 971
|
810 820 830 840
....*....|....*....|....*....|....*....|....*....
gi 156120901 1585 EQNEEKRRQLQR----------QLHEYETELEDERKQRALAVAAKKKLE 1623
Cdd:TIGR02168 972 RRLKRLENKIKElgpvnlaaieEYEELKERYDFLTAQKEDLTEAKETLE 1020
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
105-712 |
2.43e-27 |
|
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276859 [Multi-domain] Cd Length: 871 Bit Score: 121.39 E-value: 2.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 105 LRERYFSGLIYTYSGLFCV-VVNPYKQL------PIYSEKIIEMYKGKKRHE--MPPHIYAIAD---------------- 159
Cdd:cd14894 7 LTSRFDDDRIYTYINHHTMaVMNPYRLLqtarftSIYDEQVVLTYADTANAEtvLAPHPFAIAKqslvrlffdnehtmpl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 160 ----TAYRSMLQDReDQSILCTGESGAGKTENTKKVIQYLAMVASS--HKGKKDT-SITG-------------------- 212
Cdd:cd14894 87 pstiSSNRSMTEGR-GQSLFLCGESGSGKTELAKDLLKYLVLVAQPalSKGSEETcKVSGstrqpkiklftsstkstiqm 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 213 --------------------------------------------------------------ELEKQL------------ 218
Cdd:cd14894 166 rteeartialleakgvekyeivlldlhperwdemtsvsrskrlpqvhvdglffgfyeklehlEDEEQLrmyfknphaakk 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 219 ----LQANPILEAFGNAKTVKNDNSSRFGKF--IRINFDVTGY---IVGANIETYLLEKSRAIRQA------RDERTFHI 283
Cdd:cd14894 246 lsivLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPWefqICGCHISPFLLEKSRVTSERgresgdQNELNFHI 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 284 FYYLIAGAK-----EKMRNDLLLEGFN--NYTFLSN------GFVPIPAA--QDDEMFNETVEAMAIMGFTEEEQLSILR 348
Cdd:cd14894 326 LYAMVAGVNafpfmRLLAKELHLDGIDcsALTYLGRsdhklaGFVSKEDTwkKDVERWQQVIDGLDELNVSPDEQKTIFK 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 349 VVSSVLQLGNIVFKKERNTDQASMPDN---TAAQKVCHLMGI-NVTDFTRSILTPRIKV--GRDVVQKAQTKEQADFAVE 422
Cdd:cd14894 406 VLSAVLWLGNIELDYREVSGKLVMSSTgalNAPQKVVELLELgSVEKLERMLMTKSVSLqsTSETFEVTLEKGQVNHVRD 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 423 ALAKATYERLFRWILTRVNKAL----------------DKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLqql 486
Cdd:cd14894 486 TLARLLYQLAFNYVVFVMNEATkmsalstdgnkhqmdsNASAPEAVSLLKIVDVFGFEDLTHNSLDQLCINYLSEKL--- 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 487 fnhtmfileqeeYQREGiewNFIDFGLDLQPciELIERPT---------NPPGVLALLDEECWFPKATD----------K 547
Cdd:cd14894 563 ------------YAREE---QVIAVAYSSRP--HLTARDSekdvlfiyeHPLGVFASLEELTILHQSENmnaqqeekrnK 625
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 548 SFVEKLCTEQGSHPKfQKPKQLKDKTE----------FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFMAD 617
Cdd:cd14894 626 LFVRNIYDRNSSRLP-EPPRVLSNAKRhtpvllnvlpFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNSSHFCR 704
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 618 LWKDVDRivgLDQMAKMTESSLPSASKTKKGMFRTVGQlYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLE 697
Cdd:cd14894 705 MLNESSQ---LGWSPNTNRSMLGSAESRLSGTKSFVGQ-FRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQ 780
|
810
....*....|....*
gi 156120901 698 QLRCNGVLEGIRICR 712
Cdd:cd14894 781 QCRSQRLIRQMEICR 795
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1044-1740 |
1.49e-26 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 118.89 E-value: 1.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1044 KKEEKSRQELEKLKRKLDgEASDLheqIAELQAQIAELKMQ--LAKKEEELQAALGRLDDEMAqknnaLKKIRELEGHIS 1121
Cdd:COG1196 172 ERKEEAERKLEATEENLE-RLEDI---LGELERQLEPLERQaeKAERYRELKEELKELEAELL-----LLKLRELEAELE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1122 DLQEDLDSERAARNKAEKQKRDLGEELEALKTELEdtldstATQQELRAKREQEvtmlkkaldeetrshesqvqemrQKH 1201
Cdd:COG1196 243 ELEAELEELEAELEELEAELAELEAELEELRLELE------ELELELEEAQAEE-----------------------YEL 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1202 TQVVEELTEQLEQFKRAKANLDKNKQALEKENAELAGELRVLSQAKQEVEHKKKKLEVQLQELQSKYSDGEKVRAELNDK 1281
Cdd:COG1196 294 LAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1282 VHKLQNEVESVTGMLNEAEGKAIKLAKDVASLGSQLQDTQELLQEETRQKLNVSTKLRQLEDERNSLQEQLDEEMEAKQN 1361
Cdd:COG1196 374 LAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1362 LERHISTLNIQLSDSKKKLQDFASTVELLEEGKKKFQKEIESLTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLdnqrq 1441
Cdd:COG1196 454 LEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAV----- 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1442 lvsnLEKKQKKFDQLLAEEKNISSKYADERDRAEAEAREKETKALSLARALEEALeakeelertNKMLKAEMEDLVSSKD 1521
Cdd:COG1196 529 ----LIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPL---------DKIRARAALAAALARG 595
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1522 DVGKNVHELEKSKRALETQMEEMKTQLEElEDELQATEDAKLRLEVNMQALKVQFERDLQARDEQNEEKRRQLQRQLHEY 1601
Cdd:COG1196 596 AIGAAVDLVASDLREADARYYVLGDTLLG-RTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAAL 674
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1602 ETELEDERKQRALAVAAKKKLEGDLKDLELQADSAIKGREEAIKQLRKLQAQMKDFQRELEDARASRDEIFATAKENEKK 1681
Cdd:COG1196 675 LEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALE 754
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156120901 1682 AKSLEADLMQLQEDLAAAERARKQ-------ADLEKDELAEELASSVSGRNALQDEKRRLEARIAQ 1740
Cdd:COG1196 755 ELPEPPDLEELERELERLEREIEAlgpvnllAIEEYEELEERYDFLSEQREDLEEARETLEEAIEE 820
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
998-1896 |
2.71e-25 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 115.17 E-value: 2.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 998 SKERKLLEERISdlttNLAE-EEEKAKNLTKLK------NKHESMISELEVRLKKEEKSRQELEK----LKRKLDGEASD 1066
Cdd:TIGR02169 152 PVERRKIIDEIA----GVAEfDRKKEKALEELEeveeniERLDLIIDEKRQQLERLRREREKAERyqalLKEKREYEGYE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1067 LHEQIAELQAQIAELKMQLAKKEEELQAALGRLDDEMAQKNNALKKIRELEGHISDLQEdldsERAARNKAEKqkrdlgE 1146
Cdd:TIGR02169 228 LLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGE----EEQLRVKEKI------G 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1147 ELEALKTELEDTLDSTATQQELRAKREQEVTMLKKALDEETRSHESQVQEMRQKHTQVVEELTEqleqfkrAKANLDKNK 1226
Cdd:TIGR02169 298 ELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAE-------LKEELEDLR 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1227 QALEKENAELAGELRVLSQAKQEVEHKKKKLEVQLQELQSKYSDGEKVRAELNDkvhkLQNEVESVTGMLNEAEGKAIKL 1306
Cdd:TIGR02169 371 AELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELAD----LNAAIAGIEAKINELEEEKEDK 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1307 AKDVASLGSQLQDTQELLQEETRQKLNVSTKLRQLEDERNSLQEQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFAST 1386
Cdd:TIGR02169 447 ALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGT 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1387 VELLEEGKKKFQKEIESL-----------TQQYEEKAAAYDKLEKTK-------NRLQQELDDL--------------VV 1434
Cdd:TIGR02169 527 VAQLGSVGERYATAIEVAagnrlnnvvveDDAVAKEAIELLKRRKAGratflplNKMRDERRDLsilsedgvigfavdLV 606
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1435 DLDNQRQ-----------LVSNLEKKQKKFDQL--------LAEEKNISSKYADERDRAEAEAREKETKALSLARALEEA 1495
Cdd:TIGR02169 607 EFDPKYEpafkyvfgdtlVVEDIEAARRLMGKYrmvtlegeLFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGL 686
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1496 LEAKEELERTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQAL--- 1572
Cdd:TIGR02169 687 KRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELear 766
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1573 KVQFERDLQA-RDEQNEEKRRQLQRQLHEYETELEDERKQRALAVAAKKKLEGDLKDLELQADSAIKGREEAIKQLRKLQ 1651
Cdd:TIGR02169 767 IEELEEDLHKlEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLK 846
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1652 AQMKDFQRELEDARASRDEIFATAKENEKKAKSLEADLMQLQEdlaaaERARKQADLEkdelaeelassvsgrnALQDEK 1731
Cdd:TIGR02169 847 EQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKK-----ERDELEAQLR----------------ELERKI 905
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1732 RRLEARIaqleeeleeeqgnteamservrkatQQAEQLSNELATERSAAQKNenarqqlerqnkelrsklqemegavksk 1811
Cdd:TIGR02169 906 EELEAQI-------------------------EKKRKRLSELKAKLEALEEE---------------------------- 932
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1812 fkstIAALEAKIAQLEEQVEQEAREKQatakaLKQKDKKLKEALLQVEDERKMAEQYKEQAEKgnlRVKQLKRQLEEAEE 1891
Cdd:TIGR02169 933 ----LSEIEDPKGEDEEIPEEELSLED-----VQAELQRVEEEIRALEPVNMLAIQEYEEVLK---RLDELKEKRAKLEE 1000
|
....*
gi 156120901 1892 ESQRI 1896
Cdd:TIGR02169 1001 ERKAI 1005
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1113-1918 |
3.03e-25 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 114.78 E-value: 3.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1113 IRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALKTELEDTLDSTATQQELRAKREQEVTMLKKALDEETRSHES 1192
Cdd:TIGR02169 165 VAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1193 QVQEMRQkhtqVVEELTEQLEQF-KRAKANLDKNKQALEKENAELAGELRVLSQAKQEVEHKKKKLEVQLQELQSKYSDG 1271
Cdd:TIGR02169 245 QLASLEE----ELEKLTEEISELeKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDA 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1272 EKVRAELNDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLGSQLQDTQELLQE------ETRQKL-NVSTKLRQLEDE 1344
Cdd:TIGR02169 321 EERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEvdkefaETRDELkDYREKLEKLKRE 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1345 RNSLQEQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFASTVELLeegkkkfQKEIESLTQQYEEKAAAYDKLEKTKNR 1424
Cdd:TIGR02169 401 INELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDK-------ALEIKKQEWKLEQLAADLSKYEQELYD 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1425 LQQELDdlvvdldnqrQLVSNLEKKQKKFDQLLAEeKNISSKYADERDRAEAEAREKETKALSLARALEEALEAKEELER 1504
Cdd:TIGR02169 474 LKEEYD----------RVEKELSKLQRELAEAEAQ-ARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIE 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1505 TnkMLKAEMEDLVSSKDDVGKNVHELEKSK---RALETQMEEMKTQLEELEdelQATEDAKLRLEVNMQALKVQFE---- 1577
Cdd:TIGR02169 543 V--AAGNRLNNVVVEDDAVAKEAIELLKRRkagRATFLPLNKMRDERRDLS---ILSEDGVIGFAVDLVEFDPKYEpafk 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1578 ---------RDLQARDEQNEEKR-----------------------------RQLQRQLHEYETELEDERKQRALAVAAK 1619
Cdd:TIGR02169 618 yvfgdtlvvEDIEAARRLMGKYRmvtlegelfeksgamtggsraprggilfsRSEPAELQRLRERLEGLKRELSSLQSEL 697
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1620 KKLEGDLKDLELQADSAIKGREEAIKQLRKLQAQMKDFQRELEDARASRDEIFATAKENEKKAKSLEADLMQLQEDLAAA 1699
Cdd:TIGR02169 698 RRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKL 777
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1700 ERArkQADLEKDELAEELASSVSGRNALQDEKRRLEARIAQleeeleeeqgnTEAMSERVRKATQQAEQLSNELATERSA 1779
Cdd:TIGR02169 778 EEA--LNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLRE-----------IEQKLNRLTLEKEYLEKEIQELQEQRID 844
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1780 AQKNENARQQlerQNKELRSKLQEMEgavkskfkSTIAALEAKIAQLEEQVEQEAREKQATAKALKQKDKKLKEALLQVE 1859
Cdd:TIGR02169 845 LKEQIKSIEK---EIENLNGKKEELE--------EELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIE 913
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*....
gi 156120901 1860 DERKMAEQYKEQAEKGNLRVKQLKRQLEEAEEESQRInANRRKLQRELDEATESNEAMG 1918
Cdd:TIGR02169 914 KKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEE-LSLEDVQAELQRVEEEIRALE 971
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1222-1913 |
3.19e-25 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 114.65 E-value: 3.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1222 LDKNKQALEKEnAELAGELRVLSQAKQEVEHKKKKLEVQLQELQskysdgekvRAELNDKVHKLQNEVESVTGMLNEAEG 1301
Cdd:COG1196 198 LERQLEPLERQ-AEKAERYRELKEELKELEAELLLLKLRELEAE---------LEELEAELEELEAELEELEAELAELEA 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1302 KAIKLAKDVASLGSQLQDTQELLQEETRQKLNVSTKLRQLEDERNSLQEQLDEEMEAKQNLERHISTLNIQLsdskkklq 1381
Cdd:COG1196 268 ELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL-------- 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1382 dfastvELLEEGKKKFQKEIESLTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQKKFDQLLAEEK 1461
Cdd:COG1196 340 ------EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1462 NISSKYADERDRAEAEAREKETKALSLARALEEALEAKEELERtnkmlkaemedlvsskddvgknvhELEKSKRALETQM 1541
Cdd:COG1196 414 ERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE------------------------EEEALLELLAELL 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1542 EEMKTQLEELEDELQATEDAKLRLEVNMQALKVQFERDLQARDEQNEEKRRQLQRQLHEyetELEDERKQRALAVAAkkk 1621
Cdd:COG1196 470 EEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAV---LIGVEAAYEAALEAA--- 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1622 LEGDLKDLELQADSAIKGREEAIKQlrklqaqmkdfqreledARASRDEIFATAKENEKKAKSLEADLMQLQEDLAAAER 1701
Cdd:COG1196 544 LAAALQNIVVEDDEVAAAAIEYLKA-----------------AKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVAS 606
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1702 ARKQADLEKDELAEELASSVSGRNALQDEKRRLEARIAQLEEELEEEQGNTEAMSERVRKATQQAEQLSNELATERSAAQ 1781
Cdd:COG1196 607 DLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAE 686
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1782 KNENARQQLERQNKELRSKLQEmegavkskfkstIAALEAKIAQLEEQVEQEAREKQATAKALKQKDKKLKEALLQVEDE 1861
Cdd:COG1196 687 RLAEEELELEEALLAEEEEERE------------LAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALE 754
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 156120901 1862 RKMAEQYKEQAEKgnlRVKQLKRQLEE-------AEEESQRINANRRKLQRELDEATES 1913
Cdd:COG1196 755 ELPEPPDLEELER---ELERLEREIEAlgpvnllAIEEYEELEERYDFLSEQREDLEEA 810
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1326-1918 |
5.55e-25 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 113.88 E-value: 5.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1326 EETRQKL-NVSTKLRQLEDERNSLQEQLDE-EMEAKQnLERHistLNIQLSDSKKKLQDFASTVELLEEGKKKFQKEIES 1403
Cdd:COG1196 175 EEAERKLeATEENLERLEDILGELERQLEPlERQAEK-AERY---RELKEELKELEAELLLLKLRELEAELEELEAELEE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1404 LTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQKKFDQLLAEEKnisskyaDERDRAEAEAREKET 1483
Cdd:COG1196 251 LEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE-------ERRRELEERLEELEE 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1484 KALSLARALEEALEAKEELERTNKMLKAEMEDLVsskddvgKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDAKL 1563
Cdd:COG1196 324 ELAELEEELEELEEELEELEEELEEAEEELEEAE-------AELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1564 RLEVNMQALKVQfERDLQARDEQNEEKRRQLQRQLHEYETELEDERKQRALAVAAKKKLEGDLKDLELQADSAIKGREEA 1643
Cdd:COG1196 397 ELAAQLEELEEA-EEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALL 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1644 IKQLRKLQAQMKDFQRE---LEDARASRDEIFATAKENEKKAKS---------LEADLMQLQEDLAAAERARKQADLEKD 1711
Cdd:COG1196 476 EAALAELLEELAEAAARlllLLEAEADYEGFLEGVKAALLLAGLrglagavavLIGVEAAYEAALEAALAAALQNIVVED 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1712 E-----LAEELASSVSGRNALQDEKRRLEARIAQLEEELEEEQGNTEAMSERVRKATQQAEQLSNELATERSAAQKNENA 1786
Cdd:COG1196 556 DevaaaAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAA 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1787 RQQLERQNKELRSKLQEMEGAV---------KSKFKSTIAALEAKIAQLEEQVEQEAREKQATAKALKQKDKKLKEALLQ 1857
Cdd:COG1196 636 LRRAVTLAGRLREVTLEGEGGSaggsltggsRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEE 715
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 156120901 1858 VEDERKMAEQYKEQAEKGNLRVKQLKRQ----LEEAEEESQRINANRRKLQRELDEATESNEAMG 1918
Cdd:COG1196 716 RLEEELEEEALEEQLEAEREELLEELLEeeelLEEEALEELPEPPDLEELERELERLEREIEALG 780
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
851-1709 |
1.57e-24 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 112.47 E-value: 1.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 851 EEEMQAKEDELQKTKERQQKAESELKELEQKHSQLTEEKN-------LLQEQLQAE-TELYAEAEEMRVRLAAKKQELEE 922
Cdd:TIGR02169 169 DRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREkaeryqaLLKEKREYEgYELLKEKEALERQKEAIERQLAS 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 923 ILHEMEARLEEEEDRSQQLQAERKKMAQqMLDLEEQLEEEEAARQKLQLEKVTAEakIKKLEDDILVMDDQNNKLSKERK 1002
Cdd:TIGR02169 249 LEEELEKLTEEISELEKRLEEIEQLLEE-LNKKIKDLGEEEQLRVKEKIGELEAE--IASLERSIAEKERELEDAEERLA 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1003 LLEERISDLttnLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLDG---EASDLHEQIAELQAQIA 1079
Cdd:TIGR02169 326 KLEAEIDKL---LAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAEtrdELKDYREKLEKLKREIN 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1080 ELKMQLAKKEEELQAALGRLDDEMAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALKTELEDtl 1159
Cdd:TIGR02169 403 ELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDR-- 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1160 dstaTQQELRAKREQEVTMLKKALDEETRSHESQ-VQEMRQKHTQVVEELTEQLEQFKRAKA-----------------N 1221
Cdd:TIGR02169 481 ----VEKELSKLQRELAEAEAQARASEERVRGGRaVEEVLKASIQGVHGTVAQLGSVGERYAtaievaagnrlnnvvveD 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1222 LDKNKQALEKENAELAGELRVLSQAKQEVEHKKKKL---------EVQLQELQSKYSD------GEKVRAELNDKVHKLQ 1286
Cdd:TIGR02169 557 DAVAKEAIELLKRRKAGRATFLPLNKMRDERRDLSIlsedgvigfAVDLVEFDPKYEPafkyvfGDTLVVEDIEAARRLM 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1287 NEVESVT--GMLNEAEGkaiklakdVASLGSQLQDTQELLQEETRQKL-NVSTKLRQLEDERNSLQEQLDEemeakqnLE 1363
Cdd:TIGR02169 637 GKYRMVTleGELFEKSG--------AMTGGSRAPRGGILFSRSEPAELqRLRERLEGLKRELSSLQSELRR-------IE 701
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1364 RHISTLNIQLSDSKKKLQDFASTVELLEEgkkkfqkEIESLTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLV 1443
Cdd:TIGR02169 702 NRLDELSQELSDASRKIGEIEKEIEQLEQ-------EEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDL 774
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1444 SNLEKKQKKFDQLLAEEKniSSKYADERDRAEAEAREKETKALSLARALEEALEAKEELERTNKMLKAEMEDLVSSKDDV 1523
Cdd:TIGR02169 775 HKLEEALNDLEARLSHSR--IPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSI 852
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1524 GKNVHELEKSKRALETQMEEMKTQLEELEDELQatedaklrlevnmqalkvqferDLQARDEQNEEKRRQLQRQLHEYET 1603
Cdd:TIGR02169 853 EKEIENLNGKKEELEEELEELEAALRDLESRLG----------------------DLKKERDELEAQLRELERKIEELEA 910
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1604 ELEDERKQRALAVAAKKKLEGDLKDLElQADSAIKGREEAIKQLRKLQAQMKDFQRELED-------ARASRDEIFATAK 1676
Cdd:TIGR02169 911 QIEKKRKRLSELKAKLEALEEELSEIE-DPKGEDEEIPEEELSLEDVQAELQRVEEEIRAlepvnmlAIQEYEEVLKRLD 989
|
890 900 910
....*....|....*....|....*....|...
gi 156120901 1677 ENEKKAKSLEADLMQLQEDLAAAERARKQADLE 1709
Cdd:TIGR02169 990 ELKEKRAKLEEERKAILERIEEYEKKKREVFME 1022
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
966-1740 |
8.97e-24 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 110.16 E-value: 8.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 966 RQKLQLEKVTAEaKIKKLEDDIlvMDDQNNKLSKERKLLEERISDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKK 1045
Cdd:TIGR02169 200 LERLRREREKAE-RYQALLKEK--REYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1046 EEKsrqeleKLKRKLDGEASDLHEQIAELQAQIAELKMQLAKKEEELQAALGRLDDEMAQKNNALKKIRELEGHISDLQE 1125
Cdd:TIGR02169 277 LNK------KIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERK 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1126 DLDSERAARNKAEKQKRDLGEELEALKTELEDTLDSTAtqqelraKREQEVTMLKKALDEETRSHESQVQEMRQKHTQVv 1205
Cdd:TIGR02169 351 RRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELK-------DYREKLEKLKREINELKRELDRLQEELQRLSEEL- 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1206 EELTEQLEQFKRAKANLDKNKQALEKENAELAGELRVLSQAKQEVEHKKKKLEVQLQELQSKYSDGEKVRAELNDKVHKL 1285
Cdd:TIGR02169 423 ADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARAS 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1286 QNEVE---SVTGMLNEAEGKAIKLAKDVASLGSQLQ--------------------DTQELLQEETRQKLNVST-----K 1337
Cdd:TIGR02169 503 EERVRggrAVEEVLKASIQGVHGTVAQLGSVGERYAtaievaagnrlnnvvveddaVAKEAIELLKRRKAGRATflplnK 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1338 LRQLEDERNSLQEQ--------LDEEMEAKQNLERHI--STLNIQLSDSKKKLQDFASTV----ELLEE-----GKKKFQ 1398
Cdd:TIGR02169 583 MRDERRDLSILSEDgvigfavdLVEFDPKYEPAFKYVfgDTLVVEDIEAARRLMGKYRMVtlegELFEKsgamtGGSRAP 662
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1399 KEIESLTQQYEEK----AAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKK----QKKFDQLLAEEKNISSKYADE 1470
Cdd:TIGR02169 663 RGGILFSRSEPAElqrlRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKigeiEKEIEQLEQEEEKLKERLEEL 742
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1471 RDRAEAEAREKETKALSLARALEEALEAKEELERtnkmLKAEMEDLVSSKDDVGknVHELEKSKRALETQMEEMKTQLEE 1550
Cdd:TIGR02169 743 EEDLSSLEQEIENVKSELKELEARIEELEEDLHK----LEEALNDLEARLSHSR--IPEIQAELSKLEEEVSRIEARLRE 816
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1551 LEDELQATEDAKLRLEVNMQALKVQfERDLQARDEQNEEKRRQLQRQLHEYETELEDERkqralavAAKKKLEGDLKDLE 1630
Cdd:TIGR02169 817 IEQKLNRLTLEKEYLEKEIQELQEQ-RIDLKEQIKSIEKEIENLNGKKEELEEELEELE-------AALRDLESRLGDLK 888
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1631 lqadsaiKGREEAIKQLRKLQAQMKDFQRELEDARASRDEIFATAKENEKKAKSLEADLMQLQEDLAA--------AERA 1702
Cdd:TIGR02169 889 -------KERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEelsledvqAELQ 961
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|
gi 156120901 1703 RKQADLEK------------DELAEELASSVSGRNALQDEKRRLEARIAQ 1740
Cdd:TIGR02169 962 RVEEEIRAlepvnmlaiqeyEEVLKRLDELKEKRAKLEEERKAILERIEE 1011
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
807-1432 |
3.15e-23 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 108.10 E-value: 3.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 807 AKRQQQLTAMKVIQRNCAAYLKLRNWQwwrlftkvkplLQVTRQEEEMQAKEDELQKTKERQQKAESELKELEQKHSQLT 886
Cdd:COG1196 212 AERYRELKEELKELEAELLLLKLRELE-----------AELEELEAELEELEAELEELEAELAELEAELEELRLELEELE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 887 EEKNLLQEQLQAETELYAEAEEMRVRLAAKKQELEEILhemearlEEEEDRSQQLQAERKKMAQQMLDLEEQLEEEEAAR 966
Cdd:COG1196 281 LELEEAQAEEYELLAELARLEQDIARLEERRRELEERL-------EELEEELAELEEELEELEEELEELEEELEEAEEEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 967 QKLQLEKVTAEAKIKKLEDDILVMDDQNNKLSKERKLLEERISDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKE 1046
Cdd:COG1196 354 EEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAEL 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1047 EKSRQELEKLKRKLDGEASDLHEQIAELQAQIAELKMQLAKKEEELQAALGRLDDEMAQKNNALKKIRELEGHISDLQED 1126
Cdd:COG1196 434 EEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAA 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1127 LDSERAARN---------KAEKQKRDLGEELEALKTELEDTLDSTATQQELRAKREQEVTMLKKALDEETRSHESQVQEM 1197
Cdd:COG1196 514 LLLAGLRGLagavavligVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALA 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1198 RQKHTQVVEELTEQLEQFKRAKANLDKNKQALEKENAELAGELRVLSQAKQEVEHKKKKLEVQLQELQSKYSDGEKVRAE 1277
Cdd:COG1196 594 RGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAA 673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1278 LNDKVHKLQNEVEsvtgmlnEAEGKAIKLAKDVASLGSQLQDTQELLQEETRQKLNVSTKLRQLEDERNSLQEQLDEEME 1357
Cdd:COG1196 674 LLEAEAELEELAE-------RLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEE 746
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1358 AKQNLERHISTLNIQLSDSKKKLqdfastvelleegkKKFQKEIESL-------TQQYEEKAAAYDKLEKTKNRLQQELD 1430
Cdd:COG1196 747 LLEEEALEELPEPPDLEELEREL--------------ERLEREIEALgpvnllaIEEYEELEERYDFLSEQREDLEEARE 812
|
..
gi 156120901 1431 DL 1432
Cdd:COG1196 813 TL 814
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1509-1964 |
8.30e-23 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 106.56 E-value: 8.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1509 LKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKVQFERdLQARDEQNE 1588
Cdd:COG1196 230 LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELAR-LEQDIARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1589 EKRRQLQRQLHEYETELEDERKQRALAVAAKKKLEGDLKDLELQADSAIKGREEAIKQLRKLQAQMKDFQRELEDARASR 1668
Cdd:COG1196 309 ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1669 DEIFATAKENEKKAKSLEADLMQLQEDLAAAERARKQADLEKDELAEELASSVSGRNALQDEKRRLEARIAQLEEELEEE 1748
Cdd:COG1196 389 LEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1749 QGNTEAMSERVRKATQQAEQLSNELATERSAAQKNEN-----ARQQLERQNKELRSKLQEMEGAVKSKFKSTIAALEAKI 1823
Cdd:COG1196 469 LEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGflegvKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAAL 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1824 AQLeeQVEQEAREKQATAKALKQKDKKLKEALLQVEDERKMAEQYKEQAEKGNLRVkQLKRQLEEAEEESQRINANRRKL 1903
Cdd:COG1196 549 QNI--VVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVD-LVASDLREADARYYVLGDTLLGR 625
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 156120901 1904 QRELDEATESNEAMGREVTALKSKLRRGNETSFVPTRRSGGRRVIENADGSEEEMDARDAD 1964
Cdd:COG1196 626 TLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAE 686
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
990-1573 |
4.37e-22 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 103.95 E-value: 4.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 990 MDDQNNKLSKERKLLEERISDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLDGEASDLHE 1069
Cdd:TIGR04523 38 LEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1070 QIAELQAQIAELKMQLAKKEEELQAALGRLDDEMAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELE 1149
Cdd:TIGR04523 118 QKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1150 ALKTELEDTLDSTATQQELRAK---REQEVTMLKKALDEETRSHESQVQEMRQKHTQ---VVEELTEQLEQFKRAKANLD 1223
Cdd:TIGR04523 198 KLELLLSNLKKKIQKNKSLESQiseLKKQNNQLKDNIEKKQQEINEKTTEISNTQTQlnqLKDEQNKIKKQLSEKQKELE 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1224 KNKQA---LEKENAELAGELRVLSQAKQEVEHKK-----KKLEVQLQELQSKYSDGEKVRAELNDKVHKLQNEVESVTGM 1295
Cdd:TIGR04523 278 QNNKKikeLEKQLNQLKSEISDLNNQKEQDWNKElkselKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESE 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1296 LNEAEGKAIKLAKDVASLGSQLQDTQELLQEETRQKLNVSTKLRQLEDERNSLQEQLDEEMEAKQNLERHISTLNIQLSD 1375
Cdd:TIGR04523 358 NSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIK 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1376 SKKKLQDFASTVELLEEGKKKFQKEIESLTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQKKFDQ 1455
Cdd:TIGR04523 438 NNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTK 517
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1456 LLAEEKNISSKYADERDRAEAEAREKETKALSLARALEEALEAKEELERTNKM--LKAEMEDLVSSKDDVGKNVHELEKS 1533
Cdd:TIGR04523 518 KISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIeeLKQTQKSLKKKQEEKQELIDQKEKE 597
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 156120901 1534 KRALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALK 1573
Cdd:TIGR04523 598 KKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIK 637
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
865-1482 |
8.52e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 103.48 E-value: 8.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 865 KERQQKAESELKELEQKhsqLTEEKNLLQE---QLQaetELYAEAEemrvrLAAKKQELEEILHEMEARLEEEEDRSQQL 941
Cdd:COG1196 171 KERKEEAERKLEATEEN---LERLEDILGElerQLE---PLERQAE-----KAERYRELKEELKELEAELLLLKLRELEA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 942 QAERKKMAQQmldleeqleEEEAARQKLQLEKVTAEAKIKKLEDDILVMDDQNNKLSKERKLLEERISDLTTNLAEEEEK 1021
Cdd:COG1196 240 ELEELEAELE---------ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1022 AKNLtklknkhESMISELEVRLKKEEKSRQELEKLKRKLDGEASDLHEQIAELQAQIAELKMQLAKKEEELQAALGRLDD 1101
Cdd:COG1196 311 RREL-------EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1102 EMAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALKTELEDTLDSTATQQELRAKreqevtmlkk 1181
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE---------- 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1182 aLDEETRSHESQVQEMRQKHTQVVEELTEQLEQFKRAKANLDKNKQALEKENAELAGELRVLSQAKQEVEHKKKKLEVQL 1261
Cdd:COG1196 454 -LEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGV 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1262 QELQSKYSDGEKVRAELNDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLGSQLQDTQELLQEETRQKLNVSTKLRQL 1341
Cdd:COG1196 533 EAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREAD 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1342 EDERNSLQEQLDEEMEAKQN------LERHISTLNIQLSDSKKKLQDFASTVELLEEGKKKFQKEIESLTQQYEEKAAAY 1415
Cdd:COG1196 613 ARYYVLGDTLLGRTLVAARLeaalrrAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEE 692
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156120901 1416 DKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQKKFDQLLAEEKNISSKYADERDRAEAEAREKE 1482
Cdd:COG1196 693 LELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEP 759
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1272-1941 |
2.54e-21 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 102.06 E-value: 2.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1272 EKVRAELNDKVHKLQNEVESVTgmlneaEGKAIKLAKDVASLGSQLQDtqelLQEETRQKLNVSTKLRQLEDERNSLQEQ 1351
Cdd:TIGR02168 192 EDILNELERQLKSLERQAEKAE------RYKELKAELRELELALLVLR----LEELREELEELQEELKEAEEELEELTAE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1352 LDEEMEAKQNLERHISTLNIQLSDSKKKLQDFASTVELLEEGKKKFQKEIESLTQQYEEKAAAYDKLEKTKNRLQQELDD 1431
Cdd:TIGR02168 262 LQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1432 LVVDLDNQRQLVSNLEKKQKKFDQLLAEEKNISSKYADERDRAEAEAREKETKALSLARALEEaleakeelertnkmLKA 1511
Cdd:TIGR02168 342 LEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIER--------------LEA 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1512 EMEDLVSSKDDVGKNVHELEKskRALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKVQFERDLQARDeQNEEKR 1591
Cdd:TIGR02168 408 RLERLEDRRERLQQEIEELLK--KLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALD-AAEREL 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1592 RQLQRQLHEYETELEDERK--QRALAVAAKKKLEGDLKDLELQADSAIKGREEAIKQLrkLQAQMKDFqrELEDARASRD 1669
Cdd:TIGR02168 485 AQLQARLDSLERLQENLEGfsEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAA--LGGRLQAV--VVENLNAAKK 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1670 EIFATAKENEKKAKSLEADLMQLQEDLAAAERARKQADLEKDELAEELASSVSGRNALQDEKRRLeaRIAQLEEELEEEQ 1749
Cdd:TIGR02168 561 AIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGV--LVVDDLDNALELA 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1750 GNTEAmseRVRKATQQAEQLSNELATERSAAQKNeNARQQLERQNKELRSKLQEMEGAVKSKfKSTIAALEAKIAQLEEQ 1829
Cdd:TIGR02168 639 KKLRP---GYRIVTLDGDLVRPGGVITGGSAKTN-SSILERRREIEELEEKIEELEEKIAEL-EKALAELRKELEELEEE 713
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1830 VEQEAREKQATAKALKQKDKKLKEALLQVEDERKMAEQYKEQAEKGNLRVKQLKRQLEEAEEESQRINANRRKLQRELDE 1909
Cdd:TIGR02168 714 LEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQ 793
|
650 660 670
....*....|....*....|....*....|..
gi 156120901 1910 ATESNEAMGREVTALKSKLRRGNETSFVPTRR 1941
Cdd:TIGR02168 794 LKEELKALREALDELRAELTLLNEEAANLRER 825
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1326-1933 |
2.43e-20 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 98.98 E-value: 2.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1326 EETRQKLN-VSTKLRQLEDERNSLQEQLD-------------EEMEAKQNLERHISTLniQLSDSKKKLQDFASTVELLE 1391
Cdd:TIGR02168 175 KETERKLErTRENLDRLEDILNELERQLKslerqaekaerykELKAELRELELALLVL--RLEELREELEELQEELKEAE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1392 EGKKKFQKEIESLTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDN-------QRQLVSNLEKKQKKFDQLLAEEKNIS 1464
Cdd:TIGR02168 253 EELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRleqqkqiLRERLANLERQLEELEAQLEELESKL 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1465 SKYADERDRAEAEAREKETKALSLARALEEALEAKEELERTNKMLKAEMEDLVSskddvgkNVHELEKSKRALETQMEEM 1544
Cdd:TIGR02168 333 DELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRS-------KVAQLELQIASLNNEIERL 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1545 KTQLEELEDELQATEDAKLRLEVNMQALKVQferDLQARDEQNEEKRRQLQRQLHEYETELEDERKQRALAVAAKKKLEG 1624
Cdd:TIGR02168 406 EARLERLEDRRERLQQEIEELLKKLEEAELK---ELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAER 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1625 DLKDLELQADS------AIKGREEAIKQLRKLQAQMKDFQREL---------------------------EDARASRDEI 1671
Cdd:TIGR02168 483 ELAQLQARLDSlerlqeNLEGFSEGVKALLKNQSGLSGILGVLselisvdegyeaaieaalggrlqavvvENLNAAKKAI 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1672 FATAKENEKKAKSLEADLMQLQEDLAAAERARKQADLEKDELAEELASSVSGRNALQD---------------EKRRLEA 1736
Cdd:TIGR02168 563 AFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYllggvlvvddldnalELAKKLR 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1737 R-----------------IAQLEEELEEEQGNTEAMSERVRKATQQAEQLSNELATERSAAqknENARQQLERQNKELRS 1799
Cdd:TIGR02168 643 PgyrivtldgdlvrpggvITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAEL---RKELEELEEELEQLRK 719
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1800 KLQEMEGAVKSKFKStIAALEAKIAQLEEQVEQEARE-KQATAKALKQKDKKLKEALLQVEDERKMAEQyKEQAEKGNLR 1878
Cdd:TIGR02168 720 ELEELSRQISALRKD-LARLEAEVEQLEERIAQLSKElTELEAEIEELEERLEEAEEELAEAEAEIEEL-EAQIEQLKEE 797
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 156120901 1879 VKQLKRQLEEAEEESQRINANRRKLQRELDEATESNEAMGREVTALKSKLRRGNE 1933
Cdd:TIGR02168 798 LKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSE 852
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1172-1924 |
3.75e-20 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 98.67 E-value: 3.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1172 REQEVTMLKKALDEETRSHE-SQVQEMRQKHTQVVEELTEQLEQFKRAKaNLDKNKQALEKENAELAGELRVLSQAKQeV 1250
Cdd:PTZ00121 1077 KDFDFDAKEDNRADEATEEAfGKAEEAKKTETGKAEEARKAEEAKKKAE-DARKAEEARKAEDARKAEEARKAEDAKR-V 1154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1251 EHKKKKLEVQLQELQSKYSDGEKVraelndkvhklqnevesvtgmlnEAEGKAIKLAKdvaslGSQLQDTQELLQ-EETR 1329
Cdd:PTZ00121 1155 EIARKAEDARKAEEARKAEDAKKA-----------------------EAARKAEEVRK-----AEELRKAEDARKaEAAR 1206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1330 QKLNV--STKLRQLEDERNSLQEQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFASTVELLEEGKKKFQKEIESLtQQ 1407
Cdd:PTZ00121 1207 KAEEErkAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADEL-KK 1285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1408 YEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQKKFDQllAEEKNISSKYADERDRAEAEAREKETKALS 1487
Cdd:PTZ00121 1286 AEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADA--AKKKAEEAKKAAEAAKAEAEAAADEAEAAE 1363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1488 LARALEEALEAKEELERTNKMLKAEMedlVSSKDDVGKNVHELEKSKRALETQMEEMKT--QLEELEDELQATEDAKLRL 1565
Cdd:PTZ00121 1364 EKAEAAEKKKEEAKKKADAAKKKAEE---KKKADEAKKKAEEDKKKADELKKAAAAKKKadEAKKKAEEKKKADEAKKKA 1440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1566 EVNMQALKVQfERDLQARDEQNEEKRRQLQRQLHEYETELEDERKqralAVAAKKKLEGDLKdlelQADSAIKGREEAIK 1645
Cdd:PTZ00121 1441 EEAKKADEAK-KKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKK----ADEAKKKAEEAKK----KADEAKKAAEAKKK 1511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1646 QLRKLQAQMKDFQRELEDARASRdeifaTAKENEKKAKSLEADLMQLQEDLAAAERARKQADLEKDELAEELASsvsgRN 1725
Cdd:PTZ00121 1512 ADEAKKAEEAKKADEAKKAEEAK-----KADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMAL----RK 1582
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1726 AlQDEKRRLEARIAQLEEELEEEQGNTEAMSERVRKATQQAEQLSNElATERSAAQKNENARQQLERQNKELRSklQEME 1805
Cdd:PTZ00121 1583 A-EEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA-EEEKKKVEQLKKKEAEEKKKAEELKK--AEEE 1658
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1806 GAVKSKFKSTIAALEAKIAQLEEQVEQEAREKQATAKALKQKDKKLKEALLQVEDERKMAEQYKEQAEKGNLRVKQLKRQ 1885
Cdd:PTZ00121 1659 NKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKE 1738
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 156120901 1886 LEEAE---EESQRINANRRKLQRELDEATESNEAMGREVTAL 1924
Cdd:PTZ00121 1739 AEEDKkkaEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAV 1780
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
851-1711 |
4.09e-20 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 98.12 E-value: 4.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 851 EEEMQAKEDELQKTKERQQKAESELKELEQKHSQLTEEKNLLQEQLQAETELYAEAEEMRVRLAakkqELEEILHEMEAR 930
Cdd:pfam02463 159 EEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELE----EEYLLYLDYLKL 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 931 LEEEEDRSQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEkvtAEAKIKKLEDDILVMDDQNNKLSKERKLLEERISD 1010
Cdd:pfam02463 235 NEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKE---EEKEKKLQEEELKLLAKEEEELKSELLKLERRKVD 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1011 LTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKlkrkldgEASDLHEQIAELQAQIAELKMQLAKKEE 1090
Cdd:pfam02463 312 DEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEE-------EEEELEKLQEKLEQLEEELLAKKKLESE 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1091 ELQAALGRLDDEMAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALKTELEDTLDSTAT------ 1164
Cdd:pfam02463 385 RLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELkllkde 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1165 -QQELRAKREQEVTMLKKALDEETRSHESQVQEMRQKHTQVVEELTEQLEQFKRAKANL------DKNKQALEKENAELA 1237
Cdd:pfam02463 465 lELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRiisahgRLGDLGVAVENYKVA 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1238 GEL---RVLSQAKQEVEHKKKKLEVQLQELQSKYSDGEKVRAELNDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLG 1314
Cdd:pfam02463 545 ISTaviVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKV 624
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1315 SQLQ-DTQELLQEETRQKLNVSTKLRQLEDERNSLQEQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFASTVELLEEG 1393
Cdd:pfam02463 625 VEGIlKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKK 704
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1394 KKKFQKEIESLTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQKKFDQLLAEEKNISSKYADERDR 1473
Cdd:pfam02463 705 EQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTE 784
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1474 AEAEAREKETKALSLARALEEALEAKEELERTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELED 1553
Cdd:pfam02463 785 KLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEIT 864
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1554 ELQATEDAKLRLEVNMQALKVQFERDLQARDEQNEEKRRQLQRQLHEYETELEDERKQRALAVAAKKKLEGDLKDLELQA 1633
Cdd:pfam02463 865 KEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEE 944
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 156120901 1634 DSAIKGREEAIKQLRKLQAQMKDFQRELEDARASRDEIFATAKENEKKAKSLEADLMQLQEDLAAAERARKQADLEKD 1711
Cdd:pfam02463 945 ADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEF 1022
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1315-1933 |
7.31e-20 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 97.03 E-value: 7.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1315 SQLQDT-QELLQ----EETRQKL-NVSTKLRQLEDERNSLQEQLDEEMEAKQNLERHIstlniQLSDSKKKLQDFASTVE 1388
Cdd:PRK02224 149 SDRQDMiDDLLQlgklEEYRERAsDARLGVERVLSDQRGSLDQLKAQIEEKEEKDLHE-----RLNGLESELAELDEEIE 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1389 LLEEgkkkfQKEiesltQQYEEKAAAYDKLEKTKNRlQQELDDLVVDLDNQRQLVSNLEKKQKKFDQLLAEEKNISSKYA 1468
Cdd:PRK02224 224 RYEE-----QRE-----QARETRDEADEVLEEHEER-REELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELE 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1469 DERD--RAEAEAREKETKALSLARALEEALEAKeelertnkmLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKT 1546
Cdd:PRK02224 293 EERDdlLAEAGLDDADAEAVEARREELEDRDEE---------LRDRLEECRVAAQAHNEEAESLREDADDLEERAEELRE 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1547 QLEELEDELQATEDAKlrlevnmqalkvqfeRDLQARDEQNEEKRRQLQRQLHEYETELEDERKQRALAVAAKKKLEGDL 1626
Cdd:PRK02224 364 EAAELESELEEAREAV---------------EDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRERE 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1627 KDLElqadSAIKGREEAIKQLRKLQAQMK--DFQRELEDArasrdEIFATAKENEKKAKSLEADLMQLQEDLAAAErark 1704
Cdd:PRK02224 429 AELE----ATLRTARERVEEAEALLEAGKcpECGQPVEGS-----PHVETIEEDRERVEELEAELEDLEEEVEEVE---- 495
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1705 qadlEKDELAEELASSVSGRNALQDEKRRLEARIAQLEEEleeeqgnTEAMSERVRKATQQAEQLSNELATERSAAQKNE 1784
Cdd:PRK02224 496 ----ERLERAEDLVEAEDRIERLEERREDLEELIAERRET-------IEEKRERAEELRERAAELEAEAEEKREAAAEAE 564
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1785 NARQQLERQNKELRSKLQEMEGAVKSKfkSTIAALEAKIAQLEEQVEqEAREKqatakalkqkdkklKEALLQVEDERKm 1864
Cdd:PRK02224 565 EEAEEAREEVAELNSKLAELKERIESL--ERIRTLLAAIADAEDEIE-RLREK--------------REALAELNDERR- 626
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1865 aEQYKEQAE-KGNLRVKQLKRQLEEAEEESQRINANRRKLQRELDEATESNEAMGREVTALKSKLRRGNE 1933
Cdd:PRK02224 627 -ERLAEKRErKRELEAEFDEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEE 695
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
846-1479 |
9.93e-20 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 96.68 E-value: 9.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 846 QVTRQEEEMQAKEDELQKTKERQQKAESELKELEQKHSQLTEEknlLQEQLQAETELYAEAEEMRVRLAAKKQELEEIlh 925
Cdd:TIGR02169 302 EIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELERE---IEEERKRRDKLTEEYAELKEELEDLRAELEEV-- 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 926 emEARLEEEEDRSQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDDILVMDDQNNKLSKERKLLE 1005
Cdd:TIGR02169 377 --DKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQE 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1006 ERISDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLDGEASDLHEQIAELQAQIAelkmQL 1085
Cdd:TIGR02169 455 WKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVA----QL 530
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1086 AKKEEELQAAL-----GRL------DDEMAQKNNALKKIRELeGHISDL------QEDLDSERAARNKAEKQKRDLGEEL 1148
Cdd:TIGR02169 531 GSVGERYATAIevaagNRLnnvvveDDAVAKEAIELLKRRKA-GRATFLplnkmrDERRDLSILSEDGVIGFAVDLVEFD 609
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1149 EALKTELEDTLDSTATQQELRAKREQE-----VTM----------------LKKALDEETRSHESQVQEMRQKHTQVVEE 1207
Cdd:TIGR02169 610 PKYEPAFKYVFGDTLVVEDIEAARRLMgkyrmVTLegelfeksgamtggsrAPRGGILFSRSEPAELQRLRERLEGLKRE 689
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1208 LTEQLEQFKRAKANLDKNKQAL----------EKENAELAGELRVLSQAKQEVEHKKKKLEVQLQELQSKYSDGEKVRAE 1277
Cdd:TIGR02169 690 LSSLQSELRRIENRLDELSQELsdasrkigeiEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEE 769
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1278 LNDKVHKLQNEVESVTGMLN-----EAEGKAIKLAKDVASLGSQLQDTQELLQEETRQKlnvstklRQLEDERNSLQEQL 1352
Cdd:TIGR02169 770 LEEDLHKLEEALNDLEARLShsripEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEK-------EYLEKEIQELQEQR 842
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1353 DEEMEAKQNLERHISTLNIQLSDSKKKLQDFASTVELLEEGKKKFQKEIESLTQQYEEKAAAYDKLEKTKNRLQQELDDL 1432
Cdd:TIGR02169 843 IDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSEL 922
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 156120901 1433 VVDLDNQRQLVSNLEkKQKKFDQLLAEEKNISSKYADERDRAEAEAR 1479
Cdd:TIGR02169 923 KAKLEALEEELSEIE-DPKGEDEEIPEEELSLEDVQAELQRVEEEIR 968
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
875-1481 |
2.35e-19 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 95.13 E-value: 2.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 875 LKELEQKHSQLTEEKNLLQEQLQAETELYAEAEEMRVRLAAKKQELEEILHEMEARLEEEEDRSQQLQAERKKMaqqmld 954
Cdd:PRK03918 157 LDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEV------ 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 955 leEQLEEEEAARQKLQLEKVTAEAKIKKLEDDILVMDDQNNKLSKERKLLEERISDLtTNLAEEEEKAKNLTKLKNKHES 1034
Cdd:PRK03918 231 --KELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKEL-KELKEKAEEYIKLSEFYEEYLD 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1035 MISELEVRLkkeEKSRQELEKLKRKLDgEASDLHEQIAELQAQIAELKMQLAKKEEELQaALGRLDDEMAQKNNALKKIR 1114
Cdd:PRK03918 308 ELREIEKRL---SRLEEEINGIEERIK-ELEEKEERLEELKKKLKELEKRLEELEERHE-LYEEAKAKKEELERLKKRLT 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1115 ELEghISDLQEDLDSERAARNKAEKQKRDLGEELEALKTELEDTLDSTatqQELRaKREQEVTMLKKALDEETRshesqv 1194
Cdd:PRK03918 383 GLT--PEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAI---EELK-KAKGKCPVCGRELTEEHR------ 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1195 QEMRQKHTQVVEELTEQLEQFKRAKANLDKNKQALEKENAELAGELRVLSQAKQEVEHKKKKLEVQLQELQSKYSDGEKV 1274
Cdd:PRK03918 451 KELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKL 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1275 RAELNdKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLGSQLQDTQELLQEETRQKL-NVSTKLRQLEDERNSLQEQLD 1353
Cdd:PRK03918 531 KEKLI-KLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVeELEERLKELEPFYNEYLELKD 609
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1354 EEMEaKQNLERHISTLNIQLSDSKKKLQDFASTVEL----LEEGKKKF-QKEIESLTQQYEEKAAAYDKLEKTKNRLQQE 1428
Cdd:PRK03918 610 AEKE-LEREEKELKKLEEELDKAFEELAETEKRLEElrkeLEELEKKYsEEEYEELREEYLELSRELAGLRAELEELEKR 688
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 156120901 1429 LDDLVVDLDNQRQLVSNLEKKQK---KFDQLLAEEKNISSKYADERDRAEAEAREK 1481
Cdd:PRK03918 689 REEIKKTLEKLKEELEEREKAKKeleKLEKALERVEELREKVKKYKALLKERALSK 744
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1192-1933 |
3.19e-19 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 95.13 E-value: 3.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1192 SQVQEMRQKHTQVVEELTEQLEQFKRAKANLDKNKQALEK--ENAELAGELRVLSQAKQEVE-----HKKKKLEVQLQEL 1264
Cdd:TIGR02169 163 AGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERlrREREKAERYQALLKEKREYEgyellKEKEALERQKEAI 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1265 QSKYSDGEKVRAELNDKVHKLQNEVESVTGMLNEAEGKAIKLAkdvaslgsqlqdtqellqeetrqklnvstklrqlEDE 1344
Cdd:TIGR02169 243 ERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLG----------------------------------EEE 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1345 RNSLQEQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFASTVELLEEGKKKFQKEIESLTQQYEEKAAAYDKLEKTKNR 1424
Cdd:TIGR02169 289 QLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELED 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1425 LQQELDDLVVDLDNQRQLVSNLEKKQKKFDQLLAEEKNISSKYADERDRAEAEAREKETKALSLARALEEaleakeeler 1504
Cdd:TIGR02169 369 LRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINE---------- 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1505 tnkmLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALkVQFERDLQARD 1584
Cdd:TIGR02169 439 ----LEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARAS-EERVRGGRAVE 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1585 EQNEEKRR---QLQRQLHEYeteleDERKQRALAVAAKKKLEGDLKDLELQADSAIK-------GREEAIKqLRKLQAQM 1654
Cdd:TIGR02169 514 EVLKASIQgvhGTVAQLGSV-----GERYATAIEVAAGNRLNNVVVEDDAVAKEAIEllkrrkaGRATFLP-LNKMRDER 587
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1655 KDFQRELED--------------------ARASRD----EIFATAKENEKKAK--SLEADLMQLQEDLAAAERARKQADL 1708
Cdd:TIGR02169 588 RDLSILSEDgvigfavdlvefdpkyepafKYVFGDtlvvEDIEAARRLMGKYRmvTLEGELFEKSGAMTGGSRAPRGGIL 667
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1709 -------EKDELAEELASSVSGRNALQDEKRRLEARIAQLEEELEEEQGNTEAMSERVRKATQQAEQLSNELATERSAAQ 1781
Cdd:TIGR02169 668 fsrsepaELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLS 747
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1782 KNENARQQLERQNKELRSKLQEMEgAVKSKFKSTIAALEAKIAQLE--------EQVEQEAREKQATAKALKQKDKKLKE 1853
Cdd:TIGR02169 748 SLEQEIENVKSELKELEARIEELE-EDLHKLEEALNDLEARLSHSRipeiqaelSKLEEEVSRIEARLREIEQKLNRLTL 826
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1854 ALLQVEDERKMAEQY-----------KEQAEKGNLRVKQLKRQLEEAEEESQRINANRRKLQRELDEATESNEAMGREVT 1922
Cdd:TIGR02169 827 EKEYLEKEIQELQEQridlkeqiksiEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIE 906
|
810
....*....|.
gi 156120901 1923 ALKSKLRRGNE 1933
Cdd:TIGR02169 907 ELEAQIEKKRK 917
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1046-1908 |
3.98e-19 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 94.80 E-value: 3.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1046 EEKSRQeLEKLKRKLDgEASDLHEQiaelqaqiaeLKMQLAKKEEELQAALgrldDEMAQKNNALKKIRELEghiSDLQE 1125
Cdd:pfam15921 81 EEYSHQ-VKDLQRRLN-ESNELHEK----------QKFYLRQSVIDLQTKL----QEMQMERDAMADIRRRE---SQSQE 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1126 DLdseraarnkaEKQKRDLGEELEALKTELEDTLDSTATQQElrakreqevtmlkkaldeetrshesQVQEMRQKHTQVV 1205
Cdd:pfam15921 142 DL----------RNQLQNTVHELEAAKCLKEDMLEDSNTQIE-------------------------QLRKMMLSHEGVL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1206 EELTEQLEQFKRAKANLDKNKQALEKENAELAGEL--RVLSQAKQEVEHKKKKL---EVQLQELQSKYSDG-EKVRAELN 1279
Cdd:pfam15921 187 QEIRSILVDFEEASGKKIYEHDSMSTMHFRSLGSAisKILRELDTEISYLKGRIfpvEDQLEALKSESQNKiELLLQQHQ 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1280 DKVHKLQNEVE-SVTGMLNEAEgkaiklakDVASLGSQLQDTQELLQEETRQKlnVSTKLRQLEDernslqeqldeemea 1358
Cdd:pfam15921 267 DRIEQLISEHEvEITGLTEKAS--------SARSQANSIQSQLEIIQEQARNQ--NSMYMRQLSD--------------- 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1359 kqnLERHISTLNIQLSDSKKKLQDfastveLLEEGKKKFQKEIESLTQQYEEKaaayDKLEKTKNRLQQELDDLVVDLDN 1438
Cdd:pfam15921 322 ---LESTVSQLRSELREAKRMYED------KIEELEKQLVLANSELTEARTER----DQFSQESGNLDDQLQKLLADLHK 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1439 QRQLVSnLEKKQKK--FDQLLAEEKNISSKYADERDR-AEAEAREKETKALSLARALEEALEAKEELERTNKMLKAE--M 1513
Cdd:pfam15921 389 REKELS-LEKEQNKrlWDRDTGNSITIDHLRRELDDRnMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSslT 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1514 EDLVSSKDDVGKNVHELEKSKRALETQ---MEEMKTQLEELEDELQAT--EDAKLRLEVNMQALKVQFERDLQARDEQNE 1588
Cdd:pfam15921 468 AQLESTKEMLRKVVEELTAKKMTLESSertVSDLTASLQEKERAIEATnaEITKLRSRVDLKLQELQHLKNEGDHLRNVQ 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1589 EKRRQLQRQLHEYETELEDERKQralaVAAKKKLEGDlkdlelqadsaiKGREEAIKQLRK--LQAQMKDFQRELEDARA 1666
Cdd:pfam15921 548 TECEALKLQMAEKDKVIEILRQQ----IENMTQLVGQ------------HGRTAGAMQVEKaqLEKEINDRRLELQEFKI 611
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1667 SRDEIFATAKENEKKAKSLEADLMQLQEdlAAAERARKQADL--EKDELAEELASSVSGRNALQDEkrrleariaqleee 1744
Cdd:pfam15921 612 LKDKKDAKIRELEARVSDLELEKVKLVN--AGSERLRAVKDIkqERDQLLNEVKTSRNELNSLSED-------------- 675
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1745 leeeqgnTEAMSERVRKATQQAEQLSNELATERSAAQ----KNENARQQLERQNKELRSKLQEMEGAVKSKfKSTIAALE 1820
Cdd:pfam15921 676 -------YEVLKRNFRNKSEEMETTTNKLKMQLKSAQseleQTRNTLKSMEGSDGHAMKVAMGMQKQITAK-RGQIDALQ 747
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1821 AKIAQLEEQVEQEAREKQatakALKQKDKKLKEALLQVEDER-KMA-------EQYKEQAEK-GNLRVKQLKRQLEEAEE 1891
Cdd:pfam15921 748 SKIQFLEEAMTNANKEKH----FLKEEKNKLSQELSTVATEKnKMAgelevlrSQERRLKEKvANMEVALDKASLQFAEC 823
|
890 900
....*....|....*....|.
gi 156120901 1892 ES----QRINANRRKLQRELD 1908
Cdd:pfam15921 824 QDiiqrQEQESVRLKLQHTLD 844
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
852-1581 |
7.03e-19 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 94.03 E-value: 7.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 852 EEMQAKEDELQKTKERQQKAESELKELEQKHSQLTEEKNLLQEQLQAETElyAEAEEMRVRLAAKKQELEEILHEMEARL 931
Cdd:pfam15921 120 QEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCLKEDMLEDSN--TQIEQLRKMMLSHEGVLQEIRSILVDFE 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 932 eeeedrsqqlQAERKKMAQQMLDLEEQLEEEEAARQKLQLEkvtAEAKIKKLEDDILVMDDQNNKLSKERK-----LLEE 1006
Cdd:pfam15921 198 ----------EASGKKIYEHDSMSTMHFRSLGSAISKILRE---LDTEISYLKGRIFPVEDQLEALKSESQnkielLLQQ 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1007 RISDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKK-EEKSRQELEKLKRKLdgeaSDLHEQIAELQAQIAELKMQL 1085
Cdd:pfam15921 265 HQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIiQEQARNQNSMYMRQL----SDLESTVSQLRSELREAKRMY 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1086 AKKEEELQAALGRLDDEMAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALKTELEDTLDSTATQ 1165
Cdd:pfam15921 341 EDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRE 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1166 QELRAKREQEVTMLKKALdeetrshESQVQEMRQKHTQVVEELTEQLEQFKRAKANLDKNKQALEKENAELAGELRVLSQ 1245
Cdd:pfam15921 421 LDDRNMEVQRLEALLKAM-------KSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLES 493
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1246 AKQEVEHKKKKLEVQLQELQSKYSDGEKVRAELNDKVHKLQ---NEVESVTGMLNEAEGKAIKLA---KDVASLGSQLQD 1319
Cdd:pfam15921 494 SERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQhlkNEGDHLRNVQTECEALKLQMAekdKVIEILRQQIEN 573
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1320 TQELLQEETRQKLNVSTKLRQLEDERNSLQEQLDEEMEAKQNLERHISTLNIQLSDSK--------------KKLQDFAS 1385
Cdd:pfam15921 574 MTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLElekvklvnagserlRAVKDIKQ 653
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1386 TVELLEEGKKKFQKEIESLTQQYEEKAAAY----DKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQKKFDQL-LAEE 1460
Cdd:pfam15921 654 ERDQLLNEVKTSRNELNSLSEDYEVLKRNFrnksEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVaMGMQ 733
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1461 KNISSKyaderdRAEAEAREKETKALSLARALEEALEAKEELERTNkmLKAEMEDLVSSKDDVGKNVHELEKSKRALETQ 1540
Cdd:pfam15921 734 KQITAK------RGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNK--LSQELSTVATEKNKMAGELEVLRSQERRLKEK 805
|
730 740 750 760
....*....|....*....|....*....|....*....|.
gi 156120901 1541 MEEMKTQLEELEDELQATEDAKLRLEVNMQALKVQFERDLQ 1581
Cdd:pfam15921 806 VANMEVALDKASLQFAECQDIIQRQEQESVRLKLQHTLDVK 846
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
815-1604 |
7.57e-19 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 93.98 E-value: 7.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 815 AMKVIQRNCAAYLKLRNWQWWRLfTKVKPLLQVTRQEEEMQAKEDELQKTKERQQKAESELKELEQKHSQLTEEKNL-LQ 893
Cdd:TIGR02169 215 ALLKEKREYEGYELLKEKEALER-QKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLrVK 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 894 EQLQaetELYAEAEEMRVRLAAKKQELEEilhemearleeEEDRSQQLQAERKKMAQQMLDLEEQLeeeeaARQKLQLEK 973
Cdd:TIGR02169 294 EKIG---ELEAEIASLERSIAEKERELED-----------AEERLAKLEAEIDKLLAEIEELEREI-----EEERKRRDK 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 974 VTAEAKikkleddilvmddqnnKLSKERKLLEERISDLTTNLAEEEEKAKN----LTKLKNKHESMISELEVRLKKEEKS 1049
Cdd:TIGR02169 355 LTEEYA----------------ELKEELEDLRAELEEVDKEFAETRDELKDyrekLEKLKREINELKRELDRLQEELQRL 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1050 RQELEKLKRKLdgeaSDLHEQIAELQAQIAELKMQLAKKEEELQAALGRLDDEMAQKNNALKKIRELEGHISDLQEDLDS 1129
Cdd:TIGR02169 419 SEELADLNAAI----AGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAE 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1130 ERAARNKAEKQKRDLGEELEALKTELEDTLDSTAtqqELRAKREQEVTMLKKALDeetrsheSQVQEMRQKHTQVVEELT 1209
Cdd:TIGR02169 495 AEAQARASEERVRGGRAVEEVLKASIQGVHGTVA---QLGSVGERYATAIEVAAG-------NRLNNVVVEDDAVAKEAI 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1210 EQLEQFKRAKAN-LDKNKQALEKENAELAGELRVLSQAKQEVEHKKKKLEVQLQELQS---------------------- 1266
Cdd:TIGR02169 565 ELLKRRKAGRATfLPLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKYEPAFKYVFGDtlvvedieaarrlmgkyrmvtl 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1267 ----------------KYSDGEKVRAELNDKVHKLQNEVESVTGMLNeaegkaiKLAKDVASLGSQLQDTQELLQEETRQ 1330
Cdd:TIGR02169 645 egelfeksgamtggsrAPRGGILFSRSEPAELQRLRERLEGLKRELS-------SLQSELRRIENRLDELSQELSDASRK 717
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1331 KLNVSTKLRQLEDERNSLQEQLDEemeakqnLERHISTLNIQLSDSKKKLQDFASTVELLEEGKKKFQKEIESLTQQY-- 1408
Cdd:TIGR02169 718 IGEIEKEIEQLEQEEEKLKERLEE-------LEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLsh 790
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1409 ---EEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQKKFDQLLAEEKNISSKYADERDRAEAEAREKETKA 1485
Cdd:TIGR02169 791 sriPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEEL 870
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1486 LSLARALEEALEAKEELERTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELED------------ 1553
Cdd:TIGR02169 871 EELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDpkgedeeipeee 950
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156120901 1554 --------ELQATEDAKLRLE-VNMQALKvQFER------DLQARDEQNEEKRRQLQRQLHEYETE 1604
Cdd:TIGR02169 951 lsledvqaELQRVEEEIRALEpVNMLAIQ-EYEEvlkrldELKEKRAKLEEERKAILERIEEYEKK 1015
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
853-1720 |
7.82e-19 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 94.05 E-value: 7.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 853 EMQAKEDELQKTKERQQKAESELKELEQKHSQLTEEKNLLQEQLQAETelyAEAEEMRVRLAAKK--QELEEILHEMEAR 930
Cdd:PTZ00121 1061 EAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTET---GKAEEARKAEEAKKkaEDARKAEEARKAE 1137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 931 LEEEEDRSQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDdiLVMDDQNNKLSKERKLLEERISD 1010
Cdd:PTZ00121 1138 DARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEE--LRKAEDARKAEAARKAEEERKAE 1215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1011 lTTNLAEEEEKAKNLTKLKnkhesmiselEVRLKKEEKSRQELEKLKRKLDGEASDLHEQIAELQAQIaelKMQLAKKEE 1090
Cdd:PTZ00121 1216 -EARKAEDAKKAEAVKKAE----------EAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAI---KAEEARKAD 1281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1091 ELQAALGRLDDEMAQKNNALKKIRELEGHisdlQEDLDSERAARNKAEKQKRDlGEELEAlKTELEDTLDSTATQQELRA 1170
Cdd:PTZ00121 1282 ELKKAEEKKKADEAKKAEEKKKADEAKKK----AEEAKKADEAKKKAEEAKKK-ADAAKK-KAEEAKKAAEAAKAEAEAA 1355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1171 KREQEVTMLKKALDEETRSHESQVQEMRQKHTQVV---EELTEQLEQFKRaKANLDKNKQALEKENAEL---AGELRVLS 1244
Cdd:PTZ00121 1356 ADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKkkaDEAKKKAEEDKK-KADELKKAAAAKKKADEAkkkAEEKKKAD 1434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1245 QAKQEVEHKKKKLEVQLQELQSKYSDGEKVRAELNDKVHKLQNEVESVTGMlNEAEGKAIKLAKDVASLGSQLQDTQELL 1324
Cdd:PTZ00121 1435 EAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKA-DEAKKKAEEAKKKADEAKKAAEAKKKAD 1513
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1325 QEETRQKLNVSTKLRQLEDERNSLQEQLDEEM----EAKQNLERHISTLNIQLSDSKKKLQDFASTVELLEEGKKKFQKE 1400
Cdd:PTZ00121 1514 EAKKAEEAKKADEAKKAEEAKKADEAKKAEEKkkadELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEAR 1593
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1401 IESLTQQYEE----KAAAYDKLEKTKNRlQQELDDLVVDLDNQRQLVSNLEKKQKKFDQLLAEEKNISSKYADERDRAEA 1476
Cdd:PTZ00121 1594 IEEVMKLYEEekkmKAEEAKKAEEAKIK-AEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEE 1672
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1477 EAREKET--KALSLARALEEALEAKEELERTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELE-D 1553
Cdd:PTZ00121 1673 DKKKAEEakKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKkD 1752
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1554 ELQATEDAKLRLEVNMQALKVQFERDLQARDEQNEEKrrqlQRQLHEYETELEDERKQRALAVAAKKKLEGDLKDLELQA 1633
Cdd:PTZ00121 1753 EEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEED----EKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEME 1828
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1634 DSAIKgreEAIKQLRKLQAQMKDFQRELEDARASRDEifataKENEKKAKSLEADLmqLQEDLAAAERARKQADLEKDEL 1713
Cdd:PTZ00121 1829 DSAIK---EVADSKNMQLEEADAFEKHKFNKNNENGE-----DGNKEADFNKEKDL--KEDDEEEIEEADEIEKIDKDDI 1898
|
....*..
gi 156120901 1714 AEELASS 1720
Cdd:PTZ00121 1899 EREIPNN 1905
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1204-1934 |
1.03e-18 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 93.59 E-value: 1.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1204 VVEELTEQLEQFKRAKANLDKnKQALEKENAELagELRVLSQAKQEVEHKKKKLEVQLQELQSKYSDGEKVRAELNDKVH 1283
Cdd:TIGR02169 192 IIDEKRQQLERLRREREKAER-YQALLKEKREY--EGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLE 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1284 KLQNEVESVTGMLNE-AEGKAIKLAKDVASLGSQLQDTQELLQEETRQklnvstkLRQLEDERNSLQEQLDEEMEAKQNL 1362
Cdd:TIGR02169 269 EIEQLLEELNKKIKDlGEEEQLRVKEKIGELEAEIASLERSIAEKERE-------LEDAEERLAKLEAEIDKLLAEIEEL 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1363 ERHISTLNIQlsdskkklqdfastvelleegKKKFQKEIESLTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDnqrQL 1442
Cdd:TIGR02169 342 EREIEEERKR---------------------RDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLE---KL 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1443 VSNLEKKQKKFDQLLAEEKNISSKYADerdrAEAEAREKETKALSLARALEEALEAKEELERTNKMLKAEMEDLVSSKDD 1522
Cdd:TIGR02169 398 KREINELKRELDRLQEELQRLSEELAD----LNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYD 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1523 VGKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALkvqferdlqardeqneekrRQLQRQLHEYe 1602
Cdd:TIGR02169 474 LKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGV-------------------HGTVAQLGSV- 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1603 teleDERKQRALAVAAKKKLEGDLKDLELQADSAIK-------GREEAIKqLRKLQAQMKDFQRELED------------ 1663
Cdd:TIGR02169 534 ----GERYATAIEVAAGNRLNNVVVEDDAVAKEAIEllkrrkaGRATFLP-LNKMRDERRDLSILSEDgvigfavdlvef 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1664 --------ARASRD----EIFATAKENEKKAK--SLEADLMQLQEDLAAAERARKQADL-------EKDELAEELASSVS 1722
Cdd:TIGR02169 609 dpkyepafKYVFGDtlvvEDIEAARRLMGKYRmvTLEGELFEKSGAMTGGSRAPRGGILfsrsepaELQRLRERLEGLKR 688
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1723 GRNALQDEKRRLEARIAQLEEELEEEQGNTEAMSERVRKATQQAEQLSNELATERSAAQKNENARQQLERQNKELRSKLQ 1802
Cdd:TIGR02169 689 ELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIE 768
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1803 EMEgAVKSKFKSTIAALEAKIAQLE--------EQVEQEAREKQATAKALKQKDKKLKEALLQVEDERKMAEQY----KE 1870
Cdd:TIGR02169 769 ELE-EDLHKLEEALNDLEARLSHSRipeiqaelSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQridlKE 847
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156120901 1871 QAEKGNLRVKQLKRQLEEAEEESQRINANRRKLQRELDEATESNEAMGREVTALKSKLRRGNET 1934
Cdd:TIGR02169 848 QIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQ 911
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
846-1167 |
5.15e-18 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 91.27 E-value: 5.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 846 QVTRQEEEMQAKEDELQKTKERQQKAESELK-------ELEQKHSQLTEEKNLLQEQLQAETELYAEAEEMRVRLAAKKQ 918
Cdd:TIGR02168 685 KIEELEEKIAELEKALAELRKELEELEEELEqlrkeleELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIE 764
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 919 ELEEILHEMEARLEEEEDRSQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDDILVMDDQNNKLS 998
Cdd:TIGR02168 765 ELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLE 844
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 999 KERKLLEER-------ISDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLDGEASDLHEQI 1071
Cdd:TIGR02168 845 EQIEELSEDieslaaeIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKL 924
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1072 AELQAQIAELKMQLAKKEEELQAALGR-LDDEMAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEA 1150
Cdd:TIGR02168 925 AQLELRLEGLEVRIDNLQERLSEEYSLtLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDF 1004
|
330
....*....|....*..
gi 156120901 1151 LKTELEDTLDSTATQQE 1167
Cdd:TIGR02168 1005 LTAQKEDLTEAKETLEE 1021
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
836-1568 |
5.85e-18 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 91.36 E-value: 5.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 836 RLFTKVKPLLQVTRQEEEMQAKE----DELQKTKERQQKAESELKELEQKHSQLTEEKNLLQEQLQAETELYAEAEEmrV 911
Cdd:PTZ00121 1206 RKAEEERKAEEARKAEDAKKAEAvkkaEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADE--L 1283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 912 RLAAKKQELEEILHEMEARLEEEEDRsqqlQAERKKMAQQMLDL-EEQLEEEEAARQKLQLEKVTAEAKIKKLE--DDIL 988
Cdd:PTZ00121 1284 KKAEEKKKADEAKKAEEKKKADEAKK----KAEEAKKADEAKKKaEEAKKKADAAKKKAEEAKKAAEAAKAEAEaaADEA 1359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 989 VMDDQNNKLSKERKLLEERISDLTTNLAEEEEKAKNLTKLKNKHESMISElevrLKKEEKSRQELEKLKRKLD--GEASD 1066
Cdd:PTZ00121 1360 EAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADE----LKKAAAAKKKADEAKKKAEekKKADE 1435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1067 LHEQIAEL-QAQIAELKMQLAKKEEEL--QAALGRLDDEMAQKNNALKKIRELEGHISDLQEDLDSeraARNKAEKQKRd 1143
Cdd:PTZ00121 1436 AKKKAEEAkKADEAKKKAEEAKKAEEAkkKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADE---AKKAAEAKKK- 1511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1144 lgeELEALKTELEDTLDSTATQQELRAKREQEVTMLKKALDEETRSHESQVQEMRQKhtqvveelteqLEQFKRAKAnlD 1223
Cdd:PTZ00121 1512 ---ADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKK-----------AEEAKKAEE--D 1575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1224 KNKQALEKENAELAGELRVLSQAKQEVEHKKKKLEvqlqelQSKYSDGEKVRAELNDKVHKLQNEVESVTGMLNEAEGKA 1303
Cdd:PTZ00121 1576 KNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAE------EAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKA 1649
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1304 iklakdvaslgsqlqdtQELLQEETRQKLNVSTKLRQLEDERNSLQEQLDEEMEAKQNLErhistlniqlsdSKKKLQDF 1383
Cdd:PTZ00121 1650 -----------------EELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAE------------ALKKEAEE 1700
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1384 ASTVELLEEGKKKFQKEIESLTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQKKFDQLLAEEKNI 1463
Cdd:PTZ00121 1701 AKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAV 1780
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1464 SSKYADERDRAEAEAREKETKAL--SLARALEEALEAKEELERTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQM 1541
Cdd:PTZ00121 1781 IEEELDEEDEKRRMEVDKKIKDIfdNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNEN 1860
|
730 740 750
....*....|....*....|....*....|....
gi 156120901 1542 EE-------MKTQLEELEDELQATEDAKLRLEVN 1568
Cdd:PTZ00121 1861 GEdgnkeadFNKEKDLKEDDEEEIEEADEIEKID 1894
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
989-1566 |
2.07e-17 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 88.94 E-value: 2.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 989 VMDDQNNKLS--------KERKLLEERISDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKL 1060
Cdd:PRK02224 181 VLSDQRGSLDqlkaqieeKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEI 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1061 DGEASDLHEQIAE---LQAQIAELKMQLAKKEEELQAALGRLDDEMAQKNNALKKIRELEGHISDLQEDLDSERAARNKA 1137
Cdd:PRK02224 261 EDLRETIAETEREreeLAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAH 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1138 EKQKRDLGEELEALKTELEDtldstatqqelraKREQevtmlKKALDEETRSHESQVQEMRQKHTQVVEELTEQLEQFKR 1217
Cdd:PRK02224 341 NEEAESLREDADDLEERAEE-------------LREE-----AAELESELEEAREAVEDRREEIEELEEEIEELRERFGD 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1218 AKANLDknkqalekenaELAGELRVLSQAKQEVEHKKKKLEVQLQELQSKYSDGEKVRaelndkvhklqnevesvtgmln 1297
Cdd:PRK02224 403 APVDLG-----------NAEDFLEELREERDELREREAELEATLRTARERVEEAEALL---------------------- 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1298 eAEGKAIKLAKDVAslGSQLQDTqelLQEETRQKLNVSTKLRQLEDERNSLQEQLDEEMEAKQnLERHISTLNIQLSDSK 1377
Cdd:PRK02224 450 -EAGKCPECGQPVE--GSPHVET---IEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVE-AEDRIERLEERREDLE 522
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1378 KKLQDFASTVELLEEGKKKFQKEIESLTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQKKFDQLL 1457
Cdd:PRK02224 523 ELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIA 602
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1458 AEEKNISSKYADERDRAEAEAREKETkaLSLARALEEALEAKEELERTNKmLKAEMEDLVSSKDDVGKNVHELEKSKRAL 1537
Cdd:PRK02224 603 DAEDEIERLREKREALAELNDERRER--LAEKRERKRELEAEFDEARIEE-AREDKERAEEYLEQVEEKLDELREERDDL 679
|
570 580 590
....*....|....*....|....*....|..
gi 156120901 1538 ETQMEEMKTQLEELE---DELQATEDAKLRLE 1566
Cdd:PRK02224 680 QAEIGAVENELEELEelrERREALENRVEALE 711
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
828-1396 |
3.02e-17 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 89.04 E-value: 3.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 828 KLRNWQWWRLFTKVKPLLQVTRQ---EEEMQAKEDELQKTKERQqKAEsELKELEQKHsQLTEEKNLLQEQLQAEtELYA 904
Cdd:PTZ00121 1247 EERNNEEIRKFEEARMAHFARRQaaiKAEEARKADELKKAEEKK-KAD-EAKKAEEKK-KADEAKKKAEEAKKAD-EAKK 1322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 905 EAEEMRVRLAAKKQELEEILHEMEARLEEEEDRSQQLQ-AERKKMAQQMlDLEEQLEEEEAARQKLQLEKVTAEAKiKKL 983
Cdd:PTZ00121 1323 KAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEaAEEKAEAAEK-KKEEAKKKADAAKKKAEEKKKADEAK-KKA 1400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 984 EDDILVMDDQNNKLSKERKLLEERISDLTTNLAEE----EEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRK 1059
Cdd:PTZ00121 1401 EEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEakkkAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAE 1480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1060 LDGEASDLHEQIAELQAQIAELKM--QLAKKEEELQAALGRLDDEMAQKNNALKKIRELEGhisdlQEDLDSERAARNKA 1137
Cdd:PTZ00121 1481 EAKKADEAKKKAEEAKKKADEAKKaaEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKK-----AEEKKKADELKKAE 1555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1138 EKQKRDLGEELEALKTELEDTLDSTATQQELRAKREQEVTMLKKALDEETRSHESQV---QEMRQKHTQVVEELTEQLEQ 1214
Cdd:PTZ00121 1556 ELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAkkaEEAKIKAEELKKAEEEKKKV 1635
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1215 FKRAKANLDKNKQALEKENAELAGELRVLSQAKQEVEHKKKKLEVQLQElqskysDGEKVRAELNDKVHKLQNEVESVTG 1294
Cdd:PTZ00121 1636 EQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAE------EDEKKAAEALKKEAEEAKKAEELKK 1709
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1295 MLNEAEGKAIKLAKDVASLGSQLQDTQELLQEETRQklnvSTKLRQLEDERNSLQEQLDEEMEAKQNLERHISTL----- 1369
Cdd:PTZ00121 1710 KEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKK----AEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVieeel 1785
|
570 580 590
....*....|....*....|....*....|.
gi 156120901 1370 ----NIQLSDSKKKLQDFASTVELLEEGKKK 1396
Cdd:PTZ00121 1786 deedEKRRMEVDKKIKDIFDNFANIIEGGKE 1816
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
851-1399 |
3.40e-17 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 88.20 E-value: 3.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 851 EEEMQAKEDELQKTKERQQKAESELKELEQKHSQLTEEKnllqEQLQAETELYAEAEEMRVRLAAKKQELEEILHEMEAR 930
Cdd:PRK03918 192 EELIKEKEKELEEVLREINEISSELPELREELEKLEKEV----KELEELKEEIEELEKELESLEGSKRKLEEKIRELEER 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 931 LEEEEDRSQQLQAERKKMaqqmldleeqleeeeaarQKLQlEKVTAEAKIKKLEDDILvmdDQNNKLSKERKLLEERISD 1010
Cdd:PRK03918 268 IEELKKEIEELEEKVKEL------------------KELK-EKAEEYIKLSEFYEEYL---DELREIEKRLSRLEEEING 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1011 LTTNLAEEEEKAKNLTKLKNKHESM---ISELEVRLKKEEKSRQ---ELEKLKRKLDGEASdlhEQIAELQAQIAELKMQ 1084
Cdd:PRK03918 326 IEERIKELEEKEERLEELKKKLKELekrLEELEERHELYEEAKAkkeELERLKKRLTGLTP---EKLEKELEELEKAKEE 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1085 LAKKEEELQAALGRLDDEMAQKNNALKKIRELEGHISDLQEDLDSE---------RAARNKAEKQKRDLGEELEALKTEL 1155
Cdd:PRK03918 403 IEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEhrkelleeyTAELKRIEKELKEIEEKERKLRKEL 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1156 EDTLDSTATQQELRakREQEVTMLKKALDEETRSHESQVQEMRQKHTQVVEELTEQLEQFKRAKANLDKNKQALEKENAE 1235
Cdd:PRK03918 483 RELEKVLKKESELI--KLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAE 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1236 LAGELRVLSQAKQEVEHKKKK--------LEVQLQELQSKY------SDGEKVRAELNDKVHKLQNEVESVTGMLNEAEG 1301
Cdd:PRK03918 561 LEKKLDELEEELAELLKELEElgfesveeLEERLKELEPFYneylelKDAEKELEREEKELKKLEEELDKAFEELAETEK 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1302 KAIKLAKDVASLGSQLqdTQELLQEETRQKLNVSTKLRQLEDERNSLQEQLDEEMEAKQNLERHISTlniqLSDSKKKLQ 1381
Cdd:PRK03918 641 RLEELRKELEELEKKY--SEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEE----REKAKKELE 714
|
570
....*....|....*...
gi 156120901 1382 DFASTVELLEEGKKKFQK 1399
Cdd:PRK03918 715 KLEKALERVEELREKVKK 732
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1006-1710 |
6.12e-17 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 87.66 E-value: 6.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1006 ERISDLTTNLAEEEEKAKNLTKLKNKHESMIS-ELEVRLKKEEKSRQELEKLKRKLDgeasDLHEQIAELQAQIAELKMQ 1084
Cdd:COG4913 235 DDLERAHEALEDAREQIELLEPIRELAERYAAaRERLAELEYLRAALRLWFAQRRLE----LLEAELEELRAELARLEAE 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1085 LAKKEEELQAALGRLDD-EMAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALKTELEdtldstA 1163
Cdd:COG4913 311 LERLEARLDALREELDElEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFA------A 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1164 TQQELRAKREQEVTmLKKALDEETRSHESQVQEMRQKHtqvvEELTEQLEQFKRAKANLDKN--------KQALEKENAE 1235
Cdd:COG4913 385 LRAEAAALLEALEE-ELEALEEALAEAEAALRDLRREL----RELEAEIASLERRKSNIPARllalrdalAEALGLDEAE 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1236 L--AGEL---------------RVL--------------SQAKQEVEHKKKKLEVQLQELQSKYSDGEKVRAELNDKVHK 1284
Cdd:COG4913 460 LpfVGELievrpeeerwrgaieRVLggfaltllvppehyAAALRWVNRLHLRGRLVYERVRTGLPDPERPRLDPDSLAGK 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1285 LQNEVESVTGMLNEAEGKAIKLAKdVASLgSQLQD-----TQELL--QEETRQKLNVSTKLRQ--------------LED 1343
Cdd:COG4913 540 LDFKPHPFRAWLEAELGRRFDYVC-VDSP-EELRRhpraiTRAGQvkGNGTRHEKDDRRRIRSryvlgfdnraklaaLEA 617
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1344 ERNSLQEQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFASTVELLEEgkkkfQKEIESLTQQYEEKAAAYDKLEktkn 1423
Cdd:COG4913 618 ELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASA-----EREIAELEAELERLDASSDDLA---- 688
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1424 RLQQELDDLVVDLDNQRQLVSNLEKKQKKFDQllaeeknisskyadERDRAEAEAREKETKALSLARaleeaLEAKEELE 1503
Cdd:COG4913 689 ALEEQLEELEAELEELEEELDELKGEIGRLEK--------------ELEQAEEELDELQDRLEAAED-----LARLELRA 749
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1504 RTNKMLKAEMEDLVsskddvgknvheLEKSKRALETQMEEMKTQLEELEDELQATedaklrlevnMQALKVQFE---RDL 1580
Cdd:COG4913 750 LLEERFAAALGDAV------------ERELRENLEERIDALRARLNRAEEELERA----------MRAFNREWPaetADL 807
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1581 QARDEQNEEKRRQLQRQ----LHEYETELEDERKQRAlavaakkklEGDLKDLELQADSAIKGREEAIKQL--------- 1647
Cdd:COG4913 808 DADLESLPEYLALLDRLeedgLPEYEERFKELLNENS---------IEFVADLLSKLRRAIREIKERIDPLndslkripf 878
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156120901 1648 ---RKLQ--------AQMKDFQRELEDARASRDEifATAKENEKKakslEADLMQLQEDLAAAERARKQADLEK 1710
Cdd:COG4913 879 gpgRYLRlearprpdPEVREFRQELRAVTSGASL--FDEELSEAR----FAALKRLIERLRSEEEESDRRWRAR 946
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
833-1432 |
6.13e-17 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 87.72 E-value: 6.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 833 QWWRLFTKVKPLLQVTRQEEEMQAkedELQKTKERQQKAESELKELEQKHSQLTEEKNLLQEQLQAETELYAEAEEMRVR 912
Cdd:TIGR00618 291 KAAPLAAHIKAVTQIEQQAQRIHT---ELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSI 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 913 LAAKKQELEEILHEMEARLEEEEDRsQQLQAERKKMaQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDDILVMDD 992
Cdd:TIGR00618 368 REISCQQHTLTQHIHTLQQQKTTLT-QKLQSLCKEL-DILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAA 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 993 QNNKLSKERKLLEERISDLTTNLAEEEEKAKNltklknkhesmiseLEVRLKKEEKSRQELEKLKRKLDGEASDLHEQIA 1072
Cdd:TIGR00618 446 AITCTAQCEKLEKIHLQESAQSLKEREQQLQT--------------KEQIHLQETRKKAVVLARLLELQEEPCPLCGSCI 511
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1073 ELQAqiaelKMQLAKKEEELQAALGRLDDEMAQKNNALKKIR----ELEGHISDLQEDLDSERAARNKAEKQKRDLGEEL 1148
Cdd:TIGR00618 512 HPNP-----ARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYhqltSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDI 586
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1149 EALKTELEDTLDSTATQQELR-----AKREQEVTMLKKALDEETRSHESQV-QEMRQKHTQVVEELTEQLEQFKRAKANL 1222
Cdd:TIGR00618 587 PNLQNITVRLQDLTEKLSEAEdmlacEQHALLRKLQPEQDLQDVRLHLQQCsQELALKLTALHALQLTLTQERVREHALS 666
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1223 DKNKQAL-----EKENAELAGELRVLSQAKQEVEHKKKKlevqLQELQSKYSDGEKVRAELNDKVHKLQNEVESVTGMLN 1297
Cdd:TIGR00618 667 IRVLPKEllasrQLALQKMQSEKEQLTYWKEMLAQCQTL----LRELETHIEEYDREFNEIENASSSLGSDLAAREDALN 742
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1298 EAEGKAIKLAKDV--ASLGSQLQDTQELLQEETRqklnvSTKLRQLEDERNSLQEQLDEEMEAKQNLERHIST-----LN 1370
Cdd:TIGR00618 743 QSLKELMHQARTVlkARTEAHFNNNEEVTAALQT-----GAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQeipsdED 817
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 156120901 1371 IQLSDSKKKLQDFASTVELLEEgKKKFQKEIESLTQQYEEKAAAYDKLEKTKNRLQQELDDL 1432
Cdd:TIGR00618 818 ILNLQCETLVQEEEQFLSRLEE-KSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKL 878
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1110-1908 |
7.68e-17 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 87.41 E-value: 7.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1110 LKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALKTELEDT------LDSTATQQELRAK-REQEVTMLKKA 1182
Cdd:TIGR00606 212 LKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNlskimkLDNEIKALKSRKKqMEKDNSELELK 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1183 LDEETRSHESQVQEMRQKHTQVVEELTEQLEQFKRAKANLDKNKQALEKENAELAGELRVLS-QAKQEVEH-KKKKLEVQ 1260
Cdd:TIGR00606 292 MEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQlQADRHQEHiRARDSLIQ 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1261 LQELQSKYSDGEK--------------VRAELNDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLGSQLQDTQELLQE 1326
Cdd:TIGR00606 372 SLATRLELDGFERgpfserqiknfhtlVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEK 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1327 ETRQKLNVSTKLRQLEDERNSLQEQLDEEMEAKQNLER-----HISTLNIQLSDSKKKLQDFASTVELLEEGKKKFQKEI 1401
Cdd:TIGR00606 452 KQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKaeknsLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHT 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1402 ESLTQQY---EEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQKKFDQLlaeeknisskyadeRDRaeaea 1478
Cdd:TIGR00606 532 TTRTQMEmltKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQT--------------RDR----- 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1479 reketkalsLARALEEALEAKEELERTNKMLKAEMEDLVSSKDDVGK--NVHELEKSKRALETQMEEMKTQLEELEDELQ 1556
Cdd:TIGR00606 593 ---------LAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDvcGSQDEESDLERLKEEIEKSSKQRAMLAGATA 663
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1557 ATEDAKLRLEVNMQALKVQFERDLQARDEQNEEKRRqLQRQLHEYETELEDERKQralaVAAKKKLEGDLKDLELQADSA 1636
Cdd:TIGR00606 664 VYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISD-LQSKLRLAPDKLKSTESE----LKKKEKRRDEMLGLAPGRQSI 738
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1637 IKGREEAIKQLR-KLQAQMKDFQRELEDArASRDEIFATAKENEKKAKSLEAD---LMQLQEDLAAAERARKQADLEKDe 1712
Cdd:TIGR00606 739 IDLKEKEIPELRnKLQKVNRDIQRLKNDI-EEQETLLGTIMPEEESAKVCLTDvtiMERFQMELKDVERKIAQQAAKLQ- 816
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1713 lAEELASSVSGRNALQDEKRRLEARIAQLEEELeeeqgntEAMSERVRKATQQAEQLSNELATERSAAQKNENARQQLER 1792
Cdd:TIGR00606 817 -GSDLDRTVQQVNQEKQEKQHELDTVVSKIELN-------RKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEE 888
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1793 QNKELRSKLQEMEGAVKSKfKSTIAALEAKIAQLEEQVEQEAREKQATAKALKQKDKKLKEALLQVEDERKMAEQYKEQA 1872
Cdd:TIGR00606 889 QLVELSTEVQSLIREIKDA-KEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDG 967
|
810 820 830 840
....*....|....*....|....*....|....*....|.
gi 156120901 1873 EKGNLRVKQ-----LKRQLEEAEEESQRINANRRKLQRELD 1908
Cdd:TIGR00606 968 KDDYLKQKEtelntVNAQLEECEKHQEKINEDMRLMRQDID 1008
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
846-1169 |
2.01e-16 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 85.89 E-value: 2.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 846 QVTRQEEEMQAKEDELQKTKERQQKAESELKELEQKHSQLTEEKNLLQEQLQAETELYAEAEEMRVRLAAKKQELEEILH 925
Cdd:TIGR02169 696 ELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLH 775
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 926 EMEARLEEEEDRS-----QQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDDILVMDDQnnklske 1000
Cdd:TIGR02169 776 KLEEALNDLEARLshsriPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQ------- 848
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1001 RKLLEERISDLTTNLAEEEEKAKnltklknKHESMISELEVRLKKEEKSRQELEKLKRKLDGEASDLHEQIAELQAQIAE 1080
Cdd:TIGR02169 849 IKSIEKEIENLNGKKEELEEELE-------ELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSE 921
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1081 LKMQLAKKEEELqAALGRLDDEMAQKNNALKKIRELEGHISDLQEDLDSERAARNKA-----EKQKR--DLGEELEALKT 1153
Cdd:TIGR02169 922 LKAKLEALEEEL-SEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLAiqeyeEVLKRldELKEKRAKLEE 1000
|
330
....*....|....*.
gi 156120901 1154 ELEDTLDSTATQQELR 1169
Cdd:TIGR02169 1001 ERKAILERIEEYEKKK 1016
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
979-1451 |
4.91e-16 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 84.30 E-value: 4.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 979 KIKKLEDDILVMDDQNNKLSKERKLLEERISDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKR 1058
Cdd:TIGR04523 212 KNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLN 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1059 KLDGEASDLHEQIAelQAQIAELKMQLAKKEEELQaalgRLDDEMAQKNnalKKIRELEGHISDLQEDLDSERAARNKAE 1138
Cdd:TIGR04523 292 QLKSEISDLNNQKE--QDWNKELKSELKNQEKKLE----EIQNQISQNN---KIISQLNEQISQLKKELTNSESENSEKQ 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1139 KQKRDLGEELEALKTELEDTLDS----TATQQELRAKReQEVTMLKKALDEETRSHESQVQEMRQKHT----------QV 1204
Cdd:TIGR04523 363 RELEEKQNEIEKLKKENQSYKQEiknlESQINDLESKI-QNQEKLNQQKDEQIKKLQQEKELLEKEIErlketiiknnSE 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1205 VEELTEQLEQFKRAKANLDKNKQALEKENAELAGELRVLSQAKQEVEHKKKKLEVQLQELQSKYSDGEKVRAELNDKVHK 1284
Cdd:TIGR04523 442 IKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISS 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1285 LQNEVESVTGMLNEAEGKAIKLAKDVASLGSQLqdtqellqeetrqklnvstKLRQLEDERNSLQEQLDEEMEAKQNLER 1364
Cdd:TIGR04523 522 LKEKIEKLESEKKEKESKISDLEDELNKDDFEL-------------------KKENLEKEIDEKNKEIEELKQTQKSLKK 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1365 HISTLNIQLSDSKKKLQDFASTVELLEEGKKKFQKEIESLTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVS 1444
Cdd:TIGR04523 583 KQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWP 662
|
....*..
gi 156120901 1445 NLEKKQK 1451
Cdd:TIGR04523 663 EIIKKIK 669
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
851-1392 |
6.05e-16 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 84.32 E-value: 6.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 851 EEEMQAKEDelQKTKERQQKAESELKELEQKHSQLTEEKNLLQEQLQAETELYAEAEEMRVRLAAKKQELEEILHEMEAR 930
Cdd:PRK02224 193 KAQIEEKEE--KDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAET 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 931 LEEEEDRSQQLQAERkkmaqqmLDLEEQLEEEEAARQKLQLEKVTAEAkikkleddilvMDDQNNKLSKERKLLEERISD 1010
Cdd:PRK02224 271 EREREELAEEVRDLR-------ERLEELEEERDDLLAEAGLDDADAEA-----------VEARREELEDRDEELRDRLEE 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1011 LTTNLAEEEEKAKNLTKlknkhesMISELEVRLKKEEKSRQELEKLKRKLDGEASDLHEQIAELQAQIAELKMQLAKKEE 1090
Cdd:PRK02224 333 CRVAAQAHNEEAESLRE-------DADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPV 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1091 ELQAALGRLDDEMAQKNNALKKIRELEGHISDLQEDLDSERAARNK----------AEKQKRDLGEELEALKTELEDTLD 1160
Cdd:PRK02224 406 DLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAgkcpecgqpvEGSPHVETIEEDRERVEELEAELE 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1161 STATQQELRAKREQEVTMLKKALDEETRSHE--SQVQEMRQKHTQVVEELTEQLEQFKRAKANLD-------KNKQALEK 1231
Cdd:PRK02224 486 DLEEEVEEVEERLERAEDLVEAEDRIERLEErrEDLEELIAERRETIEEKRERAEELRERAAELEaeaeekrEAAAEAEE 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1232 ENAELAGELRVLSQAKQEVEHKKKKLEvQLQELQSKYSDGEKVRAELNDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVA 1311
Cdd:PRK02224 566 EAEEAREEVAELNSKLAELKERIESLE-RIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFD 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1312 slGSQLQDTQELLQEETRQKLNVSTKLRQLEDERNSLQEQ---LDEEMEAKQNL-ERHistlnIQLSDSKKKLQDFASTV 1387
Cdd:PRK02224 645 --EARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEigaVENELEELEELrERR-----EALENRVEALEALYDEA 717
|
....*
gi 156120901 1388 ELLEE 1392
Cdd:PRK02224 718 EELES 722
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
978-1805 |
8.74e-16 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 83.94 E-value: 8.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 978 AKIKKLEDDILVMDDQNNKLSKERKLLEERISDLTTNLAEEeekaknLTKLKNKHESMISELEVRLKKEEKSRQELEKLK 1057
Cdd:TIGR00606 262 SKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQ------LNDLYHNHQRTVREKERELVDCQRELEKLNKER 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1058 RKLDGEASDLHEQIAELQAQIAELKMQLAKKEEELQAALGRLddemaqknnalkkirELEGhisdLQEDLDSERAARNKA 1137
Cdd:TIGR00606 336 RLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRL---------------ELDG----FERGPFSERQIKNFH 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1138 EKQKRDLGEELEALKTELEDTLDSTATQQELRAKREQEVTMLKKALDEETRSHESQVQEMRQKHTQV------------- 1204
Cdd:TIGR00606 397 TLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELqqlegssdrilel 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1205 -------------------VEELTEQLEQFKRAKANLDKNKQALEKENAELAGELRVLSQAKQEVEHKKKKLEvQLQELQ 1265
Cdd:TIGR00606 477 dqelrkaerelskaeknslTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDE-QIRKIK 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1266 SKYSDGEKVRAELNDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLGSQLQDTQELLQEETRQKLNVSTKL------R 1339
Cdd:TIGR00606 556 SRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLfdvcgsQ 635
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1340 QLEDERNSLQEQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFASTVELLEEGKKKFQKEIESLTQQYEEKAAAYDKLE 1419
Cdd:TIGR00606 636 DEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTE 715
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1420 KTKNRLQQELDDLVVDLDNQRqlvSNLEKKQKKFDQLLAEEKNISSKYADERDRAEAEAREKET--KALSLARALEEALE 1497
Cdd:TIGR00606 716 SELKKKEKRRDEMLGLAPGRQ---SIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTimPEEESAKVCLTDVT 792
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1498 AKEELERTNKMLKAEMEDLVSSKD--DVGKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQAL--- 1572
Cdd:TIGR00606 793 IMERFQMELKDVERKIAQQAAKLQgsDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELkse 872
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1573 KVQFERDLQARdEQNEEKRRQLQRQLHEYETELEDERKQRAlavaakkKLEGDLKDLELQADSAIKGREEAIKqlrKLQA 1652
Cdd:TIGR00606 873 KLQIGTNLQRR-QQFEEQLVELSTEVQSLIREIKDAKEQDS-------PLETFLEKDQQEKEELISSKETSNK---KAQD 941
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1653 QMKDFQRELEDARASRDEIFATAKEN-EKKAKSLEADLMQLQEDLAAAERARKQADLEKDELAEELASSVSGRNALQDEK 1731
Cdd:TIGR00606 942 KVNDIKEKVKNIHGYMKDIENKIQDGkDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNL 1021
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156120901 1732 RRLEARIAQLEEELEEEQGNTEAMSERVRKATQQAEQLSNELATERSAAQKNENARQQLERQNKELRSKLQEME 1805
Cdd:TIGR00606 1022 TLRKRENELKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQ 1095
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1255-1927 |
1.66e-15 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 82.38 E-value: 1.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1255 KKLEVQLQELQSKYSDGEKVRAELNDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLGSQLQDTQEllqeetrQKLNV 1334
Cdd:TIGR04523 50 KNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKE-------QKNKL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1335 STKLRQLEDERNSLQEQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFASTVELLEEGKKKFQKEIESLTQQYEEKAAA 1414
Cdd:TIGR04523 123 EVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1415 YDKLeKTKNRLQQELDDLVVDLDNQR-QLVSNLEKKQKKFDQLLAEEKNISSKYADERDRAEAEAREKETKALSLARALE 1493
Cdd:TIGR04523 203 LSNL-KKKIQKNKSLESQISELKKQNnQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNK 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1494 EALEAKEELertnKMLKAEMEDLVSSKD-DVGKNVHElekskraletQMEEMKTQLEELEDELQATEDAKLRLEVNMQAL 1572
Cdd:TIGR04523 282 KIKELEKQL----NQLKSEISDLNNQKEqDWNKELKS----------ELKNQEKKLEEIQNQISQNNKIISQLNEQISQL 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1573 KvqfeRDLQARDEQNEEKRRQLQrqlhEYETELEDERKQRALAVAAKKKLEGDLKDLELQADSAIKGREEAIKQLRKLQA 1652
Cdd:TIGR04523 348 K----KELTNSESENSEKQRELE----EKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQ 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1653 QMKDFQRELEDARASRDEIFATAKE-------NEKKAKSLEADLMQLQEDLAAAERARKQADLEKDELAEELASSVSGRN 1725
Cdd:TIGR04523 420 EKELLEKEIERLKETIIKNNSEIKDltnqdsvKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELK 499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1726 ALQDEKRRLEariaqleeeleeeqgnteamsERVRKATQQAEQLSNELatersaaQKNENARQQLERQNKELRSKLQEMe 1805
Cdd:TIGR04523 500 KLNEEKKELE---------------------EKVKDLTKKISSLKEKI-------EKLESEKKEKESKISDLEDELNKD- 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1806 gavksKFKSTIAALEAKIAQLEEQVEQEAREKqataKALKQKDKKLKEALLQVEDERKmaEQYKEQAEKGNLrVKQLKRQ 1885
Cdd:TIGR04523 551 -----DFELKKENLEKEIDEKNKEIEELKQTQ----KSLKKKQEEKQELIDQKEKEKK--DLIKEIEEKEKK-ISSLEKE 618
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 156120901 1886 LEEAEEESQRINANRRKLQRELDEATESNEAMGREVTALKSK 1927
Cdd:TIGR04523 619 LEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNK 660
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1036-1615 |
1.96e-15 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 82.58 E-value: 1.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1036 ISELEVRLKKEEKSRQELEK-LKRKLDGEASDLHEQIAELQAQIAELKMQLAKKEEELQAA---LGRLDDEMAQK----- 1106
Cdd:pfam12128 267 YKSDETLIASRQEERQETSAeLNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALedqHGAFLDADIETaaadq 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1107 ----------NNALKKIRELEGHISDLQEDLDSERAA---RNKAE----KQKRD-LGEELEALKTELEDTLDstATQQEL 1168
Cdd:pfam12128 347 eqlpswqselENLEERLKALTGKHQDVTAKYNRRRSKikeQNNRDiagiKDKLAkIREARDRQLAVAEDDLQ--ALESEL 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1169 RAKREQEVTMLKkaldEETRSHESQVQEM--RQKHTQVVEELTEQLEQFKRAkanLDKNKQALEKENAE---LAGELRVL 1243
Cdd:pfam12128 425 REQLEAGKLEFN----EEEYRLKSRLGELklRLNQATATPELLLQLENFDER---IERAREEQEAANAEverLQSELRQA 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1244 SQAKQEVEHKKKKLEVQLQELQSKYsdgEKVRAELNDKVHKLQNEVESVTGMLNEAEGKAIklakDVASLGSQLQDTqEL 1323
Cdd:pfam12128 498 RKRRDQASEALRQASRRLEERQSAL---DELELQLFPQAGTLLHFLRKEAPDWEQSIGKVI----SPELLHRTDLDP-EV 569
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1324 LQEETRQKLNV-STKLR--------------QLEDERNSLQEQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFASTVE 1388
Cdd:pfam12128 570 WDGSVGGELNLyGVKLDlkridvpewaaseeELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALK 649
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1389 LLEEGKKKFQKEIESLTQQYEEK-AAAYDKLEKTKNRLQQELDDLVVDL-----DNQRQLVSNLEKKQKKFdQLLAEEKN 1462
Cdd:pfam12128 650 NARLDLRRLFDEKQSEKDKKNKAlAERKDSANERLNSLEAQLKQLDKKHqawleEQKEQKREARTEKQAYW-QVVEGALD 728
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1463 ISSKYADERDRAEAEAREKETKALSLARALEEALEAKEELerTNKMLKAEMEDLVSSKDDVGKNVHELEK---------- 1532
Cdd:pfam12128 729 AQLALLKAAIAARRSGAKAELKALETWYKRDLASLGVDPD--VIAKLKREIRTLERKIERIAVRRQEVLRyfdwyqetwl 806
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1533 -SKRALETQMEEMKTQLEELEDELQA-TEDAKLRLEVNMQALKVQfeRDLQARDEQNEEKRRQLQRQLHEYETELEDERK 1610
Cdd:pfam12128 807 qRRPRLATQLSNIERAISELQQQLARlIADTKLRRAKLEMERKAS--EKQQVRLSENLRGLRCEMSKLATLKEDANSEQA 884
|
....*
gi 156120901 1611 QRALA 1615
Cdd:pfam12128 885 QGSIG 889
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1125-1876 |
2.32e-15 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 82.32 E-value: 2.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1125 EDLDSERAARNKAEKQKRDLGEELEALKTELEDTLDSTATQQELRAKREQEVTMLKKALDEEtrshesqVQEMRQKHTQV 1204
Cdd:TIGR00618 173 FPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREA-------LQQTQQSHAYL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1205 VEELTEQLEQFKRAKAnldknKQALEKENAELAGELRVLSQAKQEVEHKKKKLevqlqelqsKYSDGEKVRAELNDKVHK 1284
Cdd:TIGR00618 246 TQKREAQEEQLKKQQL-----LKQLRARIEELRAQEAVLEETQERINRARKAA---------PLAAHIKAVTQIEQQAQR 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1285 LQNEVESVTGMLNEAEGKAIKLAKDVASLGSQLQDTQELLQEETRqklnvstkLRQLEDERNSLQEQLDEEMEakqnLER 1364
Cdd:TIGR00618 312 IHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIH--------IRDAHEVATSIREISCQQHT----LTQ 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1365 HISTLNIQLSDSKKKLQDFASTVELL--EEGKKKFQKEIESLTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQL 1442
Cdd:TIGR00618 380 HIHTLQQQKTTLTQKLQSLCKELDILqrEQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKI 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1443 VSN-LEKKQKKFDQLLAEEKNISSkyaderdraeaeaREKETKALSLARALEEALEAKEELERTNKmLKAEMEDLVSSKD 1521
Cdd:TIGR00618 460 HLQeSAQSLKEREQQLQTKEQIHL-------------QETRKKAVVLARLLELQEEPCPLCGSCIH-PNPARQDIDNPGP 525
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1522 DVGK------NVHELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKvqferdlqardEQNEEKRRQLQ 1595
Cdd:TIGR00618 526 LTRRmqrgeqTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSK-----------EDIPNLQNITV 594
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1596 RQLHEYETELEDERKQRALAVAAKKKLEGDLKDLELQADSAIKGREEAIKQLRKLQAQMK-DFQRELEDARASRDEIFAT 1674
Cdd:TIGR00618 595 RLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTlTQERVREHALSIRVLPKEL 674
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1675 AKENEKKAKSLEADLMQLQEDLAAAErarkQADLEKDELAEELASSVSGRNALQDEKRRLEARIAQLEEELEEEQGNTEA 1754
Cdd:TIGR00618 675 LASRQLALQKMQSEKEQLTYWKEMLA----QCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMH 750
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1755 MSERVRKATQQAEQLSNELAT-ERSAAQKNENARQQLERQNKELRSK---LQEMEGAVKSKFKSTIAALEA---KIAQLE 1827
Cdd:TIGR00618 751 QARTVLKARTEAHFNNNEEVTaALQTGAELSHLAAEIQFFNRLREEDthlLKTLEAEIGQEIPSDEDILNLqceTLVQEE 830
|
730 740 750 760
....*....|....*....|....*....|....*....|....*....
gi 156120901 1828 EQVEQEAREKQATAKALKQKDKKLKEALLQVEDERKMAEQYKEQAEKGN 1876
Cdd:TIGR00618 831 EQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLN 879
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
846-1467 |
2.38e-15 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 81.99 E-value: 2.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 846 QVTRQEEEMQAKEDELQKTKERQQKAESELKELEQKHSQLTEEKNLLQEQlqaetelyaeaeemrvrlaakKQELEEILH 925
Cdd:TIGR04523 118 QKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQ---------------------KEELENELN 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 926 EMEARLEEEEDRSQQLQAERKKMaqqmldleeqleeeeaarQKLQLEKVTAEAKIKKLEDDILVMDDQNNKLSKERKLLE 1005
Cdd:TIGR04523 177 LLEKEKLNIQKNIDKIKNKLLKL------------------ELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQ 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1006 ERISDLTTNLAEEEEKaknLTKLKNKHESMISELevrlkkeEKSRQELEKLKRKLdgeaSDLHEQIAELQAQIAELKMQl 1085
Cdd:TIGR04523 239 QEINEKTTEISNTQTQ---LNQLKDEQNKIKKQL-------SEKQKELEQNNKKI----KELEKQLNQLKSEISDLNNQ- 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1086 akKEEELqaalgrlddemaqknnalkkIRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALKTELEdtlDSTATQ 1165
Cdd:TIGR04523 304 --KEQDW--------------------NKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELT---NSESEN 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1166 QELRAKREQEVTMLKKALDEEtrshesqvqemrqkhtqvvEELTEQLEQFKRAKANLDKNKQALEKENAELAGELRVLSQ 1245
Cdd:TIGR04523 359 SEKQRELEEKQNEIEKLKKEN-------------------QSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQ 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1246 AKQEVEHKKKKLEVQLQELQSKYSDGEKVRAELNDKVHKLQNEVESVtgmlneaEGKAIKLAKDVASLGSQLQDTQELLQ 1325
Cdd:TIGR04523 420 EKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESL-------ETQLKVLSRSINKIKQNLEQKQKELK 492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1326 EETRQKLNVSTKLRQLEDERNSLQEQLDEEMEAKQNLERHISTLNIQLSDSKKKLQ--DFASTVELLEEGKKKFQKEIES 1403
Cdd:TIGR04523 493 SKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNkdDFELKKENLEKEIDEKNKEIEE 572
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 156120901 1404 LTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKK----QKKFDQLLAEEKNISSKY 1467
Cdd:TIGR04523 573 LKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKElekaKKENEKLSSIIKNIKSKK 640
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
850-1656 |
2.70e-15 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 82.33 E-value: 2.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 850 QEEEMQAKEDELQKTKER----------QQKAESELKELEQKHSQLTEEKNLLQEQL-QAETELYAEAEEMRVRLAAKKQ 918
Cdd:pfam02463 203 KEQAKKALEYYQLKEKLEleeeyllyldYLKLNEERIDLLQELLRDEQEEIESSKQEiEKEEEKLAQVLKENKEEEKEKK 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 919 ELEEILHEMEARLEEEEDRSQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDDILVMDDQNNKLS 998
Cdd:pfam02463 283 LQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 999 KERKLLEERISDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLDGEASDLHEQIAELQAQI 1078
Cdd:pfam02463 363 KLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELK 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1079 AELKMQLAKKEEELQAALGRLDDEMAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALKTELE-D 1157
Cdd:pfam02463 443 QGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVgG 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1158 TLDSTATQQELRAKREQEVTMLKKALDEETRSHESQVQEMRQKHTQVVEELTEQLEQFKRAKANLDKNKQALEKENAELA 1237
Cdd:pfam02463 523 RIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPI 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1238 GELRVLSQAKQEVEHKKKKLEVQLQELQSKYSDGEKVRAELNDKVHKLQNEVESVTGMLNE--AEGKAIKLAKDVASLGS 1315
Cdd:pfam02463 603 LNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEvkASLSELTKELLEIQELQ 682
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1316 QLQDTQELLQEETRQKLNVSTKLRQLEDERNSLQEQLDEEMEAKQNLERHISTLNIQLSDSKKKlqdfASTVELLEEGKK 1395
Cdd:pfam02463 683 EKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKID----EEEEEEEKSRLK 758
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1396 KFQKEIESLTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQKKFDQLLAEEKNISSKyADERDRAE 1475
Cdd:pfam02463 759 KEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEK-IKEEELEE 837
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1476 AEAREKETKALSLARALEEALEAKEELERTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDEL 1555
Cdd:pfam02463 838 LALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKEN 917
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1556 QATEDAKLRLEVNMQALKVQFERDLQARDEQN--EEKRRQLQRQLHEYETELEDERKQRALAVAAKKKLEGDLKDLELQA 1633
Cdd:pfam02463 918 EIEERIKEEAEILLKYEEEPEELLLEEADEKEkeENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEK 997
|
810 820
....*....|....*....|...
gi 156120901 1634 DSAIKGREEAIKQLRKLQAQMKD 1656
Cdd:pfam02463 998 ERLEEEKKKLIRAIIEETCQRLK 1020
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
846-1566 |
3.59e-15 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 81.76 E-value: 3.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 846 QVTRQEEEMQAKEDELQKTKERQQKAESELKELEQKHSQLTEEKNLLQEQLQAETElyaeaeemrvrlaaKKQELEEILh 925
Cdd:pfam01576 455 KNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEE--------------AKRNVERQL- 519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 926 emearleeeedrsQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEkvtAEAKIKKLEDDILVMDdqnnKLSKERKLLE 1005
Cdd:pfam01576 520 -------------STLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRE---LEALTQQLEEKAAAYD----KLEKTKNRLQ 579
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1006 ERISDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLDGEASDLHEQIAELQAQIAELkmql 1085
Cdd:pfam01576 580 QELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALSLARALEEALEAKEEL---- 655
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1086 akkEEELQAALGRLDDEMAQKNNALKKIRELeghisdlqedldseraarnkaEKQKRDLGEELEALKTELEDTLDSTATQ 1165
Cdd:pfam01576 656 ---ERTNKQLRAEMEDLVSSKDDVGKNVHEL---------------------ERSKRALEQQVEEMKTQLEELEDELQAT 711
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1166 QELRAKREQEVTMLKKALDEETRSHESQVQEMRQKHTQVVEELTEQLEQFKRAKANLDKNKQALEKENAELAGELRVLSQ 1245
Cdd:pfam01576 712 EDAKLRLEVNMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANK 791
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1246 AKQEVEHKKKKLEVQLQELQSKYSDGEKVRAElndkvhklqnevesVTGMLNEAEGKAIKLAKDVASLgsqlqdtQELLQ 1325
Cdd:pfam01576 792 GREEAVKQLKKLQAQMKDLQRELEEARASRDE--------------ILAQSKESEKKLKNLEAELLQL-------QEDLA 850
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1326 EETRQKlnvstklRQLEDERNSLQEQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFASTVELLEEGKKKFQKEIESLT 1405
Cdd:pfam01576 851 ASERAR-------RQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLT 923
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1406 QQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVsnlekkQKKFDQLLAEeknISSKYADERDRAEAEAREKETKA 1485
Cdd:pfam01576 924 TELAAERSTSQKSESARQQLERQNKELKAKLQEMEGTV------KSKFKSSIAA---LEAKIAQLEEQLEQESRERQAAN 994
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1486 LSLaraleealeakeelERTNKMLKaemeDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRL 1565
Cdd:pfam01576 995 KLV--------------RRTEKKLK----EVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEASRANAARRKL 1056
|
.
gi 156120901 1566 E 1566
Cdd:pfam01576 1057 Q 1057
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1074-1929 |
3.72e-15 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 81.94 E-value: 3.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1074 LQAQIAELKMQLAKKEEELQAALGRLDDEMAQKNNALKKIREleghisdlQEDLDSERAARNKAEKQKRDLGEELEALKT 1153
Cdd:pfam02463 140 QGGKIEIIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEE--------TENLAELIIDLEELKLQELKLKEQAKKALE 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1154 ELEDTLDSTATQQELRAKREQEVTMLKKALDEETRSHESQVQEMRQKHTQVVEELTEQLEQFKRAKANLDKNKqalEKEN 1233
Cdd:pfam02463 212 YYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQ---EEEL 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1234 AELAGELRVLSQAKQEVEHKKKKLEVQLQELQSkysdgekvraelndKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASL 1313
Cdd:pfam02463 289 KLLAKEEEELKSELLKLERRKVDDEEKLKESEK--------------EKKKAEKELKKEKEEIEELEKELKELEIKREAE 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1314 GSQLQDTQELLQEETRQKLNVSTKLRQLEDERNSLQEQLDEEMEAKQNLERhISTLNIQLSDSKKKLQDFASTVELLEEG 1393
Cdd:pfam02463 355 EEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEK-EAQLLLELARQLEDLLKEEKKEELEILE 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1394 KKkfQKEIESLTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQKKFDQLLAEEKNISSKYADERDR 1473
Cdd:pfam02463 434 EE--EESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKV 511
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1474 AEAEAREKETKALSLARALEEALEAKEELERTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELED 1553
Cdd:pfam02463 512 LLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPL 591
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1554 ELQATEDAKLRLEVNMQALKVQFERDLQARDEQNEEKRRQLQRQLHEYETELEDERKQRALAVAAKKKLEGDLKDLELQA 1633
Cdd:pfam02463 592 KSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSEL 671
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1634 DSAIKGREEAIKQLRKLQAQMKDFQRELEDARASRDEIFATAKENEKKAKSLEADlmqLQEDLAAAERARKQADLEKDEL 1713
Cdd:pfam02463 672 TKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADR---VQEAQDKINEELKLLKQKIDEE 748
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1714 AEELASSVSGRNALQDEKRRLEARIAQLEEELEEEQGNTEAMSERVRKATQQAEQLSNELATERSAAQKNENARQQLERQ 1793
Cdd:pfam02463 749 EEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEE 828
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1794 NKELRSKLQEMEGAVKSKFKSTIAALEAKIAQLEEQVEQEAREKQATAKALKQKDKKLKEALLQVEDERKMAEQYKEQAE 1873
Cdd:pfam02463 829 KIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQK 908
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*.
gi 156120901 1874 KGNLRVKQLKRQLEEAEEESQRINANRRKLQRELDEATESNEAMGREVTALKSKLR 1929
Cdd:pfam02463 909 LNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKR 964
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1087-1719 |
4.65e-15 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 81.26 E-value: 4.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1087 KKEEELQAALGRLDDEMAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALKTELEDtLDSTATQQ 1166
Cdd:PRK03918 162 NAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKE-LEELKEEI 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1167 ELRAKREQEVTMLKKALDEETRSHESQVQEMRQKhtqvVEELTEQLEQFKRAKAnldknkqaLEKENAELAGELRVLSQA 1246
Cdd:PRK03918 241 EELEKELESLEGSKRKLEEKIRELEERIEELKKE----IEELEEKVKELKELKE--------KAEEYIKLSEFYEEYLDE 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1247 KQEVEHKKKKLEVQLQELQSKYSDGEKVRAELNdkvhKLQNEVESVTGMLNEAEGKAiKLAKDVASLGSQLQDTQELLQE 1326
Cdd:PRK03918 309 LREIEKRLSRLEEEINGIEERIKELEEKEERLE----ELKKKLKELEKRLEELEERH-ELYEEAKAKKEELERLKKRLTG 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1327 ETRQKLNvsTKLRQLEDERNSLQEQLDEEMEAKQNLERHISTLNIQLSDSKK-KLQDFASTVELLEEGKK----KFQKEI 1401
Cdd:PRK03918 384 LTPEKLE--KELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKaKGKCPVCGRELTEEHRKelleEYTAEL 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1402 ESLTqqyEEKAAAYDKLEKTKNRLqqelddlvVDLDNQRQLVSNLEKKQKKFDQLLAEEKNISSKYADERDRAEAEAREK 1481
Cdd:PRK03918 462 KRIE---KELKEIEEKERKLRKEL--------RELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKL 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1482 ETKALSLaraleealeaKEELERTNKMLKaEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMK-TQLEELEDELQATE- 1559
Cdd:PRK03918 531 KEKLIKL----------KGEIKSLKKELE-KLEELKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKELEp 599
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1560 ---------DAKLRLEVNMQALKVQFERDLQARDEQNEEKRR--QLQRQLHEYETELEDERKQRalavaakkklegdLKD 1628
Cdd:PRK03918 600 fyneylelkDAEKELEREEKELKKLEEELDKAFEELAETEKRleELRKELEELEKKYSEEEYEE-------------LRE 666
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1629 LELQADSAIKGREEAIKQLRKLQAQMKdfqRELEDARASRDEIFATAKENEKKAKSLEaDLMQLQEDLAAAERARKQADL 1708
Cdd:PRK03918 667 EYLELSRELAGLRAELEELEKRREEIK---KTLEKLKEELEEREKAKKELEKLEKALE-RVEELREKVKKYKALLKERAL 742
|
650
....*....|..
gi 156120901 1709 EK-DELAEELAS 1719
Cdd:PRK03918 743 SKvGEIASEIFE 754
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1243-1898 |
8.14e-15 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 80.73 E-value: 8.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1243 LSQAKQEVEHKKKKLEvQLQELQSKYSDGEKVRAELNdkvhklqnevesvtgmLNEAEGKAIKLAKD---VASLGSQLQD 1319
Cdd:COG4913 237 LERAHEALEDAREQIE-LLEPIRELAERYAAARERLA----------------ELEYLRAALRLWFAqrrLELLEAELEE 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1320 TQELLQEETRQKLNVSTKLRQLEDERNSLQEQLDE-EMEAKQNLERHISTLNIQLSDSKKKLQDFASTVELLEEgkkKFQ 1398
Cdd:COG4913 300 LRAELARLEAELERLEARLDALREELDELEAQIRGnGGDRLEQLEREIERLERELEERERRRARLEALLAALGL---PLP 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1399 KEIESLTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLdnqRQLVSNLEKKQKKFDQLLAEEKNISSKYADERDRAEAEA 1478
Cdd:COG4913 377 ASAEEFAALRAEAAALLEALEEELEALEEALAEAEAAL---RDLRRELRELEAEIASLERRKSNIPARLLALRDALAEAL 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1479 REKETKALSLAraleealeakeelertnkmlkaemeDLVsskddvgkNVHELEKS-----KRALETQmeemKTQL---EE 1550
Cdd:COG4913 454 GLDEAELPFVG-------------------------ELI--------EVRPEEERwrgaiERVLGGF----ALTLlvpPE 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1551 LEDE-LQATEDAKLRLEVNMQALKVQFERDLQARDEQNE--EK------------RRQLQRQLH----EYETELEDERkq 1611
Cdd:COG4913 497 HYAAaLRWVNRLHLRGRLVYERVRTGLPDPERPRLDPDSlaGKldfkphpfrawlEAELGRRFDyvcvDSPEELRRHP-- 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1612 RALAVAAKKKLEGDL--KDLELQADS-------AIKGREEAIKQLRKLQAQMKDFQRELEDARASRDEI---------FA 1673
Cdd:COG4913 575 RAITRAGQVKGNGTRheKDDRRRIRSryvlgfdNRAKLAALEAELAELEEELAEAEERLEALEAELDALqerrealqrLA 654
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1674 TAKENEKKAKSLEADLMQLQEDLAAAERAR---KQADLEKDELAEELASSVSGRNALQDEKRRLEARIAQLEEELEEEQG 1750
Cdd:COG4913 655 EYSWDEIDVASAEREIAELEAELERLDASSddlAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQD 734
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1751 NTEAMSERVRKA-TQQAEQLSNELATERSAAQKNENARQQLERQNKELRSKLQEMEGAV---KSKFKSTIAALEAKIAQL 1826
Cdd:COG4913 735 RLEAAEDLARLElRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMrafNREWPAETADLDADLESL 814
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 156120901 1827 EeqvEQEAREKQATAKALKQKDKKLKEALLQvederkmaeqyKEQAEKGNLrVKQLKRQLEEAEEESQRINA 1898
Cdd:COG4913 815 P---EYLALLDRLEEDGLPEYEERFKELLNE-----------NSIEFVADL-LSKLRRAIREIKERIDPLND 871
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1260-1878 |
9.24e-15 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 80.49 E-value: 9.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1260 QLQELQSKYSDGEKVRAELNDKVHKLQNEV---ESVTGMLNEAEGKAIKLAKDVASLGSQLQDTQELLQeetrqklnvst 1336
Cdd:PRK03918 156 GLDDYENAYKNLGEVIKEIKRRIERLEKFIkrtENIEELIKEKEKELEEVLREINEISSELPELREELE----------- 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1337 KLRQLEDERNSLQEQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFASTVELLEEgKKKFQKEIESLTQQYEEKAAAYD 1416
Cdd:PRK03918 225 KLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEE-KVKELKELKEKAEEYIKLSEFYE 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1417 KLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQKKFDQLLAEEKNISSKYADERDRAEAEAREKEtkalslaraleeal 1496
Cdd:PRK03918 304 EYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKA-------------- 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1497 eakeelertnkmLKAEMEDLvsSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKVQF 1576
Cdd:PRK03918 370 ------------KKEELERL--KKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAK 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1577 ERDLQARDEQNEEKRRQLqrqLHEYETELEDERKQRALAVAAKKKLEGDLKDLE--LQADSAIKGREEAIKQLRKLQAQM 1654
Cdd:PRK03918 436 GKCPVCGRELTEEHRKEL---LEEYTAELKRIEKELKEIEEKERKLRKELRELEkvLKKESELIKLKELAEQLKELEEKL 512
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1655 KDFQRE-LEDARASRDEIFATAKENEKKAKSLEADLMQLQE---DLAAAERARKQADLEKDELAEELAS-SVSGRNALQD 1729
Cdd:PRK03918 513 KKYNLEeLEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEElkkKLAELEKKLDELEEELAELLKELEElGFESVEELEE 592
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1730 EKRRLEaRIAQLEEELEEEQGNTEAMSERVRKATQQAEQLSNELATERSAAQKNENARQQLER-----QNKELRSKLQEM 1804
Cdd:PRK03918 593 RLKELE-PFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKkyseeEYEELREEYLEL 671
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156120901 1805 EGAVKSKfKSTIAALEAKIAQLEEQVEQEAREKQATAKAlKQKDKKLKEALLQVEDERKMAEQYKEQAEKGNLR 1878
Cdd:PRK03918 672 SRELAGL-RAELEELEKRREEIKKTLEKLKEELEEREKA-KKELEKLEKALERVEELREKVKKYKALLKERALS 743
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1458-1955 |
1.84e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 79.80 E-value: 1.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1458 AEEKNISSKYADERDRAEAEAREKETKALSLARALEEALEAKEELERTNKMLKAE----MEDLVSSKDD----VGKNVHE 1529
Cdd:PTZ00121 1083 AKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEdarkAEEARKAEDAkrveIARKAED 1162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1530 ---LEKSKRALETQMEEMKTQLEELE--DELQATEDAKLRLEVNM--------QALKVQFERDLQARDEQNEEKRRQLQR 1596
Cdd:PTZ00121 1163 arkAEEARKAEDAKKAEAARKAEEVRkaEELRKAEDARKAEAARKaeeerkaeEARKAEDAKKAEAVKKAEEAKKDAEEA 1242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1597 QLHEYETELEDERKQRALAVAAKKKLEGDLKDLELQADSAIKGREEAIK--QLRKLQAQMK--DFQRELEDARASrDEIF 1672
Cdd:PTZ00121 1243 KKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKadEAKKAEEKKKadEAKKKAEEAKKA-DEAK 1321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1673 ATAKENEKKAKSLEAdlmQLQEDLAAAERARKQADLEKDELAEELASSVSGRNALQDEKRRLEAriaqleeelEEEQGNT 1752
Cdd:PTZ00121 1322 KKAEEAKKKADAAKK---KAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADA---------AKKKAEE 1389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1753 EAMSERVRKATQQAEQLSNELATERSAAQKNENARQQLERQNK--ELRSKLQEMEGAVKSKFKSTIA--ALEAKIAQLEE 1828
Cdd:PTZ00121 1390 KKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKadEAKKKAEEAKKADEAKKKAEEAkkAEEAKKKAEEA 1469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1829 QVEQEAREKQATAKALKQKDKKLKEALLQVEDERKMAEQYKEQAEKGNLRVKQLKRQLEEAEEESQRINANRRKLQRELD 1908
Cdd:PTZ00121 1470 KKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKAD 1549
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 156120901 1909 EATESNEAMGREVTALKSKLRRGNETSFVPTRRSGGRRVIENADGSE 1955
Cdd:PTZ00121 1550 ELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEE 1596
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1405-1929 |
4.18e-14 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 78.29 E-value: 4.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1405 TQQYEEKAAAYDKLEKTKNRLQQELDDLVvdldnqrqlvsNLEKKQkkfdQLLAEEKNISSkyadERDRAEAE--AREKE 1482
Cdd:pfam01576 1 TRQEEEMQAKEEELQKVKERQQKAESELK-----------ELEKKH----QQLCEEKNALQ----EQLQAETElcAEAEE 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1483 TKALSLARaleealeakeelertnkmlKAEMEDLVSskdDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDA- 1561
Cdd:pfam01576 62 MRARLAAR-------------------KQELEEILH---ELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAAr 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1562 -KLRLE-VNMQALKVQFERDLQARDEQN---EEKRRQLQRQLHEYETELEDERKQRALAVAAKKKLEGDLKDLELQADSA 1636
Cdd:pfam01576 120 qKLQLEkVTTEAKIKKLEEDILLLEDQNsklSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKE 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1637 IKGREEAIKQLRKLQAQMKDFQRELEDARASRDEIFATAKENEKKAKSLEADLMQLQEDLAAAERARKQADLEKDELAEE 1716
Cdd:pfam01576 200 EKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQED 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1717 LASSVSGRNALQDEKRRLEARIAQLEEELEEEQGNTEAMSERVRKATQQAEQLSNELATE-RSAAQKNENARQQLERQNK 1795
Cdd:pfam01576 280 LESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELKKALEEEtRSHEAQLQEMRQKHTQALE 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1796 ELRSKLqEMEGAVKSKFKSTIAALEAKIAQLEEQVEQEAREKQATAKALKQKDKKLKEALLQVEDERKMAEQYKEQAEKG 1875
Cdd:pfam01576 360 ELTEQL-EQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKL 438
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 156120901 1876 NLRVKQLKRQLEEAEEESQRINANRRKLQRELDEATESNEAMGREVTALKSKLR 1929
Cdd:pfam01576 439 QSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLR 492
|
|
| Myosin_N |
pfam02736 |
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ... |
31-76 |
8.31e-14 |
|
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the N-terminus of many but not all myosins. The function of this domain is unknown.
Pssm-ID: 460670 Cd Length: 45 Bit Score: 67.07 E-value: 8.31e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 156120901 31 AAKKLVWVPSEKQGFEAASIKEEKGDEVIVELvENGKKVTVGKDDI 76
Cdd:pfam02736 1 DAKKLVWVPDPKEGFVKGEIKEEEGDKVTVET-EDGKTVTVKKDDV 45
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1096-1798 |
9.96e-14 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 77.26 E-value: 9.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1096 LGRLDD----EMAQKNNALKKIRELEGHISDLQEdldSERAARnKAEKQKRDLgEELEALKTELEDTLDSTATQQELRAK 1171
Cdd:COG4913 206 IGDLDDfvreYMLEEPDTFEAADALVEHFDDLER---AHEALE-DAREQIELL-EPIRELAERYAAARERLAELEYLRAA 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1172 -----REQEVTMLKKALDEETRSHESQVQEMRQkHTQVVEELTEQLEQFKRAKANLD-KNKQALEKEnaelageLRVLSQ 1245
Cdd:COG4913 281 lrlwfAQRRLELLEAELEELRAELARLEAELER-LEARLDALREELDELEAQIRGNGgDRLEQLERE-------IERLER 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1246 AKQEVEHKKKKLEVQLQELQSKYSDGEKVRAELNDKVHKLqnevesvtgmlneaegkaiklakdVASLGSQLQDTQELLQ 1325
Cdd:COG4913 353 ELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAAL------------------------LEALEEELEALEEALA 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1326 EETRQKLNVSTKLRQLEDERNSLQEQ---LDEEM-EAKQNLERHistlniqLSDSKKKLQDFAstvELLE--EGKKKFQK 1399
Cdd:COG4913 409 EAEAALRDLRRELRELEAEIASLERRksnIPARLlALRDALAEA-------LGLDEAELPFVG---ELIEvrPEEERWRG 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1400 EIESL-----------TQQYEEKAAAYDKLeKTKNRLQ-QELDDLVVDLDNQR----QLVSNLEKKQKKFDQLLAEEkni 1463
Cdd:COG4913 479 AIERVlggfaltllvpPEHYAAALRWVNRL-HLRGRLVyERVRTGLPDPERPRldpdSLAGKLDFKPHPFRAWLEAE--- 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1464 sskYADERDRA---EAEAREKETKALSLARALEEALEAKEELERtnkmlKAEMEDLVSSKDDVGKnVHELEKSKRALETQ 1540
Cdd:COG4913 555 ---LGRRFDYVcvdSPEELRRHPRAITRAGQVKGNGTRHEKDDR-----RRIRSRYVLGFDNRAK-LAALEAELAELEEE 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1541 MEEMKTQLEELEDELQATEDAKLRLEvnmQALKVQFER-DLQARDEQNEEKRRQ-------------LQRQLHEYETELE 1606
Cdd:COG4913 626 LAEAEERLEALEAELDALQERREALQ---RLAEYSWDEiDVASAEREIAELEAElerldassddlaaLEEQLEELEAELE 702
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1607 DERKQRALAVAAKKKLEGDLKDLELQADSAIKGREEAIKQLRKLQAQMKDFQRELEDARASRDEIfatakenekkAKSLE 1686
Cdd:COG4913 703 ELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVEREL----------RENLE 772
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1687 ADLMQLQEDLAAAE----RARKQADLEKDELAEELASSVSGRNALQDEKRRLEA-RIAQleeeleeeqgNTEAMSERVRK 1761
Cdd:COG4913 773 ERIDALRARLNRAEeeleRAMRAFNREWPAETADLDADLESLPEYLALLDRLEEdGLPE----------YEERFKELLNE 842
|
730 740 750
....*....|....*....|....*....|....*...
gi 156120901 1762 ATQQA-EQLSNELATERsaaqknENARQQLERQNKELR 1798
Cdd:COG4913 843 NSIEFvADLLSKLRRAI------REIKERIDPLNDSLK 874
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
942-1715 |
1.14e-13 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 76.93 E-value: 1.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 942 QAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDDILVMDDQNNKLSKERKLLEERISDLTTNLAEEEEK 1021
Cdd:pfam02463 173 EALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1022 AKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLDG-------EASDLHEQIAELQAQIAELKMQLAKKEEELQA 1094
Cdd:pfam02463 253 IESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKeeeelksELLKLERRKVDDEEKLKESEKEKKKAEKELKK 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1095 ALGRLDDEMAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALKTELEDTLDSTATQQELRAKREQ 1174
Cdd:pfam02463 333 EKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLE 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1175 EVTMLKKALDEETRSHESQVQEMRQKHTQVVEELTEQLEQFKRAKANLDKNKQALEKENAELAGELRVLSQAKQEVEHKK 1254
Cdd:pfam02463 413 LARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSR 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1255 KKLEVQLQELQSKYSDGEKVRAELNDKVHKLQNEVESVTGMLNEAEGK---AIKLAKDVASLGSQLQDTQELLQEETRQK 1331
Cdd:pfam02463 493 QKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENykvAISTAVIVEVSATADEVEERQKLVRALTE 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1332 LNVSTKLRQLEDERNSLQEQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFASTVELLEEGKKKFQKEIESLTQQYEEK 1411
Cdd:pfam02463 573 LPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGV 652
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1412 AAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQKKFDQLLAEEKNISSKYADERDRAEAEAREKETKALSLARA 1491
Cdd:pfam02463 653 SLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQD 732
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1492 LEEALEAKEELERTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDaklRLEVNMQA 1571
Cdd:pfam02463 733 KINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEE---ELRALEEE 809
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1572 LKVQFERDLQARDEQNEEKRRQLQRQLHEYETELEDERKQRALAVAAKKKLEGDLKDLELQADSAIKGREEAIKQLRKLQ 1651
Cdd:pfam02463 810 LKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELE 889
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156120901 1652 AQMKDFQRELEDARASRDEIFATAKENEKKAKSLEADLMQLQEDLAAAERARKQADLEKDELAE 1715
Cdd:pfam02463 890 SKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEEN 953
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1100-1911 |
1.96e-13 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 76.03 E-value: 1.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1100 DDEMAQKNNALKKiRELEGHISDLQEDLDSErAARNKAEKQKRDLgEELEALKTELEDTLDSTATQQELRAKREQEVTML 1179
Cdd:pfam12128 208 DDGVVPPKSRLNR-QQVEHWIRDIQAIAGIM-KIRPEFTKLQQEF-NTLESAELRLSHLHFGYKSDETLIASRQEERQET 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1180 KKALDEETRSHESQVQEMRQKHTQVVEELTEQLEQFKRAKANLDKNKQALEKENAElagelrvlsQAKQEVEhkkkklev 1259
Cdd:pfam12128 285 SAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIE---------TAAADQE-------- 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1260 QLQELQSKYSDGEKVRAELNDKVHKLQNEVESVTGMLNEaegkaiKLAKDVASLGSQLQDTQEllqEETRQKLNVSTKLR 1339
Cdd:pfam12128 348 QLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKE------QNNRDIAGIKDKLAKIRE---ARDRQLAVAEDDLQ 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1340 QLEDE-RNSLQEQLDEEMEAKQNLERHISTLNIQL------SDSKKKLQDFASTVELLEEGKKKFQKEIESLtqQYEEKA 1412
Cdd:pfam12128 419 ALESElREQLEAGKLEFNEEEYRLKSRLGELKLRLnqatatPELLLQLENFDERIERAREEQEAANAEVERL--QSELRQ 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1413 A------AYDKLEKTKNRLQQ---ELDDLVVDLDNQR-QLVSNLEKKQKKFDQLLAeeKNISSKYADERDRAEAEAREKE 1482
Cdd:pfam12128 497 ArkrrdqASEALRQASRRLEErqsALDELELQLFPQAgTLLHFLRKEAPDWEQSIG--KVISPELLHRTDLDPEVWDGSV 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1483 TKALSL-ARALEEALEAKEELERTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDA 1561
Cdd:pfam12128 575 GGELNLyGVKLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLD 654
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1562 KLRLEVNMQALKVQFERDLQARDEQNEEKRRQLQRQLHEYETEL--------EDERKQRALAVAAKKKLEGDLKDLELQA 1633
Cdd:pfam12128 655 LRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHqawleeqkEQKREARTEKQAYWQVVEGALDAQLALL 734
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1634 DSAIKGREEAIKqlRKLQAQMKDFQRELedarASRDEifatakeNEKKAKSLEADLMQLQEDLAAAERaRKQADLEKDEL 1713
Cdd:pfam12128 735 KAAIAARRSGAK--AELKALETWYKRDL----ASLGV-------DPDVIAKLKREIRTLERKIERIAV-RRQEVLRYFDW 800
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1714 AEELASSvsgrnalqdEKRRLEARIAQLEEELEEEQGNTEAMSERVRKATQQAEqlsnelaTERSAAQKnenarqQLERQ 1793
Cdd:pfam12128 801 YQETWLQ---------RRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLE-------MERKASEK------QQVRL 858
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1794 NKELRSKLQEMEGAVKSKFKSTIAALEAKIAQLEEQVEQEAREKQATAKALKQKDKKLKEALLQ------VEDERKMAEQ 1867
Cdd:pfam12128 859 SENLRGLRCEMSKLATLKEDANSEQAQGSIGERLAQLEDLKLKRDYLSESVKKYVEHFKNVIADhsgsglAETWESLREE 938
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156120901 1868 YKEQAEKG-----------------NLRVKQLKRQLEEA---------------EEESQRINANRRKLQRELDEAT 1911
Cdd:pfam12128 939 DHYQNDKGirlldyrklvpyleqwfDVRVPQSIMVLREQvsilgvdltefydvlADFDRRIASFSRELQREVGEEA 1014
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1509-1961 |
2.89e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 75.72 E-value: 2.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1509 LKAEMEDLVSSKDDVGKnvheLEKSKRALEtQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKVQferDLQARDEQNE 1588
Cdd:COG4913 230 LVEHFDDLERAHEALED----AREQIELLE-PIRELAERYAAARERLAELEYLRAALRLWFAQRRLE---LLEAELEELR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1589 EKRRQLQRQLHEYETELEDERKQRALAVAAKKKLEGDLKDlELQADsaIKGREEAIKQLRKLQAQMKDFQRELE-DARAS 1667
Cdd:COG4913 302 AELARLEAELERLEARLDALREELDELEAQIRGNGGDRLE-QLERE--IERLERELEERERRRARLEALLAALGlPLPAS 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1668 RDEIFATAKENEKKAKSLEADLMQLQEDLAAAERARKQADLEKDELAEELASSVSGRNALQDEKRRLEARIAQLEEELEE 1747
Cdd:COG4913 379 AEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLDEA 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1748 E-----------------QG------NTEAMS--------------------------ERVRKATQQAEQ-------LSN 1771
Cdd:COG4913 459 ElpfvgelievrpeeerwRGaiervlGGFALTllvppehyaaalrwvnrlhlrgrlvyERVRTGLPDPERprldpdsLAG 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1772 ELATERSAAQ---KNENAR----------QQLER------------QNKELRSKlqEMEGAVKSKF------KSTIAALE 1820
Cdd:COG4913 539 KLDFKPHPFRawlEAELGRrfdyvcvdspEELRRhpraitragqvkGNGTRHEK--DDRRRIRSRYvlgfdnRAKLAALE 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1821 AKIAQLEEQVeQEAREKQATAKALKQKDKKLKEALLQVED-----------ERKMA--EQYKEQAEKGNLRVKQLKRQLE 1887
Cdd:COG4913 617 AELAELEEEL-AEAEERLEALEAELDALQERREALQRLAEyswdeidvasaEREIAelEAELERLDASSDDLAALEEQLE 695
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 156120901 1888 EAEEESQRINANRRKLQRELDEATESNEAMGREVTALKSKLRRGNETSFVPTRRSGGRRVIE-NADGSEEEMDAR 1961
Cdd:COG4913 696 ELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAaLGDAVERELREN 770
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
845-1652 |
5.26e-13 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 74.87 E-value: 5.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 845 LQVTRQEEEMQAKEDEL-----QKTKERQQK---AESELKELEQKHSQLTEEKNLLQEQ----LQAETELYAEAEEMRVR 912
Cdd:pfam12128 272 TLIASRQEERQETSAELnqllrTLDDQWKEKrdeLNGELSAADAAVAKDRSELEALEDQhgafLDADIETAAADQEQLPS 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 913 LAAKKQELEEILhemEARLEEEEDRSQQLQAERKKMAQQMLDLEEQLEEEEAA-RQKLQLEKVTAEAKIKKLEDDI-LVM 990
Cdd:pfam12128 352 WQSELENLEERL---KALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKiREARDRQLAVAEDDLQALESELrEQL 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 991 DDQNNKLSKERKLLEERISDLTTNLAE---EEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLDgEASDL 1067
Cdd:pfam12128 429 EAGKLEFNEEEYRLKSRLGELKLRLNQataTPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRD-QASEA 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1068 HEQIA----ELQAQIAELKMQLAKKEEELQAALG------------------------------------------RLDD 1101
Cdd:pfam12128 508 LRQASrrleERQSALDELELQLFPQAGTLLHFLRkeapdweqsigkvispellhrtdldpevwdgsvggelnlygvKLDL 587
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1102 EMAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALKTELEDTL----DSTATQQELRAKREQEVT 1177
Cdd:pfam12128 588 KRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARtalkNARLDLRRLFDEKQSEKD 667
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1178 MLKKALDEETRSHESQVQEMRQKHTQVVEELTEQLEQFKRAKANLDKNKQALEKEnaeLAGELRV-LSQAKQEVEHKKKK 1256
Cdd:pfam12128 668 KKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQV---VEGALDAqLALLKAAIAARRSG 744
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1257 LEVQLQELQSKYSDGEKVRAELNDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLGSQLQDTQELLQEETRqklNVST 1336
Cdd:pfam12128 745 AKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLATQLS---NIER 821
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1337 KLRQLEDERNSLQEQLdEEMEAKQNLERHIS-TLNIQLSDSKKKLQDFASTVELLEEgkkkfqkeiesltqqyeekAAAY 1415
Cdd:pfam12128 822 AISELQQQLARLIADT-KLRRAKLEMERKASeKQQVRLSENLRGLRCEMSKLATLKE-------------------DANS 881
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1416 DKLEKTKNRLQQELDDLvvdLDNQRQLVSNLEKKQKKFDQLLAeeKNISSKYADERDRAEAEAREKETKALSLARALEEA 1495
Cdd:pfam12128 882 EQAQGSIGERLAQLEDL---KLKRDYLSESVKKYVEHFKNVIA--DHSGSGLAETWESLREEDHYQNDKGIRLLDYRKLV 956
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1496 LEAKEELERTNKMLKAEMEDLVSSKD-DVGKNVHELEKSKRALETQMEEMKTQLEELEDeLQATEDAKLRleVNMQALKV 1574
Cdd:pfam12128 957 PYLEQWFDVRVPQSIMVLREQVSILGvDLTEFYDVLADFDRRIASFSRELQREVGEEAF-FEGVSESAVR--IRSKVSEL 1033
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 156120901 1575 QFERDLQArdeQNEEKRRQLQRQLHEYETELEDERKQRALAVAAKKKLEGDLKDL-ELQADSAIKGREEAIKQLRKLQA 1652
Cdd:pfam12128 1034 EYWPELRV---FVKAFRLWKSDGFGELPDEEYTQAMRRASDILPSAALSGGLNDLlEIELRLTENGSDKIIRNEKQLNE 1109
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
840-1257 |
5.34e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 74.72 E-value: 5.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 840 KVKPLLQVTRQEEEMQAKEDELQKTKERQQKAESELKELEQKHSQLTEEKNLLQEQLQAETELYAEAEEMRVRLAAKKQE 919
Cdd:PRK03918 274 EIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKR 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 920 LEEI--LHEMEARLEEEEDRSQQLQAERK-----KMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDDI----- 987
Cdd:PRK03918 354 LEELeeRHELYEEAKAKKEELERLKKRLTgltpeKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIeelkk 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 988 -----------LVMDDQNN----------KLSKERKLLEERISDLTTNLAEEEEKAKNLTKLKNKHE--SMISELEVRLK 1044
Cdd:PRK03918 434 akgkcpvcgreLTEEHRKElleeytaelkRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKElaEQLKELEEKLK 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1045 -----KEEKSRQELEKLKRKLDGEASDLH------EQIAELQAQIAELKMQLAKKEEELQAALGRLddemaqKNNALKKI 1113
Cdd:PRK03918 514 kynleELEKKAEEYEKLKEKLIKLKGEIKslkkelEKLEELKKKLAELEKKLDELEEELAELLKEL------EELGFESV 587
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1114 RELEGHISDLQEDLDSERAARNkAEKQKRDLGEELEALKTELEDTLDSTA-TQQELRAKREQEVTMLKKALDEETRSHES 1192
Cdd:PRK03918 588 EELEERLKELEPFYNEYLELKD-AEKELEREEKELKKLEEELDKAFEELAeTEKRLEELRKELEELEKKYSEEEYEELRE 666
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 156120901 1193 QVQEMRQKHTQVVEELTEQLEQFKRAKANLDKNKQALEkENAELAGELRVLSQAKQEVEHKKKKL 1257
Cdd:PRK03918 667 EYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELE-EREKAKKELEKLEKALERVEELREKV 730
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1000-1740 |
5.54e-13 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 74.99 E-value: 5.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1000 ERKLLEERISDLTTNLAEEEEKaknLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLD--GEASDLHEQIAELQAQ 1077
Cdd:COG3096 279 ERRELSERALELRRELFGARRQ---LAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNlvQTALRQQEKIERYQED 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1078 IAELKMQLAKKEEELQAALGRLDDEMAQKNNALKKIRELEGHISDLQEDLDSE-------RAARNKAEKQKR-------- 1142
Cdd:COG3096 356 LEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQqtraiqyQQAVQALEKARAlcglpdlt 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1143 --DLGEELEALKTElEDTLDSTATQQELR------AKREQEVTM--LKKALDEETRS--HESQVQEMRQKHTQvvEELTE 1210
Cdd:COG3096 436 peNAEDYLAAFRAK-EQQATEEVLELEQKlsvadaARRQFEKAYelVCKIAGEVERSqaWQTARELLRRYRSQ--QALAQ 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1211 QLEQFKRAKANLDKNKQalEKENAE-LAGELRVlsQAKQEVEHKKKkLEVQLQELQSKYSDGEKVRAELNDKVHKLQNEV 1289
Cdd:COG3096 513 RLQQLRAQLAELEQRLR--QQQNAErLLEEFCQ--RIGQQLDAAEE-LEELLAELEAQLEELEEQAAEAVEQRSELRQQL 587
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1290 ESVTGMLNEAEGKA---IKLAKDVASLGSQLQDTQELLQEETRQKLNVSTKLRQLEDERNSLQEQldeemeaKQNLERHI 1366
Cdd:COG3096 588 EQLRARIKELAARApawLAAQDALERLREQSGEALADSQEVTAAMQQLLEREREATVERDELAAR-------KQALESQI 660
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1367 STLNIQLSDSKKKLQDFASTV--ELLEEGkkkfqkeiesltqqYEEKA---AAY--------------DKLEKTKNRLQ- 1426
Cdd:COG3096 661 ERLSQPGGAEDPRLLALAERLggVLLSEI--------------YDDVTledAPYfsalygparhaivvPDLSAVKEQLAg 726
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1427 -------------------------QELDDLVVDLDNQRQL-VSNLEK--------KQKKFDQLLAEEKNISSKYADER- 1471
Cdd:COG3096 727 ledcpedlyliegdpdsfddsvfdaEELEDAVVVKLSDRQWrYSRFPEvplfgraaREKRLEELRAERDELAEQYAKASf 806
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1472 -----DRAEAEAREKETKALSLARALEEAleakeelertnkmlkAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKT 1546
Cdd:COG3096 807 dvqklQRLHQAFSQFVGGHLAVAFAPDPE---------------AELAALRQRRSELERELAQHRAQEQQLRQQLDQLKE 871
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1547 QL----------------------EELEDELQATEDAKL----------RLEVNMQALKV---QFERdLQARDEQNEEKR 1591
Cdd:COG3096 872 QLqllnkllpqanlladetladrlEELREELDAAQEAQAfiqqhgkalaQLEPLVAVLQSdpeQFEQ-LQADYLQAKEQQ 950
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1592 RQLQRQLH------------EYETELEDERKQRALAVAAKKKLEgdlkdlelQADSAikgREEAIKQLRKLQAQMKDFQR 1659
Cdd:COG3096 951 RRLKQQIFalsevvqrrphfSYEDAVGLLGENSDLNEKLRARLE--------QAEEA---RREAREQLRQAQAQYSQYNQ 1019
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1660 ELEDARASRDeifatAKENEKKAKSLEADLMQLQEDLAAAERARkqadLEKDELAEELASSVSGRNALQDEKRRLEARIA 1739
Cdd:COG3096 1020 VLASLKSSRD-----AKQQTLQELEQELEELGVQADAEAEERAR----IRRDELHEELSQNRSRRSQLEKQLTRCEAEMD 1090
|
.
gi 156120901 1740 Q 1740
Cdd:COG3096 1091 S 1091
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1050-1870 |
7.02e-13 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 74.60 E-value: 7.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1050 RQELEKLKRKLDGEasdlHEQIAELQAQIAELKMQLAKKEEELQAAlgrlDDEMAQKNNALK---KIRELEGHISDLQED 1126
Cdd:COG3096 291 RRELFGARRQLAEE----QYRLVEMARELEELSARESDLEQDYQAA----SDHLNLVQTALRqqeKIERYQEDLEELTER 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1127 LDSERAARNKAEKQKRDLGEELEA-------LKTELED---TLDSTAT-----QQELRAKREQEVTMLKKALDEE---TR 1188
Cdd:COG3096 363 LEEQEEVVEEAAEQLAEAEARLEAaeeevdsLKSQLADyqqALDVQQTraiqyQQAVQALEKARALCGLPDLTPEnaeDY 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1189 SHESQVQEmrQKHTQVVEELTEQLEQFKRAKANLDKNKQALEKENAELAGElRVLSQAKQEVEH--KKKKLEVQLQELQS 1266
Cdd:COG3096 443 LAAFRAKE--QQATEEVLELEQKLSVADAARRQFEKAYELVCKIAGEVERS-QAWQTARELLRRyrSQQALAQRLQQLRA 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1267 KYSDGEKvRAELNDKVHKLQNEvesvtgmLNEAEGKAIKLAKDVASLGSQLQDTQELLQEETRQKLNVSTKLRQLEDERN 1346
Cdd:COG3096 520 QLAELEQ-RLRQQQNAERLLEE-------FCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLR 591
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1347 SLQEQLDEE----MEAKQNLERHISTLNIQLSDSKKKLQDFASTVE----------LLEEGKKKFQKEIESLTQqyeeKA 1412
Cdd:COG3096 592 ARIKELAARapawLAAQDALERLREQSGEALADSQEVTAAMQQLLErereatverdELAARKQALESQIERLSQ----PG 667
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1413 AAYD-KLEKTKNRLQQEL-----DDLVVD--------LDNQRQ--LVSNLEKKQKKFDQLlaeEKNISSKYADERDRAEA 1476
Cdd:COG3096 668 GAEDpRLLALAERLGGVLlseiyDDVTLEdapyfsalYGPARHaiVVPDLSAVKEQLAGL---EDCPEDLYLIEGDPDSF 744
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1477 EAREKETKALSLAraleealeakeelertnkmlkaemeDLVSSKDdvgknvHELEKSK---------RALETQMEEMKTQ 1547
Cdd:COG3096 745 DDSVFDAEELEDA-------------------------VVVKLSD------RQWRYSRfpevplfgrAAREKRLEELRAE 793
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1548 LEELEDELqatedAKLRLEVN-MQALKVQFERDL-----QARDEQNEEKRRQLQRQLHEYETELEDERKQralavaakkk 1621
Cdd:COG3096 794 RDELAEQY-----AKASFDVQkLQRLHQAFSQFVgghlaVAFAPDPEAELAALRQRRSELERELAQHRAQ---------- 858
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1622 legdlkdlELQADSAIKGREEAIKQLRKLQAQM------------KDFQRELEDARASRDEIF---ATAKENEKKAKSLE 1686
Cdd:COG3096 859 --------EQQLRQQLDQLKEQLQLLNKLLPQAnlladetladrlEELREELDAAQEAQAFIQqhgKALAQLEPLVAVLQ 930
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1687 ADLMQ---LQEDLAAAERARKQADLEKDELAEELA--------SSVSGRNALQDEKRRLEARIAQLEEELEEEQgnteam 1755
Cdd:COG3096 931 SDPEQfeqLQADYLQAKEQQRRLKQQIFALSEVVQrrphfsyeDAVGLLGENSDLNEKLRARLEQAEEARREAR------ 1004
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1756 sERVRKATQQAEQLSNELATERSAAQkneNARQQLerqnKELRSKLQEMEGAVKSkfkSTIAALEAKIAQLEEQVEQEAR 1835
Cdd:COG3096 1005 -EQLRQAQAQYSQYNQVLASLKSSRD---AKQQTL----QELEQELEELGVQADA---EAEERARIRRDELHEELSQNRS 1073
|
890 900 910 920
....*....|....*....|....*....|....*....|..
gi 156120901 1836 EKQATAK-------ALKQKDKKLKEALLQVEDERKMAEQYKE 1870
Cdd:COG3096 1074 RRSQLEKqltrceaEMDSLQKRLRKAERDYKQEREQVVQAKA 1115
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
999-1738 |
9.59e-13 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 73.84 E-value: 9.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 999 KERKLLEERISDLTTNLAEEEEKaknLTKLKNKHESMISELEvRLKKEEKS-RQELEKLKRKLD--GEASDLHEQIAELQ 1075
Cdd:PRK04863 279 NERRVHLEEALELRRELYTSRRQ---LAAEQYRLVEMARELA-ELNEAESDlEQDYQAASDHLNlvQTALRQQEKIERYQ 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1076 AQIAELKMQLAKKEEELQAALGRLDDEMAQKNNALKKIRELEGHISDLQEDLDSE--RA-----ARNKAEKQKRDLG--- 1145
Cdd:PRK04863 355 ADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQqtRAiqyqqAVQALERAKQLCGlpd 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1146 ----------EELEALKTELEDTLDSTATQ----QELRAKREQEVTMLKKALDEETRS------------HES------Q 1193
Cdd:PRK04863 435 ltadnaedwlEEFQAKEQEATEELLSLEQKlsvaQAAHSQFEQAYQLVRKIAGEVSRSeawdvarellrrLREqrhlaeQ 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1194 VQEMRQKHTQVVEELTEQ------LEQF-KRAKANLDkNKQALEKENAELAGELRVLSQAKQEVEHKKKKLEVQLQELQS 1266
Cdd:PRK04863 515 LQQLRMRLSELEQRLRQQqraerlLAEFcKRLGKNLD-DEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQA 593
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1267 KYSDGEKVRAELndkvHKLQNEVESvtgmLNEAEGKAIKLAKDVASLgsqLQDTQELLQEETRQKLNVSTKLRQLEDERN 1346
Cdd:PRK04863 594 RIQRLAARAPAW----LAAQDALAR----LREQSGEEFEDSQDVTEY---MQQLLERERELTVERDELAARKQALDEEIE 662
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1347 SLQE----------QLDE--------------------EMEAKQNLERHISTLNiQLSDSKKKL---------------- 1380
Cdd:PRK04863 663 RLSQpggsedprlnALAErfggvllseiyddvsledapYFSALYGPARHAIVVP-DLSDAAEQLagledcpedlyliegd 741
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1381 -QDFASTVELLEEGKKkfqkeieSLTQQYEEKAAAYDKL-----------EKTKNRLQQELDDLVVDLDNQRQLVSNLEK 1448
Cdd:PRK04863 742 pDSFDDSVFSVEELEK-------AVVVKIADRQWRYSRFpevplfgraarEKRIEQLRAEREELAERYATLSFDVQKLQR 814
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1449 KQKKFDQLLAEEKNISSKYADERDRAEAEAREKE-TKALSLARALEEALEAKEELERTNKMLKAEMEDLVSSKDDvgknv 1527
Cdd:PRK04863 815 LHQAFSRFIGSHLAVAFEADPEAELRQLNRRRVElERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNLLAD----- 889
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1528 helekskralETQMEEmktqLEELEDELQATEDAKL----------RLEVNMQALKV---QFERdLQARDEQNEEKRRQL 1594
Cdd:PRK04863 890 ----------ETLADR----VEEIREQLDEAEEAKRfvqqhgnalaQLEPIVSVLQSdpeQFEQ-LKQDYQQAQQTQRDA 954
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1595 QRQLHEYeTEL---------EDERKQRALAVAAKKKLEGDLKDLELQadsaikgREEAIKQLRKLQAQMKDFQRELEDAR 1665
Cdd:PRK04863 955 KQQAFAL-TEVvqrrahfsyEDAAEMLAKNSDLNEKLRQRLEQAEQE-------RTRAREQLRQAQAQLAQYNQVLASLK 1026
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 156120901 1666 ASRDeifatAKENEKKAKSLEADLMQLQEDLAAAERARKQadleKDELAEELASSVSGRNALQDEKRRLEARI 1738
Cdd:PRK04863 1027 SSYD-----AKRQMLQELKQELQDLGVPADSGAEERARAR----RDELHARLSANRSRRNQLEKQLTFCEAEM 1090
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1339-1930 |
9.68e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 73.80 E-value: 9.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1339 RQLEDERNSLQEQLDEEMEAKQNLE---RHISTLnIQLSDSKKKLQDFASTVELLEEGKKKFQKEIESltQQYEEKAAAY 1415
Cdd:COG4913 221 PDTFEAADALVEHFDDLERAHEALEdarEQIELL-EPIRELAERYAAARERLAELEYLRAALRLWFAQ--RRLELLEAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1416 DKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKK--QKKFDQLLAEEKnisskyadERDRAEAEAREKETKALSLARALE 1493
Cdd:COG4913 298 EELRAELARLEAELERLEARLDALREELDELEAQirGNGGDRLEQLER--------EIERLERELEERERRRARLEALLA 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1494 EALEAKEELErtnKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALK 1573
Cdd:COG4913 370 ALGLPLPASA---EEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALR 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1574 VQFERDLQARDEQ-----------NEEKRRQ--LQRQLHEYETEL--EDERKQRALAVAAKKKLEG------------DL 1626
Cdd:COG4913 447 DALAEALGLDEAElpfvgelievrPEEERWRgaIERVLGGFALTLlvPPEHYAAALRWVNRLHLRGrlvyervrtglpDP 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1627 KDLELQADS-----AIK------------GRE------EAIKQLRK------LQAQMKDFQRELE-DARASRDEIFATAK 1676
Cdd:COG4913 527 ERPRLDPDSlagklDFKphpfrawleaelGRRfdyvcvDSPEELRRhpraitRAGQVKGNGTRHEkDDRRRIRSRYVLGF 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1677 ENEKKAKSLEADLMQLQEDLAAAERARKQADLEKDELAE--ELASSVSGRNALQDEKRRLEARIAQLEEELEE-EQGNTE 1753
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQErrEALQRLAEYSWDEIDVASAEREIAELEAELERlDASSDD 686
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1754 --AMSERVRKATQQAEQLSNELATERSAAQKNENARQQLERQNKELRSKLQEMEGAVKskfkstiaalEAKIAQLEEQVE 1831
Cdd:COG4913 687 laALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLAR----------LELRALLEERFA 756
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1832 QEAREK--QATAKALKQKDKKLKEALLQVEDE-RKMAEQYKEQ--AEKGNLRVkqlkrQLEEAEE--------ESQRINA 1898
Cdd:COG4913 757 AALGDAveRELRENLEERIDALRARLNRAEEElERAMRAFNREwpAETADLDA-----DLESLPEylalldrlEEDGLPE 831
|
650 660 670
....*....|....*....|....*....|..
gi 156120901 1899 NRRKLQRELdeatesNEAMGREVTALKSKLRR 1930
Cdd:COG4913 832 YEERFKELL------NENSIEFVADLLSKLRR 857
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
848-1298 |
1.12e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 73.54 E-value: 1.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 848 TRQEEEMQAKEDELQKTKERQQKAESELKELEQKHSQLTEEKNLLQEQLQAETELYAEAEEMRVRLAAKKQELEEILhem 927
Cdd:PRK02224 359 EELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATL--- 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 928 eARLEEEEDRSQQLQAERK-----------KMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEdDILVMDDQNNK 996
Cdd:PRK02224 436 -RTARERVEEAEALLEAGKcpecgqpvegsPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAE-DLVEAEDRIER 513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 997 LSKERKLLEERISDLTTNLAEEEEKAKNLTKLKNKHESmiselEVRLKKEeksrqeleklkrkldgEASDLHEQIAELQA 1076
Cdd:PRK02224 514 LEERREDLEELIAERRETIEEKRERAEELRERAAELEA-----EAEEKRE----------------AAAEAEEEAEEARE 572
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1077 QIAELKMQLAKKEEELQaalgrlddemaqknnALKKIRELEGHISDLQEDLDS---ERAARNKAEKQKRDLGEELEALKT 1153
Cdd:PRK02224 573 EVAELNSKLAELKERIE---------------SLERIRTLLAAIADAEDEIERlreKREALAELNDERRERLAEKRERKR 637
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1154 ELEDTLDSTATqQELRAKREQEVTMLkkaldeetrshesqvqemrqkhtqvvEELTEQLEQFKRAKANLDKNKQALEKEN 1233
Cdd:PRK02224 638 ELEAEFDEARI-EEAREDKERAEEYL--------------------------EQVEEKLDELREERDDLQAEIGAVENEL 690
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 156120901 1234 AELAgELRvlsQAKQEVEHKKKKLEV---QLQELQSKYSDgekVRAELNdkvhklQNEVESVTGMLNE 1298
Cdd:PRK02224 691 EELE-ELR---ERREALENRVEALEAlydEAEELESMYGD---LRAELR------QRNVETLERMLNE 745
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
964-1475 |
1.14e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 73.80 E-value: 1.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 964 AARQKLQLekvtAEAKIKKLEDDILVMDDQNNKLSKERKLLEERISDLTTNLAEEeeKAKNLTKLKNKhesmISELEVRL 1043
Cdd:COG4913 285 FAQRRLEL----LEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGN--GGDRLEQLERE----IERLEREL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1044 KKEEKSRQELEKLKRKLDGEASDLHEQIAELQAQIAELKMQLAKKEEELQAALGRLDDEMAQKNNALKK----IRELEGH 1119
Cdd:COG4913 355 EERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELREleaeIASLERR 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1120 ISDLQEDLDSERAARNKAEKQKRD----LGEELEALKTE------LEDTLDSTAT------QQELRAKREQEVTMLKKAL 1183
Cdd:COG4913 435 KSNIPARLLALRDALAEALGLDEAelpfVGELIEVRPEEerwrgaIERVLGGFALtllvppEHYAAALRWVNRLHLRGRL 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1184 D-EETRSHESQVQEMRQKHTQVVEELT--------------------------EQLEQFKRA-------KAN-----LDK 1224
Cdd:COG4913 515 VyERVRTGLPDPERPRLDPDSLAGKLDfkphpfrawleaelgrrfdyvcvdspEELRRHPRAitragqvKGNgtrheKDD 594
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1225 NK----------------QALEKENAELAGELRVLSQAKQEVEHKKKKLEVQLQELQ--SKYSDGEKVRAELNDKVHKLQ 1286
Cdd:COG4913 595 RRrirsryvlgfdnraklAALEAELAELEEELAEAEERLEALEAELDALQERREALQrlAEYSWDEIDVASAEREIAELE 674
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1287 NEVESvtgmLNEAEGkaiklakDVASLGSQLQDTQELLQEETRQKLNVSTKLRQLEDERNSLQEQLDEEMEAKQNLERHI 1366
Cdd:COG4913 675 AELER----LDASSD-------DLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLA 743
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1367 STLNIQLSDSKKKLQDFAstvELLEEGKKKFQKEIESLTqqyEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQ------- 1439
Cdd:COG4913 744 RLELRALLEERFAAALGD---AVERELRENLEERIDALR---ARLNRAEEELERAMRAFNREWPAETADLDADleslpey 817
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 156120901 1440 ----RQLVSN-LEKKQKKFDQLLAEE-----KNISSKYADERDRAE 1475
Cdd:COG4913 818 lallDRLEEDgLPEYEERFKELLNENsiefvADLLSKLRRAIREIK 863
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
835-1593 |
1.21e-12 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 73.47 E-value: 1.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 835 WRLFTKVKPLLQVTRQEEEMQAKEDELQKTKERQQKAESELKELEQKHSQLTEEKNLLQEQLQAETELYAEAEEMRVRLA 914
Cdd:pfam02463 287 ELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQE 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 915 AKKQELEEILhemearleeeedrsqqlqaERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDDILvmDDQN 994
Cdd:pfam02463 367 KLEQLEEELL-------------------AKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLL--KEEK 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 995 NKLSKERKLLEERISDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLDGEAsdlheqiAEL 1074
Cdd:pfam02463 426 KEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKL-------EER 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1075 QAQIAELKMQLAKKEEELQAALGRLDDEMAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRdLGEELEALKTE 1154
Cdd:pfam02463 499 SQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKL-VRALTELPLGA 577
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1155 LEDTLDSTATQQELRAKREQEVTMLKKALDEETRSHESQVQEMRQKHTQVVEELTEQLEQFKRAKANLDKNKQALEKENA 1234
Cdd:pfam02463 578 RKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEG 657
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1235 ELAGELRvlsQAKQEVEHKKKKLEVQLQELQSKYSDGEKVRAELNDKVHKLQN---EVESVTGMLNEAEGKAIKLAKDVA 1311
Cdd:pfam02463 658 LAEKSEV---KASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQRekeELKKLKLEAEELLADRVQEAQDKI 734
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1312 SLGSQLQDTQELLQEETRQKLNVSTKLRQLEDERNSLQEQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFASTVELLE 1391
Cdd:pfam02463 735 NEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEA 814
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1392 EGKKKFQKEIESLTQQYEEKAAAYDKLEKTKNRLQQELDDLV-VDLDNQRQLVSNLEKKQKKFDQLLAEEKNISSKYADE 1470
Cdd:pfam02463 815 ELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELeRLEEEITKEELLQELLLKEEELEEQKLKDELESKEEK 894
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1471 RDRAEAEAREKETKALSLARALEEALEAKEELERTNKMLKAEMEDLVS----SKDDVGKNVHELEKSKRALETQMEEMKT 1546
Cdd:pfam02463 895 EKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLeeadEKEKEENNKEEEEERNKRLLLAKEELGK 974
|
730 740 750 760
....*....|....*....|....*....|....*....|....*..
gi 156120901 1547 QLEELEDELQATEDAKLRLEVNMQALKVQFERDLQARDEQNEEKRRQ 1593
Cdd:pfam02463 975 VNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKE 1021
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1075-1292 |
2.06e-12 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 70.95 E-value: 2.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1075 QAQIAELKMQLAKKEEELQAALGRLDDEMAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALKTE 1154
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1155 LEDTLDSTATQ--QELRAKREQEVTMLKKALDeetrshESQVQEMRQKHTQVVEELTEQLEQFKRAKANLDKNKQALEKE 1232
Cdd:COG4942 99 LEAQKEELAELlrALYRLGRQPPLALLLSPED------FLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1233 NAELAGELRVLSQAKQEVEHKKKKLEVQLQELQSKYSDGEKVRAELNDKVHKLQNEVESV 1292
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
998-1732 |
3.50e-12 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 71.92 E-value: 3.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 998 SKERKLLEERISDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLDGEASDLHEQIAELQAQ 1077
Cdd:TIGR00618 162 SKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQS 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1078 IAELKMQLAKKEEELQaalgrLDDEMAQKNNALKKIRELEGHISDLQEDLDSER---------AARNKAEKQKRDLGEEL 1148
Cdd:TIGR00618 242 HAYLTQKREAQEEQLK-----KQQLLKQLRARIEELRAQEAVLEETQERINRARkaaplaahiKAVTQIEQQAQRIHTEL 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1149 EALKTELEDTLDSTATQQELRAKREQEVTMLKKALDEETR-SHESQVQEMRQKHTQVVEELTEQLEQFKRAKANLDKNKQ 1227
Cdd:TIGR00618 317 QSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHiRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQ 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1228 ALEKENAELAGElrvlsQAKQEVEHKKKKLEVQLQELQSKYSDGEKVRAELndkvhkLQNEVESVTGMLNEAEGKAIKLA 1307
Cdd:TIGR00618 397 SLCKELDILQRE-----QATIDTRTSAFRDLQGQLAHAKKQQELQQRYAEL------CAAAITCTAQCEKLEKIHLQESA 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1308 KDVASLGSQLQDTQELLQEETRQKLNVSTKLRQLEDERNSLQEQLDE-EMEAKQNLERHIST-LNIQLSDSKKKLQDFAS 1385
Cdd:TIGR00618 466 QSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHpNPARQDIDNPGPLTrRMQRGEQTYAQLETSEE 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1386 TVE----LLEEGKKKFQKEIESLTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQKKFDQLLAEEK 1461
Cdd:TIGR00618 546 DVYhqltSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQ 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1462 NISSKYADERDRAEAEAREKETKALSLARALEEALEAKEELERTNKMLKAEMEDLVSSkddvgknvhELEKSKRALETQM 1541
Cdd:TIGR00618 626 DLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQ---------KMQSEKEQLTYWK 696
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1542 EEMKTQLEELEDELQATEDAKLRLEVNMQALKVQfERDLQARDEQNEEKRRQLQRQLHEYETELEDERKQRALAVAAKKK 1621
Cdd:TIGR00618 697 EMLAQCQTLLRELETHIEEYDREFNEIENASSSL-GSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQ 775
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1622 LEGDLKDLELQADSAIKGREEAIKQLRKLQAQMKDFQRELEDARASRDEIFATAKENEK-KAKSLEADLMQLQEDLAAAE 1700
Cdd:TIGR00618 776 TGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLsRLEEKSATLGEITHQLLKYE 855
|
730 740 750
....*....|....*....|....*....|....
gi 156120901 1701 RARKQADLEKDELAE--ELASSVSGRNALQDEKR 1732
Cdd:TIGR00618 856 ECSKQLAQLTQEQAKiiQLSDKLNGINQIKIQFD 889
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1337-1932 |
5.50e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 71.22 E-value: 5.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1337 KLRQLEDERNSLQEQLDEEMEAKQNLERHISTLNIQLSDSKKK---LQDFASTVELLEEGKKKFQKEIESLTQQYEEKAA 1413
Cdd:PRK02224 207 RLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERreeLETLEAEIEDLRETIAETEREREELAEEVRDLRE 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1414 AYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQKKFDQLLAEE-------KNISSKYADERDRAEAEAREKETKAl 1486
Cdd:PRK02224 287 RLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECrvaaqahNEEAESLREDADDLEERAEELREEA- 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1487 slaraleealeakeelertnKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLE 1566
Cdd:PRK02224 366 --------------------AELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELR 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1567 VNMQALkvqfERDLQARDEQNEEKRRQLQR-QLHEYETELEDERKQRALA--VAAKKKLEGDLKDLELQADSaIKGREEA 1643
Cdd:PRK02224 426 EREAEL----EATLRTARERVEEAEALLEAgKCPECGQPVEGSPHVETIEedRERVEELEAELEDLEEEVEE-VEERLER 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1644 IKQLRKLQAQMKDFQRELEDARASRDEIFATAKENEKKAKSLEADLMQLQEDLAAAERARKQADLEKDELAEELASSVSG 1723
Cdd:PRK02224 501 AEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSK 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1724 RNALQDEKRRLEariaqleeeleeeqgnteamservRKATQQAEQlsnelatersaaqknENARQQLERQNkELRSKLQE 1803
Cdd:PRK02224 581 LAELKERIESLE------------------------RIRTLLAAI---------------ADAEDEIERLR-EKREALAE 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1804 MEgavkSKFKSTIAALEAKIAQLEEQVEQEAREKqatakaLKQKDKKLKEALLQVEDE--RKMAEQYKEQAEKGNlrVKQ 1881
Cdd:PRK02224 621 LN----DERRERLAEKRERKRELEAEFDEARIEE------AREDKERAEEYLEQVEEKldELREERDDLQAEIGA--VEN 688
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 156120901 1882 LKRQLEEAEEESQRINANRRKLQRELDEATESNEAMGRevtaLKSKLRRGN 1932
Cdd:PRK02224 689 ELEELEELRERREALENRVEALEALYDEAEELESMYGD----LRAELRQRN 735
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
845-1552 |
1.04e-11 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 70.46 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 845 LQVTRQEEEMQAKEDELQKTKERQQKAESELKELEqkhsqltEEKNLLQEQLQAETELyaeaeemrvrLAAKKQELEEIL 924
Cdd:TIGR00606 398 LVIERQEDEAKTAAQLCADLQSKERLKQEQADEIR-------DEKKGLGRTIELKKEI----------LEKKQEELKFVI 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 925 HEMEARLEEEEDRSQQLQAERKKMAQQMLDLEEQLEEEEAARQK-LQLEKVTAEAKIKKLEDDILVMD------DQNNKL 997
Cdd:TIGR00606 461 KELQQLEGSSDRILELDQELRKAERELSKAEKNSLTETLKKEVKsLQNEKADLDRKLRKLDQEMEQLNhhtttrTQMEML 540
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 998 SKERKLLEERI-------SDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLDGEASDLHEQ 1070
Cdd:TIGR00606 541 TKDKMDKDEQIrkiksrhSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQ 620
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1071 IAELQAQIAElkmqlAKKEEELQAALGRLDDEMAQKNNALKKIRELEGHISDLQEDLDSERAA-------RNKAEKQKRD 1143
Cdd:TIGR00606 621 LSSYEDKLFD-----VCGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSccpvcqrVFQTEAELQE 695
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1144 LGEELEALKTELEDTLDSTATQQELRAKREQEVTMLKKALDEETRSHESQVQEMRQKHTQVVEELteqleqfKRAKANLD 1223
Cdd:TIGR00606 696 FISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDI-------QRLKNDIE 768
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1224 KNKQALEKENAELAG------ELRVLSQAKQEVEHKKKKLEVQLQELQSkySDGEKVRAELNDKVHKLQNEVESVTGMLN 1297
Cdd:TIGR00606 769 EQETLLGTIMPEEESakvcltDVTIMERFQMELKDVERKIAQQAAKLQG--SDLDRTVQQVNQEKQEKQHELDTVVSKIE 846
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1298 EaegkaikLAKDVASLGSQLQDTQELLQEETRQKLNVSTKLRQledeRNSLQEQLDEEMEAKQNLERHISTLNIQLSDSK 1377
Cdd:TIGR00606 847 L-------NRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQR----RQQFEEQLVELSTEVQSLIREIKDAKEQDSPLE 915
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1378 KKLQDFASTVELL----EEGKKKFQKEIESLTQQYEEKAAAYDKLEktkNRLQQELDDLVVDLDNQRQLV----SNLEKK 1449
Cdd:TIGR00606 916 TFLEKDQQEKEELisskETSNKKAQDKVNDIKEKVKNIHGYMKDIE---NKIQDGKDDYLKQKETELNTVnaqlEECEKH 992
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1450 QKKFDQ-LLAEEKNISSKYADERDRAEAEAREKETKALSLARALEEALEAKEELERTNKMlKAEMEDLVSSKDDVGKNVH 1528
Cdd:TIGR00606 993 QEKINEdMRLMRQDIDTQKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQVLQM-KQEHQKLEENIDLIKRNHV 1071
|
730 740
....*....|....*....|....
gi 156120901 1529 ELEKSKRALETQMEEMKTQLEELE 1552
Cdd:TIGR00606 1072 LALGRQKGYEKEIKHFKKELREPQ 1095
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
846-1170 |
1.30e-11 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 69.77 E-value: 1.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 846 QVTRQEEEMQAKEDELQKTKERQQKaESELKELEQKHsQLTEEKNLLQEQLQAETELYAEAEEM---------RVRLAAK 916
Cdd:pfam17380 281 QKAVSERQQQEKFEKMEQERLRQEK-EEKAREVERRR-KLEEAEKARQAEMDRQAAIYAEQERMamerereleRIRQEER 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 917 KQELEEIlhemeARLEEEEDRSQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDDILVMDDQNNK 996
Cdd:pfam17380 359 KRELERI-----RQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEAR 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 997 LSKERKLLEERISDLTTNLAEEEEKAKNLTKLKNKHESMISElEVRLKKEEKSRQELEKLKRKLdgeasdlheqiaeLQA 1076
Cdd:pfam17380 434 QREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRK-KLELEKEKRDRKRAEEQRRKI-------------LEK 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1077 QIAELKMQLAKKEEELQAalgrLDDEMAQKNNALKKirELEGHISDLQEDLDSERAARNKAEKQKRDLGEE---LEALKT 1153
Cdd:pfam17380 500 ELEERKQAMIEEERKRKL----LEKEMEERQKAIYE--EERRREAEEERRKQQEMEERRRIQEQMRKATEErsrLEAMER 573
|
330 340
....*....|....*....|
gi 156120901 1154 ELE---DTLDSTATQQELRA 1170
Cdd:pfam17380 574 EREmmrQIVESEKARAEYEA 593
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1277-1928 |
1.73e-11 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 69.66 E-value: 1.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1277 ELNDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLGSQLQDTQELLQEETRQKLNVSTKLRQLEDERNSLQEQLDEEM 1356
Cdd:TIGR04523 37 QLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1357 EAKQNLERHISTLNIQLSDSKKKLQDFASTVELLEEGKKKFQKEIESLTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDL 1436
Cdd:TIGR04523 117 EQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1437 DNQRQLVSNLEKKQKKFDQLLAEEKNISSKYADERDRAEAEAREKETKALSLARALEEALEAKEELERTNKMLKAEMEDL 1516
Cdd:TIGR04523 197 LKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKEL 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1517 VSSKddvgKNVHELEKskraletQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKVqfeRDLQARDEQNEEKRRQLQR 1596
Cdd:TIGR04523 277 EQNN----KKIKELEK-------QLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKL---EEIQNQISQNNKIISQLNE 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1597 QLheyetelederkqralavaakKKLEGDLKDLELQADSAIKGREEAIKQLRKLQAQMKDFQRELEDARASRDEIFATAK 1676
Cdd:TIGR04523 343 QI---------------------SQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQ 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1677 ENEKKAKSLEADLMQLQEDLAAAERarkqadlEKDELAEELASSVSGRNALQDEKRRLEARIAQLEEELEEEQGNTEAMS 1756
Cdd:TIGR04523 402 NQEKLNQQKDEQIKKLQQEKELLEK-------EIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLS 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1757 ERVRKATQQAEQLSNELATERSAAQKNENARQQLERQNKELRSKLQEMEGAVKsKFKSTIAALEAKIAQLEEQVEQEARE 1836
Cdd:TIGR04523 475 RSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIE-KLESEKKEKESKISDLEDELNKDDFE 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1837 --KQATAKALKQKDKKLKEALLQVEDERKMAEQYKEQAEKGNLRVKQLKRQLEEAEEESQrinanrrKLQRELDEATESN 1914
Cdd:TIGR04523 554 lkKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKIS-------SLEKELEKAKKEN 626
|
650
....*....|....
gi 156120901 1915 EAMGREVTALKSKL 1928
Cdd:TIGR04523 627 EKLSSIIKNIKSKK 640
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1528-1915 |
2.15e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 69.03 E-value: 2.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1528 HELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEVnmqalkVQFERDLQARDEQNEEKRRQLQRQLHEYETELED 1607
Cdd:COG4717 91 AELQEELEELEEELEELEAELEELREELEKLEKLLQLLPL------YQELEALEAELAELPERLEELEERLEELRELEEE 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1608 ERKQRALAVAAKKKLEGDLKDLELQA----DSAIKGREEAIKQLRKLQAQMKDFQRELEDARASRDEIFATAKENEKKAK 1683
Cdd:COG4717 165 LEELEAELAELQEELEELLEQLSLATeeelQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEER 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1684 SLEADLMQLQEDLAAAERARKQADLEKDELAEELASSVSGRNALQDEKRRLEARIAQLEEELEEEQGNTEAMSERVRKAT 1763
Cdd:COG4717 245 LKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEEL 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1764 QQAEQLSNELATERSAAQKNENAR-QQLERQNKELRSKLQemegavkskfkstIAALEAKIAQLEEQV----EQEAREKQ 1838
Cdd:COG4717 325 LAALGLPPDLSPEELLELLDRIEElQELLREAEELEEELQ-------------LEELEQEIAALLAEAgvedEEELRAAL 391
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 156120901 1839 ATAKALKQKDKKLKEALLQVEDERKMAEQYKEQAEKGNLRVK--QLKRQLEEAEEESQRINANRRKLQRELDEATESNE 1915
Cdd:COG4717 392 EQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEEleELEEELEELEEELEELREELAELEAELEQLEEDGE 470
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1693-1931 |
3.62e-11 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 67.10 E-value: 3.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1693 QEDLAAAERARKQADLEKDELAEELASSVSGRNALQDEKRRLEARIAQLEEELEEEQGNTEAMSERVRKATQQAEQLSNE 1772
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1773 LATERSAAQKNENARQQLERQNK-ELRSKLQEMEGAVKSK--FKSTIAALEAKIAQLEEQVEQEAREKQATAKALKQKDK 1849
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPlALLLSPEDFLDAVRRLqyLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1850 KLKEallQVEDERKMAEQYKEQAEKgnlrVKQLKRQLEEAEEESQRINANRRKLQRELDEATESNEAMGREVTALKSKLR 1929
Cdd:COG4942 179 LLAE---LEEERAALEALKAERQKL----LARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAAL 251
|
..
gi 156120901 1930 RG 1931
Cdd:COG4942 252 KG 253
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
803-1469 |
3.66e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 69.01 E-value: 3.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 803 RKAFAKRQQQLTAMKVIQRNCAAYLKLRNWQWWRLFTKVKPLLQVTRQEEEMQAKEDELQKTKERQQKAESELKELEQKH 882
Cdd:PTZ00121 1372 KKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKK 1451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 883 SQlteeknllQEQLQAEtELYAEAEEMRVRLAAKKqeleeilhemearleeeedrsqqlQAERKKMAQQMLDLEEQleee 962
Cdd:PTZ00121 1452 KA--------EEAKKAE-EAKKKAEEAKKADEAKK------------------------KAEEAKKADEAKKKAEE---- 1494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 963 eaARQKLQLEKVTAEAKIKKleddilvmdDQNNKLSKERKLLEERisdlttnLAEEEEKAKNLTKL--KNKHESMISELE 1040
Cdd:PTZ00121 1495 --AKKKADEAKKAAEAKKKA---------DEAKKAEEAKKADEAK-------KAEEAKKADEAKKAeeKKKADELKKAEE 1556
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1041 VRlKKEEKSRQELEKLKRKLDGEASDLHEQIAELQAQIAELKMQLAKKEEELQAALGRLDDEMAQKNNALKKIRELEGHI 1120
Cdd:PTZ00121 1557 LK-KAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKV 1635
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1121 SDLQEDLDSE--RAARNKAEKQKRDLGEELEALKTElEDTLDSTATQQELRAKREQEVTMLKKAldEETRSHEsQVQEMR 1198
Cdd:PTZ00121 1636 EQLKKKEAEEkkKAEELKKAEEENKIKAAEEAKKAE-EDKKKAEEAKKAEEDEKKAAEALKKEA--EEAKKAE-ELKKKE 1711
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1199 QKHTQVVEELTEQlEQFKRAKANLDKNKQALEKENAElagELRVLSQAKQEVEHKKKKLEVQLQELQSKYSdgEKVRAEL 1278
Cdd:PTZ00121 1712 AEEKKKAEELKKA-EEENKIKAEEAKKEAEEDKKKAE---EAKKDEEEKKKIAHLKKEEEKKAEEIRKEKE--AVIEEEL 1785
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1279 NDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLgsqLQDTQELLQEETRQKLNVSTKLRQLEDErnslqeqLDEEMEA 1358
Cdd:PTZ00121 1786 DEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLV---INDSKEMEDSAIKEVADSKNMQLEEADA-------FEKHKFN 1855
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1359 KQNLERHISTLNIQLSDSKKKLQDFASTVELLEEGKKKFQKEIESLTQQYEEKAAAYDkleKTKNRLQQElDDLVVDLDN 1438
Cdd:PTZ00121 1856 KNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDKDDIEREIPNNNMAGKNND---IIDDKLDKD-EYIKRDAEE 1931
|
650 660 670
....*....|....*....|....*....|.
gi 156120901 1439 QRQLVSNLEKKQKKFDqllaeekNISSKYAD 1469
Cdd:PTZ00121 1932 TREEIIKISKKDMCIN-------DFSSKFCD 1955
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1504-1892 |
4.95e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 68.17 E-value: 4.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1504 RTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLE---VNMQALKVQfERDL 1580
Cdd:PRK03918 172 KEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEelkEEIEELEKE-LESL 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1581 QARDEQNEEKRRQLQRQLHEYETELEDERKQRALAVAAKKKLEGDLKDLELQaDSAIKGREEAIKQLRKLQAQMKDFQRE 1660
Cdd:PRK03918 251 EGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFY-EEYLDELREIEKRLSRLEEEINGIEER 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1661 LEDARASRDEIfataKENEKKAKSLEADLMQLQEDLAAAERAR-----------KQADLEKDELAEELASSVSGRNALQD 1729
Cdd:PRK03918 330 IKELEEKEERL----EELKKKLKELEKRLEELEERHELYEEAKakkeelerlkkRLTGLTPEKLEKELEELEKAKEEIEE 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1730 EKRRLEARIAQLEEELEEEQGNTEAMSERVRKATQQAEQLSNE----LATERSAAQKN-ENARQQLERQNKELRSKLQEM 1804
Cdd:PRK03918 406 EISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEhrkeLLEEYTAELKRiEKELKEIEEKERKLRKELREL 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1805 EGAVK-----SKFKSTIAALEAKIAQLEEQVEQEAREKQATAKALKQKDKKLKEALLQVEDERKMAEQYKEQAEKGNLRV 1879
Cdd:PRK03918 486 EKVLKkeselIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKL 565
|
410
....*....|...
gi 156120901 1880 KQLKRQLEEAEEE 1892
Cdd:PRK03918 566 DELEEELAELLKE 578
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1316-1735 |
8.51e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 67.10 E-value: 8.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1316 QLQDTQELLQEETRQKLNVSTKLRQLEDERNSLQEQLD--EEMEAKQNLERHISTLNIQLSDSKKKLQDFASTVELLEEg 1393
Cdd:COG4717 82 EAEEKEEEYAELQEELEELEEELEELEAELEELREELEklEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRE- 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1394 kkkFQKEIESLTQQYEE-KAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQKKFDQLLAEEKNISSKYADERD 1472
Cdd:COG4717 161 ---LEEELEELEAELAElQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELE 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1473 RAEAEAREKETKALSLARALEEALEAKEELERTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELE 1552
Cdd:COG4717 238 AAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELE 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1553 DELQATEDAKLRLEVNMQA--LKVQFERDLQARDEQNEEKRRQLQRQLHEYETEL-----------EDERKQRALAVAAK 1619
Cdd:COG4717 318 EEELEELLAALGLPPDLSPeeLLELLDRIEELQELLREAEELEEELQLEELEQEIaallaeagvedEEELRAALEQAEEY 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1620 KKLEGDLKDLELQADSAIKGREEAIKQLRK--LQAQMKDFQRELEDARASRDEIFATAKENEKKAKSLEADlmqlqEDLA 1697
Cdd:COG4717 398 QELKEELEELEEQLEELLGELEELLEALDEeeLEEELEELEEELEELEEELEELREELAELEAELEQLEED-----GELA 472
|
410 420 430
....*....|....*....|....*....|....*...
gi 156120901 1698 AAERARKQADLEKDELAEELASSVSGRNALQDEKRRLE 1735
Cdd:COG4717 473 ELLQELEELKAELRELAEEWAALKLALELLEEAREEYR 510
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
846-1370 |
8.96e-11 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 67.35 E-value: 8.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 846 QVTRQEEEMQAKEDELQKTKERQQKaesELKELEQKHSQLTEEKNLLQEQLQAETELYAEAEEMrvrlaaKKQELEEILH 925
Cdd:TIGR04523 240 EINEKTTEISNTQTQLNQLKDEQNK---IKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDL------NNQKEQDWNK 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 926 EMEARLEEEEDRSQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDDILVMDDQNNKLSKERKLLE 1005
Cdd:TIGR04523 311 ELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1006 ERISDLTTNLAEEEEKAKNLtklknkhESMISELEVRLKKEEKSRQELEKLKRKLDGEASDLHEQIAELQAQIAELKmql 1085
Cdd:TIGR04523 391 SQINDLESKIQNQEKLNQQK-------DEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLD--- 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1086 aKKEEELQaalgrlddemaqknnalKKIRELEGHISDLQEDLDseraARNKAEKQKRDLGEELEALKTELEDTLDSTATQ 1165
Cdd:TIGR04523 461 -NTRESLE-----------------TQLKVLSRSINKIKQNLE----QKQKELKSKEKELKKLNEEKKELEEKVKDLTKK 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1166 QELRAKREQEVTMLKKALDEETRSHESQVQEMRQKHT-----QVVEELTEQLEQFKRAKANLDKNKQALEKENAELAGEL 1240
Cdd:TIGR04523 519 ISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKkenleKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEK 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1241 RVLSQAKQEVEHKKKKLEVQLQELQSKYSDGEKVRAELNDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLGSQLQDT 1320
Cdd:TIGR04523 599 KDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDDI 678
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1321 QELLQEETRQKLNVSTK----------LRQLEDERNSLQEQLDEEMEAKQNLERHISTLN 1370
Cdd:TIGR04523 679 IELMKDWLKELSLHYKKyitrmirikdLPKLEEKYKEIEKELKKLDEFSKELENIIKNFN 738
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
850-1263 |
9.77e-11 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 67.05 E-value: 9.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 850 QEEEMQAKEDELQKTKERQQKAESELKELEQ----KHSQLTEEKNLLQEQlqaETELY--AEAEEMRVRLAAKKQELEEI 923
Cdd:pfam05483 368 EQQRLEKNEDQLKIITMELQKKSSELEEMTKfknnKEVELEELKKILAED---EKLLDekKQFEKIAEELKGKEQELIFL 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 924 LHEMEARLeeeedRSQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAkikkleddilvmddqnNKLSKERKL 1003
Cdd:pfam05483 445 LQAREKEI-----HDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHC----------------DKLLLENKE 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1004 LEERISDLTTNLAEEEEKAKNltkLKNKHESMISELEVRLKKEEKSRQELEKLKRKLDGEASDLHEQIAELQAQIAELKM 1083
Cdd:pfam05483 504 LTQEASDMTLELKKHQEDIIN---CKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEY 580
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1084 QLAKKEEELQAALGRLDDEMAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALKTELEDTLDSTA 1163
Cdd:pfam05483 581 EVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQ 660
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1164 TQQELRAKREQ--------------EVTMLKKALDEETRSHESQVQEMRQKHT----QVVEELTEQLEQFKRAKANLDKN 1225
Cdd:pfam05483 661 KEIEDKKISEEklleevekakaiadEAVKLQKEIDKRCQHKIAEMVALMEKHKhqydKIIEERDSELGLYKNKEQEQSSA 740
|
410 420 430
....*....|....*....|....*....|....*...
gi 156120901 1226 KQALEKENAELAGELRVLSQAKQEVEHKKKKLEVQLQE 1263
Cdd:pfam05483 741 KAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKE 778
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
967-1732 |
1.16e-10 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 66.67 E-value: 1.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 967 QKLQLEKVTAEAKIKKLEDDilvMDDQNNKLSKERKLLEE---RISDLTTNLAEEEEKAKNLTKLKNKHESMISELEV-- 1041
Cdd:pfam05483 88 EKIKKWKVSIEAELKQKENK---LQENRKIIEAQRKAIQElqfENEKVSLKLEEEIQENKDLIKENNATRHLCNLLKEtc 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1042 -----RLKKEEKSRQELEKLKRKLDGEASDLHEQIAELQAQIAELKMQLAKKEEELQAALGRLDDEMAQKNN-------- 1108
Cdd:pfam05483 165 arsaeKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEINdkekqvsl 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1109 ALKKIRELEGHISDLQEDLDSERAARNKAEkqkrdlgeelEALKTELEDTLDSTATQQELRAKREQEVTMLKKALDEEtR 1188
Cdd:pfam05483 245 LLIQITEKENKMKDLTFLLEESRDKANQLE----------EKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQ-K 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1189 SHESQVQEMRQKHTQVVEELTEQLEQFKRAKANLDKNKQALEKENAELAGELRVlsqAKQEVEHKKKKLEVQLQELQSKY 1268
Cdd:pfam05483 314 ALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRT---EQQRLEKNEDQLKIITMELQKKS 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1269 SDGEKVRAELNDKvhklqnEVEsvtgmlneaegkaiklakdVASLGSQLQDTQELLQEEtrqklnvstklRQLEDERNSL 1348
Cdd:pfam05483 391 SELEEMTKFKNNK------EVE-------------------LEELKKILAEDEKLLDEK-----------KQFEKIAEEL 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1349 QEQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFASTVElleegkkKFQKEIESLTQQYEEKAAAYDKLEKTKNRLQQE 1428
Cdd:pfam05483 435 KGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVE-------DLKTELEKEKLKNIELTAHCDKLLLENKELTQE 507
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1429 LDDLVVDLDNQRQLVSNLEKKQ----KKFDQLLAEEKNISSKYADERDRAEAEAREKETKALSLARALEEALEAKEELER 1504
Cdd:pfam05483 508 ASDMTLELKKHQEDIINCKKQEermlKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEK 587
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1505 TNKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQatedaklRLEVNMQALKVQFErdlqard 1584
Cdd:pfam05483 588 QMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVN-------KLELELASAKQKFE------- 653
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1585 eqneekrrqlqRQLHEYETELEDERkqralavAAKKKLEGDLKDLELQADSAIKGREEAIK----QLRKLQAQMKDFQRE 1660
Cdd:pfam05483 654 -----------EIIDNYQKEIEDKK-------ISEEKLLEEVEKAKAIADEAVKLQKEIDKrcqhKIAEMVALMEKHKHQ 715
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 156120901 1661 LEDARASRDEIFATAKENEKKAKSLEADL-MQLQEDLAAAERARKQADLEKDElAEELASSVSGRNALQDEKR 1732
Cdd:pfam05483 716 YDKIIEERDSELGLYKNKEQEQSSAKAALeIELSNIKAELLSLKKQLEIEKEE-KEKLKMEAKENTAILKDKK 787
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
809-1482 |
1.29e-10 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 66.99 E-value: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 809 RQQQLTAMKVIQRNCAAYLKLRNWqwwRLFTKVKPLLQVTRQEEEMQAKEDELQKTKERQQKAESELKELEQKHS---QL 885
Cdd:TIGR00606 424 KQEQADEIRDEKKGLGRTIELKKE---ILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLtetLK 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 886 TEEKNLLQEQLQAETELYAEAEEMrvrlaAKKQELEEILHEMEARLEEEEDRSQQLQAERKKMAQQMLDLEEQ---LEEE 962
Cdd:TIGR00606 501 KEVKSLQNEKADLDRKLRKLDQEM-----EQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYfpnKKQL 575
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 963 EAARQKLQLEKVTAEAKIKKLEDDILVMDDQNNKLSKERKLLEERISDLTTNLAE------EEEKAKNLTKLKNK----- 1031
Cdd:TIGR00606 576 EDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDvcgsqdEESDLERLKEEIEKsskqr 655
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1032 ---------HESMISELEVRLKKEEKSRQELEKLKRKLDGEASDLHEQIAELQAQIAELKMQLAKKEEELQAALGRLDDE 1102
Cdd:TIGR00606 656 amlagatavYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGR 735
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1103 MAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALKTELEDTLDSTATQQELRAKREQEVTMLKKA 1182
Cdd:TIGR00606 736 QSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKL 815
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1183 LDEETRSHESQVQEMRQKHTQVVEELTEQLEQFKRAKANLDKNKQALEKENAELAGELRVLSQAKQEVEHKKKKLEVQLQ 1262
Cdd:TIGR00606 816 QGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELST 895
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1263 ELQSKYSDGEKVRAE---LNDKVHKLQNEVESVTGMLNEAEGKAiklakdvaslgsqlQDTQELLQEETRQKLNvstklr 1339
Cdd:TIGR00606 896 EVQSLIREIKDAKEQdspLETFLEKDQQEKEELISSKETSNKKA--------------QDKVNDIKEKVKNIHG------ 955
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1340 QLEDERNSLQEQLDEEMEAKQNlerHISTLNIQLSDSKKKLQDFASTVELLEEGKKKfQKEIESLTQQYEEKAAAYDKLE 1419
Cdd:TIGR00606 956 YMKDIENKIQDGKDDYLKQKET---ELNTVNAQLEECEKHQEKINEDMRLMRQDIDT-QKIQERWLQDNLTLRKRENELK 1031
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156120901 1420 KTKNRLQQELDDLvvDLDNQRQLVSNLEKKQKKFDQLLAEEKNISSK---YADERDRAEAEAREKE 1482
Cdd:TIGR00606 1032 EVEEELKQHLKEM--GQMQVLQMKQEHQKLEENIDLIKRNHVLALGRqkgYEKEIKHFKKELREPQ 1095
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
846-1661 |
1.55e-10 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 66.61 E-value: 1.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 846 QVTRQEEEMQAKEDELQKTKERQQKAESELKELEQKHSQLTEEKNLLQEQLQAETelyAEAEEMRVRLAAKKQELEEILH 925
Cdd:TIGR00606 313 TVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARD---SLIQSLATRLELDGFERGPFSE 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 926 EMEARLEEEEDRSQQLQAerkKMAQQMLDleeqleeeeaarqKLQLEKVTAEAKIKKLEDDilvMDDQNNKLSKERKLLE 1005
Cdd:TIGR00606 390 RQIKNFHTLVIERQEDEA---KTAAQLCA-------------DLQSKERLKQEQADEIRDE---KKGLGRTIELKKEILE 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1006 ERISDLTTNLAEEEEKAKNLTKLKNKHESMI-SELEVRLKKEEKSRQELEKLKRKLDGEASDLHEQIAELQAQIAELKMQ 1084
Cdd:TIGR00606 451 KKQEELKFVIKELQQLEGSSDRILELDQELRkAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHH 530
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1085 LAKKEEELQAALGRLDDEMAQKNNALKKIRELEGHISD------LQEDLDSERAARNKAEKQKRDLGEELEALKTeledt 1158
Cdd:TIGR00606 531 TTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYfpnkkqLEDWLHSKSKEINQTRDRLAKLNKELASLEQ----- 605
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1159 lDSTATQQELRAKREQEVTMLKKALDE-ETRSHESQVQEMRQKhtqvVEELTEQLEQFKRAKANLDKNKQALEKENAELA 1237
Cdd:TIGR00606 606 -NKNHINNELESKEEQLSSYEDKLFDVcGSQDEESDLERLKEE----IEKSSKQRAMLAGATAVYSQFITQLTDENQSCC 680
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1238 GELRVLSQAKQEVEHKKKKLE-------VQLQELQSKYSDGEKVRAELNDKVHKLQNEVESVTGMLNEAEGKAIKLAKDV 1310
Cdd:TIGR00606 681 PVCQRVFQTEAELQEFISDLQsklrlapDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDI 760
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1311 ASLGSQLQDTQELLqeetrQKLNVSTKLRQLEDERNSLQEQLDEEMEakqNLERHISTLNIQLSDSkkklqDFASTVELL 1390
Cdd:TIGR00606 761 QRLKNDIEEQETLL-----GTIMPEEESAKVCLTDVTIMERFQMELK---DVERKIAQQAAKLQGS-----DLDRTVQQV 827
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1391 EEGKKKFQKEIESLTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDldnQRQLVSNLEKKQKKFDQLLAEEKNISSKYADE 1470
Cdd:TIGR00606 828 NQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSE---KLQIGTNLQRRQQFEEQLVELSTEVQSLIREI 904
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1471 RDRAEAEAREKETKALSLARALEEALEAKEelerTNKMLKAEMEDLVSSKDDVGKNVHELEKS-KRALETQMEEMKTQLE 1549
Cdd:TIGR00606 905 KDAKEQDSPLETFLEKDQQEKEELISSKET----SNKKAQDKVNDIKEKVKNIHGYMKDIENKiQDGKDDYLKQKETELN 980
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1550 ELEDELQATEDAKLRLEVNMQALKVQFE-RDLQARDEQNEEKRRQLQRQLheyeTELEDERKQRALAVAAKKKLEGDLKD 1628
Cdd:TIGR00606 981 TVNAQLEECEKHQEKINEDMRLMRQDIDtQKIQERWLQDNLTLRKRENEL----KEVEEELKQHLKEMGQMQVLQMKQEH 1056
|
810 820 830
....*....|....*....|....*....|....*
gi 156120901 1629 LELQADSAIKGREE--AIKQLRKLQAQMKDFQREL 1661
Cdd:TIGR00606 1057 QKLEENIDLIKRNHvlALGRQKGYEKEIKHFKKEL 1091
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1345-1802 |
1.85e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 65.94 E-value: 1.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1345 RNSLQEQLDEEMEAKQNLERHISTLNI-QLSDSKKKLQDFASTVELLEEgkkkFQKEIESLTQQYEEKAAAYDKLEKTKN 1423
Cdd:COG4717 44 RAMLLERLEKEADELFKPQGRKPELNLkELKELEEELKEAEEKEEEYAE----LQEELEELEEELEELEAELEELREELE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1424 RLQQELDdLVVDLDNQRQLVSNLEKKQKKFDQLLAEEKNISSKyADERDRAEAEAREKETKALSLARaleealeakeele 1503
Cdd:COG4717 120 KLEKLLQ-LLPLYQELEALEAELAELPERLEELEERLEELREL-EEELEELEAELAELQEELEELLE------------- 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1504 RTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDAK--------------------- 1562
Cdd:COG4717 185 QLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEErlkearlllliaaallallgl 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1563 --------------LRLEVNMQALKVQFERDLQARDEQNEEKRRQLQRQLHEYETELEDERKQRALAVAAKKKLEGDLKD 1628
Cdd:COG4717 265 ggsllsliltiagvLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLD 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1629 LELQADSAIKGREEAIKQLRkLQAQMKDFQRELEDARASRDEIFATAKENEKKAKSLEADLMQLQEDLAAAERARKQ--A 1706
Cdd:COG4717 345 RIEELQELLREAEELEEELQ-LEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEEllE 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1707 DLEKDELAEELASSVSGRNALQDEKRRLEARIAQLEEELEEEQGnteamSERVRKATQQAEQLSNELATERSAAQKNENA 1786
Cdd:COG4717 424 ALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEE-----DGELAELLQELEELKAELRELAEEWAALKLA 498
|
490
....*....|....*.
gi 156120901 1787 RQQLERQNKELRSKLQ 1802
Cdd:COG4717 499 LELLEEAREEYREERL 514
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1240-1929 |
1.86e-10 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 66.61 E-value: 1.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1240 LRVLSQAKQEVEHKKKKLEVQLQELQSKYSDGEKVRAELNDKVHKLQNEVESVTGMLNEAEGKAIKLaKDVASLGSQLQD 1319
Cdd:TIGR00606 188 LETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRL-KEIEHNLSKIMK 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1320 TQELLQEETRQKLNVSTKLRQLEDERNSLQEQLDEEM-EAKQNLERHISTLNIQLSDSKKKLQDFASTVELLEEGKKKFQ 1398
Cdd:TIGR00606 267 LDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLnDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1399 KEIESLTQQYE---EKAAAYDkLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQKKFDQLLAEEKNISSKYADERDRAE 1475
Cdd:TIGR00606 347 VEQGRLQLQADrhqEHIRARD-SLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQ 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1476 AEAREKETKALSLARALEEALEAKEELERTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQmeemktqleeledEL 1555
Cdd:TIGR00606 426 EQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKA-------------EK 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1556 QATEDAKLRLEVNMQALKVQFERDLQARDEQNEEKRRQ---------LQRQLHEYETELEDERKQRALAVAA-------- 1618
Cdd:TIGR00606 493 NSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHtttrtqmemLTKDKMDKDEQIRKIKSRHSDELTSllgyfpnk 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1619 -------------KKKLEGDLKDLELQADSAIKGREEAIKQLRKLQAQMKDFQRELEDARASRDE--------------- 1670
Cdd:TIGR00606 573 kqledwlhskskeINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEesdlerlkeeiekss 652
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1671 ---------------------------------IFATAKENEKKAKSLEADLMQLQEDLAAAERARKQADLEKDELAEEL 1717
Cdd:TIGR00606 653 kqramlagatavysqfitqltdenqsccpvcqrVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLA 732
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1718 ASSVSGRNALQDEKRRLEARIAQLEEELEEEQGNTEAmSERVRKATQQAEQLSNELATERSAAQKNENARQQLERQNKEL 1797
Cdd:TIGR00606 733 PGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEE-QETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQ 811
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1798 RSKLQEMEGAVK----SKFKSTIAALEAKIAQLEEQVEQEAREKQATAKALKQKDKKLKEALLQVEDERKMAEQYKEQAE 1873
Cdd:TIGR00606 812 AAKLQGSDLDRTvqqvNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLV 891
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1874 KGNLRVKQLKRQLEEAEEESQRINANRRKLQRELDEAT----ESNEAMGREVTALKSKLR 1929
Cdd:TIGR00606 892 ELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELIsskeTSNKKAQDKVNDIKEKVK 951
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1529-1756 |
3.29e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 64.40 E-value: 3.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1529 ELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKVQfERDLQARDEQNEEKRRQLQRQLHEYETELEDE 1608
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARR-IRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1609 RKQRA--LAVAAKKKLEGDLKDLELQADSAikgreEAIKQLRKLQAQMKDFQRELEDARASRDEIFATAKENEKKAKSLE 1686
Cdd:COG4942 103 KEELAelLRALYRLGRQPPLALLLSPEDFL-----DAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1687 ADLMQLQEDLAAAERARKQADLEKDELAEELASSVSGRNALQDEKRRLEARIAQLEEELEEEQGNTEAMS 1756
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
992-1218 |
4.73e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 63.63 E-value: 4.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 992 DQNNKLSKERKLLEERISDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLDGEASDLHEQI 1071
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1072 AELQAQIAELKMQLAKKEEELQAALGRLDDEMAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEAL 1151
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156120901 1152 KTELEDTLDSTATQQELRAKREQEVTMLKKALDEETRSHESQVQEMRQKHTQVVEELTEQLEQFKRA 1218
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
863-1482 |
4.87e-10 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 64.74 E-value: 4.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 863 KTKERQQKAESELKELEQKHSQLTeekNLLQEQLQAETELYAEAEEMRVRLAAKkqeleeilhemearLEEEEDRSQQLQ 942
Cdd:pfam05483 166 RSAEKTKKYEYEREETRQVYMDLN---NNIEKMILAFEELRVQAENARLEMHFK--------------LKEDHEKIQHLE 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 943 AERKKMAQQmldleeqleeeeaARQKLQLEKVTAEAKIKKLEDDILVMDDQNNKLSKerklLEERISDLTTNLAEEEEKA 1022
Cdd:pfam05483 229 EEYKKEIND-------------KEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQ----LEEKTKLQDENLKELIEKK 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1023 KNLTK-LKNKHESMISELEVRLKKEEK---SRQELEKLKRKLDGEASDLHEQIAELQAQIAELKMQLAKKEEELQAALGR 1098
Cdd:pfam05483 292 DHLTKeLEDIKMSLQRSMSTQKALEEDlqiATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQR 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1099 LDDEMAQknnaLKKIR-ELEGHISDLQEDLDSERAARNKAEKQKRDLGEElealKTELEDTLDSTATQQELRAKrEQEVT 1177
Cdd:pfam05483 372 LEKNEDQ----LKIITmELQKKSSELEEMTKFKNNKEVELEELKKILAED----EKLLDEKKQFEKIAEELKGK-EQELI 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1178 MLKKALDEETRSHESQVQEMR---QKHTQVVEELTEQLEQFKRAKANLDKNKQALEKENAELAGELR----VLSQAKQEV 1250
Cdd:pfam05483 443 FLLQAREKEIHDLEIQLTAIKtseEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASdmtlELKKHQEDI 522
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1251 EHKKKKLEVQLQELQSKYSDGEKVRAELNDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLGSQLQDTQELLQEETRQ 1330
Cdd:pfam05483 523 INCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQ 602
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1331 KLNVSTKLRQLEDERNSLQEQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFASTVE------------LLEEGKK--- 1395
Cdd:pfam05483 603 IENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQkeiedkkiseekLLEEVEKaka 682
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1396 ------KFQKEIESLTQQYEEKAAAYdkLEKTKNrlqqELDDLVVDLDNQRQLVSNLEKKQKKFDQLLAEE-KNISSKYA 1468
Cdd:pfam05483 683 iadeavKLQKEIDKRCQHKIAEMVAL--MEKHKH----QYDKIIEERDSELGLYKNKEQEQSSAKAALEIElSNIKAELL 756
|
650
....*....|....
gi 156120901 1469 DERDRAEAEAREKE 1482
Cdd:pfam05483 757 SLKKQLEIEKEEKE 770
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
850-1073 |
5.04e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 63.63 E-value: 5.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 850 QEEEMQAKEDELQKTKERQQKAESELKELEQKHSQLTEEKNLLQEQLQAETELYAEAEEMRVRLAAKKQELE-EILHEME 928
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEkEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 929 ARLEEEEDRSQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDdilvMDDQNNKLSKERKLLEERI 1008
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEE----LRADLAELAALRAELEAER 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 156120901 1009 SDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLDGEASDLHEQIAE 1073
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1649-1910 |
5.79e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 64.69 E-value: 5.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1649 KLQAQMKDFQRELEDARASRDEIFATAKENEKKAKSLEA------DLMQLQEDLAAAERA-----RKQADLEKDELAEEL 1717
Cdd:TIGR02168 169 KYKERRKETERKLERTRENLDRLEDILNELERQLKSLERqaekaeRYKELKAELRELELAllvlrLEELREELEELQEEL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1718 ASSVSGRNALQDEKRRLEARIAQLEEELEEeqgnteaMSERVRKATQQAEQLSNELATERSAAQKNENARQQLERQNKEL 1797
Cdd:TIGR02168 249 KEAEEELEELTAELQELEEKLEELRLEVSE-------LEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEEL 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1798 RSKLQEMEgAVKSKFKSTIAALEAKIAQLEEQVEQEAREKQATAKALKQKDKKLKEALLQVEDERKMAEQYKEQAEKGNL 1877
Cdd:TIGR02168 322 EAQLEELE-SKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNN 400
|
250 260 270
....*....|....*....|....*....|...
gi 156120901 1878 RVKQLKRQLEEAEEESQRINANRRKLQRELDEA 1910
Cdd:TIGR02168 401 EIERLEARLERLEDRRERLQQEIEELLKKLEEA 433
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1526-1927 |
8.65e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 64.39 E-value: 8.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1526 NVHELEKSKRALETQMEEMKTQLEELE-------DELQATEDAKLRLEvnmQALKVQFERDLQARDEQNEEKRRQLQRQL 1598
Cdd:PTZ00121 1054 GNHEGKAEAKAHVGQDEGLKPSYKDFDfdakednRADEATEEAFGKAE---EAKKTETGKAEEARKAEEAKKKAEDARKA 1130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1599 HEYETELEDERKQRALAVAAKKKLEGDLKDLELQADSAIKGREEAIKQLRKLQAQMKDFQRELEDARASRDEIFATAKEN 1678
Cdd:PTZ00121 1131 EEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEE 1210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1679 EKKAKSLEAdlmqlQEDLAAAERARKQADLEKDElaEELASSVSGRNALQDEKRRlEARIAQLEEELEEEQGNTEAMSER 1758
Cdd:PTZ00121 1211 ERKAEEARK-----AEDAKKAEAVKKAEEAKKDA--EEAKKAEEERNNEEIRKFE-EARMAHFARRQAAIKAEEARKADE 1282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1759 VRKATQ--QAEQL--SNELATERSAAQKNENARQQLERQNKELRSKlqEMEGAVKSKFKSTIAALEAKIAQlEEQVEQEA 1834
Cdd:PTZ00121 1283 LKKAEEkkKADEAkkAEEKKKADEAKKKAEEAKKADEAKKKAEEAK--KKADAAKKKAEEAKKAAEAAKAE-AEAAADEA 1359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1835 REKQATAKALKQK---DKKLKEALLQVEDERKMAEQYKEQAEKGNLRVKQLKRQLEE---AEEESQRINANRR--KLQRE 1906
Cdd:PTZ00121 1360 EAAEEKAEAAEKKkeeAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAkkkADEAKKKAEEKKKadEAKKK 1439
|
410 420
....*....|....*....|.
gi 156120901 1907 LDEATESNEAMGREVTALKSK 1927
Cdd:PTZ00121 1440 AEEAKKADEAKKKAEEAKKAE 1460
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1414-1910 |
1.16e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.54 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1414 AYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQKKFDQLLAEEKNISSKyaDERDRAEAEAREKETKALslarale 1493
Cdd:PRK03918 163 AYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSE--LPELREELEKLEKEVKEL------- 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1494 ealeakeelertnKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELED------ELQATEDAKLRLEV 1567
Cdd:PRK03918 234 -------------EELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEkvkelkELKEKAEEYIKLSE 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1568 NMQALKVQfERDLQARDEQNEEKRRQLQRQLHEYEtelEDERKQRALavaaKKKLEGDLKDLElqadsAIKGREEAIKQL 1647
Cdd:PRK03918 301 FYEEYLDE-LREIEKRLSRLEEEINGIEERIKELE---EKEERLEEL----KKKLKELEKRLE-----ELEERHELYEEA 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1648 RKLQAQMKDFQRELEDAraSRDEIFATAKENEKKAKSLEADLMQLQEDLAAAERARKQADLEKDELAE-ELASSVSGRNA 1726
Cdd:PRK03918 368 KAKKEELERLKKRLTGL--TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKaKGKCPVCGREL 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1727 LQDEKRRLEARIAQLEEELEEEQGNTEAMSERVRKATQQAEQLSN---ELATERSAAQKNENARQQLERQNKE------- 1796
Cdd:PRK03918 446 TEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKkesELIKLKELAEQLKELEEKLKKYNLEelekkae 525
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1797 ----LRSKLQEMEGAVKSKFK--STIAALEAKIAQLEEQVEQEAREKQATAKALKQKD----KKLKEALLQVED------ 1860
Cdd:PRK03918 526 eyekLKEKLIKLKGEIKSLKKelEKLEELKKKLAELEKKLDELEEELAELLKELEELGfesvEELEERLKELEPfyneyl 605
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 156120901 1861 ERKMAEQYKEQAEKgnlRVKQLKRQLEEAEEESQRINANRRKLQRELDEA 1910
Cdd:PRK03918 606 ELKDAEKELEREEK---ELKKLEEELDKAFEELAETEKRLEELRKELEEL 652
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1287-1710 |
1.35e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 63.25 E-value: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1287 NEVESVTGMLNEAEGKA---IKLAKDVASLGSQLQDTQELLQE--ETRQKLNVSTKLRQLEDERNSLQEQLDEEMEAKQN 1361
Cdd:COG4717 71 KELKELEEELKEAEEKEeeyAELQEELEELEEELEELEAELEElrEELEKLEKLLQLLPLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1362 LERHISTLNIQLSDSKKKLQDFAST----VELLEEGKKKFQKEIESLTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLD 1437
Cdd:COG4717 151 LEERLEELRELEEELEELEAELAELqeelEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1438 N--QRQLVSNLEKKQKKFDQLLAEEKNISSKYADERDRAEAEAREKETKALSLA----------RALEEALEAKEELERT 1505
Cdd:COG4717 231 QleNELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGllallflllaREKASLGKEAEELQAL 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1506 NKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQ--ATEDAKLRLEVNMQALKVQFERDLQAR 1583
Cdd:COG4717 311 PALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEelQLEELEQEIAALLAEAGVEDEEELRAA 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1584 DEQNEEkRRQLQRQLHEYETELEDERK--QRALAVAAKKKLEGDLKDLELQADSAIKGREEAIKQLRKLQAQMKDF--QR 1659
Cdd:COG4717 391 LEQAEE-YQELKEELEELEEQLEELLGelEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLeeDG 469
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 156120901 1660 ELEDARASRDEIFATAKENEKKAKSLEADLMQLQEDLAAAERARKQADLEK 1710
Cdd:COG4717 470 ELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERLPPVLER 520
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
936-1165 |
1.93e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 61.70 E-value: 1.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 936 DRSQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDDILVMDDQNNKLSKERKLLEERISDLTTNL 1015
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1016 AEEEEKAKNLTKLKNKHeSMISELEVRLKKEekSRQELEKLKRKLDGEASDLHEQIAELQAQIAELKMQLAKKEEELQAA 1095
Cdd:COG4942 100 EAQKEELAELLRALYRL-GRQPPLALLLSPE--DFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1096 LGRLDDEMAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALKTELEDTLDSTATQ 1165
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1677-1903 |
3.45e-09 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 61.96 E-value: 3.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1677 ENEKKAKSLEADLMQLQEDLAAAERARKQ---------ADLEKDELAEELASSVSGRNALQDEKRRLEARIAQLEEELEE 1747
Cdd:COG3206 172 EARKALEFLEEQLPELRKELEEAEAALEEfrqknglvdLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGS 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1748 EQGNTEAM--SERVRKATQQAEQLSNELATERSAAQKNENARQQLERQNKELRSKLQEMEGAVKSKFKSTIAALEAKIAQ 1825
Cdd:COG3206 252 GPDALPELlqSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREAS 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1826 LEEQVEQEarekQATAKALKQKDKKLKEALLQVEDERKMAEQYKEQAEKGNLRVKQLK---RQLEEAEEESQRINANRRK 1902
Cdd:COG3206 332 LQAQLAQL----EARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEALTVgnvRVIDPAVVPLKPVSPKKLL 407
|
.
gi 156120901 1903 L 1903
Cdd:COG3206 408 I 408
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1538-1780 |
3.72e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 61.00 E-value: 3.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1538 ETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKVQFErDLQARDEQNEEKRRQLQRQLHEYETELEDERKQRALAVA 1617
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYN-ELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1618 AKKKLEGDLKDLE--LQADSAikgrEEAIKQLRKLQAQMKDFQRELEDARASRDEIFATAKENEKKAKSLEADLMQLQED 1695
Cdd:COG3883 94 ALYRSGGSVSYLDvlLGSESF----SDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1696 LAAAERARKQADLEKDELAEELASSVSGRNALQDEKRRLEARIAQLEEELEEEQGNTEAMSERVRKATQQAEQLSNELAT 1775
Cdd:COG3883 170 KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGA 249
|
....*
gi 156120901 1776 ERSAA 1780
Cdd:COG3883 250 GAAGA 254
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
846-1377 |
3.86e-09 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 62.05 E-value: 3.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 846 QVTRQEEEMQAKEDELQKTKERQQKAESELKELEQKHSQLTEEKNLLQEQLQAETELYAEAEEmrvrlaAKKQELEEILH 925
Cdd:pfam05483 269 KANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTE------EKEAQMEELNK 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 926 EMEARLEEEEDRSQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDDILVMDDQNNKLSKERKLLE 1005
Cdd:pfam05483 343 AKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLD 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1006 ERISdlTTNLAEE-EEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLDGEASDLHEQIAELQAQIAELKMQ 1084
Cdd:pfam05483 423 EKKQ--FEKIAEElKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLE 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1085 LAKKEEELQAALGRLDDEMAQKNNALKKIRELEGHISDLQEdldSERAARNKAEKQKRDLGEELEALKTELEDTLDSTAT 1164
Cdd:pfam05483 501 NKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEE---KEMNLRDELESVREEFIQKGDEVKCKLDKSEENARS 577
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1165 QQELRAKREQEVTMLKKA---LDEETRSHESQVQEMRQKHTQVVEELTEQLEQFKRAKANLdkNKQALEKENAELAGElR 1241
Cdd:pfam05483 578 IEYEVLKKEKQMKILENKcnnLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKV--NKLELELASAKQKFE-E 654
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1242 VLSQAKQEVEHKKKKLEVQLQELqskysdgEKVRAELNDKVhKLQNEVE-----SVTGMLNEAEGKAIKLAKDVASLGSQ 1316
Cdd:pfam05483 655 IIDNYQKEIEDKKISEEKLLEEV-------EKAKAIADEAV-KLQKEIDkrcqhKIAEMVALMEKHKHQYDKIIEERDSE 726
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 156120901 1317 LQDTQELLQEETRQKLNVSTKLRQLEDERNSLQEQLDEEMEAKQNLERHISTLNIQLSDSK 1377
Cdd:pfam05483 727 LGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKDKK 787
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1679-1932 |
5.28e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.47 E-value: 5.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1679 EKKAKSLEADLMQLQEDLAAAERARKQAD-LEK-DELAEELASSVSGRNALQDEKRRLEARIAQleeeleeeqgnteams 1756
Cdd:COG4913 224 FEAADALVEHFDDLERAHEALEDAREQIElLEPiRELAERYAAARERLAELEYLRAALRLWFAQ---------------- 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1757 ervrkatQQAEQLSNELATERSAAQKNENARQQLERQNKELRSKLQEMEGAvkskfkstIAALE-AKIAQLEEQVEQEAR 1835
Cdd:COG4913 288 -------RRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQ--------IRGNGgDRLEQLEREIERLER 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1836 EKQATAKALKQKDKKLKEALLQVEDErkmAEQYKEQAEKGNLRVKQLKRQLEEAEEESQRINANRRKLQRELDEATesne 1915
Cdd:COG4913 353 ELEERERRRARLEALLAALGLPLPAS---AEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELE---- 425
|
250
....*....|....*..
gi 156120901 1916 amgREVTALKSklRRGN 1932
Cdd:COG4913 426 ---AEIASLER--RKSN 437
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
851-1404 |
6.07e-09 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 61.46 E-value: 6.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 851 EEEMQAKEDELQKTKERQQKAESELKELeqkhSQLTEEKNLLQEQLQAETELYAEAEEMRVRLAAKKQELEEILHEMEAR 930
Cdd:PRK01156 217 LKEIERLSIEYNNAMDDYNNLKSALNEL----SSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKIINDPVYK 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 931 LEEEEDRSQQLQAERKKMAQQMLDLEEQLEEEEAARQKLqlekvtaeAKIKKLEDDILVMDDQNNKLSKERKLLEERISD 1010
Cdd:PRK01156 293 NRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKL--------SVLQKDYNDYIKKKSRYDDLNNQILELEGYEMD 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1011 LTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLDGEASDLHEQIAELQAQIAELKMQLAKKEE 1090
Cdd:PRK01156 365 YNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSR 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1091 ELQAALGRLDDEMAQKNNALKKIRELEGHISDLQEDLDSEraaRNKAEKQKRDLGEELEALKtELEDTLDSTATQQELRA 1170
Cdd:PRK01156 445 NMEMLNGQSVCPVCGTTLGEEKSNHIINHYNEKKSRLEEK---IREIEIEVKDIDEKIVDLK-KRKEYLESEEINKSINE 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1171 KReqevtmLKKALDEETRSHESQVQEMRQKHTQvVEELTEQLEQFKRakANLDKNKQALEKENAELAG-ELRVLSQAKQE 1249
Cdd:PRK01156 521 YN------KIESARADLEDIKIKINELKDKHDK-YEEIKNRYKSLKL--EDLDSKRTSWLNALAVISLiDIETNRSRSNE 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1250 VEHKKKKLEVQLQELQSKYSDgekVRAELNDKVHKLQNEVESVTGMLNEAEGKAI---KLAKDVASLGSQLQDTQELlqe 1326
Cdd:PRK01156 592 IKKQLNDLESRLQEIEIGFPD---DKSYIDKSIREIENEANNLNNKYNEIQENKIlieKLRGKIDNYKKQIAEIDSI--- 665
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 156120901 1327 ETRQKlNVSTKLRQLEDERNSLQEQLDeemEAKQNLERHISTLNIQLSDSkKKLQDFASTVELLEEGKKKFQKEIESL 1404
Cdd:PRK01156 666 IPDLK-EITSRINDIEDNLKKSRKALD---DAKANRARLESTIEILRTRI-NELSDRINDINETLESMKKIKKAIGDL 738
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1529-1930 |
6.14e-09 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 61.51 E-value: 6.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1529 ELEKSKRALETQMEemktQLEELEDELQATEDAKLRLEVNMQALKVQFERDLQARDEQNEEKRrqlqrqlheYETELEDE 1608
Cdd:PRK04863 294 ELYTSRRQLAAEQY----RLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALRQQEKIER---------YQADLEEL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1609 RKQRALAVAAKKKLEGDLKDLELQADSAikgrEEAIKQLRKlqaQMKDFQRELeDARASRDEIFATAKENEKKAKSL--- 1685
Cdd:PRK04863 361 EERLEEQNEVVEEADEQQEENEARAEAA----EEEVDELKS---QLADYQQAL-DVQQTRAIQYQQAVQALERAKQLcgl 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1686 -EADLMQLQEDLAAAERARKQADLEKDELAEELASSVSGRNALqDEKRRLEARIAQLEEELEEEQGNTEAM--SERVRKA 1762
Cdd:PRK04863 433 pDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQF-EQAYQLVRKIAGEVSRSEAWDVARELLrrLREQRHL 511
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1763 TQQAEQLSNELATERSAAQKNENARQQLERQNKELRSKLQEMEgavksKFKSTIAALEAKIAQLEEQVEqEAREKQATak 1842
Cdd:PRK04863 512 AEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDED-----ELEQLQEELEARLESLSESVS-EARERRMA-- 583
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1843 aLKQKDKKLKEallQVEDERKMAEQYKEQAEkgnlRVKQLKRQLEEAEEESQRINANRRKLQRELDEATESNEAMGREVT 1922
Cdd:PRK04863 584 -LRQQLEQLQA---RIQRLAARAPAWLAAQD----ALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQ 655
|
....*...
gi 156120901 1923 ALKSKLRR 1930
Cdd:PRK04863 656 ALDEEIER 663
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1244-1487 |
7.49e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 60.16 E-value: 7.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1244 SQAKQEVEHKKKKLEVQLQELQSKYSDGEKVRAELNDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLGSQLQDTQel 1323
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1324 lqeetrqklnvstklRQLEDERNSLQEQLDeemeAKQNLERHiSTLNIQLS-----DSKKKLQDFASTVELLEEGKKKFQ 1398
Cdd:COG4942 97 ---------------AELEAQKEELAELLR----ALYRLGRQ-PPLALLLSpedflDAVRRLQYLKYLAPARREQAEELR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1399 KEIESLTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQKKFDQLLAEEKNISSKYADERDRAEAEA 1478
Cdd:COG4942 157 ADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
....*....
gi 156120901 1479 REKETKALS 1487
Cdd:COG4942 237 AAAAERTPA 245
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
999-1428 |
8.05e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.55 E-value: 8.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 999 KERKLLEERISDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLD-----GEASDLHEQIAE 1073
Cdd:COG4717 64 RKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQllplyQELEALEAELAE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1074 LQAQIAELKMQLaKKEEELQAALGRLDDEMAQKNNALKKIREL-----EGHISDLQEDLDSERAARNKAEKQKRDLGEEL 1148
Cdd:COG4717 144 LPERLEELEERL-EELRELEEELEELEAELAELQEELEELLEQlslatEEELQDLAEELEELQQRLAELEEELEEAQEEL 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1149 EALKTELEDTLDSTATQQELRAKREQEVTML-----------------------------------------KKALDEET 1187
Cdd:COG4717 223 EELEEELEQLENELEAAALEERLKEARLLLLiaaallallglggsllsliltiagvlflvlgllallflllaREKASLGK 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1188 RSHESQVQEMRQKHTQvvEELTEQLEQFKRAKANLDKNKQALEKENAELAGELRVLSQAKQEVEHK--KKKLEVQLQELQ 1265
Cdd:COG4717 303 EAEELQALPALEELEE--EELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEelEQEIAALLAEAG 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1266 SKYSDGEKVRAELNDKVHKLQNEVESVTGMLNEAEGKAIKLAkdvaslgsqlqdtqellqeETRQKLNVSTKLRQLEDER 1345
Cdd:COG4717 381 VEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELL-------------------EALDEEELEEELEELEEEL 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1346 NSLQEQLDEEMEAKQNLERHIStlniQLSDSKkklqdfasTVELLEEGKKKFQKEIESLTQQYEEKAAAYDKLEKTKNRL 1425
Cdd:COG4717 442 EELEEELEELREELAELEAELE----QLEEDG--------ELAELLQELEELKAELRELAEEWAALKLALELLEEAREEY 509
|
...
gi 156120901 1426 QQE 1428
Cdd:COG4717 510 REE 512
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
769-1241 |
8.47e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.08 E-value: 8.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 769 FFRTGVLahleEERDL--KITDVIMAFQAMCRgylARKAFAKRQQQLTAMKVIQRNCAAYLKLRNWQwwRLFTKVKPLLQ 846
Cdd:COG4913 212 FVREYML----EEPDTfeAADALVEHFDDLER---AHEALEDAREQIELLEPIRELAERYAAARERL--AELEYLRAALR 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 847 VTRQEEEMQAKEDELQKTKERQQKAESELKELEQKHSQLTEEKNLLQEQL-----QAETELYAEAEEMRVRLAAKKQELE 921
Cdd:COG4913 283 LWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIrgnggDRLEQLEREIERLERELEERERRRA 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 922 EILHEMEARLEEEEDRSQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDDILVMDDQNNKLSKE- 1000
Cdd:COG4913 363 RLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARl 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1001 ---RKLLEERISDLTTNL---------AEEEEK--------------------------AKNLTKLKNKHEsmISELEVR 1042
Cdd:COG4913 443 lalRDALAEALGLDEAELpfvgelievRPEEERwrgaiervlggfaltllvppehyaaaLRWVNRLHLRGR--LVYERVR 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1043 LKKEEKSRQELEK--LKRKLDGEASDLH---------------------------------------------------- 1068
Cdd:COG4913 521 TGLPDPERPRLDPdsLAGKLDFKPHPFRawleaelgrrfdyvcvdspeelrrhpraitragqvkgngtrhekddrrrirs 600
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1069 ---------EQIAELQAQIAELKMQLAKKEEELQAALGRLDdEMAQKNNALKKIRE----------LEGHISDLQEDLDS 1129
Cdd:COG4913 601 ryvlgfdnrAKLAALEAELAELEEELAEAEERLEALEAELD-ALQERREALQRLAEyswdeidvasAEREIAELEAELER 679
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1130 ERAARNKAEKqkrdLGEELEALKTELEDTLDSTATQQELRAKREQEVTMLKKALDEETRSHESQVQEMRQKHTQVVEELT 1209
Cdd:COG4913 680 LDASSDDLAA----LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERF 755
|
570 580 590
....*....|....*....|....*....|....*
gi 156120901 1210 EQL---EQFKRAKANLDKNKQALEKENAELAGELR 1241
Cdd:COG4913 756 AAAlgdAVERELRENLEERIDALRARLNRAEEELE 790
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1004-1923 |
9.77e-09 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 61.00 E-value: 9.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1004 LEERISDLTTNLAEEEEKAKNLTKLKNKHESMIS-------ELEVRLKKEEKSRQELEKLKRKLDgEASDLHEQIAELQA 1076
Cdd:PTZ00440 510 IKEKNNIVNNNFKNIEDYYITIEGLKNEIEGLIElikyylqSIETLIKDEKLKRSMKNDIKNKIK-YIEENVDHIKDIIS 588
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1077 QIAELKMQLAKKEEELQAALGRLDDEMAQKNNALKKIREL--EGHISDLQEDLD--SERAARNKAEKQKRDLGEELEALK 1152
Cdd:PTZ00440 589 LNDEIDNIIQQIEELINEALFNKEKFINEKNDLQEKVKYIlnKFYKGDLQELLDelSHFLDDHKYLYHEAKSKEDLQTLL 668
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1153 TELEdtldstATQQELRAKREQEVTMLKKALDEETRSHESQVQEMRQKHTQVVE-ELTEQLEQFKRAKANLDKNKQALEK 1231
Cdd:PTZ00440 669 NTSK------NEYEKLEFMKSDNIDNIIKNLKKELQNLLSLKENIIKKQLNNIEqDISNSLNQYTIKYNDLKSSIEEYKE 742
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1232 ENAELagelrvlSQAKQEVEHKKKKLEVQLQELQSKYSDGEKVRAELNDKVHKLQNEVESVTG---MLNEAEGKAIKLAK 1308
Cdd:PTZ00440 743 EEEKL-------EVYKHQIINRKNEFILHLYENDKDLPDGKNTYEEFLQYKDTILNKENKISNdinILKENKKNNQDLLN 815
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1309 DVASLGSQLQDTQELLQEETRQKLN------VSTKLRQLEDERNSLQEQLDEEMEAKQNLERHISTLNIqLSDSKKKLQD 1382
Cdd:PTZ00440 816 SYNILIQKLEAHTEKNDEELKQLLQkfptedENLNLKELEKEFNENNQIVDNIIKDIENMNKNINIIKT-LNIAINRSNS 894
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1383 FASTVELLEEGKKKFQKEIESLTQQYE--------EKAAAYDKLEKTKNRLQQELDDLVVDldnqrQLVSNLEKKQKKFD 1454
Cdd:PTZ00440 895 NKQLVEHLLNNKIDLKNKLEQHMKIINtdniiqknEKLNLLNNLNKEKEKIEKQLSDTKIN-----NLKMQIEKTLEYYD 969
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1455 QLlaeEKNISSKyaDERDRAEAEAREKETKALSlARALEEALEAKEELERTNKMLKAEMEDLV--SSKDDVGKNvHELEK 1532
Cdd:PTZ00440 970 KS---KENINGN--DGTHLEKLDKEKDEWEHFK-SEIDKLNVNYNILNKKIDDLIKKQHDDIIelIDKLIKEKG-KEIEE 1042
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1533 SKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKVQFErDLQARDEQNEEKRRQLQRQLHEYETELEDERKQR 1612
Cdd:PTZ00440 1043 KVDQYISLLEKMKTKLSSFHFNIDIKKYKNPKIKEEIKLLEEKVE-ALLKKIDENKNKLIEIKNKSHEHVVNADKEKNKQ 1121
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1613 ALAVAAKKKlegDLKDLELQADSAIKGREEAIKQLRKLQAQMkdfQRELEDARASRDEIFATAKENEKKAKSLEADLMQL 1692
Cdd:PTZ00440 1122 TEHYNKKKK---SLEKIYKQMEKTLKELENMNLEDITLNEVN---EIEIEYERILIDHIVEQINNEAKKSKTIMEEIESY 1195
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1693 QEDLaaaERARKQADLEKDELAEELASsvsgrNALQDEKRRLEARIAQLEEELEEEQGNTEAmSERVRKATQQAEQLSNE 1772
Cdd:PTZ00440 1196 KKDI---DQVKKNMSKERNDHLTTFEY-----NAYYDKATASYENIEELTTEAKGLKGEANR-STNVDELKEIKLQVFSY 1266
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1773 LATERSAAQKNENARQQLERQNKELRS---------------KLQEMEGAVKSKFKST---IAALEAKIAQLEE------ 1828
Cdd:PTZ00440 1267 LQQVIKENNKMENALHEIKNMYEFLISidsekilkeilnstkKAEEFSNDAKKELEKTdnlIKQVEAKIEQAKEhknkiy 1346
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1829 ------QVEQEAREKQATAKALKQKDKKLKEALLQVEDERKMAEQYKEQAEKGNLRVKQLKRQleEAEEESQRINANRRK 1902
Cdd:PTZ00440 1347 gsledkQIDDEIKKIEQIKEEISNKRKEINKYLSNIKSNKEKCDLHVRNASRGKDKIDFLNKH--EAIEPSNSKEVNIIK 1424
|
970 980
....*....|....*....|..
gi 156120901 1903 LQRELDEATE-SNEAMGREVTA 1923
Cdd:PTZ00440 1425 ITDNINKCKQySNEAMETENKA 1446
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1185-1739 |
9.84e-09 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 60.69 E-value: 9.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1185 EETRSHESQVQEMRQKHTQVVEELTEQLEQFKRAKANLDKNKQALEKENAELAGELRVLSQAKQEVEHKKKKLEVQLQEL 1264
Cdd:PRK01156 165 ERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNEL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1265 QSKYSDGEKVRAELNDKVHKLQ------NEVESVTGMLNEAEGKAIKLAK----DVASLGSQLQDTQELLQEETRQKLNV 1334
Cdd:PRK01156 245 SSLEDMKNRYESEIKTAESDLSmeleknNYYKELEERHMKIINDPVYKNRnyinDYFKYKNDIENKKQILSNIDAEINKY 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1335 STKLRQLEDernsLQEQLDEEMEAKQNLErhisTLNIQLSDSKKKLQDFASTVELLEEGKKK---FQKEIESLTQQYEE- 1410
Cdd:PRK01156 325 HAIIKKLSV----LQKDYNDYIKKKSRYD----DLNNQILELEGYEMDYNSYLKSIESLKKKieeYSKNIERMSAFISEi 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1411 ---KAAAYDKLEKTKNRLQQELDDLVVDLDN----QRQLVSNLEKKQKKFDQL------------LAEEK--NISSKYAD 1469
Cdd:PRK01156 397 lkiQEIDPDAIKKELNEINVKLQDISSKVSSlnqrIRALRENLDELSRNMEMLngqsvcpvcgttLGEEKsnHIINHYNE 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1470 ERDRAEAEAREKETKALSLaraleeALEAKEELERTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETqMEEMKTQLE 1549
Cdd:PRK01156 477 KKSRLEEKIREIEIEVKDI------DEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINE-LKDKHDKYE 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1550 ELEDELQAT--EDAKLRLEVNMQALKVQFERDLQARDEQNEEKRRQL---QRQLHEYETELEDERKQRALAVaakKKLEG 1624
Cdd:PRK01156 550 EIKNRYKSLklEDLDSKRTSWLNALAVISLIDIETNRSRSNEIKKQLndlESRLQEIEIGFPDDKSYIDKSI---REIEN 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1625 DLKDLELQadsaIKGREEAIKQLRKLQAQMKDFQRELedarASRDEIFATAKENEKKAKSLEADLMQL--QEDLAAAERA 1702
Cdd:PRK01156 627 EANNLNNK----YNEIQENKILIEKLRGKIDNYKKQI----AEIDSIIPDLKEITSRINDIEDNLKKSrkALDDAKANRA 698
|
570 580 590
....*....|....*....|....*....|....*...
gi 156120901 1703 RKQADLEKD-ELAEELASSVSGRNALQDEKRRLEARIA 1739
Cdd:PRK01156 699 RLESTIEILrTRINELSDRINDINETLESMKKIKKAIG 736
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1046-1482 |
1.82e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.40 E-value: 1.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1046 EEKSRQELEKLKRKLDGEASDLHEQIAELQAQIAELKmqlaKKEEELQAALGRLDDEMAQKNNALKKIRELEGHISDL-- 1123
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAE----EKEEEYAELQEELEELEEELEELEAELEELREELEKLek 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1124 QEDLDSERAARNKAEKQKRDLGEELEALKTELEDTldstATQQELRAKREQEVTMLKKALDEETRSHESQVQEMRQKHTQ 1203
Cdd:COG4717 124 LLQLLPLYQELEALEAELAELPERLEELEERLEEL----RELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1204 VVEELTEQLEQFKRAKANLDKNKQALEKENAELagelrvlsQAKQEVEHKKKKLEVQLQELQskysdGEKVRAELNDKVH 1283
Cdd:COG4717 200 ELEELQQRLAELEEELEEAQEELEELEEELEQL--------ENELEAAALEERLKEARLLLL-----IAAALLALLGLGG 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1284 KLQNEVESVTGMLNEAEGKAI----KLAKDVASLGSQLQDTQELLQEETRQKLNVSTKLRQL---EDERNSLQEQLDEEM 1356
Cdd:COG4717 267 SLLSLILTIAGVLFLVLGLLAllflLLAREKASLGKEAEELQALPALEELEEEELEELLAALglpPDLSPEELLELLDRI 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1357 EAKQNLERHISTLN--IQLSDSKKKLQdfastvELLEEGKKKFQKEIESLTQQYEEKAAAYDKLEKTKNRLQQELDDLVV 1434
Cdd:COG4717 347 EELQELLREAEELEeeLQLEELEQEIA------ALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEE 420
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 156120901 1435 DLDNQ---------RQLVSNLEKKQKKFDQLLAEEKNISSKYAD-ERDRAEAEAREKE 1482
Cdd:COG4717 421 LLEALdeeeleeelEELEEELEELEEELEELREELAELEAELEQlEEDGELAELLQEL 478
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
844-1630 |
2.21e-08 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 59.60 E-value: 2.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 844 LLQVTRQEEEMQAKEDELQKTKERQQKAESELKELEQKHSQLTEEKNLLQEQLQAETELYAEAEEMRvrlaAKKQELEEI 923
Cdd:TIGR00618 169 LMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREAL----QQTQQSHAY 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 924 LHEMEARLEEEEDRSQQLQAERkkmaqqmldleeqleeeeaarqklqlekvtaeAKIKKLEDDILVMDDQNNKLSKERKL 1003
Cdd:TIGR00618 245 LTQKREAQEEQLKKQQLLKQLR--------------------------------ARIEELRAQEAVLEETQERINRARKA 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1004 leERISDLTTNLAEEEEKAKN-LTKLKNKHESMISELEVR--LKKEEKSRQELEKLKRKLDgEASDLHEQIAELQAQIAE 1080
Cdd:TIGR00618 293 --APLAAHIKAVTQIEQQAQRiHTELQSKMRSRAKLLMKRaaHVKQQSSIEEQRRLLQTLH-SQEIHIRDAHEVATSIRE 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1081 LKMQlAKKEEELQAALGRLDDEMAQKNNALKKIRELEGHISDLQEDLDSERaarnkaekqkRDLGEELEALKTELEDTLD 1160
Cdd:TIGR00618 370 ISCQ-QHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAF----------RDLQGQLAHAKKQQELQQR 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1161 STATQQELRAKREQEVTMLKKALDEETRSHESQVQEMRQKHTqvveelteQLEQFKRAKANLDKNKQALEKENAELAGEL 1240
Cdd:TIGR00618 439 YAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQ--------IHLQETRKKAVVLARLLELQEEPCPLCGSC 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1241 RVLSQAKQ---EVEHKKKKLEVQLQELQSKYSDGEKVRAELNDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLGSQL 1317
Cdd:TIGR00618 511 IHPNPARQdidNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQ 590
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1318 QDTQELLQEetrqklnvSTKLRQLEDERNSLQEQLDEEMEAKQNLERHISTL-NIQLSDSKKKLQDFASTVELLEEGKKK 1396
Cdd:TIGR00618 591 NITVRLQDL--------TEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLqQCSQELALKLTALHALQLTLTQERVRE 662
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1397 FQKEIESLTQQY-EEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQKKFDQLLAEEKNISSKYADERDRAE 1475
Cdd:TIGR00618 663 HALSIRVLPKELlASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALN 742
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1476 AEAREKETKALSLARALEEALEAKEELERTNKMLKAEMEDLVSskddvgknvhELEKSKRALETQMEEMKTQLEELEDEL 1555
Cdd:TIGR00618 743 QSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAA----------EIQFFNRLREEDTHLLKTLEAEIGQEI 812
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 156120901 1556 QATEDAKLrlevnmqALKVQFERDLQARDEQNEEKRRQLQRQLHEYEtELEDERKQRALAVAAKKKLEGDLKDLE 1630
Cdd:TIGR00618 813 PSDEDILN-------LQCETLVQEEEQFLSRLEEKSATLGEITHQLL-KYEECSKQLAQLTQEQAKIIQLSDKLN 879
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1253-1913 |
2.37e-08 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 59.47 E-value: 2.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1253 KKKKLEVQLQELQSkYSDGEKVRAElndkVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLGSQLQDTQELLQEetrqkl 1332
Cdd:pfam12128 219 NRQQVEHWIRDIQA-IAGIMKIRPE----FTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAE------ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1333 nVSTKLRQLEDErnsLQEQLDEemeakqnlerhistLNIQLSDSKKKLQDFASTVELLEEGKKKFQKE-IESLTQ----- 1406
Cdd:pfam12128 288 -LNQLLRTLDDQ---WKEKRDE--------------LNGELSAADAAVAKDRSELEALEDQHGAFLDAdIETAAAdqeql 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1407 -----QYEEKAAAYDKLEKTKNRLQQELDDLV--VDLDNQRQLVSN---LEKKQKKFDQLLAEEKN----ISSKYADERD 1472
Cdd:pfam12128 350 pswqsELENLEERLKALTGKHQDVTAKYNRRRskIKEQNNRDIAGIkdkLAKIREARDRQLAVAEDdlqaLESELREQLE 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1473 RAEAEAREKEtKALSLARALEEALEAKEELERTNKMLKAEMEDLVSSKDD----VGKNVHELEKSKRALETQMEEmktQL 1548
Cdd:pfam12128 430 AGKLEFNEEE-YRLKSRLGELKLRLNQATATPELLLQLENFDERIERAREeqeaANAEVERLQSELRQARKRRDQ---AS 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1549 EELEDELQATEDAKLRLEVNMQALKVQ------FERDLQARDEQNEEK---RRQLQR--------------QLHEYETEL 1605
Cdd:pfam12128 506 EALRQASRRLEERQSALDELELQLFPQagtllhFLRKEAPDWEQSIGKvisPELLHRtdldpevwdgsvggELNLYGVKL 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1606 EDERKQRALAVAAKKKLEGDLKDLELQADSAIKGREEAIKQLRKLQAQMKDFQRELEDARASrdeifatakenekkAKSL 1685
Cdd:pfam12128 586 DLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTA--------------LKNA 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1686 EADLMQLQEDLAAAERARKQAdlekdeLAEELASSVSGRNALQDEKRRLEARIAQLEEELEEEQgnTEAMSERVRKATQQ 1765
Cdd:pfam12128 652 RLDLRRLFDEKQSEKDKKNKA------LAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQK--REARTEKQAYWQVV 723
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1766 AEQLSNELA---TERSAAQKNENARQ-QLERQNK-ELRSKlqEMEGAVKSKFKSTIAALEAKIAQLEEQVEQEAREKQAT 1840
Cdd:pfam12128 724 EGALDAQLAllkAAIAARRSGAKAELkALETWYKrDLASL--GVDPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWY 801
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 156120901 1841 AKALKQKDKKLKEALLQVEDERKMAEQykeqaekgnlrvkQLKRQLEEAEEESQRINANRRKLQRELDEATES 1913
Cdd:pfam12128 802 QETWLQRRPRLATQLSNIERAISELQQ-------------QLARLIADTKLRRAKLEMERKASEKQQVRLSEN 861
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
976-1349 |
3.37e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.63 E-value: 3.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 976 AEAKIKKLEDDilvmDDQNNKLSKERKLLEERISDLTTNLAEEEEKAKNLTKLKNKHESM---------ISELEVRLKKE 1046
Cdd:COG4717 76 LEEELKEAEEK----EEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYqelealeaeLAELPERLEEL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1047 EKSRQELEKLKRKLDgeasDLHEQIAELQAQIAELKMQL-AKKEEELQAALGRLDDEMAQKNNALKKIRELEGHISDLQE 1125
Cdd:COG4717 152 EERLEELRELEEELE----ELEAELAELQEELEELLEQLsLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1126 DLDSERAARNKAEKQKR-------------------------------------------DLGEELEALKTELEDTLDST 1162
Cdd:COG4717 228 ELEQLENELEAAALEERlkearlllliaaallallglggsllsliltiagvlflvlgllaLLFLLLAREKASLGKEAEEL 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1163 ATQQELRAKREQEVTMLKKALDEETRSHESQVQEMRQKHTQVVEELTEQLEQFKRAK--ANLDKNKQALEKENAELAGEL 1240
Cdd:COG4717 308 QALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQleELEQEIAALLAEAGVEDEEEL 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1241 RVLSQAKQEVEHKKKKLEVQLQELQSKYSDGEKVRAELNDKvhKLQNEVESVTGMLNEAEGKAIKLAKDVASLGSQLQD- 1319
Cdd:COG4717 388 RAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEE--ELEEELEELEEELEELEEELEELREELAELEAELEQl 465
|
410 420 430
....*....|....*....|....*....|.
gi 156120901 1320 -TQELLQEETRQKLNVSTKLRQLEDERNSLQ 1349
Cdd:COG4717 466 eEDGELAELLQELEELKAELRELAEEWAALK 496
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
965-1915 |
3.56e-08 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 59.29 E-value: 3.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 965 ARQKLQLEKVTAE-AKIKKLEDDILVMDdqNNKLSKERKLLEERISDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRL 1043
Cdd:TIGR01612 775 AKEKDELNKYKSKiSEIKNHYNDQINID--NIKDEDAKQNYDKSKEYIKTISIKEDEIFKIINEMKFMKDDFLNKVDKFI 852
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1044 KKEEKSrqeleklKRKLDGEASDLHEQIAELQAQIAELKMQL-AKKEEELQAALGRLDDEMAQKNNALKKIRELEGHISD 1122
Cdd:TIGR01612 853 NFENNC-------KEKIDSEHEQFAELTNKIKAEISDDKLNDyEKKFNDSKSLINEINKSIEEEYQNINTLKKVDEYIKI 925
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1123 LQEDLDSERAARNKAEKQKRDLGEELEALKtelEDTLDSTATQQELRAKREQEVTMLKKALDEET-RSHESQVQEMrqkh 1201
Cdd:TIGR01612 926 CENTKESIEKFHNKQNILKEILNKNIDTIK---ESNLIEKSYKDKFDNTLIDKINELDKAFKDASlNDYEAKNNEL---- 998
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1202 tqvveelteqLEQFKRAKANLDKNK------QALEKENAelagelrvLSQAKQEVEHKKKKL-EVQLQELQSKYSDGEKV 1274
Cdd:TIGR01612 999 ----------IKYFNDLKANLGKNKenmlyhQFDEKEKA--------TNDIEQKIEDANKNIpNIEIAIHTSIYNIIDEI 1060
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1275 RAELNDKVHKLQNEVesvtgmLNEAEGKAIKLAKDVASLgsQLQDTQELLQEETrqkLNVSTKLRQLEDERNSLQEQLDE 1354
Cdd:TIGR01612 1061 EKEIGKNIELLNKEI------LEEAEINITNFNEIKEKL--KHYNFDDFGKEEN---IKYADEINKIKDDIKNLDQKIDH 1129
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1355 EM----EAKQNLERHISTLNIQLSDskkkLQDFASTVeLLEEGKKKFQKEIESLTQQYEEKAAAYDKLEKTKNRlqqeld 1430
Cdd:TIGR01612 1130 HIkaleEIKKKSENYIDEIKAQIND----LEDVADKA-ISNDDPEEIEKKIENIVTKIDKKKNIYDEIKKLLNE------ 1198
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1431 dlvvdldnqrqlVSNLEKKQKKfdqlLAEEKNISSKYA------------DERDRAE--AEAREKETKALSLARALEEAL 1496
Cdd:TIGR01612 1199 ------------IAEIEKDKTS----LEEVKGINLSYGknlgklflekidEEKKKSEhmIKAMEAYIEDLDEIKEKSPEI 1262
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1497 EAKEELERTnkmLKAEMEDLVSSKDDVgKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNM-QALKVQ 1575
Cdd:TIGR01612 1263 ENEMGIEMD---IKAEMETFNISHDDD-KDHHIISKKHDENISDIREKSLKIIEDFSEESDINDIKKELQKNLlDAQKHN 1338
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1576 FERDLQARDEQN------EEKRRQLQRQLHEYETELEDERKQ------RALAVAAKKKLEGDLKDLELQADSAIKGRE-- 1641
Cdd:TIGR01612 1339 SDINLYLNEIANiynilkLNKIKKIIDEVKEYTKEIEENNKNikdeldKSEKLIKKIKDDINLEECKSKIESTLDDKDid 1418
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1642 EAIKQLRKLQAQMKDfqreledARASRDEIFATAKENEKK----------AKSLEADLMQLQEDLAAAERARKQADLEKD 1711
Cdd:TIGR01612 1419 ECIKKIKELKNHILS-------EESNIDTYFKNADENNENvlllfkniemADNKSQHILKIKKDNATNDHDFNINELKEH 1491
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1712 ELAEELASSVSGRNALQDEKRRLEARIAQLEEELEEEQGNTEAMSERVRKATQQAEQLSNELateRSAAQKNENARQQLE 1791
Cdd:TIGR01612 1492 IDKSKGCKDEADKNAKAIEKNKELFEQYKKDVTELLNKYSALAIKNKFAKTKKDSEIIIKEI---KDAHKKFILEAEKSE 1568
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1792 RQNKELRSKLQEMEGAVKSKFKSTIAALEA------------KIAQLEEQV-----EQEAREKQATAKALKQKDKKLKEA 1854
Cdd:TIGR01612 1569 QKIKEIKKEKFRIEDDAAKNDKSNKAAIDIqlslenfenkflKISDIKKKIndclkETESIEKKISSFSIDSQDTELKEN 1648
|
970 980 990 1000 1010 1020
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 156120901 1855 LLQVEDERKMAEQYKEQaekgnlrvkqlKRQLEEAEEESQRINANRRKLQRELDEATESNE 1915
Cdd:TIGR01612 1649 GDNLNSLQEFLESLKDQ-----------KKNIEDKKKELDELDSEIEKIEIDVDQHKKNYE 1698
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
846-1168 |
3.63e-08 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 58.37 E-value: 3.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 846 QVTRQEEEMQAKEDELQKTKERQQKAESELKELEQKHSQLTEEKNLLQEQLQAETELYAEAEEMRVRLAAKKQELEEILh 925
Cdd:pfam07888 74 QRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETEL- 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 926 emearlEEEEDRSQQLQAERKKmaqqmldleeqleeEEAARQKLQLEKVTAEAKIKKLEDDILVMDDQNNKLSKERKLLE 1005
Cdd:pfam07888 153 ------ERMKERAKKAGAQRKE--------------EEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQ 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1006 ERISDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLDGEASDLHE---QIAELQAQIAELK 1082
Cdd:pfam07888 213 DTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQarlQAAQLTLQLADAS 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1083 MQL-------AKKEEELQAA-------LGRLDDEMAQKNNALKKIR-ELEGHISDLQEDLDSERAARNKAEKQKRDLGEE 1147
Cdd:pfam07888 293 LALregrarwAQERETLQQSaeadkdrIEKLSAELQRLEERLQEERmEREKLEVELGREKDCNRVQLSESRRELQELKAS 372
|
330 340
....*....|....*....|.
gi 156120901 1148 LEALKTELEDTLdstATQQEL 1168
Cdd:pfam07888 373 LRVAQKEKEQLQ---AEKQEL 390
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1713-1912 |
5.08e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 58.10 E-value: 5.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1713 LAEELASSVSGRNALQDEKRRLEARI--AQLEEELEEEQGNTEAMSERVRKATQQAEQLSNELATERSAAQKNENARQQL 1790
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELeeAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAAL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1791 ERQNKELRSKLQEMEGAvkskfkSTIAALEAKIAQLEEQVEQEAREKQATAKALKQKDKKLKEALLQVEDE-RKMAEQYK 1869
Cdd:COG3206 246 RAQLGSGPDALPELLQS------PVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEaQRILASLE 319
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 156120901 1870 EQAEKGNLRVKQLKRQLEEAEEESQRINANRRK---LQRELDEATE 1912
Cdd:COG3206 320 AELEALQAREASLQAQLAQLEARLAELPELEAElrrLEREVEVARE 365
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1509-1710 |
5.13e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.47 E-value: 5.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1509 LKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKVQfERDLQARDEQNE 1588
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE-IAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1589 EKRRQLQRQLH------------------------EYETELEDERKQRALAVAAKKK-LEGDLKDLELQADSAIKGREEA 1643
Cdd:COG4942 104 EELAELLRALYrlgrqpplalllspedfldavrrlQYLKYLAPARREQAEELRADLAeLAALRAELEAERAELEALLAEL 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156120901 1644 IKQLRKLQAQMKDFQRELEDARASRDEIFATAKENEKKAKSLEADLMQLQEDLAAAERARKQADLEK 1710
Cdd:COG4942 184 EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAA 250
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
846-1640 |
6.95e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 58.04 E-value: 6.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 846 QVTRQEEEMQAKEDELQKTKERQQKAESELKELEQKHSQLTEEKNLLQEQLQAETELYAEAEEMRVRLAAKKQELEEI-- 923
Cdd:PRK04863 349 KIERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQALERAkq 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 924 -LHEMEARLEEEEDRSQQLQAERKKMAQQMLDLEEQLEEEEAARQklQLEKvtAEAKIKKLEDDILVMDDQNNKLSKERK 1002
Cdd:PRK04863 429 lCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHS--QFEQ--AYQLVRKIAGEVSRSEAWDVARELLRR 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1003 LLEERI------------SDLTTNLAEE---EEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLDGEASDL 1067
Cdd:PRK04863 505 LREQRHlaeqlqqlrmrlSELEQRLRQQqraERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMAL 584
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1068 HEQIAELQAQIAELKmQLAKKEEELQAALGRLDDemaQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLGEE 1147
Cdd:PRK04863 585 RQQLEQLQARIQRLA-ARAPAWLAAQDALARLRE---QSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALDEE 660
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1148 LEALkteledTLDSTATQQELRAKREQEVTMLKKALDEETRSHESQVQEMR---QKHTQVVEELTeqleqfkRAKANLdk 1224
Cdd:PRK04863 661 IERL------SQPGGSEDPRLNALAERFGGVLLSEIYDDVSLEDAPYFSALygpARHAIVVPDLS-------DAAEQL-- 725
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1225 nkQALEKENAEL---AGELRVLSQAKQEVEHKKKKLEVQLQELQSKYSDGEKV----RAELNDKVHKLQNEVESVTGMLN 1297
Cdd:PRK04863 726 --AGLEDCPEDLyliEGDPDSFDDSVFSVEELEKAVVVKIADRQWRYSRFPEVplfgRAAREKRIEQLRAEREELAERYA 803
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1298 EAEGKAIKLAKDVASL----GSQLQ-----DTQELLQEETRQKLNVSTKLRQLEDERNSLQEQLDEEMEAKQNLERHIST 1368
Cdd:PRK04863 804 TLSFDVQKLQRLHQAFsrfiGSHLAvafeaDPEAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLPR 883
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1369 LNIQLSDS-KKKLQDFASTVELLEEGK---KKFQKEIESLT----------QQYEEKAAAYDKLEKTKNRLQQELDDLvV 1434
Cdd:PRK04863 884 LNLLADETlADRVEEIREQLDEAEEAKrfvQQHGNALAQLEpivsvlqsdpEQFEQLKQDYQQAQQTQRDAKQQAFAL-T 962
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1435 DLdNQRQLVSNLEKKQkkfdQLLAEEKNISSKYADERDRAEAEAREketkalslaraleealeakeelertnkmLKAEME 1514
Cdd:PRK04863 963 EV-VQRRAHFSYEDAA----EMLAKNSDLNEKLRQRLEQAEQERTR----------------------------AREQLR 1009
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1515 DLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELedELQATEDAKLRLEVNmqalkvqfERDLQARDEQNEEKRRQL 1594
Cdd:PRK04863 1010 QAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDL--GVPADSGAEERARAR--------RDELHARLSANRSRRNQL 1079
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*..
gi 156120901 1595 QRQLHEYETEL-----------EDERKQRALAVAAKKkleGDLKDLELQADSAIKGR 1640
Cdd:PRK04863 1080 EKQLTFCEAEMdnltkklrkleRDYHEMREQVVNAKA---GWCAVLRLVKDNGVERR 1133
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1402-1791 |
7.53e-08 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 57.44 E-value: 7.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1402 ESLTQQYEEKAAAYDKLEKTKNRLQQELDDLVvdldnQRQLVSNLEKKQKKFDqllaeeknissKYADERDRAEAEAREK 1481
Cdd:pfam17380 247 EDVTTMTPEYTVRYNGQTMTENEFLNQLLHIV-----QHQKAVSERQQQEKFE-----------KMEQERLRQEKEEKAR 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1482 EtkaLSLARALEEALEAKEELERTNKMLKAEMEDLVsskddvgknvheLEKSKRALETQMEEMKTQLEELEDELQATEDA 1561
Cdd:pfam17380 311 E---VERRRKLEEAEKARQAEMDRQAAIYAEQERMA------------MERERELERIRQEERKRELERIRQEEIAMEIS 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1562 KLRlevnmqalkvQFERdLQARDEQNEEKRRQlqrqlheyetELEDERKQRALAVAAKKKLEGDLKDLELQADSAIKGRE 1641
Cdd:pfam17380 376 RMR----------ELER-LQMERQQKNERVRQ----------ELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQ 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1642 EAIKQLRKLQAQMKDFQRELEDARASRDEIFaTAKENEKKAKSLEADLMQLQEDLAAAER---------ARKQADLEKDE 1712
Cdd:pfam17380 435 REVRRLEEERAREMERVRLEEQERQQQVERL-RQQEEERKRKKLELEKEKRDRKRAEEQRrkilekeleERKQAMIEEER 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1713 LAEELASSVSGR-NALQDEKRRleaRIAQLEEELEEEQGNTEAMSERVRKATQQAEQLsNELATERSAAQK---NENARQ 1788
Cdd:pfam17380 514 KRKLLEKEMEERqKAIYEEERR---REAEEERRKQQEMEERRRIQEQMRKATEERSRL-EAMEREREMMRQiveSEKARA 589
|
...
gi 156120901 1789 QLE 1791
Cdd:pfam17380 590 EYE 592
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1070-1307 |
7.97e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 56.76 E-value: 7.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1070 QIAELQAQIAELKMQLAKKEEELQAALGRLDDEMAQKNNALKKIRELEGHISDLQEDLDserAARNKAEKQKRDLGEELE 1149
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIA---EAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1150 ALKTE------LEDTLDSTATQqelrakreqevTMLKKAldeetrsheSQVQEMRQKHTQVVEELTEQLEQFKRAKANLD 1223
Cdd:COG3883 94 ALYRSggsvsyLDVLLGSESFS-----------DFLDRL---------SALSKIADADADLLEELKADKAELEAKKAELE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1224 KNKQALEKENAELAGELRVLSQAKQEVEHKKKKLEVQLQELQSKYSDGEKVRAELNDKVHKLQNEVESVTGMLNEAEGKA 1303
Cdd:COG3883 154 AKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
....
gi 156120901 1304 IKLA 1307
Cdd:COG3883 234 AAAA 237
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1264-1458 |
8.99e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 57.33 E-value: 8.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1264 LQSKYSDGEKVRAELNDKVHKLQNEVESVtgmlnEAEGKAIKLAKDVASLGSQLQDTQELLQEETRQKLNVSTKLRQLED 1343
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEA-----EAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1344 ERNSLQEQLDEEMEAK---------QNLERHISTLNIQLSDSKKKLQDFASTV--------ELLEEGKKKFQKEIESLTQ 1406
Cdd:COG3206 241 RLAALRAQLGSGPDALpellqspviQQLRAQLAELEAELAELSARYTPNHPDVialraqiaALRAQLQQEAQRILASLEA 320
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 156120901 1407 QYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQKKFDQLLA 1458
Cdd:COG3206 321 ELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQ 372
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1470-1914 |
9.45e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.08 E-value: 9.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1470 ERDRAEAEAREKETKALSLARALEEALEAKEELERTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLE 1549
Cdd:COG4717 77 EEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLE 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1550 ---ELEDELQATEDAKLRLEVNMQALKVQFERDLQARDEQNEEKRRQLQRQLHEYETELEDERKQRALAVAAKKKLEGDL 1626
Cdd:COG4717 157 elrELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1627 KDLE----LQADSAIKGREEAIKQLRKLQAQMKDFQRELEDARASRDEIFATAKENEKKAKsleadlMQLQEDLAAAERA 1702
Cdd:COG4717 237 EAAAleerLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREK------ASLGKEAEELQAL 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1703 RKQADLEKDELAEELASSVSGRNALQDEKRRLEARIAQLEEELEEEQGNTEAMSERVRKATQQA--EQLSNELATERSAA 1780
Cdd:COG4717 311 PALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAAllAEAGVEDEEELRAA 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1781 QKNENARQQLERQNKELRSKLQEMEGAVKSKFKS-TIAALEAKIAQLEEQVEQEAREKqataKALKQKDKKLKEALLQVE 1859
Cdd:COG4717 391 LEQAEEYQELKEELEELEEQLEELLGELEELLEAlDEEELEEELEELEEELEELEEEL----EELREELAELEAELEQLE 466
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 156120901 1860 DERKMAEQYKEQAEkgnlrvkqLKRQLEEAEEESQRINANRRKLQRELDEATESN 1914
Cdd:COG4717 467 EDGELAELLQELEE--------LKAELRELAEEWAALKLALELLEEAREEYREER 513
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1383-1636 |
9.57e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 56.31 E-value: 9.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1383 FASTVELLEEGKKKFQKEIESLTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQKKFDQLLAEekn 1462
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1463 isskyaDERDRAEAEAREKETKALsLARALEEALEAKEElertnkmlkAEMEDLVSSKD--DVGKNVHELEKSKRALETQ 1540
Cdd:COG4942 88 ------LEKEIAELRAELEAQKEE-LAELLRALYRLGRQ---------PPLALLLSPEDflDAVRRLQYLKYLAPARREQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1541 MEEMKTQLEELEDELQATEDAKLRLEVNMQALKVQfERDLQARDEQNEEKRRQLQRQLHEYETELEDERKQRALAVAAKK 1620
Cdd:COG4942 152 AEELRADLAELAALRAELEAERAELEALLAELEEE-RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIA 230
|
250
....*....|....*.
gi 156120901 1621 KLEGDLKDLELQADSA 1636
Cdd:COG4942 231 RLEAEAAAAAERTPAA 246
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1015-1486 |
9.70e-08 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 57.14 E-value: 9.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1015 LAEEEEKAKNLTKLKNKHESMISELEVRLKKEEksrQELEKLKRKLDGEASDLHEQIAELQA----------QIAELKMQ 1084
Cdd:pfam10174 221 LQPDPAKTKALQTVIEMKDTKISSLERNIRDLE---DEVQMLKTNGLLHTEDREEEIKQMEVykshskfmknKIDQLKQE 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1085 LAKKEEELQAALGRLDDEMAQKNNALKKIREL-------EGHISDLQEDLDSER-------AARNKAEKQKRDLGEELEA 1150
Cdd:pfam10174 298 LSKKESELLALQTKLETLTNQNSDCKQHIEVLkesltakEQRAAILQTEVDALRlrleekeSFLNKKTKQLQDLTEEKST 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1151 LKTELEDTLDSTATqqelrakREQEVTMLKK---ALDEETRSHESQVQEMRQKHTQVVEE----------LTEQLEQFKR 1217
Cdd:pfam10174 378 LAGEIRDLKDMLDV-------KERKINVLQKkieNLQEQLRDKDKQLAGLKERVKSLQTDssntdtalttLEEALSEKER 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1218 AKANLDKNKQALEKENAElagELRVLSQAKQEVEHKKKKLEVQLQELQSKYSDGEKVRAELNDKVHKLQNEVESVtgmln 1297
Cdd:pfam10174 451 IIERLKEQREREDRERLE---ELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSL----- 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1298 eaEGKAIKLAKDVASLGSQLQDTQELlQEETRQKLNVSTKLRQLEDERNSLQEqldEEMEAKQNLERHISTL---NIQLS 1374
Cdd:pfam10174 523 --EIAVEQKKEECSKLENQLKKAHNA-EEAVRTNPEINDRIRLLEQEVARYKE---ESGKAQAEVERLLGILrevENEKN 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1375 DSKKKLQDFASTVELLEEGKKKFQKEIESLTQQYEEKAAAYD------KLEKTKNRLQQELDDLVVDLDNQRQLVSNLEK 1448
Cdd:pfam10174 597 DKDKKIAELESLTLRQMKEQNKKVANIKHGQQEMKKKGAQLLeearrrEDNLADNSQQLQLEELMGALEKTRQELDATKA 676
|
490 500 510
....*....|....*....|....*....|....*...
gi 156120901 1449 KQKKFDQLLAEEKNISSKYADERDRAEAEAREKETKAL 1486
Cdd:pfam10174 677 RLSSTQQSLAEKDGHLTNLRAERRKQLEEILEMKQEAL 714
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
846-1269 |
9.95e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.08 E-value: 9.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 846 QVTRQEEEMQAKEDELQKTKERQQKAESELKELEQKHSQLTEEKNLLQEQLQAETELyaeaeemrvrlaakkQELEEILH 925
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLY---------------QELEALEA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 926 EMEARLEEEEDRSQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDDILVMDDQNNKLSKERKLLE 1005
Cdd:COG4717 140 ELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQ 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1006 ERISDLTTNLAEEEEKAKNLTKLKNKHE--------SMISELEVRLKKEEKSRQELEKLKRKLDG----EASDLHEQIAE 1073
Cdd:COG4717 220 EELEELEEELEQLENELEAAALEERLKEarlllliaAALLALLGLGGSLLSLILTIAGVLFLVLGllalLFLLLAREKAS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1074 LQAQIAELKMQLAKKEEELQAALGRLDDEMAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQ--KRDLGEELEAL 1151
Cdd:COG4717 300 LGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEelEQEIAALLAEA 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1152 KTELEDTLDSTATQQELRAKREQEVTMLKKALDEETRSHESQVQemrqkhTQVVEELTEQLEQFKRAKANLDKNKQALEK 1231
Cdd:COG4717 380 GVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLE------ALDEEELEEELEELEEELEELEEELEELRE 453
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 156120901 1232 ENAELAGELRVL--SQAKQEVEHKKKKLEVQLQELQSKYS 1269
Cdd:COG4717 454 ELAELEAELEQLeeDGELAELLQELEELKAELRELAEEWA 493
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
846-1326 |
1.03e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 57.44 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 846 QVTRQEEEMQAKEDELQK----------TKERQQKAESELKE----LEQKHSQLTEEKNLLQEQLQAETELYAEAEEMRV 911
Cdd:pfam15921 445 QMERQMAAIQGKNESLEKvssltaqlesTKEMLRKVVEELTAkkmtLESSERTVSDLTASLQEKERAIEATNAEITKLRS 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 912 RLAAKKQELEEILHEMEARLEEEED-RSQQLQ-AERKK----MAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKI--KKL 983
Cdd:pfam15921 525 RVDLKLQELQHLKNEGDHLRNVQTEcEALKLQmAEKDKvieiLRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEIndRRL 604
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 984 E-DDILVMDDQNNKLSKErklLEERISDLTTN----LAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKR 1058
Cdd:pfam15921 605 ElQEFKILKDKKDAKIRE---LEARVSDLELEkvklVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKR 681
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1059 KLDGEASDLHEQIAELQAQIAELKMQLAKKEEELQAALGRLDDEMAQKNNALKKIRELEGHISDLQEDLDSERAARNKAE 1138
Cdd:pfam15921 682 NFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNAN 761
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1139 KQKRDLGEElealKTELEDTLDSTATQqelrakreqevtmlkkaldeetrshesqvqemRQKHTQVVEELTEQLEQFKRA 1218
Cdd:pfam15921 762 KEKHFLKEE----KNKLSQELSTVATE--------------------------------KNKMAGELEVLRSQERRLKEK 805
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1219 KANLDknkQALEKENAELAGELRVLSQAKQEVEHKKKKLEVQLQELQSK-YSDGEKVRAEL-----NDKVHKLQNEVESV 1292
Cdd:pfam15921 806 VANME---VALDKASLQFAECQDIIQRQEQESVRLKLQHTLDVKELQGPgYTSNSSMKPRLlqpasFTRTHSNVPSSQST 882
|
490 500 510
....*....|....*....|....*....|....
gi 156120901 1293 TGMLNEAEGKAIKLAKDVAslgsqlQDTQELLQE 1326
Cdd:pfam15921 883 ASFLSHHSRKTNALKEDPT------RDLKQLLQE 910
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1528-1930 |
1.07e-07 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 57.27 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1528 HELEKSKRAL---ETQMEEMKTQLEE-------LEDELQATEDaklRLEVNMQALKVQ--FER------DLQARDEQNEE 1589
Cdd:COG3096 292 RELFGARRQLaeeQYRLVEMARELEElsaresdLEQDYQAASD---HLNLVQTALRQQekIERyqedleELTERLEEQEE 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1590 KRRQLQRQLHEYETELEderkqraLAVAAKKKLEGDLKD----LELQADSAIKGREeAIKQLRKLQAQMKDFQRELEDAr 1665
Cdd:COG3096 369 VVEEAAEQLAEAEARLE-------AAEEEVDSLKSQLADyqqaLDVQQTRAIQYQQ-AVQALEKARALCGLPDLTPENA- 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1666 asrDEIFATAKEnekKAKSLEADLMQLQEDLAAAERARKQADlEKDELAEELASSVSGRNALQDEKRRLEARIAQleeel 1745
Cdd:COG3096 440 ---EDYLAAFRA---KEQQATEEVLELEQKLSVADAARRQFE-KAYELVCKIAGEVERSQAWQTARELLRRYRSQ----- 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1746 eeeqgnteamservRKATQQAEQLSNELATERSAAQKNENARQQLERQNKELRSKLQEMEgavkskfkstiaALEAKIAQ 1825
Cdd:COG3096 508 --------------QALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAE------------ELEELLAE 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1826 LEEQVE---QEAREKQATAKALKQKDKKLKEallQVEDERKMAEQYKEQAEkgnlRVKQLKRQLEEAEEESQRINANRRK 1902
Cdd:COG3096 562 LEAQLEeleEQAAEAVEQRSELRQQLEQLRA---RIKELAARAPAWLAAQD----ALERLREQSGEALADSQEVTAAMQQ 634
|
410 420
....*....|....*....|....*...
gi 156120901 1903 LQRELDEATESNEAMGREVTALKSKLRR 1930
Cdd:COG3096 635 LLEREREATVERDELAARKQALESQIER 662
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1202-1414 |
1.56e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.93 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1202 TQVVEELTEQLEQFKRAKANLDKNKQALEKENAELAGELRVLSQAKQEVEHKKKKLEVQLQELQSKYSDGEKVRAELNDK 1281
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1282 VHKLQNEVESVTGML----NEAEGKAIKLAKDVASLGSQLQDTQELLQEETRQKLNVSTKLRQLEDERNSLQEQ------ 1351
Cdd:COG4942 99 LEAQKEELAELLRALyrlgRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAEraelea 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156120901 1352 -LDEEMEAKQNLERHISTLNIQLSDSKKKLQDFASTVELLEEGKKKFQKEIESLTQQYEEKAAA 1414
Cdd:COG4942 179 lLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
877-1916 |
1.62e-07 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 56.98 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 877 ELEQKHSQLTEEKNLLQEQLQAETELYAEAEEMRVRLAAKKQELEEILHEMEARLEEEEDRSQQLQAERKKMAQQMLDLE 956
Cdd:TIGR01612 513 ELYKPDEVPSKNIIGFDIDQNIKAKLYKEIEAGLKESYELAKNWKKLIHEIKKELEEENEDSIHLEKEIKDLFDKYLEID 592
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 957 EQLEEEEAARQKLQlEKVT----AEAKIKKLEDDILVMDDQNNKLSKERKLLEERISDLTTNLAEEEEKAK--------- 1023
Cdd:TIGR01612 593 DEIIYINKLKLELK-EKIKnisdKNEYIKKAIDLKKIIENNNAYIDELAKISPYQVPEHLKNKDKIYSTIKselskiyed 671
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1024 NLTKLKNKHESMISELEVRlKKEEKSRqeLEKLKRKLDGEAS----------------------DLHEQIAELQAQI-AE 1080
Cdd:TIGR01612 672 DIDALYNELSSIVKENAID-NTEDKAK--LDDLKSKIDKEYDkiqnmetatvelhlsnienkknELLDIIVEIKKHIhGE 748
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1081 LKMQLAK-------KEEELQAALGRLDDEMAQKNNALKKIRELEGHISDlQEDLDSeraarNKAEKQKRDLGEELEALKT 1153
Cdd:TIGR01612 749 INKDLNKiledfknKEKELSNKINDYAKEKDELNKYKSKISEIKNHYND-QINIDN-----IKDEDAKQNYDKSKEYIKT 822
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1154 ELEDTLDSTATQQELRAKREQEVTMLKKALD------EETRSHESQVQEMRQKHTQVV--EELTEQLEQFKRAKANLDKN 1225
Cdd:TIGR01612 823 ISIKEDEIFKIINEMKFMKDDFLNKVDKFINfennckEKIDSEHEQFAELTNKIKAEIsdDKLNDYEKKFNDSKSLINEI 902
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1226 KQALEKEN------AELAGELRVLSQAKQEVEHKKKKlEVQLQELQSKYSDGEKvRAELNDKVHKLQNEvESVTGMLNEA 1299
Cdd:TIGR01612 903 NKSIEEEYqnintlKKVDEYIKICENTKESIEKFHNK-QNILKEILNKNIDTIK-ESNLIEKSYKDKFD-NTLIDKINEL 979
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1300 EgkaiKLAKDvASLGSQLQDTQELLQEETRQKLNVSTklrqleDERNSLQEQLDEEMEAKQNLERHISTLNIQLSDSKKK 1379
Cdd:TIGR01612 980 D----KAFKD-ASLNDYEAKNNELIKYFNDLKANLGK------NKENMLYHQFDEKEKATNDIEQKIEDANKNIPNIEIA 1048
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1380 LqdFASTVELLEEGKKKFQKEIESLTQQYEEKA-AAYDKLEKTKNRLQQ-ELDDLVV--------DLDNQRQLVSNLEKK 1449
Cdd:TIGR01612 1049 I--HTSIYNIIDEIEKEIGKNIELLNKEILEEAeINITNFNEIKEKLKHyNFDDFGKeenikyadEINKIKDDIKNLDQK 1126
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1450 QKKFDQLLAEEKNISSKYADERDRAEAEAREKETKALSLARALEEALEAKEELERTNKM--LKAEMEDLVSSKDDVGKNV 1527
Cdd:TIGR01612 1127 IDHHIKALEEIKKKSENYIDEIKAQINDLEDVADKAISNDDPEEIEKKIENIVTKIDKKknIYDEIKKLLNEIAEIEKDK 1206
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1528 HELEKSKRALETQMEEMKTQ-LEELEDELQATEDAKLRLEVNMQALKVQFERDLQARDEQNEEkrRQLQRQLHEYETELE 1606
Cdd:TIGR01612 1207 TSLEEVKGINLSYGKNLGKLfLEKIDEEKKKSEHMIKAMEAYIEDLDEIKEKSPEIENEMGIE--MDIKAEMETFNISHD 1284
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1607 DERKQRALAvaakKKLEGDLKDLELQADSAIKG--REEAIKQLRK-LQAQMKDFQRELEDARASRDEIfaTAKENEKKAK 1683
Cdd:TIGR01612 1285 DDKDHHIIS----KKHDENISDIREKSLKIIEDfsEESDINDIKKeLQKNLLDAQKHNSDINLYLNEI--ANIYNILKLN 1358
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1684 SLEADLMQLQEDLAAAERARKQADLEKDElAEELASSVSGRNALQDEKRRLEARIaqleeeleeeqgNTEAMSERVRKAT 1763
Cdd:TIGR01612 1359 KIKKIIDEVKEYTKEIEENNKNIKDELDK-SEKLIKKIKDDINLEECKSKIESTL------------DDKDIDECIKKIK 1425
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1764 QQAEQL----SNELATERSAAQKNENArqQLERQNKEL-RSKLQEMegaVKSKFKSTIAALEAKIAQLEEQVEQEAREKQ 1838
Cdd:TIGR01612 1426 ELKNHIlseeSNIDTYFKNADENNENV--LLLFKNIEMaDNKSQHI---LKIKKDNATNDHDFNINELKEHIDKSKGCKD 1500
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1839 ATAKALKQKDKKlKEALLQVEDE-RKMAEQYKEQAEKGNL------------RVKQLKRQLE-EAEEESQRINANRRKLQ 1904
Cdd:TIGR01612 1501 EADKNAKAIEKN-KELFEQYKKDvTELLNKYSALAIKNKFaktkkdseiiikEIKDAHKKFIlEAEKSEQKIKEIKKEKF 1579
|
1130
....*....|..
gi 156120901 1905 RELDEATESNEA 1916
Cdd:TIGR01612 1580 RIEDDAAKNDKS 1591
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1057-1277 |
1.65e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 55.61 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1057 KRKLDGEASDLHEQIAELQAQIAELKMQLAKKEEELQAALGRLDDEMAQKNNALKKIRELEGHISDLQEDLdserAARNK 1136
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL----GERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1137 AEKQKRDLGEELEALkteledtLDSTATQQELrakreQEVTMLKKALDEETRSHEsQVQEMRQKHTQVVEELTEQLEQFK 1216
Cdd:COG3883 94 ALYRSGGSVSYLDVL-------LGSESFSDFL-----DRLSALSKIADADADLLE-ELKADKAELEAKKAELEAKLAELE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 156120901 1217 RAKANLDKNKQALEKENAELAGELRVLSQAKQEVEHKKKKLEVQLQELQSKYSDGEKVRAE 1277
Cdd:COG3883 161 ALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1443-1855 |
1.80e-07 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 56.50 E-value: 1.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1443 VSNLEKKQKKFDQLLAEEKNISS---KYADERDRAEAEAREKETKAlslARALEEALEAKEELERTNKMLKAemedlVSS 1519
Cdd:COG3096 274 MRHANERRELSERALELRRELFGarrQLAEEQYRLVEMARELEELS---ARESDLEQDYQAASDHLNLVQTA-----LRQ 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1520 KDDVGKNVHELEKSKRALETQMEemktQLEELEDELQATEDAKLRLEVNMQALKVQFERDLQARDEQneeKRRQLQRQlh 1599
Cdd:COG3096 346 QEKIERYQEDLEELTERLEEQEE----VVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQ---QTRAIQYQ-- 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1600 EYETELEDERKQRALAVAAKKKLEGDLKDLELQADSAIKGREEAIKQLRKLQAQMKDFQRELEDARA-----SRDEIFAT 1674
Cdd:COG3096 417 QAVQALEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKiagevERSQAWQT 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1675 AKENEKKAKSLEA---DLMQLQEDLAAAE-RARKQADLEK--DELAEELASSVSGRNALQDEKRRLEARIAQLEEELEEE 1748
Cdd:COG3096 497 ARELLRRYRSQQAlaqRLQQLRAQLAELEqRLRQQQNAERllEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEA 576
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1749 QGNTEAMSERVRKATQQAEQLSNELATERSAAQKNENARQQLERQNKELRSKLQEMEGAVKSKFKSTiaALEAKIAQLEE 1828
Cdd:COG3096 577 VEQRSELRQQLEQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEVTAAMQQLLEREREAT--VERDELAARKQ 654
|
410 420
....*....|....*....|....*..
gi 156120901 1829 QVEQEAREKQATAKALKQKDKKLKEAL 1855
Cdd:COG3096 655 ALESQIERLSQPGGAEDPRLLALAERL 681
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1450-1867 |
1.99e-07 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 56.06 E-value: 1.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1450 QKKFDQLLAEEKNISSKYADERDRAEAEAREKETKALSLARALEEALEAKEELERTNKMLKAEMEDLVSSKDDVGKNVHE 1529
Cdd:pfam07888 33 QNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1530 LEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKVQFERDLQARDEQnEEKRRQLQRQLHEYETELeder 1609
Cdd:pfam07888 113 LSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEE-EAERKQLQAKLQQTEEEL---- 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1610 kqRALAvaakKKLEGDLKDLELQADSAIKGREEAIKQLRKL-QAQMKDFQRE--LEDARASRDEIFATakenEKKAKSLE 1686
Cdd:pfam07888 188 --RSLS----KEFQELRNSLAQRDTQVLQLQDTITTLTQKLtTAHRKEAENEalLEELRSLQERLNAS----ERKVEGLG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1687 ADL--MQLQEDLAAAE--RARKQADLEKDELAEELASSVSGRNALQDEKRRLEARIAQLEEELEEEQGNTEAMSERVRKA 1762
Cdd:pfam07888 258 EELssMAAQRDRTQAElhQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEE 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1763 TQQAEQLSNELATERSAaqkNENARQQLERQNKELRSKLQEMEGAvKSKFKSTIAALEAKIAQLEEQVEQEAREKQATAK 1842
Cdd:pfam07888 338 RMEREKLEVELGREKDC---NRVQLSESRRELQELKASLRVAQKE-KEQLQAEKQELLEYIRQLEQRLETVADAKWSEAA 413
|
410 420
....*....|....*....|....*
gi 156120901 1843 ALkqKDKKLKEALLQVEDERKMAEQ 1867
Cdd:pfam07888 414 LT--STERPDSPLSDSEDENPEALQ 436
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1207-1934 |
2.01e-07 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 56.50 E-value: 2.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1207 ELTEQLEQFKRAKANlDKNKQALEKEN-AELAGELRVLSQAKQEVEHKKKKLEVQLQELQSKYSDGEKV---RAELNDKV 1282
Cdd:COG3096 282 ELSERALELRRELFG-ARRQLAEEQYRlVEMARELEELSARESDLEQDYQAASDHLNLVQTALRQQEKIeryQEDLEELT 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1283 HKL--QNE-VESVTGMLNEAEGKAIKLAKDVASLGSQLQDTQELLQEETRQKLNVSTKLRQLEDERNSLQ------EQLD 1353
Cdd:COG3096 361 ERLeeQEEvVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAIQYQQAVQALEKARALCGlpdltpENAE 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1354 EEMEA----KQNLERHISTLNIQLSDSKKKLQDFASTVELLE------EGKKKFQKEIESLTQQYEEKAAAydkleKTKN 1423
Cdd:COG3096 441 DYLAAfrakEQQATEEVLELEQKLSVADAARRQFEKAYELVCkiagevERSQAWQTARELLRRYRSQQALA-----QRLQ 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1424 RLQQELDDLVVDLDNQRQLVSNLEKKQKKFDQLLAEEKNIsskyadERDRAEAEAREKEtkalsLARALEEALEAKEELE 1503
Cdd:COG3096 516 QLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEEL------EELLAELEAQLEE-----LEEQAAEAVEQRSELR 584
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1504 RTNKMLKAEMEDLVSSkddvgknvhelEKSKRALETQMEEMKTQLEELEDELQATEDAklrlevnMQALkVQFERDLQAR 1583
Cdd:COG3096 585 QQLEQLRARIKELAAR-----------APAWLAAQDALERLREQSGEALADSQEVTAA-------MQQL-LEREREATVE 645
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1584 DEQNEEKRRQLQRQLHEYETE--LEDERkqralAVAAKKKLEGDL-----KDLELQ-----------ADSAIKGR--EEA 1643
Cdd:COG3096 646 RDELAARKQALESQIERLSQPggAEDPR-----LLALAERLGGVLlseiyDDVTLEdapyfsalygpARHAIVVPdlSAV 720
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1644 IKQLRKLQAQMKDFQRELEDARASRDEIFaTAKENEKkaksleADLMQLQE--------------DLAAAERARKQADLE 1709
Cdd:COG3096 721 KEQLAGLEDCPEDLYLIEGDPDSFDDSVF-DAEELED------AVVVKLSDrqwrysrfpevplfGRAAREKRLEELRAE 793
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1710 KDELAEELASSVSGRNALQDEKRRLEARIAQleEELEEEQGNTEAMSERVRKATQQAE-QLSNELATERSAAQKNENARQ 1788
Cdd:COG3096 794 RDELAEQYAKASFDVQKLQRLHQAFSQFVGG--HLAVAFAPDPEAELAALRQRRSELErELAQHRAQEQQLRQQLDQLKE 871
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1789 QLERQNK------------------ELRSKLQEMEGAVKS--KFKSTIAALEAKIAQLEEQVEQEAREKQATaKALKQKD 1848
Cdd:COG3096 872 QLQLLNKllpqanlladetladrleELREELDAAQEAQAFiqQHGKALAQLEPLVAVLQSDPEQFEQLQADY-LQAKEQQ 950
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1849 KKLKEALLQVED--ERKMAEQYKEQAE---KGNLRVKQLKRQLEEAEEESQRINANRRKLQRELDEATesneamgREVTA 1923
Cdd:COG3096 951 RRLKQQIFALSEvvQRRPHFSYEDAVGllgENSDLNEKLRARLEQAEEARREAREQLRQAQAQYSQYN-------QVLAS 1023
|
810
....*....|.
gi 156120901 1924 LKSKLRRGNET 1934
Cdd:COG3096 1024 LKSSRDAKQQT 1034
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1050-1240 |
2.39e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 53.78 E-value: 2.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1050 RQELEKLKR--KLDGEASDLHEQIAELQAQIAELKMQLAKKEEELQAALGRLDDEMAQKNNALKKIRELEGHISDLQEDL 1127
Cdd:COG1579 3 PEDLRALLDlqELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1128 DSERAARnkaekqkrdlgeELEALKTELEdtldstaTQQELRAKREQEVtmlkKALDEETRSHESQVQEMRQKHTQVVEE 1207
Cdd:COG1579 83 GNVRNNK------------EYEALQKEIE-------SLKRRISDLEDEI----LELMERIEELEEELAELEAELAELEAE 139
|
170 180 190
....*....|....*....|....*....|...
gi 156120901 1208 LTEQLEQFKRAKANLDKNKQALEKENAELAGEL 1240
Cdd:COG1579 140 LEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1191-1448 |
2.58e-07 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 55.79 E-value: 2.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1191 ESQVQEMRQKH--TQVVEELTEQLEQFKRAKANLDKnKQALEKENAELAgelrvlSQAKQEVEhkkkKLEVQLQELQSKY 1268
Cdd:PHA02562 182 QIQTLDMKIDHiqQQIKTYNKNIEEQRKKNGENIAR-KQNKYDELVEEA------KTIKAEIE----ELTDELLNLVMDI 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1269 SDGEKVRAELNDKVHKLQNEVESVTgmlneaegKAIKLAKD---VASLGSQLQDTQELLQEETRQKLNVSTKLRQLEDER 1345
Cdd:PHA02562 251 EDPSAALNKLNTAAAKIKSKIEQFQ--------KVIKMYEKggvCPTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAI 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1346 NSLQEQLDEEMEA---KQNLERHISTLNIQLSDSKKKLqdfastvelleegkKKFQKEIESLTQQYEEKAAAYDKLEKTK 1422
Cdd:PHA02562 323 DELEEIMDEFNEQskkLLELKNKISTNKQSLITLVDKA--------------KKVKAAIEELQAEFVDNAEELAKLQDEL 388
|
250 260
....*....|....*....|....*.
gi 156120901 1423 NRLQQELDDLVVDLDnQRQLVSNLEK 1448
Cdd:PHA02562 389 DKIVKTKSELVKEKY-HRGIVTDLLK 413
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1033-1246 |
2.63e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 55.79 E-value: 2.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1033 ESMISELEVRLkkeEKSRQELEKLKRK-----LDGEASDLHEQIAELQAQIAELKMQLAKKEEELQAALGRLDDEMAQKN 1107
Cdd:COG3206 181 EEQLPELRKEL---EEAEAALEEFRQKnglvdLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALP 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1108 NALKK--IRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALKTELEDTLDS--TATQQELRAKREQEvtmlkKAL 1183
Cdd:COG3206 258 ELLQSpvIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRilASLEAELEALQARE-----ASL 332
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 156120901 1184 DEETRSHESQVQEMRQKHTQvVEELTEQLEQFKRAKANLDKNKQALEKENAELAGELRVLSQA 1246
Cdd:COG3206 333 QAQLAQLEARLAELPELEAE-LRRLEREVEVARELYESLLQRLEEARLAEALTVGNVRVIDPA 394
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1089-1466 |
2.70e-07 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 56.07 E-value: 2.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1089 EEELQAALgrlddemaqknNALKKIRELEGHISDLQEDLDSERAARNKAEKQKrdlgEELEALKTELEDtldstATQQEL 1168
Cdd:PRK11281 38 EADVQAQL-----------DALNKQKLLEAEDKLVQQDLEQTLALLDKIDRQK----EETEQLKQQLAQ-----APAKLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1169 RAKREqeVTMLKKALDEETRSH---------ESQVQEMRQKHTQVVEELTE-------QLEQFKRAKANLDKNKQALEKE 1232
Cdd:PRK11281 98 QAQAE--LEALKDDNDEETRETlstlslrqlESRLAQTLDQLQNAQNDLAEynsqlvsLQTQPERAQAALYANSQRLQQI 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1233 NAELAG----------ELRVLSQAKQ-----EVEHKKKKLEV--QLQELqskysdGEKVRAELNDKVHKLQNEVESVTGM 1295
Cdd:PRK11281 176 RNLLKGgkvggkalrpSQRVLLQAEQallnaQNDLQRKSLEGntQLQDL------LQKQRDYLTARIQRLEHQLQLLQEA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1296 LNEaegKAIKLAKDVASLGSQLQDTQE-----LLQEETRQKLNVSTKLRQLEDERNSLQEQ-------LDEEMEAKQNLE 1363
Cdd:PRK11281 250 INS---KRLTLSEKTVQEAQSQDEAARiqanpLVAQELEINLQLSQRLLKATEKLNTLTQQnlrvknwLDRLTQSERNIK 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1364 RHISTLNIQLSDSK---KKLQDFASTVELLEEGKK--KFQKEIESLTQQYEE--KAAAY-DKLEKT---------KNRLQ 1426
Cdd:PRK11281 327 EQISVLKGSLLLSRilyQQQQALPSADLIEGLADRiaDLRLEQFEINQQRDAlfQPDAYiDKLEAGhksevtdevRDALL 406
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 156120901 1427 QE-------LDDLVVDLDNQRQLVSNLEKKQKkfdQLLAEEKNISSK 1466
Cdd:PRK11281 407 QLlderrelLDQLNKQLNNQLNLAINLQLNQQ---QLLSVSDSLQST 450
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1171-1883 |
2.76e-07 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 55.88 E-value: 2.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1171 KREQEVTMLKKALDEETRSHESQVQEMR---QKHTQVVEELTEQLEQFKRAKANLDKNKQALEKENAELAGELRVLSQAK 1247
Cdd:pfam05483 85 KEAEKIKKWKVSIEAELKQKENKLQENRkiiEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRHLCNLLKETC 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1248 QEVEHKKKKLEVQLQELQSKYSD------------------GEKVRAELNDKV----HKLQNEVESVTGMLNEAEGKAIK 1305
Cdd:pfam05483 165 ARSAEKTKKYEYEREETRQVYMDlnnniekmilafeelrvqAENARLEMHFKLkedhEKIQHLEEEYKKEINDKEKQVSL 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1306 LAKDVASLGSQLQDTQELLqEETRQKLNvstklrQLEDERNSLQEQLDEEMEAKQNLERhistlniQLSDSKKKLQDFAS 1385
Cdd:pfam05483 245 LLIQITEKENKMKDLTFLL-EESRDKAN------QLEEKTKLQDENLKELIEKKDHLTK-------ELEDIKMSLQRSMS 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1386 TVELLEEGKKKFQKEIESLTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQ-RQLVSNLEKKQKKFDQLLAEEKNIS 1464
Cdd:pfam05483 311 TQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELlRTEQQRLEKNEDQLKIITMELQKKS 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1465 SKYADERDRAEAEAREKETKALSLArALEEALEAKEELERTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEM 1544
Cdd:pfam05483 391 SELEEMTKFKNNKEVELEELKKILA-EDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHY 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1545 KTQLEELEDELQATEDAKLRLEVNMQALKVQferdlqardeqneekRRQLQRQLHEYETELedeRKQRALAVAAKKKLEG 1624
Cdd:pfam05483 470 LKEVEDLKTELEKEKLKNIELTAHCDKLLLE---------------NKELTQEASDMTLEL---KKHQEDIINCKKQEER 531
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1625 DLKDLELQADSAIKGREEAIKQLRKLQAQMKDFQRELEDARASRDEIFATAKENEKKAKSLEADLMQLQEDLAAAERARK 1704
Cdd:pfam05483 532 MLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIE 611
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1705 QADLEKDELAEELASSVSGRNALQDEKRRLEARIAQLEEELEEEQGNTEAMSErVRKATQqaEQLSNELATERSAAQKNE 1784
Cdd:pfam05483 612 ELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIE-DKKISE--EKLLEEVEKAKAIADEAV 688
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1785 NARQQLERQNKELRSKLQEMEGAVKSKFKSTIAALEAKIAQLEEQVEQEAREKQATAKALKQKDKKLKEALLQVEDERKM 1864
Cdd:pfam05483 689 KLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEE 768
|
730
....*....|....*....
gi 156120901 1865 AEQYKEQAEKGNLRVKQLK 1883
Cdd:pfam05483 769 KEKLKMEAKENTAILKDKK 787
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1084-1918 |
2.91e-07 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 56.11 E-value: 2.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1084 QLAKKEEELQAALGRLDDEMAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRdLGEELEALKTELEDTLDSTA 1163
Cdd:COG3096 286 RALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTALR-QQEKIERYQEDLEELTERLE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1164 TQQELRAKREQEVTMLkkaldeETRSHESQVQemrqkhtqvVEELTEQLEQFKRAkanLD-------KNKQALE-KENAE 1235
Cdd:COG3096 365 EQEEVVEEAAEQLAEA------EARLEAAEEE---------VDSLKSQLADYQQA---LDvqqtraiQYQQAVQaLEKAR 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1236 LAGELRVLS--QAKQEVEHKKKKLEV---QLQELQSKYSDGEKVRAELnDKVHKLqneVESVTGML--NEAEGKAIKLAK 1308
Cdd:COG3096 427 ALCGLPDLTpeNAEDYLAAFRAKEQQateEVLELEQKLSVADAARRQF-EKAYEL---VCKIAGEVerSQAWQTARELLR 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1309 DVASLGSQLQDTQELlqeetRQKLnvsTKLRQLEDERNSLQEQLDE-------EMEAKQNLERHISTLNIQLSDSKKKLQ 1381
Cdd:COG3096 503 RYRSQQALAQRLQQL-----RAQL---AELEQRLRQQQNAERLLEEfcqrigqQLDAAEELEELLAELEAQLEELEEQAA 574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1382 DFASTVELLEEGKKKFQKEIESLTQQYEEKAAAYDKLEKTKNRLQQELDDLVvDLDNQRQLVSNLEKKQKKFDQLLAEEK 1461
Cdd:COG3096 575 EAVEQRSELRQQLEQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQ-EVTAAMQQLLEREREATVERDELAARK 653
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1462 nisskyaderDRAEAEARE-------KETKALSLAraleealeakeelERTNKMLKAEMEDLVSSKDD------VGKNVH 1528
Cdd:COG3096 654 ----------QALESQIERlsqpggaEDPRLLALA-------------ERLGGVLLSEIYDDVTLEDApyfsalYGPARH 710
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1529 ELekskraLETQMEEMKTQLEELEDELqatEDAKLrlevnmqalkvqFERDLQARDEQ----NEEKRRQL----QRQLhE 1600
Cdd:COG3096 711 AI------VVPDLSAVKEQLAGLEDCP---EDLYL------------IEGDPDSFDDSvfdaEELEDAVVvklsDRQW-R 768
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1601 YETELEDERKQRAlavAAKKKLEgdlkDLELQADSAIKGREEAIKQLRKLQAQMKDFQR----------------ELEDA 1664
Cdd:COG3096 769 YSRFPEVPLFGRA---AREKRLE----ELRAERDELAEQYAKASFDVQKLQRLHQAFSQfvgghlavafapdpeaELAAL 841
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1665 RASRDEIFATAKENEKKAKSLEADLMQLQEDLAAAERARKQADLEKDELAEELassvsgrnaLQDEKRRLEAriAQLEEE 1744
Cdd:COG3096 842 RQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQANLLADETLADR---------LEELREELDA--AQEAQA 910
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1745 LEEEQGNTeamservrkatqqAEQLSNELATERSAAQKNENARQQLERQNKELRsklqemegavksKFKSTIAALEAKIA 1824
Cdd:COG3096 911 FIQQHGKA-------------LAQLEPLVAVLQSDPEQFEQLQADYLQAKEQQR------------RLKQQIFALSEVVQ 965
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1825 QLEEQVEQEAREKQATAKALkqkDKKLKEALLQVEDERkmaeqykeqaEKGNLRVKQLKRQLEEAEEESQRINANRRKLQ 1904
Cdd:COG3096 966 RRPHFSYEDAVGLLGENSDL---NEKLRARLEQAEEAR----------REAREQLRQAQAQYSQYNQVLASLKSSRDAKQ 1032
|
890
....*....|....
gi 156120901 1905 RELDEATESNEAMG 1918
Cdd:COG3096 1033 QTLQELEQELEELG 1046
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1196-1911 |
3.16e-07 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 55.50 E-value: 3.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1196 EMRQKHTQVVEELTEQLEQFKRAKANLDKNKQALEKENAELAGELRVLSQAKQEVEHKKK----KLEVQLQELQSKYSDG 1271
Cdd:pfam05483 71 ENSEGLSRLYSKLYKEAEKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEkvslKLEEEIQENKDLIKEN 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1272 EKVRAELNDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLGSQLQDTQELLQEETRQKLNVSTKLRQLEDERNSLQEQ 1351
Cdd:pfam05483 151 NATRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1352 LDEEMEAKqnlERHISTLNIQLSDSKKKLQDFAStveLLEEGKKKFQKEIESLTQQYEEKAAAYDKlektKNRLQQELDD 1431
Cdd:pfam05483 231 YKKEINDK---EKQVSLLLIQITEKENKMKDLTF---LLEESRDKANQLEEKTKLQDENLKELIEK----KDHLTKELED 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1432 LVVDL----DNQRQLVSNLEKKQKKFDQLLAEEKNISSKYADERDRAEAEAREKETKALSLARALEEALEAKEELERTNK 1507
Cdd:pfam05483 301 IKMSLqrsmSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLK 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1508 MLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKT------QLEELEDELQATEDAKLRLevnMQALKVQFErDLQ 1581
Cdd:pfam05483 381 IITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKlldekkQFEKIAEELKGKEQELIFL---LQAREKEIH-DLE 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1582 ARDEQNEEKRRQLQRQLHEYETELEDERkqralavaakkklegdLKDLELQADSAIKGREEaikqlRKLQAQMKDFQREL 1661
Cdd:pfam05483 457 IQLTAIKTSEEHYLKEVEDLKTELEKEK----------------LKNIELTAHCDKLLLEN-----KELTQEASDMTLEL 515
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1662 EDaraSRDEIFATAKENE---KKAKSLEADLMQLQEDLaaaERARKQADLEKDELAEELASSVSGRNALQDEKRRLEARI 1738
Cdd:pfam05483 516 KK---HQEDIINCKKQEErmlKQIENLEEKEMNLRDEL---ESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQM 589
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1739 AQLEEELEEEQGNTEAMSERVRKATQQAEQLSNELATERSAAQKNENARQQLERQNKELRSKLQEM-------------- 1804
Cdd:pfam05483 590 KILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIidnyqkeiedkkis 669
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1805 -EGAVKSKFKSTIAALEAkiAQLEEQVEQEAREKQATAKALKQKDKKLKEALLQVEDERKMAEQYKEQ----------AE 1873
Cdd:pfam05483 670 eEKLLEEVEKAKAIADEA--VKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQeqssakaaleIE 747
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 156120901 1874 KGNLRVK--QLKRQLEEAEEEsqrinanRRKLQRELDEAT 1911
Cdd:pfam05483 748 LSNIKAEllSLKKQLEIEKEE-------KEKLKMEAKENT 780
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1545-1851 |
4.04e-07 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 55.34 E-value: 4.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1545 KTQLEELEDELQATEDAKLRLEvnmqalkvqfERdlQARDEQNEEKRRQLQRQLHEYETELEDERKQRALAVAAKKKLEG 1624
Cdd:PRK05035 435 KAEIRAIEQEKKKAEEAKARFE----------AR--QARLEREKAAREARHKKAAEARAAKDKDAVAAALARVKAKKAAA 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1625 DLKDLELQADSAIKGREEAIKQLRKLQAQmkdfqreledARASRDEifATAKENEKKAKsleadlmqlqedlAAAERARK 1704
Cdd:PRK05035 503 TQPIVIKAGARPDNSAVIAAREARKAQAR----------ARQAEKQ--AAAAADPKKAA-------------VAAAIARA 557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1705 QADleKDELAEELASSVSgrnALQDEKRRLEARIAQLEEeleeeqgnteamservRKATQQAEQLSNELATERSAAQKNE 1784
Cdd:PRK05035 558 KAK--KAAQQAANAEAEE---EVDPKKAAVAAAIARAKA----------------KKAAQQAASAEPEEQVAEVDPKKAA 616
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156120901 1785 N----ARQQLERQNKELRSKLQEMEGAVKSKFKSTIAALEAKIAQLEEQVEQEARE----KQATAKAL-KQKDKKL 1851
Cdd:PRK05035 617 VaaaiARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAKARKAAQQQANAEPEEAedpkKAAVAAAIaRAKAKKA 692
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1033-1159 |
4.95e-07 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 54.86 E-value: 4.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1033 ESMISELEVRLKKEEKSRQELEKLK-----RKLDGEASDLHEQIAELQAQIAELKMQLAKKE---EELQAALGRLDDEMA 1104
Cdd:COG2433 379 EEALEELIEKELPEEEPEAEREKEHeerelTEEEEEIRRLEEQVERLEAEVEELEAELEEKDeriERLERELSEARSEER 458
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 156120901 1105 QKNNALKKIRELEGHISDLQEDLDSEraaRNKAEKQKRDLGEELEALKTELEDTL 1159
Cdd:COG2433 459 REIRKDREISRLDREIERLERELEEE---RERIEELKRKLERLKELWKLEHSGEL 510
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
939-1278 |
5.23e-07 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 54.74 E-value: 5.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 939 QQLQAERKKMAQQMLDLEEQLEEEEAARQKlQLEKvTAEAKIKKLEDDILVMDDQNnKLSKERKLLEERIsdlttnlaEE 1018
Cdd:pfam17380 287 RQQQEKFEKMEQERLRQEKEEKAREVERRR-KLEE-AEKARQAEMDRQAAIYAEQE-RMAMERERELERI--------RQ 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1019 EEKAKNLTKLKNKHESM----ISELE----VRLKKEEKSRQELEKLKRKLDGEasdlHEQIAELQAQIAELKMQLAKKEE 1090
Cdd:pfam17380 356 EERKRELERIRQEEIAMeisrMRELErlqmERQQKNERVRQELEAARKVKILE----EERQRKIQQQKVEMEQIRAEQEE 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1091 ELQAALGRLDDEMAQKnnaLKKIRELEghisdLQEDLDSERAARNKAEKQKRDLGEELEALKTELEDTLDSTATQQELRA 1170
Cdd:pfam17380 432 ARQREVRRLEEERARE---MERVRLEE-----QERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEE 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1171 KreqevtmlKKALDEETRSHESQVQEMRQKHTQVVEELteqleqfKRAKANLDKNKQALEKENAELAGELRVLSQAKQEV 1250
Cdd:pfam17380 504 R--------KQAMIEEERKRKLLEKEMEERQKAIYEEE-------RRREAEEERRKQQEMEERRRIQEQMRKATEERSRL 568
|
330 340
....*....|....*....|....*...
gi 156120901 1251 EHKKKKLEVQLQELQSkysdgEKVRAEL 1278
Cdd:pfam17380 569 EAMEREREMMRQIVES-----EKARAEY 591
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1635-1928 |
6.35e-07 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 54.92 E-value: 6.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1635 SAIKGREEAIKQLRKLQAQMKDFQRELEDARASRDEIfataKENEKKAKSLEADLMQLQEDLAAAerarkQADLE--KDE 1712
Cdd:PRK11281 39 ADVQAQLDALNKQKLLEAEDKLVQQDLEQTLALLDKI----DRQKEETEQLKQQLAQAPAKLRQA-----QAELEalKDD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1713 LAEELASSVSGRNALQDEKRRLEARIAQLEEELEEEQGNTEAMS-----ERVRKAT----QQAEQLSNELATER------ 1777
Cdd:PRK11281 110 NDEETRETLSTLSLRQLESRLAQTLDQLQNAQNDLAEYNSQLVSlqtqpERAQAALyansQRLQQIRNLLKGGKvggkal 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1778 SAAQKNE-NARQQ-LERQNKELRsklQEMEGAVK--SKFKSTIAALEAKIAQLEEQVE--QEArekqATAKALKQKDKKL 1851
Cdd:PRK11281 190 RPSQRVLlQAEQAlLNAQNDLQR---KSLEGNTQlqDLLQKQRDYLTARIQRLEHQLQllQEA----INSKRLTLSEKTV 262
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 156120901 1852 KEALLQVEDERKMAEQYKEQAEKGNLRVKQ-LKRQLEEAEEESQRinaNRRKLQReLDEATESNEAMGREVTALKSKL 1928
Cdd:PRK11281 263 QEAQSQDEAARIQANPLVAQELEINLQLSQrLLKATEKLNTLTQQ---NLRVKNW-LDRLTQSERNIKEQISVLKGSL 336
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
844-1443 |
6.83e-07 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 54.81 E-value: 6.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 844 LLQVTRQEE---EMQAKEDELQKTKERQQKAESELKELE--QKHSQLTEEKNLLQEQLQAETELYAEAEEMRVRLAAKKQ 918
Cdd:PRK10246 246 LNWLTRLDElqqEASRRQQALQQALAAEEKAQPQLAALSlaQPARQLRPHWERIQEQSAALAHTRQQIEEVNTRLQSTMA 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 919 ELEEILHEMEARleeeedrSQQLQAERKKMAQQMldleeqleeeeAARQKLQL---EKVTAEAKIKKLEDDILVMDDQNN 995
Cdd:PRK10246 326 LRARIRHHAAKQ-------SAELQAQQQSLNTWL-----------AEHDRFRQwnnELAGWRAQFSQQTSDREQLRQWQQ 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 996 KLSKERKLLEErISDLTTNLAEEEekaknltklknkhesmISELEVRLKKEEKSRQELEKLKrkldGEASDLHEQIAELQ 1075
Cdd:PRK10246 388 QLTHAEQKLNA-LPAITLTLTADE----------------VAAALAQHAEQRPLRQRLVALH----GQIVPQQKRLAQLQ 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1076 AQIAELKMQLAKKEEELqaALGRLD-DEMAQKNNALKKIRELEGHISDLQE----------------------------D 1126
Cdd:PRK10246 447 VAIQNVTQEQTQRNAAL--NEMRQRyKEKTQQLADVKTICEQEARIKDLEAqraqlqagqpcplcgstshpaveayqalE 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1127 LDSERAARNKAEKQKRDLGEELEALKTELeDTLDSTATQQELRAKR----EQEVTM------------------LKKALD 1184
Cdd:PRK10246 525 PGVNQSRLDALEKEVKKLGEEGAALRGQL-DALTKQLQRDESEAQSlrqeEQALTQqwqavcaslnitlqpqddIQPWLD 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1185 EETRsHESQVQEMRQKHTqVVEELTEQLEQFKRAKANLDKNKQALEKENAELA-------GELRVLSQAKQEVEHKKKKL 1257
Cdd:PRK10246 604 AQEE-HERQLRLLSQRHE-LQGQIAAHNQQIIQYQQQIEQRQQQLLTALAGYAltlpqedEEASWLATRQQEAQSWQQRQ 681
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1258 EvQLQELQSKYSDGEKVRAELNDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLGSQLQDTQELLQEETRQkLNVSTK 1337
Cdd:PRK10246 682 N-ELTALQNRIQQLTPLLETLPQSDDLPHSEETVALDNWRQVHEQCLSLHSQLQTLQQQDVLEAQRLQKAQAQ-FDTALQ 759
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1338 LRQLEDERNSLQEQLDEEMEA-----KQNLERHISTLNIQLSDSKKKLQD-FASTVELLEEG--KKKFQKEIESLTQQYE 1409
Cdd:PRK10246 760 ASVFDDQQAFLAALLDEETLTqleqlKQNLENQRQQAQTLVTQTAQALAQhQQHRPDGLDLTvtVEQIQQELAQLAQQLR 839
|
650 660 670
....*....|....*....|....*....|....*....
gi 156120901 1410 EKAAAYDKL-----EKTKNRLQQEldDLVVDLDNQRQLV 1443
Cdd:PRK10246 840 ENTTRQGEIrqqlkQDADNRQQQQ--ALMQQIAQATQQV 876
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1450-1912 |
7.18e-07 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 54.67 E-value: 7.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1450 QKKFDQLLAEEKNISskyADERDRAEAEAREKETKALSLARALEEALEAKEELERTNkmLKAEMEDLVSSKDDVGKNVHE 1529
Cdd:TIGR00606 172 KQKFDEIFSATRYIK---ALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQ--ITSKEAQLESSREIVKSYENE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1530 LEKSKRALEtQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKVQFERDLQARDEQNEEKRRQLQRQLHEYE------- 1602
Cdd:TIGR00606 247 LDPLKNRLK-EIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKErelvdcq 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1603 TELEDERKQRALAVAAKKKLEGDLKDLELQAD---SAIKGREEAIKQLrKLQAQMKDFQRELEDARASRDEIFATAKENE 1679
Cdd:TIGR00606 326 RELEKLNKERRLLNQEKTELLVEQGRLQLQADrhqEHIRARDSLIQSL-ATRLELDGFERGPFSERQIKNFHTLVIERQE 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1680 KKAKSLEADLMQLQEDLAAAERARKQADLEKDELAEelassvsgrnALQDEKRRLEARIAQLEEELEEEQgNTEAMSERV 1759
Cdd:TIGR00606 405 DEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGR----------TIELKKEILEKKQEELKFVIKELQ-QLEGSSDRI 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1760 RKATQQAEQLSNELaterSAAQKNENARQQLERQnKELRSKlqemegavKSKFKSTIAALEAKIAQLE------EQVEQE 1833
Cdd:TIGR00606 474 LELDQELRKAEREL----SKAEKNSLTETLKKEV-KSLQNE--------KADLDRKLRKLDQEMEQLNhhtttrTQMEML 540
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 156120901 1834 AREKQATAKALKQKDKKLKEALLQVEDERKMAEQYKEQAEKGNLRVKQLKRQLEEAEEESQRINANRRKLQRELDEATE 1912
Cdd:TIGR00606 541 TKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEE 619
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
995-1288 |
7.90e-07 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 53.53 E-value: 7.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 995 NKLSKERKLLEERISDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLDGEASDLHEQIAEL 1074
Cdd:pfam19220 79 SAAEGELEELVARLAKLEAALREAEAAKEELRIELRDKTAQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQRA 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1075 QAQIAELKMQLAKKEEELQAALGRLDDEMAQKNNALKKIRELEG-------HISDLQEDLDSERAARNKAEKQkrdLGEE 1147
Cdd:pfam19220 159 EGELATARERLALLEQENRRLQALSEEQAAELAELTRRLAELETqldatraRLRALEGQLAAEQAERERAEAQ---LEEA 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1148 LEALKTEL-----------------EDTLDSTATQQELRAKREQEVTMLKKALDEETRSHESQVQEMRQKHTQvveeLTE 1210
Cdd:pfam19220 236 VEAHRAERaslrmklealtaraaatEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLER----RTQ 311
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 156120901 1211 QLEQFKRAKANLDKNKQALEKenaELAGELRVLSQAKQEVEHKKKKLEVQLQELQSKYSDGEKVRAELNDkvhKLQNE 1288
Cdd:pfam19220 312 QFQEMQRARAELEERAEMLTK---ALAAKDAALERAEERIASLSDRIAELTKRFEVERAALEQANRRLKE---ELQRE 383
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1006-1274 |
1.05e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 52.61 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1006 ERISDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLDGEASDLHEQIAELQAQIAELKmql 1085
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELK--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1086 aKKEEELQAALGRLDDEMAQKNNALKKIRELEGHISDLQEDLDSER----------AARNKAEKQKRDLGEELEALKTEL 1155
Cdd:COG1340 78 -EERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEwrqqtevlspEEEKELVEKIKELEKELEKAKKAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1156 EDTLDSTATQQELRAKREQ--EVTMLKKALDEETRSHESQVQEMRQKHTQVVEELTEQLEQFKRAKANLDKNKQ---ALE 1230
Cdd:COG1340 157 EKNEKLKELRAELKELRKEaeEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEeiiELQ 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 156120901 1231 KENAELAGELRVLS--QAKQEVEHKKKKLEVQLQELQSKYSDGEKV 1274
Cdd:COG1340 237 KELRELRKELKKLRkkQRALKREKEKEELEEKAEEIFEKLKKGEKL 282
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
846-1706 |
1.11e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 54.19 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 846 QVTRQEEEMQAKEDELQKTKERQQKAESELKELEQKHSQLTEEK-------NLLQE--QLQAETELY-AEAEEMRVRLAA 915
Cdd:COG3096 286 RALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYqaasdhlNLVQTalRQQEKIERYqEDLEELTERLEE 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 916 KKQELEEIlhemEARLEEEEDRSQQLQAERKKMAQQMLDLeeqleeeeaaRQKLQLEKVTAEAKIKKLeddilvmddqnN 995
Cdd:COG3096 366 QEEVVEEA----AEQLAEAEARLEAAEEEVDSLKSQLADY----------QQALDVQQTRAIQYQQAV-----------Q 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 996 KLSKERKLLEEriSDLT-TNLAEEEEKAKnlTKLKNKHESMIsELEVRLKKEEKSRQELEK---LKRKLDGE--ASDLHE 1069
Cdd:COG3096 421 ALEKARALCGL--PDLTpENAEDYLAAFR--AKEQQATEEVL-ELEQKLSVADAARRQFEKayeLVCKIAGEveRSQAWQ 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1070 QIAELQAQIAELKMQlAKKEEELQAALGRLDDEMAQKNNALKKIRELEGHIS---DLQEDLDSERAArnkAEKQKRDLGE 1146
Cdd:COG3096 496 TARELLRRYRSQQAL-AQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGqqlDAAEELEELLAE---LEAQLEELEE 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1147 ELE---ALKTELEDTLDSTATQQELRAKREQEVTMLKKALdEETRSHESQVQEMRQKHTQVVEELTEQLEQFKRAKANLD 1223
Cdd:COG3096 572 QAAeavEQRSELRQQLEQLRARIKELAARAPAWLAAQDAL-ERLREQSGEALADSQEVTAAMQQLLEREREATVERDELA 650
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1224 KNKQALEKenaelagELRVLSQAKQEVEHKKKKLEVQLQ-ELQSK-YSD-------------GEKVRA----ELN---DK 1281
Cdd:COG3096 651 ARKQALES-------QIERLSQPGGAEDPRLLALAERLGgVLLSEiYDDvtledapyfsalyGPARHAivvpDLSavkEQ 723
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1282 VHKLQNEVESVtgMLNEAEGKAIklakDVASLGSQLQDTQELLQEETRQkLNVST--------------KLRQLEDERNS 1347
Cdd:COG3096 724 LAGLEDCPEDL--YLIEGDPDSF----DDSVFDAEELEDAVVVKLSDRQ-WRYSRfpevplfgraarekRLEELRAERDE 796
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1348 LQEQLDEEMEAKQNLERhistLNIQLSD--SKKKLQDFASTVElleegkkkfqKEIESLTQQYEEKAAAYDKLEKTKNRL 1425
Cdd:COG3096 797 LAEQYAKASFDVQKLQR----LHQAFSQfvGGHLAVAFAPDPE----------AELAALRQRRSELERELAQHRAQEQQL 862
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1426 QQELDDLVVDLDNQRQLVSNLEkkqkkfdqLLAEEknisskyaDERDRAEaEAREKETKALSLARALEEALEAKeelert 1505
Cdd:COG3096 863 RQQLDQLKEQLQLLNKLLPQAN--------LLADE--------TLADRLE-ELREELDAAQEAQAFIQQHGKAL------ 919
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1506 nkmlkAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQ-----ATEDAKLRLEVN---MQALKVQFE 1577
Cdd:COG3096 920 -----AQLEPLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQrrphfSYEDAVGLLGENsdlNEKLRARLE 994
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1578 RDLQARDEQNeEKRRQLQRQLHEYETELEDERKQRALAVAAKKKLEGDLKDLELQADSaikGREEaikqlrKLQAQMKDF 1657
Cdd:COG3096 995 QAEEARREAR-EQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELGVQADA---EAEE------RARIRRDEL 1064
|
890 900 910 920
....*....|....*....|....*....|....*....|....*....
gi 156120901 1658 QRELEDARASRDEIFATAKENEKKAKSLEADLMQLQEDLAAAERARKQA 1706
Cdd:COG3096 1065 HEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVQA 1113
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
851-1031 |
1.12e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 53.23 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 851 EEEMQAKEDELQKTKERQQKAESELKELEQKHSQLTEEKNLLQEQLQAE----TELYAEAEEMRVRLAAKKQELEE---- 922
Cdd:COG4942 33 QQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALeaelAELEKEIAELRAELEAQKEELAEllra 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 923 -------------------------------ILHEMEARLEEEEDRSQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQL 971
Cdd:COG4942 113 lyrlgrqpplalllspedfldavrrlqylkyLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEA 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 972 EKVTAEAKIKKLEDDILVMDDQNNKLSKERKLLEERISDLTTNLAEEEEKAKNLTKLKNK 1031
Cdd:COG4942 193 LKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1587-1912 |
1.46e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 53.80 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1587 NEEKRRQLQRQLHEYETELEDERKQRALA----------VAAKKKLEGDLK-DLE------------LQADSAIKGREEA 1643
Cdd:COG3096 276 HANERRELSERALELRRELFGARRQLAEEqyrlvemareLEELSARESDLEqDYQaasdhlnlvqtaLRQQEKIERYQED 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1644 IKQLR-KLQAQMkDFQRELEDARASRDEIFATAKENEKKAKSLEADL-----------MQLQEDLAAAERARKQ---ADL 1708
Cdd:COG3096 356 LEELTeRLEEQE-EVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYqqaldvqqtraIQYQQAVQALEKARALcglPDL 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1709 EKDELAEELASSVSGRNALQDEKRRLEARIAqleeeleeeqgnteaMSERVRKATQQAEQLSNELATERSAAQKNENARQ 1788
Cdd:COG3096 435 TPENAEDYLAAFRAKEQQATEEVLELEQKLS---------------VADAARRQFEKAYELVCKIAGEVERSQAWQTARE 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1789 QLeRQNKELRSKLQEMEgavkskfkstiaALEAKIAQLEEQVEQEaREKQATAKALKQKDKKLKEALLQVEDERKMAEQy 1868
Cdd:COG3096 500 LL-RRYRSQQALAQRLQ------------QLRAQLAELEQRLRQQ-QNAERLLEEFCQRIGQQLDAAEELEELLAELEA- 564
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 156120901 1869 keqaekgnlrvkqlkrQLEEAEEESQRINANRRKLQRELDEATE 1912
Cdd:COG3096 565 ----------------QLEELEEQAAEAVEQRSELRQQLEQLRA 592
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1056-1298 |
1.69e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.10 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1056 LKRKLDGEASDLHEQIAELQAQIAELKMQLAKKEEELQaalgrlddEMAQKNNalkkIRELEGHISDLQEDLDSERAARN 1135
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAALE--------EFRQKNG----LVDLSEEAKLLLQQLSELESQLA 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1136 KAEKQKRDLGEELEALKTELEDTLDSTATQQElrakreqevtmlkkalDEETRSHESQVQEMRQKHTQVVEELTEQLEQF 1215
Cdd:COG3206 230 EARAELAEAEARLAALRAQLGSGPDALPELLQ----------------SPVIQQLRAQLAELEAELAELSARYTPNHPDV 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1216 KRAKANLDKNKQALEKENAELAGELRVlsqAKQEVEHKKKKLEVQLQELQSKYSDGEKVRAELNDkvhkLQNEVESVTGM 1295
Cdd:COG3206 294 IALRAQIAALRAQLQQEAQRILASLEA---ELEALQAREASLQAQLAQLEARLAELPELEAELRR----LEREVEVAREL 366
|
...
gi 156120901 1296 LNE 1298
Cdd:COG3206 367 YES 369
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1033-1249 |
1.70e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.52 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1033 ESMISELEVRLKKEEKSRQELEKLKRKLDGEASDLHEQIAELQAQIAELKMQLAKKEEELQAALGRLDDEMAQKNNALKK 1112
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1113 IRELEGHISDLQEDLDSE----------------RAARNKAEKQKRDLgEELEALKTELEDTLDSTATQQELRAKREQEV 1176
Cdd:COG3883 95 LYRSGGSVSYLDVLLGSEsfsdfldrlsalskiaDADADLLEELKADK-AELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 156120901 1177 TMLKKALDEETRSHESQVQEMRQKHTQVVEELTEQLEQFKRAKANLDKNKQALEKENAELAGELRVLSQAKQE 1249
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASA 246
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1317-1896 |
1.80e-06 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 53.21 E-value: 1.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1317 LQDTQELLQEETRQKlnvsTKLRQLEDERNSLQEQLDEEMEAKQNLERHISTLNIQLSDSKKKLQdfastvELLEEGKKK 1396
Cdd:pfam05557 12 SQLQNEKKQMELEHK----RARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALR------EQAELNRLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1397 fQKEIESLTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQKKFDQLLAEEKNISSKYADERDRAEA 1476
Cdd:pfam05557 82 -KKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1477 ---EAREKETKALSLARALEEALEAKEELERTNKMLK--AEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEEL 1551
Cdd:pfam05557 161 qqsSLAEAEQRIKELEFEIQSQEQDSEIVKNSKSELAriPELEKELERLREHNKHLNENIENKLLLKEEVEDLKRKLERE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1552 E---DELQATEDAKLRLEVNMQA---------LKVQFERDLQARDEQNEEKRRQLQRQLHEYETELEDERKQRALAVAAK 1619
Cdd:pfam05557 241 EkyrEEAATLELEKEKLEQELQSwvklaqdtgLNLRSPEDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQEL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1620 KKLEGDLKDLElqadsaiKGREEAIKQLRKLQAQMKDFQRELEDARASrdeifatakenekkAKSLEADLMQLQEDLAAA 1699
Cdd:pfam05557 321 AQYLKKIEDLN-------KKLKRHKALVRRLQRRVLLLTKERDGYRAI--------------LESYDKELTMSNYSPQLL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1700 ERARKQADLEKDelaeelassvsgrnaLQDEKRRLEARI--AQLEEELEEEQGNTEAMSERVRKATQQAEQLSNELATER 1777
Cdd:pfam05557 380 ERIEEAEDMTQK---------------MQAHNEEMEAQLsvAEEELGGYKQQAQTLERELQALRQQESLADPSYSKEEVD 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1778 SAAQKNEN---ARQQLERQNKELRSKLQEMEGAVKSKFKSTiaaleaKIAQLEEQVEQEARE-KQATAKALKQKDKKLKE 1853
Cdd:pfam05557 445 SLRRKLETlelERQRLREQKNELEMELERRCLQGDYDPKKT------KVLHLSMNPAAEAYQqRKNQLEKLQAEIERLKR 518
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 156120901 1854 ALLQVEDERKMAEQYKEQAEKGNLR-VKQLKRQLEEAEEESQRI 1896
Cdd:pfam05557 519 LLKKLEDDLEQVLRLPETTSTMNFKeVLDLRKELESAELKNQRL 562
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
1057-1357 |
1.83e-06 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 52.93 E-value: 1.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1057 KRKLDGEASDLHE-QIAELQAQIAELKMQLAKKEEELQAALGRLDDEMAQKnnaLKKirELEGHISD------LQEDLDS 1129
Cdd:PLN03229 416 ERKVNMKKREAVKtPVRELEGEVEKLKEQILKAKESSSKPSELALNEMIEK---LKK--EIDLEYTEaviamgLQERLEN 490
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1130 ERAARNKAEKQK----RDLGEELEALKTELEDTLDSTATQQELRAKREqevtMLK-----KALDEETRSHESQVQEMRQK 1200
Cdd:PLN03229 491 LREEFSKANSQDqlmhPVLMEKIEKLKDEFNKRLSRAPNYLSLKYKLD----MLNefsraKALSEKKSKAEKLKAEINKK 566
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1201 HTQVVE--ELTEQLEQFKRAKAN--------LDKN-KQALEKENAELAGEL-RVLSQAKQEVEHKKKK-----LEVQLQE 1263
Cdd:PLN03229 567 FKEVMDrpEIKEKMEALKAEVASsgassgdeLDDDlKEKVEKMKKEIELELaGVLKSMGLEVIGVTKKnkdtaEQTPPPN 646
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1264 LQSKYsdgEKVRAELNDKVHKLQNevesVTGMLNEAEGKAIKLAKDVASLGSQLQDTQELLQEETRQKLNVSTKLRQLED 1343
Cdd:PLN03229 647 LQEKI---ESLNEEINKKIERVIR----SSDLKSKIELLKLEVAKASKTPDVTEKEKIEALEQQIKQKIAEALNSSELKE 719
|
330
....*....|....
gi 156120901 1344 ERNSLQEQLDEEME 1357
Cdd:PLN03229 720 KFEELEAELAAARE 733
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
996-1115 |
1.94e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 51.08 E-value: 1.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 996 KLSKERKLLEERISDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKS-------------RQELEKLKRKLDG 1062
Cdd:COG1579 28 ELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnvrnnkeyealQKEIESLKRRISD 107
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 156120901 1063 ---EASDLHEQIAELQAQIAELKMQLAKKEEELQAALGRLDDEMAQKNNALKKIRE 1115
Cdd:COG1579 108 ledEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEA 163
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1520-1740 |
1.97e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.10 E-value: 1.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1520 KDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQA----------TEDAKLRLEvNMQALKVQFeRDLQARDEQNEE 1589
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEfrqknglvdlSEEAKLLLQ-QLSELESQL-AEARAELAEAEA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1590 KRRQLQRQLHEYETELEDERKQRALAvaakkKLEGDLKDLELQADSAIKGREEAIKQLRKLQAQMKDFQRELED-ARASR 1668
Cdd:COG3206 241 RLAALRAQLGSGPDALPELLQSPVIQ-----QLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQeAQRIL 315
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156120901 1669 DEIFATAKENEKKAKSLEADLMQLQEDLAA-AERARKQADLEKD-ELAEELASSVSgrnalqdeKRRLEARIAQ 1740
Cdd:COG3206 316 ASLEAELEALQAREASLQAQLAQLEARLAElPELEAELRRLEREvEVARELYESLL--------QRLEEARLAE 381
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1063-1934 |
2.02e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 53.04 E-value: 2.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1063 EASDLHEQIAELQAQIAELKMQLAKKEEelqaALGRLDDEMAQKNNALKkirELEGHISDLQEDLDSERAARNKAEKQKR 1142
Cdd:PRK04863 280 ERRVHLEEALELRRELYTSRRQLAAEQY----RLVEMARELAELNEAES---DLEQDYQAASDHLNLVQTALRQQEKIER 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1143 dLGEELEALKTELEDTLDSTATQQELRAKREQEVTMLKKALDEeTRSHESQVQemrqkhtQVVEELTEQLEQFKRAKANL 1222
Cdd:PRK04863 353 -YQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDE-LKSQLADYQ-------QALDVQQTRAIQYQQAVQAL 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1223 DKNKQALEKENAELAGELRVLSQAK---QEVEHKKKKLEVQLQELQSKYSDGEKVrAELndkVHKLQNEVESvtgmlNEA 1299
Cdd:PRK04863 424 ERAKQLCGLPDLTADNAEDWLEEFQakeQEATEELLSLEQKLSVAQAAHSQFEQA-YQL---VRKIAGEVSR-----SEA 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1300 EGKAIKLAKDVASLGSQLQDTQELLQE--ETRQKLNvstKLRQLEDERNSLQEQLDEEMEAKQNLERHISTLNIQLSDSK 1377
Cdd:PRK04863 495 WDVARELLRRLREQRHLAEQLQQLRMRlsELEQRLR---QQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLS 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1378 KKLQDFASTVELLEEGKKKFQKEIESLTQQYEEKAAAYDKLEKTKNRLQQELDDlVVDLDNQRQlvsnlekkqkkfdQLL 1457
Cdd:PRK04863 572 ESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALARLREQSGEEFED-SQDVTEYMQ-------------QLL 637
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1458 AEEKNISSkyadERDRAEAEAREKETKALSLA-RALEEALEAKEELERTNKMLKAEMEDLVSSkDDVGKN---------- 1526
Cdd:PRK04863 638 ERERELTV----ERDELAARKQALDEEIERLSqPGGSEDPRLNALAERFGGVLLSEIYDDVSL-EDAPYFsalygparha 712
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1527 --VHELEKSKRALETQmEEMKTQLEELEDELQATEDAKLRLEVNMQALKVQF-ERDLQ-------------ARDEQNEEK 1590
Cdd:PRK04863 713 ivVPDLSDAAEQLAGL-EDCPEDLYLIEGDPDSFDDSVFSVEELEKAVVVKIaDRQWRysrfpevplfgraAREKRIEQL 791
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1591 RRQLQRQLHEYETELEDERKQRALAVAAKKKLEGDLkDLELQADSAikgreeaiKQLRKLQAQMKDFQRELEDArasrde 1670
Cdd:PRK04863 792 RAEREELAERYATLSFDVQKLQRLHQAFSRFIGSHL-AVAFEADPE--------AELRQLNRRRVELERALADH------ 856
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1671 ifatakenEKKAKSLEADLMQLQEDLAAAERARKQADLEKDElaeelassvsgrnALQDEKRRLEARIAQleeeleeeqg 1750
Cdd:PRK04863 857 --------ESQEQQQRSQLEQAKEGLSALNRLLPRLNLLADE-------------TLADRVEEIREQLDE---------- 905
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1751 nteamservrkaTQQAEQLsnelatersaAQKNENARQQLERQNKELRSKLQEmegavkskfkstiaaleakIAQLEEQV 1830
Cdd:PRK04863 906 ------------AEEAKRF----------VQQHGNALAQLEPIVSVLQSDPEQ-------------------FEQLKQDY 944
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1831 EQearekqatAKALKQKDKKLKEALLQVeDERKMAEQYKEQAE---KGNLRVKQLKRQLEEAEEESQRInanRRKLQREL 1907
Cdd:PRK04863 945 QQ--------AQQTQRDAKQQAFALTEV-VQRRAHFSYEDAAEmlaKNSDLNEKLRQRLEQAEQERTRA---REQLRQAQ 1012
|
890 900
....*....|....*....|....*..
gi 156120901 1908 DEATESNEAMgrevTALKSKLRRGNET 1934
Cdd:PRK04863 1013 AQLAQYNQVL----ASLKSSYDAKRQM 1035
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1112-1321 |
2.24e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.14 E-value: 2.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1112 KIRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALKTELEDTLDSTATQQELRAKREQEVTMLKKALDEETRShe 1191
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1192 SQVQEMRQKHTQVV------EELTEQLEQFKRAKANLDKNKQALEKENAELAGELRVLSQAKQEVEHKKKKLEVQLQELQ 1265
Cdd:COG3883 95 LYRSGGSVSYLDVLlgsesfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 156120901 1266 SKYSDGEKVRAELNDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLGSQLQDTQ 1321
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
965-1132 |
2.52e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 52.71 E-value: 2.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 965 ARQKLQlekvTAEAKIK--KLEDDILVMDDQNNKLSKERKLLEERISDLTTNLAEEEEKAKNLTKLKNKHESMISELeVR 1042
Cdd:COG3206 187 LRKELE----EAEAALEefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPEL-LQ 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1043 LKKEEKSRQELEKLKRKLDGEASDL---HEQIAELQAQIAELKMQLAKKE-----------EELQAALGRLDDEMAQKNN 1108
Cdd:COG3206 262 SPVIQQLRAQLAELEAELAELSARYtpnHPDVIALRAQIAALRAQLQQEAqrilasleaelEALQAREASLQAQLAQLEA 341
|
170 180
....*....|....*....|....
gi 156120901 1109 ALKKIRELEGHISDLQEDLDSERA 1132
Cdd:COG3206 342 RLAELPELEAELRRLEREVEVARE 365
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1529-1928 |
2.59e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 52.66 E-value: 2.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1529 ELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKVQFErdlQARDEQNEEKRRQLQRQLHEYETELEDE 1608
Cdd:TIGR00618 250 EAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAH---IKAVTQIEQQAQRIHTELQSKMRSRAKL 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1609 RKQRALAVAAKKKLEgdlkdlelqadsaikgreEAIKQLRKLQAQMKDFQRELEDARASRDEIfatakeneKKAKSLEAD 1688
Cdd:TIGR00618 327 LMKRAAHVKQQSSIE------------------EQRRLLQTLHSQEIHIRDAHEVATSIREIS--------CQQHTLTQH 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1689 LMQLQEDLAAAERARKQADLEKDELAEELASSV---SGRNALQDEKRRLEARIAQLEEELEEEQGNTEAMSERVRKATQQ 1765
Cdd:TIGR00618 381 IHTLQQQKTTLTQKLQSLCKELDILQREQATIDtrtSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIH 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1766 AEQLSNELATERSAAQKNENARQQLERQNKELRSKLQEMEGAVKSKFKSTIAALEAKIAQLEEQVEQeaREKQATAKALK 1845
Cdd:TIGR00618 461 LQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLT--RRMQRGEQTYA 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1846 QKDKKLKEALLQVEDERKMAEQYKEQAEKGNLRVKQLKRQLEEAEEESQRINANRRKLQRELDEATESNEAMGREVTALK 1925
Cdd:TIGR00618 539 QLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALL 618
|
...
gi 156120901 1926 SKL 1928
Cdd:TIGR00618 619 RKL 621
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1473-1832 |
2.76e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 52.65 E-value: 2.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1473 RAEAEAREKETKALSLARALEEALEAKEELERTNKMLKAEMEDLVSSKDDVGKnvhELEKSKRALETQMEEMKTQlEELE 1552
Cdd:PRK04863 276 RHANERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQ---DYQAASDHLNLVQTALRQQ-EKIE 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1553 DELQATEDAKLRLEVNMQALKVQFER--DLQARDEQNEEKRRQLQRQLHEYETELeDERKQRAL----AVAAKKKLEGDL 1626
Cdd:PRK04863 352 RYQADLEELEERLEEQNEVVEEADEQqeENEARAEAAEEEVDELKSQLADYQQAL-DVQQTRAIqyqqAVQALERAKQLC 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1627 KDLELQADSAIKGREEAIKQLRKLQAQMKDFQRELEDARA-------------------SRDEIFATAKENEKKAKS--- 1684
Cdd:PRK04863 431 GLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAahsqfeqayqlvrkiagevSRSEAWDVARELLRRLREqrh 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1685 LEADLMQLQEDLAAAERA-RKQADLEK------------------------------DELAEELASSVSGRNALQDEKRR 1733
Cdd:PRK04863 511 LAEQLQQLRMRLSELEQRlRQQQRAERllaefckrlgknlddedeleqlqeelearlESLSESVSEARERRMALRQQLEQ 590
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1734 LEARIAQLeeeleeeqgntEAMSERVRKATQQAEQLSNELATERSAAQKNENARQQLERQNKELRsklQEMEGavkskfk 1813
Cdd:PRK04863 591 LQARIQRL-----------AARAPAWLAAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELT---VERDE------- 649
|
410
....*....|....*....
gi 156120901 1814 stiaaLEAKIAQLEEQVEQ 1832
Cdd:PRK04863 650 -----LAARKQALDEEIER 663
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1191-1427 |
4.57e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.94 E-value: 4.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1191 ESQVQEMRQKHTQVVEELTEQLEQFKRAKANLDKNKQALEKENAELAGElrvlSQAKQEVEhkkkklevQLQELQSKYSD 1270
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLS----EEAKLLLQ--------QLSELESQLAE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1271 gekVRAELNDkvhkLQNEVESVTGMLNEAEGKAIKLAKD--VASLGSQLQDTQELLQEETRQKLNVSTKLRQLEDERNSL 1348
Cdd:COG3206 231 ---ARAELAE----AEARLAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAAL 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1349 QEQLDEEMEA--------KQNLERHISTLNIQLSDSKKKLQDFASTvelleegkkkfQKEIESLTQQYEEKAAAYDKLEk 1420
Cdd:COG3206 304 RAQLQQEAQRilasleaeLEALQAREASLQAQLAQLEARLAELPEL-----------EAELRRLEREVEVARELYESLL- 371
|
....*..
gi 156120901 1421 tkNRLQQ 1427
Cdd:COG3206 372 --QRLEE 376
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1321-1536 |
5.10e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.92 E-value: 5.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1321 QELLQEETRQKLN-VSTKLRQLEDERNSLQEQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFASTVELLEEGKKKFQK 1399
Cdd:COG4942 18 QADAAAEAEAELEqLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1400 EIESLTQQYEEKAAAYDKLEKTKNRL----QQELDDLVVDLDNQRQLVSNLEKKQKKFDQLLAEEKNISSKYADERDRAE 1475
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRQPPLAlllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 156120901 1476 AEAREKETKALSLARALEEALEAKEELERTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRA 1536
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
851-1095 |
5.60e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.98 E-value: 5.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 851 EEEMQAKEDELQKTKERQQKAESELKELEQKHSQLTEEKNLLQEQLQaetELYAEAEEMRVRLAAKKQELEeilhemear 930
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELE---ALQAEIDKLQAEIAEAEAEIE--------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 931 leeeedrsqQLQAERKKMAQQMldleeqleeeeaARQKLQLEKVTAEAKIKKLEDDIlvmdDQNNKLSKERKLLEERISD 1010
Cdd:COG3883 83 ---------ERREELGERARAL------------YRSGGSVSYLDVLLGSESFSDFL----DRLSALSKIADADADLLEE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1011 LTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLDGEASDLHEQIAELQAQIAELKMQLAKKEE 1090
Cdd:COG3883 138 LKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAA 217
|
....*
gi 156120901 1091 ELQAA 1095
Cdd:COG3883 218 AAAAA 222
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
849-1428 |
7.12e-06 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 51.29 E-value: 7.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 849 RQEEEMQAKEDELQKTKERQQKAESELKELeQKHSQLTEEKNLLQE-QLQAETELYAEAEEMRVRLAAKKQELEEILHEM 927
Cdd:pfam07111 43 GQGPGRRGRSLELEGSQALSQQAELISRQL-QELRRLEEEVRLLREtSLQQKMRLEAQAMELDALAVAEKAGQAEAEGLR 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 928 EARLEEEEDRSQQLQAERKKMAQQMLDLEEQLEEEEAARQKlQLEKVTAEAKikKLEDDILVMDDQNNKLSKERKLLEER 1007
Cdd:pfam07111 122 AALAGAEMVRKNLEEGSQRELEEIQRLHQEQLSSLTQAHEE-ALSSLTSKAE--GLEKSLNSLETKRAGEAKQLAEAQKE 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1008 ISDLTTNLAEEEEKAKNLTKLKNKHESMISEL---EVRLKKEEKSRQELEKLKRKLDGEASDLHEQIAELQAQIAELKMQ 1084
Cdd:pfam07111 199 AELLRKQLSKTQEELEAQVTLVESLRKYVGEQvppEVHSQTWELERQELLDTMQHLQEDRADLQATVELLQVRVQSLTHM 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1085 LAKKEEELQAALGRLDD---EMAQKNNAL-----------------------KKIRELEGHISDLQEDLDSERAARNKAE 1138
Cdd:pfam07111 279 LALQEEELTRKIQPSDSlepEFPKKCRSLlnrwrekvfalmvqlkaqdlehrDSVKQLRGQVAELQEQVTSQSQEQAILQ 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1139 KQKRDLGEELE-------ALKTELEDTLDSTATQQELRAKREQEVTMLKKALDEETRSHESQVQEMRQKHTQvVEELTEQ 1211
Cdd:pfam07111 359 RALQDKAAEVEvermsakGLQMELSRAQEARRRQQQQTASAEEQLKFVVNAMSSTQIWLETTMTRVEQAVAR-IPSLSNR 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1212 LEQFKRaKANLDKNKQALEKENAELAGELRVLSQAKQEVEhkkKKLEVQLQELQSKYSdgeKVRAELNDKVHKLQNEVES 1291
Cdd:pfam07111 438 LSYAVR-KVHTIKGLMARKVALAQLRQESCPPPPPAPPVD---ADLSLELEQLREERN---RLDAELQLSAHLIQQEVGR 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1292 VTgmlNEAEGKAIKLAKDVASLGSQLQDTQELLQEETRQKLNVSTKLRQLEDERNSLQEQLDEEMEA-KQNLERHIST-- 1368
Cdd:pfam07111 511 AR---EQGEAERQQLSEVAQQLEQELQRAQESLASVGQQLEVARQGQQESTEEAASLRQELTQQQEIyGQALQEKVAEve 587
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 156120901 1369 --LNIQLSDSKKKLQdfastvelleEGKKKFQKEIESLtQQYEEKAAAYDKLEKTKNRLQQE 1428
Cdd:pfam07111 588 trLREQLSDTKRRLN----------EARREQAKAVVSL-RQIQHRATQEKERNQELRRLQDE 638
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
841-1407 |
7.54e-06 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 50.98 E-value: 7.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 841 VKPLLQVTRQEEEMQAKEDELQKTKERQQKAESELKELEQKHSQLTEEKNLLQEQLQAETELYAEAEEMRVRLA------ 914
Cdd:pfam10174 160 IKKLLEMLQSKGLPKKSGEEDWERTRRIAEAEMQLGHLEVLLDQKEKENIHLREELHRRNQLQPDPAKTKALQTviemkd 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 915 AKKQELEEILHEMEARLEEEEDRSQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDDILVMDDQN 994
Cdd:pfam10174 240 TKISSLERNIRDLEDEVQMLKTNGLLHTEDREEEIKQMEVYKSHSKFMKNKIDQLKQELSKKESELLALQTKLETLTNQN 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 995 NKLSKERKLLEErisdlttNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLDGEASDLHE----- 1069
Cdd:pfam10174 320 SDCKQHIEVLKE-------SLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDmldvk 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1070 --QIAELQAQIAELKMQLAKKEEELQAALGRLDDEMAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRdlgEE 1147
Cdd:pfam10174 393 erKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDRERL---EE 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1148 LEALKTELEDTLDSTATQQELRAKREQEVTMLKkaldEETRSHESQVQEMRQKHTQVVEELTEQLEQFKRAKANLDKnkq 1227
Cdd:pfam10174 470 LESLKKENKDLKEKVSALQPELTEKESSLIDLK----EHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKK--- 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1228 alekenaelAGELRVLSQAKQEVEHKKKKLEvqlQELQSKYSDGEKVRAELN---DKVHKLQNEVESVTGMLNEAEGKAI 1304
Cdd:pfam10174 543 ---------AHNAEEAVRTNPEINDRIRLLE---QEVARYKEESGKAQAEVErllGILREVENEKNDKDKKIAELESLTL 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1305 KLAKDVASLGSQLQDTQELLQEETRQKLNVSTKlRQLEDERNSLQEQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFA 1384
Cdd:pfam10174 611 RQMKEQNKKVANIKHGQQEMKKKGAQLLEEARR-REDNLADNSQQLQLEELMGALEKTRQELDATKARLSSTQQSLAEKD 689
|
570 580
....*....|....*....|...
gi 156120901 1385 STVELLEEGKKKFQKEIESLTQQ 1407
Cdd:pfam10174 690 GHLTNLRAERRKQLEEILEMKQE 712
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1373-1905 |
7.70e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 51.06 E-value: 7.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1373 LSDSKKKLQDFASTVELLEEGKKKFQKEIESLTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQKK 1452
Cdd:PRK01156 171 LKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDM 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1453 FDQLLAEEKNISSKYADERDRA------EAEAREKETKALSLARALEEALEAKEELERTNKMLKAEMEDLVSSKDDVGKN 1526
Cdd:PRK01156 251 KNRYESEIKTAESDLSMELEKNnyykelEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKK 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1527 VHELEKSKraleTQMEEMKTQLEELE---DELQATEDAKLRLEVNMQALKVQFERDLQARDEQNEEKRRQLQRQlheyET 1603
Cdd:PRK01156 331 LSVLQKDY----NDYIKKKSRYDDLNnqiLELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQ----EI 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1604 ELEDERKQRALAVAAKKKLEGDLKDLELQADSAIKGREEAIKQLRKLQAQMKdfqRELEDARASRDEIFATAKENEKKAK 1683
Cdd:PRK01156 403 DPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSV---CPVCGTTLGEEKSNHIINHYNEKKS 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1684 SLEADLMQLQEDLAAAERARKQADLEKDELA-EELASSVSGRNALQDEKRRLEaRIAQLEEELEEEQGNTEAMSERVRKA 1762
Cdd:PRK01156 480 RLEEKIREIEIEVKDIDEKIVDLKKRKEYLEsEEINKSINEYNKIESARADLE-DIKIKINELKDKHDKYEEIKNRYKSL 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1763 TQQAEQLSNELATERSAAQKN---ENARQQLERQNKELR---SKLQEMEGA---VKSKFKSTIAALEAKIAQLEEQVeQE 1833
Cdd:PRK01156 559 KLEDLDSKRTSWLNALAVISLidiETNRSRSNEIKKQLNdleSRLQEIEIGfpdDKSYIDKSIREIENEANNLNNKY-NE 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1834 AREKQATAKALKQKDKKLKEALLQVEDERKMAEQYKEQAEKGNLRVKQLKRQLEEA------------------EEESQR 1895
Cdd:PRK01156 638 IQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAkanrarlestieilrtriNELSDR 717
|
570
....*....|
gi 156120901 1896 INANRRKLQR 1905
Cdd:PRK01156 718 INDINETLES 727
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1037-1344 |
7.82e-06 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 49.92 E-value: 7.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1037 SELEVRLK-KEEKSRQELEKLKRKLDGEASDLHEQIAELQAQIAELKMQLAKKEEELQAALGRLDDEMAQKnnalkkiRE 1115
Cdd:pfam00038 28 KLLETKISeLRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLR-------TS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1116 LEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALKT-------ELEDTLDSTATQQELRAKREQEVTmlkkaldeetr 1188
Cdd:pfam00038 101 AENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKnheeevrELQAQVSDTQVNVEMDAARKLDLT----------- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1189 sheSQVQEMRQKHTQVVEELTEQLEQFKRAKanLDKNKQALEKENAElagelrvLSQAKQEV---EHKKKKLEVQLQELQ 1265
Cdd:pfam00038 170 ---SALAEIRAQYEEIAAKNREEAEEWYQSK--LEELQQAAARNGDA-------LRSAKEEItelRRTIQSLEIELQSLK 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 156120901 1266 SKYSDGEKVRAELNDkvhKLQNEVESVTGMLNEAEGkaiKLAKDVASLGSQLQDTQELLQEETRQKLNVSTKLRQLEDE 1344
Cdd:pfam00038 238 KQKASLERQLAETEE---RYELQLADYQELISELEA---ELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGE 310
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1753-1934 |
8.04e-06 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 51.17 E-value: 8.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1753 EAMSERVRKATQQAEQLSNELATErsaAQKNEnARQQLERQNKELRSKLQemegavKSKFKSTIAALEAKIAQLEEQVEQ 1832
Cdd:PTZ00491 639 EPVDERTRDSLQKSVQLAIEITTK---SQEAA-ARHQAELLEQEARGRLE------RQKMHDKAKAEEQRTKLLELQAES 708
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1833 EAREKQATAKAlkQKDKKLKEALLQVEDERKMAE--QYKEQAEKGNLRVKQLKRQLEEAEEEsQRINANRRKLQRELDEa 1910
Cdd:PTZ00491 709 AAVESSGQSRA--EALAEAEARLIEAEAEVEQAElrAKALRIEAEAELEKLRKRQELELEYE-QAQNELEIAKAKELAD- 784
|
170 180 190
....*....|....*....|....*....|
gi 156120901 1911 TESN------EAMGREvtALKSKLRRGNET 1934
Cdd:PTZ00491 785 IEATkferivEALGRE--TLIAIARAGPEL 812
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1676-1928 |
8.05e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 50.89 E-value: 8.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1676 KENEKKAKSLEADLMQLQEDLA-AAERARKQADLEKDELAE--ELASSVSGRNALQDEKRRLEARIAQLEEELEEEQGNT 1752
Cdd:pfam17380 288 QQQEKFEKMEQERLRQEKEEKArEVERRRKLEEAEKARQAEmdRQAAIYAEQERMAMERERELERIRQEERKRELERIRQ 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1753 EAMSERVRKaTQQAEQLSNElatersAAQKNENARQQLER------QNKELRSKLQEMEGAVKSKFKSTIAALEAKIAQL 1826
Cdd:pfam17380 368 EEIAMEISR-MRELERLQME------RQQKNERVRQELEAarkvkiLEEERQRKIQQQKVEMEQIRAEQEEARQREVRRL 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1827 EEQ-------VEQEAREKQATAKALKQKDKKLKEALLQVEDE-----------RKMAEQYKEQAEKGNL----RVKQLKR 1884
Cdd:pfam17380 441 EEEraremerVRLEEQERQQQVERLRQQEEERKRKKLELEKEkrdrkraeeqrRKILEKELEERKQAMIeeerKRKLLEK 520
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 156120901 1885 QLEE-----AEEESQRINANRRKLQRELDEATESNEAMgREVTALKSKL 1928
Cdd:pfam17380 521 EMEErqkaiYEEERRREAEEERRKQQEMEERRRIQEQM-RKATEERSRL 568
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1066-1659 |
8.74e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 51.06 E-value: 8.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1066 DLHEQIAELQAQIAELKMQlakkeeelqaalgrLDDEMAQKNNALKKIRELEGHISDLQEDLDSERAARNkaekqkrdlg 1145
Cdd:PRK01156 187 YLEEKLKSSNLELENIKKQ--------------IADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALN---------- 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1146 eELEALKTELEDTLDSTATQQELRAKREQEVTMLKKALDEETRSHESQVQEMRqkhtqvveeltEQLEQFKRAKANLDKN 1225
Cdd:PRK01156 243 -ELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKIINDPVYKNR-----------NYINDYFKYKNDIENK 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1226 KQALEKENAELagelrvlsqakQEVEHKKKKLEVqLQELQSKYSDGEKVRAELNDKVHKLQNEVESVTGMLNEAEGKAIK 1305
Cdd:PRK01156 311 KQILSNIDAEI-----------NKYHAIIKKLSV-LQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKK 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1306 L------AKDVASLGSQLQDTQELLQEETRQKLN-VSTKLRQLEDERNSLQEQLDEEMEAKQNLERHISTLNIQLSDSkk 1378
Cdd:PRK01156 379 IeeysknIERMSAFISEILKIQEIDPDAIKKELNeINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVCP-- 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1379 klqdfASTVELLEEGkkkfqkeIESLTQQYEEKAAaydKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKkqKKFDQLLA 1458
Cdd:PRK01156 457 -----VCGTTLGEEK-------SNHIINHYNEKKS---RLEEKIREIEIEVKDIDEKIVDLKKRKEYLES--EEINKSIN 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1459 EEKNISSKYADERD--RAEAEAREKETKALSLARALEEALEAKEELERT--NKMLKA----EMEDLVSSKDDVGKNVHEL 1530
Cdd:PRK01156 520 EYNKIESARADLEDikIKINELKDKHDKYEEIKNRYKSLKLEDLDSKRTswLNALAVisliDIETNRSRSNEIKKQLNDL 599
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1531 EKSKRALETQMEEMKT----QLEELEDELQATEDAKLRLEVNMQAL-----KVQFERDLQARDEQNEEKRRQLQRQLHEY 1601
Cdd:PRK01156 600 ESRLQEIEIGFPDDKSyidkSIREIENEANNLNNKYNEIQENKILIeklrgKIDNYKKQIAEIDSIIPDLKEITSRINDI 679
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 156120901 1602 ETELEDERKQRALAVAAKKKLEGDLKDLEL---QADSAIKGREEAIKQLRKLQAQMKDFQR 1659
Cdd:PRK01156 680 EDNLKKSRKALDDAKANRARLESTIEILRTrinELSDRINDINETLESMKKIKKAIGDLKR 740
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
972-1284 |
8.83e-06 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.
Pssm-ID: 463796 [Multi-domain] Cd Length: 712 Bit Score: 50.83 E-value: 8.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 972 EKVTAEAKIKKLEDDILVMDDQNNKLSKERKLLEERISDLTTNLAEE---EEKAKNLTKLKNKHES----------MISE 1038
Cdd:pfam13166 90 ESIEIQEKIAKLKKEIKDHEEKLDAAEANLQKLDKEKEKLEADFLDEcwkKIKRKKNSALSEALNGfkyeanfksrLLRE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1039 LE-------VRLKKEEK----------SRQELEK----------------LKRKLDGEASDLHEQIAELQAQI-AELKMQ 1084
Cdd:pfam13166 170 IEkdnfnagVLLSDEDRkaalatvfsdNKPEIAPltfnvidfdalekaeiLIQKVIGKSSAIEELIKNPDLADwVEQGLE 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1085 LAKKE------------EELQAALGR-LDDEMAQKNNALKK-IRELEGHISDLQEDLDSeRAARNKAEKQKRDLGEELEA 1150
Cdd:pfam13166 250 LHKAHldtcpfcgqplpAERKAALEAhFDDEFTEFQNRLQKlIEKVESAISSLLAQLPA-VSDLASLLSAFELDVEDIES 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1151 LKTELEDTLDSTatQQELRAKREQEVTMLK-KALDEETRSHESQVQ----------EMRQKHTQVVEELTEQLEQFKRAK 1219
Cdd:pfam13166 329 EAEVLNSQLDGL--RRALEAKRKDPFKSIElDSVDAKIESINDLVAsineliakhnEITDNFEEEKNKAKKKLRLHLVEE 406
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 156120901 1220 AnlDKNKQALEKENAELAGELRVLSQAKQEVEHKKKKLEVQLQELQSKYSDGEKVRAELNDKVHK 1284
Cdd:pfam13166 407 F--KSEIDEYKDKYAGLEKAINSLEKEIKNLEAEIKKLREEIKELEAQLRDHKPGADEINKLLKA 469
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
936-1140 |
9.52e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.21 E-value: 9.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 936 DRSQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDDIlvmDDQNNKLSKERKLLEERISDL---- 1011
Cdd:COG3883 23 KELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEI---AEAEAEIEERREELGERARALyrsg 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1012 -----------TTNLAEEEEKAKNLTKLKNKHESMISELEvrlkkeeKSRQELEKLKRKLDGEASDLHEQIAELQAQIAE 1080
Cdd:COG3883 100 gsvsyldvllgSESFSDFLDRLSALSKIADADADLLEELK-------ADKAELEAKKAELEAKLAELEALKAELEAAKAE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1081 LKMQLAKKEEELQAALGRLDDEMAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQ 1140
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
|
| COG5283 |
COG5283 |
Phage-related tail protein [Mobilome: prophages, transposons]; |
909-1314 |
9.74e-06 |
|
Phage-related tail protein [Mobilome: prophages, transposons];
Pssm-ID: 444094 [Multi-domain] Cd Length: 747 Bit Score: 50.62 E-value: 9.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 909 MRVRLAAKKQELEEILHEMEARLEEEEDRSQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDDIL 988
Cdd:COG5283 1 LQVILGAVDKPFKSALESAKQRVAALAQALKALEAPTRALARALERAKQAAARLQTKYNKLRQSLQRLRQALDQAGIDTR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 989 VMDDQNNKLSKERKLLEERISDLTTNLAEEEEKAKNLTKLKNKHESMIS--------------------ELE-------- 1040
Cdd:COG5283 81 QLSAAQRRLRSSLEQTNRQLERQQQRLARLGARQDRLKAARARLQRLAGagaaaaaigaalaasvkpaiDFEdamadvaa 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1041 -VRLKKEEKSRQELEKLKRKLDGEASDLHEQIAELQAQIAELKMqlakKEEELQAALGRL-------DDEMAQKNNALKK 1112
Cdd:COG5283 161 tVDLDKSSEQFKALGKQARELSAQTPQSADDIAAGQAALAQAGV----SAEDILAFTPTAaklatafDTDAEEAAEIAAK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1113 IRELEG-HISDLQEDLDSERAARNKAEKQKRDLGEEL-------EALKTELEDTLDSTATQQELRAKREQEVTMLKKALD 1184
Cdd:COG5283 237 ILNAFKlPADDVERLGDALNYAGNNGATSLADLADALpyvgpvaKALGVSGKEAAALGAALADAGIEGEEAGTALRNMLT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1185 EETRSHESQVQEMRQ----------KHTQVVEELTEQLE--------QFKRAKANLDKNKQALE---------------- 1230
Cdd:COG5283 317 RLTSPTKAAAKALKKlgidtqdskgNLRGLAKILAKQMQkdaqgalaELLKALKKLDAAKRAAAlkqlfgeeavsalapl 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1231 -------KENAELAGELRVLSQAKQEVEHKKKKLEVQLQELQSKYSD-----GEKVRAELNDKVHKLQNEVESVTGMLNE 1298
Cdd:COG5283 397 lqngdelRKQLAVAEAAAAQGSMDKEAAKRTDTLAGQLKLLKNALENlgisiGEALLPALRELAQALTPVVGKLADWAKA 476
|
490
....*....|....*.
gi 156120901 1299 AEGKAIKLAKDVASLG 1314
Cdd:COG5283 477 NPGLIKTIVKVAAALA 492
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
852-1055 |
1.08e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 50.60 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 852 EEMQAKEDELQKT-KERQQKAESELKELEQKHSQLTEEKNLLQEQLQaetELYAEAE-EMRVRLAAKKQELEEILHE--M 927
Cdd:PRK00409 519 NELIASLEELERElEQKAEEAEALLKEAEKLKEELEEKKEKLQEEED---KLLEEAEkEAQQAIKEAKKEADEIIKElrQ 595
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 928 EARLEEEEDRSQQLQAERKKMAQQMLDLEEQLEEEEAARQKLqleKVTAEAKIKKLED--DILVMDDQNN--------KL 997
Cdd:PRK00409 596 LQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEEL---KVGDEVKYLSLGQkgEVLSIPDDKEaivqagimKM 672
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 156120901 998 SKERKLLEerisdLTTNLAEEEEKAKNLTKLKNKHESMisELEVRLKKEEKSRQELEK 1055
Cdd:PRK00409 673 KVPLSDLE-----KIQKPKKKKKKKPKTVKPKPRTVSL--ELDLRGMRYEEALERLDK 723
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
836-1233 |
1.10e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 836 RLFTKVKPLLQVTRQEEEMQAKEDELQKTKERQQKAES------ELKELEQKHSQLTEEKNLLQEQLQAETELYAEAEEM 909
Cdd:COG4717 89 EYAELQEELEELEEELEELEAELEELREELEKLEKLLQllplyqELEALEAELAELPERLEELEERLEELRELEEELEEL 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 910 RVRLAAKKQELEEILHEMEARLEEE-----------EDRSQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEA 978
Cdd:COG4717 169 EAELAELQEELEELLEQLSLATEEElqdlaeeleelQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEA 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 979 KIKKLEDDILVMDDQNNKLSKERK---------------LLEERISDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRL 1043
Cdd:COG4717 249 RLLLLIAAALLALLGLGGSLLSLIltiagvlflvlgllaLLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAAL 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1044 K-KEEKSRQELEKLKRKLDgEASDLHEQIAELQAQIaELKMQLAKKEEELQAALGRLDDEMAQKNNALKKIRELEGHISD 1122
Cdd:COG4717 329 GlPPDLSPEELLELLDRIE-ELQELLREAEELEEEL-QLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEE 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1123 LQEDLDSERAARNK--AEKQKRDLGEELEALKTELEDTLDSTATQQELRAKREQEVTMLKKaldeetrshESQVQEMRQK 1200
Cdd:COG4717 407 LEEQLEELLGELEEllEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEE---------DGELAELLQE 477
|
410 420 430
....*....|....*....|....*....|....*.
gi 156120901 1201 HTQVVEELTEQLEQFKR---AKANLDKNKQALEKEN 1233
Cdd:COG4717 478 LEELKAELRELAEEWAAlklALELLEEAREEYREER 513
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1234-1618 |
1.30e-05 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 49.68 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1234 AELAGELRVLSQAKQEVEHKKKKLEVQLQELQSKYSDGEKVRAELNDKVHKLQNEVESVTGMLNEAEGkaiklakDVASL 1313
Cdd:pfam19220 16 ADRLEDLRSLKADFSQLIEPIEAILRELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEG-------ELEEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1314 GSQLQDTQELLQEETRQKLNVSTKLRQLEDERNSLQEQLDEEMEAKQNLERHISTLNIQLSDSKKKLQ----DFASTVE- 1388
Cdd:pfam19220 89 VARLAKLEAALREAEAAKEELRIELRDKTAQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQraegELATAREr 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1389 --LLEEGKKKFQKEIESLTQQYEEKAAAYDKLEKTKNRLQQELDDLvvdldnQRQLVSNLEKKQKKFDQLLAEEKNISSK 1466
Cdd:pfam19220 169 laLLEQENRRLQALSEEQAAELAELTRRLAELETQLDATRARLRAL------EGQLAAEQAERERAEAQLEEAVEAHRAE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1467 YADERDRAEA-EAREKET-KALSLARALEEAleakeeleRTNKMLKAE--MEDLVSSKDDVGKNVHELEKSKRALETQME 1542
Cdd:pfam19220 243 RASLRMKLEAlTARAAATeQLLAEARNQLRD--------RDEAIRAAErrLKEASIERDTLERRLAGLEADLERRTQQFQ 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1543 EMKTQLEELEDE-------LQATEDAKLRLEVNMQALKVQFErDLQARDEQneeKRRQLQRQLHEYETELEDERKQRALA 1615
Cdd:pfam19220 315 EMQRARAELEERaemltkaLAAKDAALERAEERIASLSDRIA-ELTKRFEV---ERAALEQANRRLKEELQRERAERALA 390
|
...
gi 156120901 1616 VAA 1618
Cdd:pfam19220 391 QGA 393
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1173-1481 |
1.35e-05 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 50.22 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1173 EQEVTMLKKALDEETRSHE---SQVQEMRQKHTQVVEELTEQLEQFKRAKANLDKNKQALEKENAELAgEL--------- 1240
Cdd:PRK04778 118 EEDIEQILEELQELLESEEknrEEVEQLKDLYRELRKSLLANRFSFGPALDELEKQLENLEEEFSQFV-ELtesgdyvea 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1241 -RVLSQAKQEVEHKKKKLEV--------------QLQELQSKYsdgekvrAELNDKVHKLQNevesvtgmlneaegkaIK 1305
Cdd:PRK04778 197 rEILDQLEEELAALEQIMEEipellkelqtelpdQLQELKAGY-------RELVEEGYHLDH----------------LD 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1306 LAKDVASLGSQLQDTQELLqEETRQKlNVSTKLRQLEDERNSLQEQLDEEMEAKQNLERHISTLNIQLSDSKKKlqdfas 1385
Cdd:PRK04778 254 IEKEIQDLKEQIDENLALL-EELDLD-EAEEKNEEIQERIDQLYDILEREVKARKYVEKNSDTLPDFLEHAKEQ------ 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1386 tvelleegKKKFQKEIESLTQQY---EEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQ----LVSNLEKKQKKFDQLLA 1458
Cdd:PRK04778 326 --------NKELKEEIDRVKQSYtlnESELESVRQLEKQLESLEKQYDEITERIAEQEIayseLQEELEEILKQLEEIEK 397
|
330 340
....*....|....*....|...
gi 156120901 1459 EEKNISSKYADERDrAEAEAREK 1481
Cdd:PRK04778 398 EQEKLSEMLQGLRK-DELEAREK 419
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1071-1361 |
1.53e-05 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 50.22 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1071 IAELQAQIAELKMQlAKKEEELQAALGrlDDEMAQKNNAL---KKIRELEgHISDLQEDLDS--ERAARNKAEKQKRDLG 1145
Cdd:NF012221 1537 TSESSQQADAVSKH-AKQDDAAQNALA--DKERAEADRQRleqEKQQQLA-AISGSQSQLEStdQNALETNGQAQRDAIL 1612
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1146 EELEALKTELE------DTLDSTATQQELRAKREQE------VTMLKKALDEETRSHESQVQEMRQKHTQVVEELTEQLE 1213
Cdd:NF012221 1613 EESRAVTKELTtlaqglDALDSQATYAGESGDQWRNpfagglLDRVQEQLDDAKKISGKQLADAKQRHVDNQQKVKDAVA 1692
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1214 QFKRAKANLDKNKQalekeNAELAGElrvlsQAKQEVEHKKKKLEVQLQELQSKYSDGEkvrAELNDKVHKLQNEVESVT 1293
Cdd:NF012221 1693 KSEAGVAQGEQNQA-----NAEQDID-----DAKADAEKRKDDALAKQNEAQQAESDAN---AAANDAQSRGEQDASAAE 1759
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156120901 1294 GMLNEA--EGKAIKLAKDV-----ASLGSQLQDTQELLQEETRQKLNVSTKLRQLEDERNS--LQEQLDEEMEAKQN 1361
Cdd:NF012221 1760 NKANQAqaDAKGAKQDESDkpnrqGAAGSGLSGKAYSVEGVAEPGSHINPDSPAAADGRFSegLTEQEQEALEGATN 1836
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1610-1922 |
1.58e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.52 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1610 KQRALAVAAKKKLEGDLKDLELQADSAIKGREEAIKQLRKLQAQMKDFQRELEDARASRDEIFATAKENEKKAKSLEADL 1689
Cdd:COG4372 10 KARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1690 MQLQEDLAAAERARKQADLEKDELAEELASSVSGRNALQDEKRRLEARIAQLEEELEEEQGNTEAMSERVRKATQQAEQL 1769
Cdd:COG4372 90 QAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAAL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1770 SNELatersAAQKNENARQQLERQNKELRSKLQEMEGAVKSKFKSTIAALEAKIAQLEEQVEQEAREKQATAKALKQKDK 1849
Cdd:COG4372 170 EQEL-----QALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALEL 244
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 156120901 1850 KLKEALLQVEDERKMAEQYKEQAEKGNLRVKQLKRQLEEAEEESQRINANRRKLQRELDEATESNEAMGREVT 1922
Cdd:COG4372 245 EEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDAL 317
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
802-1074 |
1.60e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.30 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 802 ARKAFAKRQQQLTAMkviQRNCAAYLKLRNWQWwrlftkvkPLLQVTRQEEEMQAKEDELqktkERQQKAESELKELEQK 881
Cdd:COG4913 629 AEERLEALEAELDAL---QERREALQRLAEYSW--------DEIDVASAEREIAELEAEL----ERLDASSDDLAALEEQ 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 882 HSQLTEEKNLLQEQLqaetelyaeaEEMRVRLAAKKQELEEILHEMEARLEEEEDRSQQLQAERKKMAQQMLDLEEQLEE 961
Cdd:COG4913 694 LEELEAELEELEEEL----------DELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAV 763
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 962 EEAARQKLQLEKVTAEAKIKKLEDDIlvmddqNNKLSKERKLLEERISDLTTNLAEEEEKAKNLTKLKNKHesmISELEV 1041
Cdd:COG4913 764 ERELRENLEERIDALRARLNRAEEEL------ERAMRAFNREWPAETADLDADLESLPEYLALLDRLEEDG---LPEYEE 834
|
250 260 270
....*....|....*....|....*....|....*
gi 156120901 1042 RLK--KEEKSRQELEKLKRKLDGEASDLHEQIAEL 1074
Cdd:COG4913 835 RFKelLNENSIEFVADLLSKLRRAIREIKERIDPL 869
|
|
| EzrA |
COG4477 |
Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome ... |
1191-1481 |
1.61e-05 |
|
Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443574 [Multi-domain] Cd Length: 567 Bit Score: 49.84 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1191 ESQVQEMRQKHTQVVEELTEQLEQFKRAKANLDKNKQALEKENAELAGELRVLSQAKQEVEHKKKKLEVQLQELQSKYSD 1270
Cdd:COG4477 110 EQLLDEIEEEIEEILEELEELLESEEKNREEIEELKEKYRELRKTLLAHRHSFGPAAEELEKQLEELEPEFEEFEELTES 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1271 GEKVRA-----ELNDKVHKLQNEVESVTGMLNEAEGK-----------------------AIKLAKDVASLGSQLQDTQE 1322
Cdd:COG4477 190 GDYLEAreileQLEEELNALEELMEEIPPLLKELQTElpdqleelksgyremkeqgyvleHLNIEKEIEQLEEQLKEALE 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1323 LLqEETRQKlNVSTKLRQLEDERNSLQEQLDEEMEAKQNLERHISTLniqlsdsKKKLQDfastvelLEEGKKKFQKEIE 1402
Cdd:COG4477 270 LL-EELDLD-EAEEELEEIEEEIDELYDLLEKEVEAKKYVDKNQEEL-------EEYLEH-------LKEQNRELKEEID 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1403 SLTQQY---EEKAAAYDKLEKTKNRLQQELDDLVVDLDNQR----QLVSNLEKKQKKFDQLLAEEKNISSKYADERDRaE 1475
Cdd:COG4477 334 RVQQSYrlnENELEKVRNLEKQIEELEKRYDEIDERIEEEKvaysELQEELEEIEEQLEEIEEEQEEFSEKLKSLRKD-E 412
|
....*.
gi 156120901 1476 AEAREK 1481
Cdd:COG4477 413 LEAREK 418
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
851-1676 |
1.87e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 49.95 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 851 EEEMQAKEDELQKTKE--RQQKA----ESELKELEQK---HSQLTEEKNLLQEQLQAETELY-AEAEEMRVRLAAKKQEL 920
Cdd:COG3096 326 EQDYQAASDHLNLVQTalRQQEKieryQEDLEELTERleeQEEVVEEAAEQLAEAEARLEAAeEEVDSLKSQLADYQQAL 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 921 --------------------EEILHEMEARLEEEEDRSQQLQAERKKMAQQMLDLEEQLEEEEAARQklQLEKvtAEAKI 980
Cdd:COG3096 406 dvqqtraiqyqqavqalekaRALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARR--QFEK--AYELV 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 981 KKLEDDIlvmdDQNNKLSKERKLLEE---------RISDLTTNLAEEEEKAKNltklKNKHESMISELEVRLKKEEKSRQ 1051
Cdd:COG3096 482 CKIAGEV----ERSQAWQTARELLRRyrsqqalaqRLQQLRAQLAELEQRLRQ----QQNAERLLEEFCQRIGQQLDAAE 553
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1052 ELEKLKRKLDGEASDLHEQIAELQAQIAELKMQL----AKKEE---------ELQAALGRLDDEMAQknnALKKIRELEG 1118
Cdd:COG3096 554 ELEELLAELEAQLEELEEQAAEAVEQRSELRQQLeqlrARIKElaarapawlAAQDALERLREQSGE---ALADSQEVTA 630
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1119 HisdLQEDLDSERAA---RNKAEKQKRDLGEELEALkteledTLDSTATQQELRAKREQEVTMLKKALDEETRSHESQVQ 1195
Cdd:COG3096 631 A---MQQLLEREREAtveRDELAARKQALESQIERL------SQPGGAEDPRLLALAERLGGVLLSEIYDDVTLEDAPYF 701
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1196 EMR---QKHTQVVEELteqleqfKRAKANLDKNKQALEK----ENAELAGELRVLsqakqEVEHKKKKLEVQLQELQSKY 1268
Cdd:COG3096 702 SALygpARHAIVVPDL-------SAVKEQLAGLEDCPEDlyliEGDPDSFDDSVF-----DAEELEDAVVVKLSDRQWRY 769
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1269 SDGEKV----RAELNDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVAS----LGSQLQ-----DTQELLQEETRQKLNVS 1335
Cdd:COG3096 770 SRFPEVplfgRAAREKRLEELRAERDELAEQYAKASFDVQKLQRLHQAfsqfVGGHLAvafapDPEAELAALRQRRSELE 849
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1336 TKLRQLEDERNSLQEQLDEEMEAKQNLERHISTLNI------------------QLSDSKKKLQDFASTVELLEEgkkkF 1397
Cdd:COG3096 850 RELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQANLladetladrleelreeldAAQEAQAFIQQHGKALAQLEP----L 925
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1398 QKEIESLTQQYEEKAAAYDKLEKTKNRLQQELDDLVvdldnqrQLVSNLEK-KQKKFDQLLAEEKNISSKYADERDRAEA 1476
Cdd:COG3096 926 VAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFALS-------EVVQRRPHfSYEDAVGLLGENSDLNEKLRARLEQAEE 998
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1477 EAREKETKALSLARALEEALeakeelertnkmlkAEMEDLVSSKDdvgknvhelekskrALETQMEEMKTQLEELedELQ 1556
Cdd:COG3096 999 ARREAREQLRQAQAQYSQYN--------------QVLASLKSSRD--------------AKQQTLQELEQELEEL--GVQ 1048
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1557 ATEDAKLRLEVNMQALKVQFERDLQARDEQN------EEKRRQLQRQLHEYETELEDERKQ---------RALAVAAKKK 1621
Cdd:COG3096 1049 ADAEAEERARIRRDELHEELSQNRSRRSQLEkqltrcEAEMDSLQKRLRKAERDYKQEREQvvqakagwcAVLRLARDND 1128
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*.
gi 156120901 1622 LEGDLKDLELQADSAIKGREEAIKQLRKLQAQMKDFQrELEDA-RASRDEIFATAK 1676
Cdd:COG3096 1129 VERRLHRRELAYLSADELRSMSDKALGALRLAVADNE-HLRDAlRLSEDPRRPERK 1183
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1642-1847 |
2.11e-05 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 49.30 E-value: 2.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1642 EAIKQLRKLQAQMKDFQRELEDARASRDEIFATA-KENEkkakslEADLMQLQEDLAAAERARKQADLEKDELAEELASS 1720
Cdd:COG0497 169 ALKKELEELRADEAERARELDLLRFQLEELEAAAlQPGE------EEELEEERRRLSNAEKLREALQEALEALSGGEGGA 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1721 VSgrnALQDEKRRLEaRIAQleeeleeEQGNTEAMSERVRKATQQAEQLSNELATERSAAQKNENARQQLE-RQN----- 1794
Cdd:COG0497 243 LD---LLGQALRALE-RLAE-------YDPSLAELAERLESALIELEEAASELRRYLDSLEFDPERLEEVEeRLAllrrl 311
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 156120901 1795 ---------------KELRSKLQEMEGAvkskfKSTIAALEAKIAQLEEQVEQEARE----KQATAKALKQK 1847
Cdd:COG0497 312 arkygvtveellayaEELRAELAELENS-----DERLEELEAELAEAEAELLEAAEKlsaaRKKAAKKLEKA 378
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
1318-1730 |
2.31e-05 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 49.66 E-value: 2.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1318 QDTQELLQEETRQKLNVSTKLR------------QLEDERnsLQEQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFAS 1385
Cdd:PTZ00108 900 EDYKEFLESETLKEKDVIVDYRdystantvhftvKLNDGV--LEQWEEEGIEKVFKLKSTISTTNMVLFDENGKIKKYSD 977
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1386 TVELLEEgkkkFqkeiesltqqYEEKAAAYdklEKTKNRLQQELDDLVVDLDNQRQLV-----SNLEKKQKKFDQLLAE- 1459
Cdd:PTZ00108 978 ALDILKE----F----------YLVRLDLY---KKRKEYLLGKLERELARLSNKVRFIkhvinGELVITNAKKKDLVKEl 1040
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1460 EKNISSKYADERDRAEAE--AREKETKALSLARALEEALEAKEELERTNKMLKAEMEDLVsskddvgknvheLEKSKRaL 1537
Cdd:PTZ00108 1041 KKLGYVRFKDIIKKKSEKitAEEEEGAEEDDEADDEDDEEELGAAVSYDYLLSMPIWSLT------------KEKVEK-L 1107
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1538 ETQMEEMKTQLEELEdelqATEDAKLRLEvNMQALKVQFErdlqaRDEQNEEKRRQLQRQLHEYETELEDERKQRALAVA 1617
Cdd:PTZ00108 1108 NAELEKKEKELEKLK----NTTPKDMWLE-DLDKFEEALE-----EQEEVEEKEIAKEQRLKSKTKGKASKLRKPKLKKK 1177
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1618 AKKKLEGDlKDLELQADSAIKGREEAIKQLRKLQAQMKDFQREledaRASRDEIFATAKENEKKAKSLEADLMQLQEDLA 1697
Cdd:PTZ00108 1178 EKKKKKSS-ADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSN----SSGSDQEDDEEQKTKPKKSSVKRLKSKKNNSSK 1252
|
410 420 430
....*....|....*....|....*....|....*
gi 156120901 1698 AAERARKQA--DLEKDELAEELASSVSGRNALQDE 1730
Cdd:PTZ00108 1253 SSEDNDEFSsdDLSKEGKPKNAPKRVSAVQYSPPP 1287
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1537-1906 |
2.45e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 49.12 E-value: 2.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1537 LETQMEEMKTQLEELedeLQATEDAKLRLEVNMQALKVQferdlqarDEQNEEKRRQLQRQLHEYETELEDERKQRALAV 1616
Cdd:pfam07888 32 LQNRLEECLQERAEL---LQAQEAANRQREKEKERYKRD--------REQWERQRRELESRVAELKEELRQSREKHEELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1617 AAKKKLEGDLKDLELQADSAIKGREEAIKQLRKLQAQMKDFQRELEDARASRDEIFATAKENEKKAKSLEADLMQLQEDL 1696
Cdd:pfam07888 101 EKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1697 AAAERARKQADLEKDELAEELASSVSGRNALQDEKRRLEARIAQLEEELEEEQGNTEAMS---ERVRKATQQAEQLSNEL 1773
Cdd:pfam07888 181 QQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRslqERLNASERKVEGLGEEL 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1774 ATERSAAQKNENARQQLERQNKELRSKLQEMEGAVKSKfkstiaaleakiaqlEEQVEQEAREKQATAKALKQKDKKLKE 1853
Cdd:pfam07888 261 SSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREG---------------RARWAQERETLQQSAEADKDRIEKLSA 325
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 156120901 1854 ALLQVEDERKMAEQYKEQAEKGNLRVKQLKR-QLEEAEEESQRINANRRKLQRE 1906
Cdd:pfam07888 326 ELQRLEERLQEERMEREKLEVELGREKDCNRvQLSESRRELQELKASLRVAQKE 379
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1372-1595 |
3.30e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.29 E-value: 3.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1372 QLSDSKKKLQDFASTVELLEEGKKKFQKEIESLTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQK 1451
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1452 K-------FDQLLAeekniSSKYADERDRAEAeareketkalsLARALEEALEAKEELERTNKMLKAEMEDLVSSKDDVG 1524
Cdd:COG3883 97 RsggsvsyLDVLLG-----SESFSDFLDRLSA-----------LSKIADADADLLEELKADKAELEAKKAELEAKLAELE 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 156120901 1525 KNVHELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKVQFERDLQARDEQNEEKRRQLQ 1595
Cdd:COG3883 161 ALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
965-1356 |
3.56e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 49.14 E-value: 3.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 965 ARQKLQLEKV-----TAEAKIKKLEDDILVMDDQNNKLSKER----------KLLEERISDLTT---NLAEEEEKAKNLT 1026
Cdd:PRK11281 76 DRQKEETEQLkqqlaQAPAKLRQAQAELEALKDDNDEETRETlstlslrqleSRLAQTLDQLQNaqnDLAEYNSQLVSLQ 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1027 KLKNKHESMISELEVRLkkeeksrQELEK-LKRKLDGEASDLHEQIAELQAQIAELKMQLAKKEEELQAALGRLDDEMAQ 1105
Cdd:PRK11281 156 TQPERAQAALYANSQRL-------QQIRNlLKGGKVGGKALRPSQRVLLQAEQALLNAQNDLQRKSLEGNTQLQDLLQKQ 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1106 KNNALKKIRELEGHISDLQEDLDSERaarnkaekqkrdlgeelealKTELEDTLDSTATQQElrAKREQEVTMLKKALDE 1185
Cdd:PRK11281 229 RDYLTARIQRLEHQLQLLQEAINSKR--------------------LTLSEKTVQEAQSQDE--AARIQANPLVAQELEI 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1186 ETRSHESQVQEmrqkhTQVVEELTEQLEQFKRAKANLDKNKQALEKENAELAGEL---RVLSQAKQEVEHKK--KKLEVQ 1260
Cdd:PRK11281 287 NLQLSQRLLKA-----TEKLNTLTQQNLRVKNWLDRLTQSERNIKEQISVLKGSLllsRILYQQQQALPSADliEGLADR 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1261 LQELQSKYSDGEKVRAEL---NDKVHKL-QNEVESVTGMLNEAegkaiklakdvasLGSQLQDTQELLQEETRQ---KLN 1333
Cdd:PRK11281 362 IADLRLEQFEINQQRDALfqpDAYIDKLeAGHKSEVTDEVRDA-------------LLQLLDERRELLDQLNKQlnnQLN 428
|
410 420
....*....|....*....|....*..
gi 156120901 1334 VSTKL----RQLEDERNSLQEQLDEEM 1356
Cdd:PRK11281 429 LAINLqlnqQQLLSVSDSLQSTLTQQI 455
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1221-1412 |
3.76e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 48.62 E-value: 3.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1221 NLDKNKQALEKENAElagelRVLSQAKQEVEHKKKKLEVQLQElqskysdgekvraelndKVHKLQNEVEsvtgmlneae 1300
Cdd:PRK12704 27 KIAEAKIKEAEEEAK-----RILEEAKKEAEAIKKEALLEAKE-----------------EIHKLRNEFE---------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1301 gkaiklaKDVASLGSQLQDTQELLQeetRQKLNVSTKLRQLEDERNSLQEQLDEEMEAKQNLERHISTLNIQLSDSKKKL 1380
Cdd:PRK12704 75 -------KELRERRNELQKLEKRLL---QKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQEL 144
|
170 180 190
....*....|....*....|....*....|....*...
gi 156120901 1381 QDFAS-TVE-----LLEEGKKKFQKEIESLTQQYEEKA 1412
Cdd:PRK12704 145 ERISGlTAEeakeiLLEKVEEEARHEAAVLIKEIEEEA 182
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
846-1212 |
3.78e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.14 E-value: 3.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 846 QVTRQEEEMQAKEDELQKTKERQQKAESELKELEQKHSQLTEEKNLLQEQLQAetelyAEAEEmrvRLAAKKQELEEILh 925
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDV-----ASAER---EIAELEAELERLD- 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 926 emearleEEEDRSQQLQAERKKmaqqmldleeqleeeeaarqklqlekvtAEAKIKKLEDDIlvmddqnNKLSKERKLLE 1005
Cdd:COG4913 682 -------ASSDDLAALEEQLEE----------------------------LEAELEELEEEL-------DELKGEIGRLE 719
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1006 ERISDLTTNLAEEEEKAKNLTKLKNKHESmiSELEVRLKKEEKSRQElEKLKRKLDGEASDLHEQIAELQAQIAELkMQL 1085
Cdd:COG4913 720 KELEQAEEELDELQDRLEAAEDLARLELR--ALLEERFAAALGDAVE-RELRENLEERIDALRARLNRAEEELERA-MRA 795
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1086 AKKE-----EELQAALGRLDDEMAQ----KNNAL----KKIREL-----EGHISDLQEDLDSERAArnkAEKQKRDLGEE 1147
Cdd:COG4913 796 FNREwpaetADLDADLESLPEYLALldrlEEDGLpeyeERFKELlnensIEFVADLLSKLRRAIRE---IKERIDPLNDS 872
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 156120901 1148 LEALKTELEDTLdstatQQELRAKREQEVTMLKKALDEETRSHESQVQEMRQKHTQVVEELTEQL 1212
Cdd:COG4913 873 LKRIPFGPGRYL-----RLEARPRPDPEVREFRQELRAVTSGASLFDEELSEARFAALKRLIERL 932
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1688-1917 |
3.78e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 48.90 E-value: 3.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1688 DLMQLQEDLAAAERARKQADLEkdeLAEELASSVsgrNALQDEKRRLEaRIAQ---------LEEELEEEQGNTEAMSER 1758
Cdd:PRK10929 24 DEKQITQELEQAKAAKTPAQAE---IVEALQSAL---NWLEERKGSLE-RAKQyqqvidnfpKLSAELRQQLNNERDEPR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1759 VRKAT-------QQAEQLSNELATE-RSAAQKNENARQ------QLERQNKELRSKLQEMEGAVKSKFKSTIAALEAKIA 1824
Cdd:PRK10929 97 SVPPNmstdaleQEILQVSSQLLEKsRQAQQEQDRAREisdslsQLPQQQTEARRQLNEIERRLQTLGTPNTPLAQAQLT 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1825 QLeeqveqearekQATAKALKQKDKKLKEALLQV----EDERKMAEQYKEQAEKGNLRVKQLKRQLeeaeeESQRinanr 1900
Cdd:PRK10929 177 AL-----------QAESAALKALVDELELAQLSAnnrqELARLRSELAKKRSQQLDAYLQALRNQL-----NSQR----- 235
|
250
....*....|....*..
gi 156120901 1901 rklQRELDEATESNEAM 1917
Cdd:PRK10929 236 ---QREAERALESTELL 249
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1105-1331 |
4.71e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.90 E-value: 4.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1105 QKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALKTELEdtldstATQQELrAKREQEVTMLKKALD 1184
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEID------KLQAEI-AEAEAEIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1185 EETRSheSQVQEMRQKHTQVV---EELTEQLEQFKRAKANLDKNKQALEKenaelagelrvLSQAKQEVEHKKKKLEVQL 1261
Cdd:COG3883 90 ERARA--LYRSGGSVSYLDVLlgsESFSDFLDRLSALSKIADADADLLEE-----------LKADKAELEAKKAELEAKL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1262 QELQSKYSDGEKVRAELNDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLGSQLQDTQELLQEETRQK 1331
Cdd:COG3883 157 AELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAA 226
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1233-1854 |
5.00e-05 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 48.20 E-value: 5.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1233 NAELAGELRVLSQAKQEVEHKKKKLEVQLQELQSKYSDGEKVRAELNDKVHKLQNEVESVTGMLNEAEgkaiklakdvAS 1312
Cdd:pfam05557 1 RAELIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAE----------EA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1313 LGSQLQDTQELLQEETRQKLNVSTKLRQLEDERNSLQEQLDEEMEAKQNLERHistlNIQLSDSKKKLQDFASTVELLEE 1392
Cdd:pfam05557 71 LREQAELNRLKKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRA----ELELQSTNSELEELQERLDLLKA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1393 GKKKFQKEIESLTQQYEEKAAAYDKLEKTKNRLQQELDDLVVdLDNQRQLVSNLEKKQKKFDQLLAEEKNISSKYADeRD 1472
Cdd:pfam05557 147 KASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEI-VKNSKSELARIPELEKELERLREHNKHLNENIEN-KL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1473 RAEAEAREKETKalsLARALEEALEAKEELERTNKMLkAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEE-- 1550
Cdd:pfam05557 225 LLKEEVEDLKRK---LEREEKYREEAATLELEKEKLE-QELQSWVKLAQDTGLNLRSPEDLSRRIEQLQQREIVLKEEns 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1551 -LEDELQATEDAKLRLEVNMQALKVQFErDLQARDEQNEEKRRQLQRQLheyetelederkqrALAVAAKKKLEGDLK-- 1627
Cdd:pfam05557 301 sLTSSARQLEKARRELEQELAQYLKKIE-DLNKKLKRHKALVRRLQRRV--------------LLLTKERDGYRAILEsy 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1628 DLELQADSAIKGREEAIKQLRKLQAQMKDFQRELEdARASRDEIFATAKENEKKAKSLEADLMQLQEDLAAAERARKQAD 1707
Cdd:pfam05557 366 DKELTMSNYSPQLLERIEEAEDMTQKMQAHNEEME-AQLSVAEEELGGYKQQAQTLERELQALRQQESLADPSYSKEEVD 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1708 LEKDELAEELASsvsgRNALQDEKRRLEARIAQLEEELEEEQGNTEAMSERVRKATQQAEQLSNELatersaaqknENAR 1787
Cdd:pfam05557 445 SLRRKLETLELE----RQRLREQKNELEMELERRCLQGDYDPKKTKVLHLSMNPAAEAYQQRKNQL----------EKLQ 510
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156120901 1788 QQLERQnKELRSKLQEMEGAVKSKFKSTIAALEAKIAQLEEQVEQEAREKQATAKALKQKDKKLKEA 1854
Cdd:pfam05557 511 AEIERL-KRLLKKLEDDLEQVLRLPETTSTMNFKEVLDLRKELESAELKNQRLKEVFQAKIQEFRDV 576
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
980-1268 |
5.10e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 48.36 E-value: 5.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 980 IKKLEDDILVMD-------DQNNKLSKERKLLEERISDLTTNLAEEEEKAKNLTKLKNKHESMISELEvRLKKEEKSRQE 1052
Cdd:PLN02939 137 IQNAEKNILLLNqarlqalEDLEKILTEKEALQGKINILEMRLSETDARIKLAAQEKIHVEILEEQLE-KLRNELLIRGA 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1053 LEK-LKRKLDGEASDLHEQIAELQAQIAELKMQLAKKEEElQAALGRLDDEMAQKNNALkkiRELEGHISDLQEDLDSER 1131
Cdd:PLN02939 216 TEGlCVHSLSKELDVLKEENMLLKDDIQFLKAELIEVAET-EERVFKLEKERSLLDASL---RELESKFIVAQEDVSKLS 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1132 AARNKAEKQKRD-LGEELEALKTELEDTLDSTATQQELRAKreqeVTMLKKALDEETRSHES-QVQEMRQKHTQVVEelt 1209
Cdd:PLN02939 292 PLQYDCWWEKVEnLQDLLDRATNQVEKAALVLDQNQDLRDK----VDKLEASLKEANVSKFSsYKVELLQQKLKLLE--- 364
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 156120901 1210 eqlEQFKRAKANLDKNKQALEKENAELAGELRVLSQakqevEHKKKKLEVQLQELQSKY 1268
Cdd:PLN02939 365 ---ERLQASDHEIHSYIQLYQESIKEFQDTLSKLKE-----ESKKRSLEHPADDMPSEF 415
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
852-1080 |
5.42e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.52 E-value: 5.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 852 EEMQAKEDELQKTKERQQKAESELKELEQKHSQLTEEKNLLQEQLQAETELYAEAEEMRVRLAAKKQELEEILHEMEARL 931
Cdd:PRK03918 518 EELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKEL 597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 932 EEEEDRSQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDDILVMDDqnnklsKERKLLEERISDL 1011
Cdd:PRK03918 598 EPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSE------EEYEELREEYLEL 671
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 156120901 1012 TTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLDgEASDLHEQIAELQAQIAE 1080
Cdd:PRK03918 672 SRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALE-RVEELREKVKKYKALLKE 739
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1640-1893 |
5.89e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 48.00 E-value: 5.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1640 REEAIKQLRKLQA-QMKDFQRELEDARASR--------DEIFATAKENEKKAKSLEADLMQLQEDlaAAERARKQADLEK 1710
Cdd:PRK05771 18 KDEVLEALHELGVvHIEDLKEELSNERLRKlrslltklSEALDKLRSYLPKLNPLREEKKKVSVK--SLEELIKDVEEEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1711 DELAEELASSVSGRNALQDEKRRLEARIAQ--------LEEELEEEQGNTEA----MSERVRKATQQAEQLSNELATERS 1778
Cdd:PRK05771 96 EKIEKEIKELEEEISELENEIKELEQEIERlepwgnfdLDLSLLLGFKYVSVfvgtVPEDKLEELKLESDVENVEYISTD 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1779 aaqKNE------NARQQLERQNKELRS-KLQEMEGAVKSKFKSTIAALEAKIAQLEeqveqeaREKQATAKALKQKDKKL 1851
Cdd:PRK05771 176 ---KGYvyvvvvVLKELSDEVEEELKKlGFERLELEEEGTPSELIREIKEELEEIE-------KERESLLEELKELAKKY 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 156120901 1852 KEALLQVED----ERKMAEQYKEQAEKGNL----------RVKQLKRQLEEAEEES 1893
Cdd:PRK05771 246 LEELLALYEyleiELERAEALSKFLKTDKTfaiegwvpedRVKKLKELIDKATGGS 301
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1025-1449 |
6.15e-05 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 47.93 E-value: 6.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1025 LTKLKNKHESMISELEVRLKKEEKSRQELEKLKrkldgeasdlhEQIAELQAQIAELKMQLAKKEEELQAALGRLDDEMA 1104
Cdd:pfam06160 95 LDDIEEDIKQILEELDELLESEEKNREEVEELK-----------DKYRELRKTLLANRFSYGPAIDELEKQLAEIEEEFS 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1105 QKNN---------ALKKIRELEGHISDLQEDLDseraarnkaekqkrDLGEELEALKTELEDTLDstatqqELRAKREQe 1175
Cdd:pfam06160 164 QFEEltesgdyleAREVLEKLEEETDALEELME--------------DIPPLYEELKTELPDQLE------ELKEGYRE- 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1176 vtMLKKALDEETRSHESQVQEMRQKhtqvVEELTEQLEQFKRAKAnlDKNKQALEKENAELAGELRVLSQAKQEVEHKKK 1255
Cdd:pfam06160 223 --MEEEGYALEHLNVDKEIQQLEEQ----LEENLALLENLELDEA--EEALEEIEERIDQLYDLLEKEVDAKKYVEKNLP 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1256 KLEVQLQELQSKYsdgekvraelndkvHKLQNEVESVT---GMLNEAEGKAIKLAKDVASLGSQLQDTQELLQEET---- 1328
Cdd:pfam06160 295 EIEDYLEHAEEQN--------------KELKEELERVQqsyTLNENELERVRGLEKQLEELEKRYDEIVERLEEKEvays 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1329 --RQKLNVSTK-LRQLEDERNSLQEQL----DEEMEAKQNLERhistLNIQLSDSKKKLQdfastvelleegkkkfQKEI 1401
Cdd:pfam06160 361 elQEELEEILEqLEEIEEEQEEFKESLqslrKDELEAREKLDE----FKLELREIKRLVE----------------KSNL 420
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 156120901 1402 ESLTQQYEE-KAAAYDKLEKTKNRLQQ---ELDDLVVDLDNQRQLVSNLEKK 1449
Cdd:pfam06160 421 PGLPESYLDyFFDVSDEIEDLADELNEvplNMDEVNRLLDEAQDDVDTLYEK 472
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1757-1913 |
6.41e-05 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 47.69 E-value: 6.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1757 ERVRKATQQAEQLSNELATERSAAQKNENARQQLERQNKELRSKLQEMEGAVKSKfkSTIAALEAKIAQLEEQVEQEARE 1836
Cdd:pfam05262 210 EDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKPA--DTSSPKEDKQVAENQKREIEKAQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1837 ---KQATAKALKQKDKKLKEALLQVEDERKMAEQYKEQAekgnlrvkqlKRQLEEAEEESQRI-NANRRKLQRELDEATE 1912
Cdd:pfam05262 288 ieiKKNDEEALKAKDHKAFDLKQESKASEKEAEDKELEA----------QKKREPVAEDLQKTkPQVEAQPTSLNEDAID 357
|
.
gi 156120901 1913 S 1913
Cdd:pfam05262 358 S 358
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1230-1414 |
6.43e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.52 E-value: 6.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1230 EKENAELAGELRVLSQAKQEVEHKKKKLEVQLQELQSKYSDGEKVRAELNDKVHKLQNEVESVTGMLNEAEGKAIKLAKD 1309
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1310 VASLGSQL---------QDTQELLQ---------EETRQKLN-VSTKLRQLEDERNSLQEQLDEEMEAKQNLERHISTLN 1370
Cdd:COG3883 95 LYRSGGSVsyldvllgsESFSDFLDrlsalskiaDADADLLEeLKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 156120901 1371 IQLSDSKKKLQDFASTVELLEEGKKKFQKEIESLTQQYEEKAAA 1414
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1020-1155 |
6.60e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 47.90 E-value: 6.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1020 EKAK-NLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLDGEASDLHEQIAELQAQIAELKMQLakkEEELQAALgr 1098
Cdd:PRK00409 505 EEAKkLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEA---EKEAQQAI-- 579
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 156120901 1099 lddemaqknNALKKirELEGHISDLQEDLDSERAA--RNKAEKQKRDLGEELEALKTEL 1155
Cdd:PRK00409 580 ---------KEAKK--EADEIIKELRQLQKGGYASvkAHELIEARKRLNKANEKKEKKK 627
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
940-1087 |
6.68e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.46 E-value: 6.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 940 QLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDDILVMDDQ--NNKLSKERKLLEERISDLTTNLAE 1017
Cdd:COG1579 28 ELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgNVRNNKEYEALQKEIESLKRRISD 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1018 EEEKAKNLTKLKNKHESMISELEVRLKKEEKsrqELEKLKRKLDGEASDLHEQIAELQAQIAELKMQLAK 1087
Cdd:COG1579 108 LEDEILELMERIEELEEELAELEAELAELEA---ELEEKKAELDEELAELEAELEELEAEREELAAKIPP 174
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
883-1264 |
7.02e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 47.58 E-value: 7.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 883 SQLTEEKNLLQEQLQAETELYAEAEEMRVRLAAKKQELEEILHEMEARLEEEEDRSQQLQAERKKMAQQMLDLEEQLEEE 962
Cdd:pfam07888 34 NRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEEL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 963 EAARQKLQLEKVTAEAKIKKLEDDILVMDDQNNKLSKERKLLEERISDLTTNLAEEEEKAKNLtklknkhESMISELEVR 1042
Cdd:pfam07888 114 SEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQL-------QAKLQQTEEE 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1043 LKKEEKSRQELEKLKRKLDGEASDLHEQIAELQAQIAELKmqlaKKEEELQAALGRLDDEMAQKNNALKKIRELEGHISD 1122
Cdd:pfam07888 187 LRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAH----RKEAENEALLEELRSLQERLNASERKVEGLGEELSS 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1123 LQEDLDSERAARNKAEKQKRDLGEELEalkteledtlDSTATQQELRAKREQEVTMLKKALDEETRSHESQVQEMRQKHT 1202
Cdd:pfam07888 263 MAAQRDRTQAELHQARLQAAQLTLQLA----------DASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEE 332
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 156120901 1203 QVVEELTEQleqfKRAKANLDKNKQALEKENAELAGELRVLSQAKQEVEHKKKKLEVQLQEL 1264
Cdd:pfam07888 333 RLQEERMER----EKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQEL 390
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1051-1712 |
7.46e-05 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 47.82 E-value: 7.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1051 QELEKLKRKLDGEASDLHEQIAELQAQIAELK-MQLAKKE-----EELQAALGrlDDEMAQKNNALKKIRELEGHISDLQ 1124
Cdd:pfam07111 73 QELRRLEEEVRLLRETSLQQKMRLEAQAMELDaLAVAEKAgqaeaEGLRAALA--GAEMVRKNLEEGSQRELEEIQRLHQ 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1125 EDLDSERAARNKAEKQKRDLGEELEALKTELEDTLDSTATQQelrAKREQEVTMLKKALDEETRSHESQVQemrqkhtqv 1204
Cdd:pfam07111 151 EQLSSLTQAHEEALSSLTSKAEGLEKSLNSLETKRAGEAKQL---AEAQKEAELLRKQLSKTQEELEAQVT--------- 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1205 veeLTEQLEQFKRAKANLDKNKQALEKENAELAGELRVLSQAKQEVEHKKKKLEVQLQELqskysdgekvraelndkVHK 1284
Cdd:pfam07111 219 ---LVESLRKYVGEQVPPEVHSQTWELERQELLDTMQHLQEDRADLQATVELLQVRVQSL-----------------THM 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1285 LQNEVESVTGMLNEAEGKAIKLAKDVASLGSQLQDTQELLQEETR-QKLNVSTKLRQLEDERNSLQEQLDEEMEAKQNLE 1363
Cdd:pfam07111 279 LALQEEELTRKIQPSDSLEPEFPKKCRSLLNRWREKVFALMVQLKaQDLEHRDSVKQLRGQVAELQEQVTSQSQEQAILQ 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1364 RhistlniqlsdskkKLQDFASTVELLEEGKKKFQKEIesltqqyeekaaayDKLEKTKNRLQQELDDLVVDLdnqRQLV 1443
Cdd:pfam07111 359 R--------------ALQDKAAEVEVERMSAKGLQMEL--------------SRAQEARRRQQQQTASAEEQL---KFVV 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1444 SNLEKKQKKFDQLLAEEKNISSKYADERDRAEAEAREKETkalslaraleealeakeelertnkmlkaeMEDLVSSKDDV 1523
Cdd:pfam07111 408 NAMSSTQIWLETTMTRVEQAVARIPSLSNRLSYAVRKVHT-----------------------------IKGLMARKVAL 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1524 GKNVHELEKSKRALETQMEEMKTQLEELEDElqatedaKLRLEVNMQALKVQFERDLQARDEQNEEKRRQLQRQLHEYET 1603
Cdd:pfam07111 459 AQLRQESCPPPPPAPPVDADLSLELEQLREE-------RNRLDAELQLSAHLIQQEVGRAREQGEAERQQLSEVAQQLEQ 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1604 ELedERKQRALAvAAKKKLEGDLKDLELQADSAIKGREEAIKQLR---------------KLQAQMKDFQRELEDARASR 1668
Cdd:pfam07111 532 EL--QRAQESLA-SVGQQLEVARQGQQESTEEAASLRQELTQQQEiygqalqekvaevetRLREQLSDTKRRLNEARREQ 608
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 156120901 1669 DEIFATAKENEKKA---KSLEADLMQLQEDLAAAER---ARKQADLEKDE 1712
Cdd:pfam07111 609 AKAVVSLRQIQHRAtqeKERNQELRRLQDEARKEEGqrlARRVQELERDK 658
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1039-1406 |
7.52e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 47.58 E-value: 7.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1039 LEVRLKKEEKSRQEL----EKLKRKLDGEASDLHEQIAELQAQIAELKMQLAKKEEELQAA-------------LGRLDD 1101
Cdd:pfam07888 32 LQNRLEECLQERAELlqaqEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSrekheeleekykeLSASSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1102 EMAQKNNAL--------KKIRELEGHISDLQE-------DLDSERAARNKAEKQKRDLGEELEALKTELEdtldstATQQ 1166
Cdd:pfam07888 112 ELSEEKDALlaqraaheARIRELEEDIKTLTQrvleretELERMKERAKKAGAQRKEEEAERKQLQAKLQ------QTEE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1167 ELRaKREQEVTMLKKALDEEtrshESQVQEMRQKHTQVVEELTEqleqfkrakanldknKQALEKENAELAGELRVLSQA 1246
Cdd:pfam07888 186 ELR-SLSKEFQELRNSLAQR----DTQVLQLQDTITTLTQKLTT---------------AHRKEAENEALLEELRSLQER 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1247 KQEVEHKKKKLEvqlQELQSKYSDGEKVRAELndkvHKLQNEVESVTGMLNEAegkAIKLAKDVASLGSQLQDTQELLQE 1326
Cdd:pfam07888 246 LNASERKVEGLG---EELSSMAAQRDRTQAEL----HQARLQAAQLTLQLADA---SLALREGRARWAQERETLQQSAEA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1327 ETRQKLNVSTKLRQLEDernSLQEQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFASTVELLEEGKKKFQKEIESLTQ 1406
Cdd:pfam07888 316 DKDRIEKLSAELQRLEE---RLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLE 392
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1661-1867 |
7.88e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.84 E-value: 7.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1661 LEDARASRDEIFataKENEKKAKSLEADLMQLQEDLAAAERARK---QADLEKDELAEELASSVSGRNALQDEKRRLEAR 1737
Cdd:COG4717 48 LERLEKEADELF---KPQGRKPELNLKELKELEEELKEAEEKEEeyaELQEELEELEEELEELEAELEELREELEKLEKL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1738 IAQLEEELEEEQGNteamsERVRKATQQAEQLSNELATERSAAQKNENARQQLERQNKELRSKLQEMEGAVKSKFKSTIA 1817
Cdd:COG4717 125 LQLLPLYQELEALE-----AELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAE 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 156120901 1818 ALEaKIAQLEEQVEQEAREKQATAKALKQKDKKLKEALLQVEDERKMAEQ 1867
Cdd:COG4717 200 ELE-ELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEA 248
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
867-1363 |
8.00e-05 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 47.87 E-value: 8.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 867 RQQKAESELKELEQKHSQLTEEKNLLQEQLQA----ETELYAEAEEMRVRLAAKKQELEEIlhemeARLEEEEDRSQQLQ 942
Cdd:PRK10246 420 EQRPLRQRLVALHGQIVPQQKRLAQLQVAIQNvtqeQTQRNAALNEMRQRYKEKTQQLADV-----KTICEQEARIKDLE 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 943 AERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDDIlvmddqnNKLSKERKLLEERISDLTTNLAEEEEKA 1022
Cdd:PRK10246 495 AQRAQLQAGQPCPLCGSTSHPAVEAYQALEPGVNQSRLDALEKEV-------KKLGEEGAALRGQLDALTKQLQRDESEA 567
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1023 KNLTK----LKNKHESMISELEVRLKKEEKSR---QELEKLKRKLD--GEASDLHEQIAELQAQIAELKMQLAKKEEELQ 1093
Cdd:PRK10246 568 QSLRQeeqaLTQQWQAVCASLNITLQPQDDIQpwlDAQEEHERQLRllSQRHELQGQIAAHNQQIIQYQQQIEQRQQQLL 647
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1094 AALGRLDDEMAQKNNalkkireleghisdlQEDLDSERAARNKAEKQKRDLGEELEALKTELEDTLDSTATQQELRAKRE 1173
Cdd:PRK10246 648 TALAGYALTLPQEDE---------------EASWLATRQQEAQSWQQRQNELTALQNRIQQLTPLLETLPQSDDLPHSEE 712
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1174 QEVTMLKKALDEETRSHESQVQEMRQKHTQVVEELTEQLEQFKRAKANLDKNKQAlekenAELAGELRvlSQAKQEVEHK 1253
Cdd:PRK10246 713 TVALDNWRQVHEQCLSLHSQLQTLQQQDVLEAQRLQKAQAQFDTALQASVFDDQQ-----AFLAALLD--EETLTQLEQL 785
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1254 KKKLEVQLQElqskysdgekvraelndkVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLGSQLQDTQELLQEETRQKLN 1333
Cdd:PRK10246 786 KQNLENQRQQ------------------AQTLVTQTAQALAQHQQHRPDGLDLTVTVEQIQQELAQLAQQLRENTTRQGE 847
|
490 500 510
....*....|....*....|....*....|
gi 156120901 1334 VSTKLRQLEDERNSLQEQLDEEMEAKQNLE 1363
Cdd:PRK10246 848 IRQQLKQDADNRQQQQALMQQIAQATQQVE 877
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1506-1909 |
8.63e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 47.60 E-value: 8.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1506 NKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDeLQATEDAKLRlevnmQALKVQFERDLQARDE 1585
Cdd:PRK11281 58 DKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEA-LKDDNDEETR-----ETLSTLSLRQLESRLA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1586 QNEEKRRQLQRQLHEYETEL-----EDERKQRALAVAAKKKlegdlkdleLQADSAIKGREEAIKQLRKLQAQMKDFQRE 1660
Cdd:PRK11281 132 QTLDQLQNAQNDLAEYNSQLvslqtQPERAQAALYANSQRL---------QQIRNLLKGGKVGGKALRPSQRVLLQAEQA 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1661 LEDARasrdeifatakeNEKKAKSLEA-----DLMQLQEDLAAAERARKQADLekdelaEELASSVSGRNALQDEKrrlE 1735
Cdd:PRK11281 203 LLNAQ------------NDLQRKSLEGntqlqDLLQKQRDYLTARIQRLEHQL------QLLQEAINSKRLTLSEK---T 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1736 ARIAQLEEELEEEQGN----TEA-----MSERVRKATQQAEQLSnelatersaaQKNENARQQLER-----QN-KELRSK 1800
Cdd:PRK11281 262 VQEAQSQDEAARIQANplvaQELeinlqLSQRLLKATEKLNTLT----------QQNLRVKNWLDRltqseRNiKEQISV 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1801 LQemeGA-VKSK--FK--------STIAALEAKIAQLeeQVEQ----EAREK----QATAKALKQKDK-----KLKEALL 1856
Cdd:PRK11281 332 LK---GSlLLSRilYQqqqalpsaDLIEGLADRIADL--RLEQfeinQQRDAlfqpDAYIDKLEAGHKsevtdEVRDALL 406
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 156120901 1857 QVEDER-KMAEQYkeqaekgnlrVKQLKRQLEEA---EEESQRINANRRKLQRELDE 1909
Cdd:PRK11281 407 QLLDERrELLDQL----------NKQLNNQLNLAinlQLNQQQLLSVSDSLQSTLTQ 453
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1184-1415 |
8.79e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.13 E-value: 8.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1184 DEETRSHESQVQEMRQKHTQVVEELTEQLEQFKRAKANLDKNKQALEKENAELAGELRVLSQAKQEVEHKKKKLEVQLQE 1263
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1264 LQSKYSDGEKVRA--------ELNDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLGSQLQDTQELLQEETRQKLNVS 1335
Cdd:COG3883 95 LYRSGGSVSYLDVllgsesfsDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1336 TK-------LRQLEDERNSLQEQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFASTVELLEEGKKKFQKEIESLTQQY 1408
Cdd:COG3883 175 AQqaeqealLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGA 254
|
....*..
gi 156120901 1409 EEKAAAY 1415
Cdd:COG3883 255 AGAAAGS 261
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1522-1934 |
8.83e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 47.71 E-value: 8.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1522 DVGKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKVQFERDlqardeqnEEKRRQLQRQLHEY 1601
Cdd:TIGR04523 58 NLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKND--------KEQKNKLEVELNKL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1602 ETELEDERKQRALAVAAKKKLEGDLKDLELQADSAIKGREEAIKQLRKLQAQMKDFQRELEDARASR---DEIFATAKEN 1678
Cdd:TIGR04523 130 EKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLlklELLLSNLKKK 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1679 EKKAKSLEADLMQLQEDLAAAErarKQADLEKDELaeelassvsgrNALQDEKRRLEARIAQLEEELEEEQGNTEAMSER 1758
Cdd:TIGR04523 210 IQKNKSLESQISELKKQNNQLK---DNIEKKQQEI-----------NEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKE 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1759 VRKATQQAEQLSNELATERSAAQKNENARQQleRQNKELRSKLQEMEGAvKSKFKSTIAALEAKIAQLEEQVEQEAREKQ 1838
Cdd:TIGR04523 276 LEQNNKKIKELEKQLNQLKSEISDLNNQKEQ--DWNKELKSELKNQEKK-LEEIQNQISQNNKIISQLNEQISQLKKELT 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1839 ATAKALKQKDKKLKEALLQVEDERKMAEQYKEQAEKGNLRVKQLKRQLEEAEEESQRINANRRKLQRELDEATESNEAMG 1918
Cdd:TIGR04523 353 NSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLK 432
|
410
....*....|....*.
gi 156120901 1919 REVTALKSKLRRGNET 1934
Cdd:TIGR04523 433 ETIIKNNSEIKDLTNQ 448
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1119-1901 |
8.98e-05 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 47.90 E-value: 8.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1119 HISDLQEDLDSERAARNKAEKQKRDLGEELEALKTELEDTLDSTAT-------------QQELRAKREQEVTMLKKAlDE 1185
Cdd:NF041483 16 HLSRFEAEMDRLKTEREKAVQHAEDLGYQVEVLRAKLHEARRSLASrpaydgadigyqaEQLLRNAQIQADQLRADA-ER 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1186 ETRSHESQVQEMRQKHTQVVEEL-----TEQLEQFKRAKANLDKNKQALE---KENAELAGELRVL--SQAKQEVEHKKK 1255
Cdd:NF041483 95 ELRDARAQTQRILQEHAEHQARLqaelhTEAVQRRQQLDQELAERRQTVEshvNENVAWAEQLRARteSQARRLLDESRA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1256 KLEvqlQELQSKYSDGEKVRAELNdkvHKLQNEVESVtgmlnEAEGKAIklakdvasLGSQLQDTQELLQEETRQKLNVS 1335
Cdd:NF041483 175 EAE---QALAAARAEAERLAEEAR---QRLGSEAESA-----RAEAEAI--------LRRARKDAERLLNAASTQAQEAT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1336 TKLRQLedeRNSLQEQLDEEMEAKQNLERhisTLNIQLSDSKKKLQDFASTVE-LLEEGKKKFQKEIESLTQQYEEK--- 1411
Cdd:NF041483 236 DHAEQL---RSSTAAESDQARRQAAELSR---AAEQRMQEAEEALREARAEAEkVVAEAKEAAAKQLASAESANEQRtrt 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1412 ---------AAAYDKLEKTKNRLQQELDDLVVDLDnqrQLVSNLEKKQKkfdQLLAEEKnisskyADERDRAEAEAREKE 1482
Cdd:NF041483 310 akeeiarlvGEATKEAEALKAEAEQALADARAEAE---KLVAEAAEKAR---TVAAEDT------AAQLAKAARTAEEVL 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1483 TKALSLARALEEALEAKEELERTNKmlKAEMEDLVSSKDDVGknvhelEKSKRALETQMEEMKTQLEELEDELQatedaK 1562
Cdd:NF041483 378 TKASEDAKATTRAAAEEAERIRREA--EAEADRLRGEAADQA------EQLKGAAKDDTKEYRAKTVELQEEAR-----R 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1563 LRLEVNmqalkvQFERDLQARDEQ-NEEKRRQLQRQLHEYETELEDerkqralaVAAKKKLEGDLKDLELQADSAiKGRE 1641
Cdd:NF041483 445 LRGEAE------QLRAEAVAEGERiRGEARREAVQQIEEAARTAEE--------LLTKAKADADELRSTATAESE-RVRT 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1642 EAIKQLRKLQAQMKDfqrELEDARASRDEIFATAKENEKKAKS-LEADLMQLQEDLAAAERARK-QADLEKDELAEELAS 1719
Cdd:NF041483 510 EAIERATTLRRQAEE---TLERTRAEAERLRAEAEEQAEEVRAaAERAARELREETERAIAARQaEAAEELTRLHTEAEE 586
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1720 SVSGRNALQDEKRRLEARIAQLEEELEEEQgNTEAmSERVRKATQQAEQLSNELATErsAAQKNENARQQLERQNKELRS 1799
Cdd:NF041483 587 RLTAAEEALADARAEAERIRREAAEETERL-RTEA-AERIRTLQAQAEQEAERLRTE--AAADASAARAEGENVAVRLRS 662
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1800 KLQEMEGAVKSKFKSTIAALEAKIAQLEEQVEQEAREkqATAKALKQKDKKLKEALLQVEDERKMAEQYKEQA-EKGNLR 1878
Cdd:NF041483 663 EAAAEAERLKSEAQESADRVRAEAAAAAERVGTEAAE--ALAAAQEEAARRRREAEETLGSARAEADQERERArEQSEEL 740
|
810 820
....*....|....*....|....*
gi 156120901 1879 VKQLKRQLEEAEEESQRI--NANRR 1901
Cdd:NF041483 741 LASARKRVEEAQAEAQRLveEADRR 765
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
657-681 |
9.25e-05 |
|
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.
Pssm-ID: 276814 [Multi-domain] Cd Length: 170 Bit Score: 45.03 E-value: 9.25e-05
10 20
....*....|....*....|....*
gi 156120901 657 YKEQLGKLMTTLRNTTPNFVRCIIP 681
Cdd:cd01363 146 INESLNTLMNVLRATRPHFVRCISP 170
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1757-1933 |
9.34e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.45 E-value: 9.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1757 ERVRKATQQAEQLSNELATERSAAQKNENARQQLERQNKELRSKLQEMEGAVKskfkstIAALEAKIAQLEEQVEQEARE 1836
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ------LLPLYQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1837 kqatAKALKQKDKKLKEALLQVEDERKMAEQYKEQAEKGNLRVKQLKR-QLEEAEEESQRINANRRKLQRELDEATESNE 1915
Cdd:COG4717 148 ----LEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEeELQDLAEELEELQQRLAELEEELEEAQEELE 223
|
170
....*....|....*...
gi 156120901 1916 AMGREVTALKSKLRRGNE 1933
Cdd:COG4717 224 ELEEELEQLENELEAAAL 241
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
998-1220 |
1.04e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 47.23 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 998 SKERKLLEERISDLTTNLAEEEEKAKNLTKLKNKHESMISEL-EVRLKKEEKSRQELEKLKRKLDGEASDLHEQIAELQA 1076
Cdd:PRK05771 35 DLKEELSNERLRKLRSLLTKLSEALDKLRSYLPKLNPLREEKkKVSVKSLEELIKDVEEELEKIEKEIKELEEEISELEN 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1077 QIAELKmqlaKKEEELQaALGRLDDEMAQKNN---------ALKKIRELEGHISDLQEDLDSERAARNK-------AEKQ 1140
Cdd:PRK05771 115 EIKELE----QEIERLE-PWGNFDLDLSLLLGfkyvsvfvgTVPEDKLEELKLESDVENVEYISTDKGYvyvvvvvLKEL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1141 KRDLGEELEALKTELEDTLDSTATQQELRAKREQevtmlKKALDEETRSHESQVQEMRQKHTQVVEELTEQLEQFK-RAK 1219
Cdd:PRK05771 190 SDEVEEELKKLGFERLELEEEGTPSELIREIKEE-----LEEIEKERESLLEELKELAKKYLEELLALYEYLEIELeRAE 264
|
.
gi 156120901 1220 A 1220
Cdd:PRK05771 265 A 265
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1141-1310 |
1.17e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.08 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1141 KRDLGEELEALKTELEDTLDstATQQELRAKREQEVTMLKKALDEETRSHESQVQEMRQKHTQVVEELTEQLEQFKRAKA 1220
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILE--EAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1221 NLDKNKQALEKENAELAGELRVLSQAKQEVEHKKKKLEVQLQELqSKYSdGEKVRAELNDKV-HKLQNEVES-VTGMLNE 1298
Cdd:PRK12704 104 LLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERI-SGLT-AEEAKEILLEKVeEEARHEAAVlIKEIEEE 181
|
170
....*....|..
gi 156120901 1299 AEGKAIKLAKDV 1310
Cdd:PRK12704 182 AKEEADKKAKEI 193
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
846-1325 |
1.24e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 47.04 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 846 QVTRQEEEMQAKEDELQKTKERqqkaeseLKELEQKHSQLTEeknlLQEQLQAETELYAEAEEmrvrlaaKKQELEEILH 925
Cdd:pfam05557 119 QIQRAELELQSTNSELEELQER-------LDLLKAKASEAEQ----LRQNLEKQQSSLAEAEQ-------RIKELEFEIQ 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 926 EMEARLEEEEDRSQQLQ--AERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLE---DDILVMDDQNNKLSKE 1000
Cdd:pfam05557 181 SQEQDSEIVKNSKSELAriPELEKELERLREHNKHLNENIENKLLLKEEVEDLKRKLEREEkyrEEAATLELEKEKLEQE 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1001 RKLLEERISDLTTNLAEEEEKAKNLTKLKNK---HESMISELEVRLKKEEKSRQELEKLKRKLDGEASDLHEQIAELQAQ 1077
Cdd:pfam05557 261 LQSWVKLAQDTGLNLRSPEDLSRRIEQLQQReivLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKAL 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1078 IAELKMQLA---KKEEELQAALGRLDDEMAQKNNALKK---IRELEGHISDLQEDLDSERAARNKAEkqkrdlgEELEAL 1151
Cdd:pfam05557 341 VRRLQRRVLlltKERDGYRAILESYDKELTMSNYSPQLlerIEEAEDMTQKMQAHNEEMEAQLSVAE-------EELGGY 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1152 KteledtLDSTATQQELRAKREQEVTmlkkaldEETRSHESQVQEMRQKhtqvVEELTEQLEQFKRakanlDKNKQALEK 1231
Cdd:pfam05557 414 K------QQAQTLERELQALRQQESL-------ADPSYSKEEVDSLRRK----LETLELERQRLRE-----QKNELEMEL 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1232 ENAELAGelrVLSQAKQEVEHkkKKLEVQLQELQSKYSDGEKVRAE---LNDKVHKLQNEVESVTGM----LNEAEGKAI 1304
Cdd:pfam05557 472 ERRCLQG---DYDPKKTKVLH--LSMNPAAEAYQQRKNQLEKLQAEierLKRLLKKLEDDLEQVLRLpettSTMNFKEVL 546
|
490 500
....*....|....*....|.
gi 156120901 1305 KLAKDVASLGSQLQDTQELLQ 1325
Cdd:pfam05557 547 DLRKELESAELKNQRLKEVFQ 567
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1512-1754 |
1.28e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.75 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1512 EMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALkvqfERDLQARDEQNEEKR 1591
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEA----EAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1592 RQLQRQ----------------------LHEYETELEDERKQRALAVAAKKKLEGDLKDLELQADSAIKGREEAIKQLRK 1649
Cdd:COG3883 93 RALYRSggsvsyldvllgsesfsdfldrLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1650 LQAQMKDFQRELEDARASRDEIFATAKENEKKAKSLEADLMQLQEDLAAAERARKQADLEKDELAEELASSVSGRNALQD 1729
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAA 252
|
250 260
....*....|....*....|....*
gi 156120901 1730 EKRRLEARIAQLEEELEEEQGNTEA 1754
Cdd:COG3883 253 GAAGAAAGSAGAAGAAAGAAGAGAA 277
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
999-1459 |
1.29e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 47.04 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 999 KERKLLEERISDLTTNLAEEEEKAKNLT-------KLKNKHESMISELEVRLKKEEKSRQELEKLKRKLDGEASDLHEQI 1071
Cdd:pfam05557 27 RARIELEKKASALKRQLDRESDRNQELQkrirlleKREAEAEEALREQAELNRLKKKYLEALNKKLNEKESQLADAREVI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1072 AELQAQIAELKMQLAKKEEELQAALGRLDDEMAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRDL------G 1145
Cdd:pfam05557 107 SCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIqsqeqdS 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1146 EELEALKTELEDTLDSTATQQELRAKREQEVTML--KKALDEETRSHESQVQEMRQKHTQVV------EELTEQLEQFKR 1217
Cdd:pfam05557 187 EIVKNSKSELARIPELEKELERLREHNKHLNENIenKLLLKEEVEDLKRKLEREEKYREEAAtlelekEKLEQELQSWVK 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1218 AKAN-----------------LDKNKQALEKENAELAGELRVLSQAKQEVEHKKKKLEVQLQELQSKYSDGEKVRAELND 1280
Cdd:pfam05557 267 LAQDtglnlrspedlsrrieqLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQR 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1281 KVHKLQNEVESVTGMLnEAEGKAIKLAKDVASLGSQLQDTQELLQEETRQKLNVSTKLRQLEDERNSLQEQ---LDEEME 1357
Cdd:pfam05557 347 RVLLLTKERDGYRAIL-ESYDKELTMSNYSPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQaqtLERELQ 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1358 AK--QNLERHISTLNIQLSDSKKKLQDFASTVELLEEGKKKFQKEIESLTQQ---------------------YEEKAAA 1414
Cdd:pfam05557 426 ALrqQESLADPSYSKEEVDSLRRKLETLELERQRLREQKNELEMELERRCLQgdydpkktkvlhlsmnpaaeaYQQRKNQ 505
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 156120901 1415 YDKLEKTKNRLQQELDDLVVDLDNQRQL-VSNLEKKQKKFDQLLAE 1459
Cdd:pfam05557 506 LEKLQAEIERLKRLLKKLEDDLEQVLRLpETTSTMNFKEVLDLRKE 551
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1278-1530 |
1.47e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 46.55 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1278 LNDKVHKLQNEVESVTGMLNEAEGKaIKLAKDvaslgsqLQDTQELLQEETRQKL-NVSTKLRQLEDERNSLQEQLDEEM 1356
Cdd:PHA02562 172 NKDKIRELNQQIQTLDMKIDHIQQQ-IKTYNK-------NIEEQRKKNGENIARKqNKYDELVEEAKTIKAEIEELTDEL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1357 EA----KQNLERHISTLNIQLSDSKKKLQDFASTVELLEEGKkkfqkEIESLTQQYEEKAAAYDKLEKTKNRLQQELDDL 1432
Cdd:PHA02562 244 LNlvmdIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEKGG-----VCPTCTQQISEGPDRITKIKDKLKELQHSLEKL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1433 VVDLDNQRQLVSNLEKKQKKFDQLLAEEKNIssKYADERDRAEAEAREKETKALSLARALEEALEakeelertnKMLKAE 1512
Cdd:PHA02562 319 DTAIDELEEIMDEFNEQSKKLLELKNKISTN--KQSLITLVDKAKKVKAAIEELQAEFVDNAEEL---------AKLQDE 387
|
250
....*....|....*...
gi 156120901 1513 MEDLVSSKDDVGKNVHEL 1530
Cdd:PHA02562 388 LDKIVKTKSELVKEKYHR 405
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1103-1267 |
1.60e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.30 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1103 MAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALKTELEDTLDS-------TATQQELRAKREQE 1175
Cdd:COG1579 2 MPEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEikrleleIEEVEARIKKYEEQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1176 VTMLKKALDEETRSHESQVQEMRQKHTQvvEELTEQLEQFKRAKANLDKNKQALEKENAELAGELRVLSQAKQEVEHKKK 1255
Cdd:COG1579 82 LGNVRNNKEYEALQKEIESLKRRISDLE--DEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELE 159
|
170
....*....|..
gi 156120901 1256 KLEVQLQELQSK 1267
Cdd:COG1579 160 ELEAEREELAAK 171
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1201-1441 |
1.67e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 46.61 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1201 HTQVVEELTEQLEQFKRAKANLDK---NKQALEKENAELAGELRVLSQAK-QEVEhkkkklEVQLQELQSKYSDGEKVRA 1276
Cdd:COG0497 153 LEELLEEYREAYRAWRALKKELEElraDEAERARELDLLRFQLEELEAAAlQPGE------EEELEEERRRLSNAEKLRE 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1277 ELNDKVHKLQNEVESVTGMLNEAegkaIKLAKDVASLGSQLQDTQELLQEetrqklnVSTKLRQLEDERNSLQEQLDEEM 1356
Cdd:COG0497 227 ALQEALEALSGGEGGALDLLGQA----LRALERLAEYDPSLAELAERLES-------ALIELEEAASELRRYLDSLEFDP 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1357 EAKQNLERHISTLNiQLsdsKKKlqdFASTVELLEEGKKKFQKEIESLTQQYEEKAAaydkLEKTKNRLQQELDDLVVDL 1436
Cdd:COG0497 296 ERLEEVEERLALLR-RL---ARK---YGVTVEELLAYAEELRAELAELENSDERLEE----LEAELAEAEAELLEAAEKL 364
|
....*
gi 156120901 1437 DNQRQ 1441
Cdd:COG0497 365 SAARK 369
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1074-1219 |
1.85e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 46.39 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1074 LQAQIAELKMQLAKKEEELQAALGRLDDEMAQKNNAL-KKIRELEGHISDLQEDLdseraarnkaekqkrdlgEELEALK 1152
Cdd:COG2433 382 LEELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLeEQVERLEAEVEELEAEL------------------EEKDERI 443
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156120901 1153 TELEDTLDSTATQQELRAKREQEVTmlkkALDEETRSHESQVQEMRQKhtqvVEELTEQLEQFKRAK 1219
Cdd:COG2433 444 ERLERELSEARSEERREIRKDREIS----RLDREIERLERELEEERER----IEELKRKLERLKELW 502
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1299-1489 |
1.87e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.98 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1299 AEGKAIKLAKDVASLGSQLQDTQELLQEETRQKLNVSTKLRQLEDERNSLQEQLD----EEMEAKQNLERHISTLNIQLS 1374
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDklqaEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1375 DSKKK---------------LQDFASTVELLEEGKKKFQKEIESLTQQYEEkaaaydkLEKTKNRLQQELDDLVVDLDNQ 1439
Cdd:COG3883 94 ALYRSggsvsyldvllgsesFSDFLDRLSALSKIADADADLLEELKADKAE-------LEAKKAELEAKLAELEALKAEL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 156120901 1440 RQLVSNLEKKQKKFDQLLAEEKNISSKYADERDRAEAEAREKETKALSLA 1489
Cdd:COG3883 167 EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
855-1218 |
1.93e-04 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 46.29 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 855 QAKEDELQKTKERQQKAESELKELEQKHSQLTEEKNLLQEQlqAETELYAEAEEMrvrlaaKKQELEEILHEMEARLEEE 934
Cdd:pfam09731 81 EPKEEKKQVKIPRQSGVSSEVAEEEKEATKDAAEAKAQLPK--SEQEKEKALEEV------LKEAISKAESATAVAKEAK 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 935 EDRSQQLQAERKKMAQQMLDLEEQLEEeeAARQKLQLEKVTAEAKIKKLEDDILVMDDQNNKLSKERKLLEERISDLTTN 1014
Cdd:pfam09731 153 DDAIQAVKAHTDSLKEASDTAEISREK--ATDSALQKAEALAEKLKEVINLAKQSEEEAAPPLLDAAPETPPKLPEHLDN 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1015 LAEEEEKAKNLTKLKNKHESMISElevrlkKEEKSRQELEK--------LKRKLDGEASDLHEQIAELQAQIAELKMQLA 1086
Cdd:pfam09731 231 VEEKVEKAQSLAKLVDQYKELVAS------ERIVFQQELVSifpdiipvLKEDNLLSNDDLNSLIAHAHREIDQLSKKLA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1087 --KKEEELQAALGRLDDEMAQKNNALKKIRELEGHISDLQEDLDSERAARNK--AEKQKRDLGEELEALKTELEDTLDST 1162
Cdd:pfam09731 305 elKKREEKHIERALEKQKEELDKLAEELSARLEEVRAADEAQLRLEFEREREeiRESYEEKLRTELERQAEAHEEHLKDV 384
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 156120901 1163 ATQQELRAKREQEvtmlkkaldeetRSHESQVQEMRQKHTQVVEELTEQLEQFKRA 1218
Cdd:pfam09731 385 LVEQEIELQREFL------------QDIKEKVEEERAGRLLKLNELLANLKGLEKA 428
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1589-1844 |
1.93e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 45.68 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1589 EKRRQLQRQLHEYETELEDERKQRALAVAAKKKL-EGDLKDLELQADSAIKGREEAIKQLRKLQAQMKDFQRELEDARAS 1667
Cdd:pfam00038 18 DKVRFLEQQNKLLETKISELRQKKGAEPSRLYSLyEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1668 RDEifatakenekkaksLEADLMQLQEDLAAAERARKQADLEKDELAEELASSvsgRNALQDEKRRLEARIAQLEEELEE 1747
Cdd:pfam00038 98 RTS--------------AENDLVGLRKDLDEATLARVDLEAKIESLKEELAFL---KKNHEEEVRELQAQVSDTQVNVEM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1748 EQGN----TEAMSE-------RVRKATQQAEQL-SNELATERSAAQKNENARQQLERQNKELRSKLQEMEGAVKSkFKST 1815
Cdd:pfam00038 161 DAARkldlTSALAEiraqyeeIAAKNREEAEEWyQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQS-LKKQ 239
|
250 260
....*....|....*....|....*....
gi 156120901 1816 IAALEAKIAQLEEQVEQEAREKQATAKAL 1844
Cdd:pfam00038 240 KASLERQLAETEERYELQLADYQELISEL 268
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1684-1840 |
2.01e-04 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 45.88 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1684 SLEADLMQLQEDLAAAERARKQAdlekDELAEELASSVSGRNALQDEKRRLEARIAQLEEELEEEQGNTEAMSERVRKAT 1763
Cdd:pfam00529 62 SAEAQLAKAQAQVARLQAELDRL----QALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPIGG 137
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156120901 1764 QQAEQlsneLATERSAAQKNENARQQLERQNKELRSKLQEMEGAVKSKFKSTIAALEAKIAQLEEQVEQEAREKQAT 1840
Cdd:pfam00529 138 ISRES----LVTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSGAQLQIAEAEAELKLAKLDLERT 210
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1533-1770 |
2.05e-04 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 45.52 E-value: 2.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1533 SKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALkvqferdlqarDEQNEEKRRQLQRQLHEYETELEDERkqr 1612
Cdd:pfam09787 41 SSTALTLELEELRQERDLLREEIQKLRGQIQQLRTELQEL-----------EAQQQEEAESSREQLQELEEQLATER--- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1613 alavAAKKKLEGDLKDLELQADSAikgREEAIKQLRKLQAQMKDFQRELEDARA---SRDEIFATAKENEKKAKSLEADL 1689
Cdd:pfam09787 107 ----SARREAEAELERLQEELRYL---EEELRRSKATLQSRIKDREAEIEKLRNqltSKSQSSSSQSELENRLHQLTETL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1690 MQLQEDLAA--AERARKQADLEKDELAEELASSVSGRN---ALQDEKRRLEARIAQLEEELEEEQGNTEAMSERVRKATQ 1764
Cdd:pfam09787 180 IQKQTMLEAlsTEKNSLVLQLERMEQQIKELQGEGSNGtsiNMEGISDGEGTRLRNVPGLFSESDSDRAGMYGKVRKAAS 259
|
....*.
gi 156120901 1765 QAEQLS 1770
Cdd:pfam09787 260 VIDKFS 265
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1602-1818 |
2.13e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.98 E-value: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1602 ETELEDERKQRALAVAAKKKLEGDLKDLELQADSAIKGREEAIKQLRKLQAQMKDFQRELEDARAS----RDEIFATAKE 1677
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEieerREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1678 NEKK------------AKSLEADLMQL----------QEDLAAAERARKQADLEKDELAEELASSVSGRNALQDEKRRLE 1735
Cdd:COG3883 95 LYRSggsvsyldvllgSESFSDFLDRLsalskiadadADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1736 ARIAQLEEELEEEQGNTEAMSERVRKATQQAEQLSNELATERSAAQKNENARQQLERQNKELRSKLQEMEGAVKSKFKST 1815
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGA 254
|
...
gi 156120901 1816 IAA 1818
Cdd:COG3883 255 AGA 257
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1703-1930 |
2.25e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.21 E-value: 2.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1703 RKQADLEKDELAEELASSVSGRNALQDEKRRLEA---RIAQLEEELEEEQGNTEAMSERVRKATQQAEQLSN---ELATE 1776
Cdd:PRK03918 171 IKEIKRRIERLEKFIKRTENIEELIKEKEKELEEvlrEINEISSELPELREELEKLEKEVKELEELKEEIEElekELESL 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1777 RSAAQKNENARQQLERQNKELRSKLQEMEGAVK---------------SKFKSTIAALEAKIAQLEEQVEQEAREKQATA 1841
Cdd:PRK03918 251 EGSKRKLEEKIRELEERIEELKKEIEELEEKVKelkelkekaeeyiklSEFYEEYLDELREIEKRLSRLEEEINGIEERI 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1842 KALKQKDKKLKEALLQVEDERKMAEQYKEQAEKGNlRVKQLKRQLEEAEEEsqRINANRRKLQRELDEATESNEAMGREV 1921
Cdd:PRK03918 331 KELEEKEERLEELKKKLKELEKRLEELEERHELYE-EAKAKKEELERLKKR--LTGLTPEKLEKELEELEKAKEEIEEEI 407
|
....*....
gi 156120901 1922 TALKSKLRR 1930
Cdd:PRK03918 408 SKITARIGE 416
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1697-1947 |
2.30e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.59 E-value: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1697 AAAERARKQADLEKDELAEELASSVSGRNALQDEKRRLEARIAQLEEELEEEQGNTEAMSERVRKATQQAEQLSNELATE 1776
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1777 RSAAQKNENARQQLER-----------QNKELRSKLQEMEGAVKSKFKSTIAALEAKIAQLEEQVEQEAREKQATAKALK 1845
Cdd:COG3883 92 ARALYRSGGSVSYLDVllgsesfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1846 QKDKKLKEALLQVEDERKMAEQYKEQAEKGNLRVKQLKRQLEEAEEESQRINANRRKLQRELDEATESNEAMGREVTALK 1925
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGA 251
|
250 260
....*....|....*....|..
gi 156120901 1926 SKLRRGNETSFVPTRRSGGRRV 1947
Cdd:COG3883 252 AGAAGAAAGSAGAAGAAAGAAG 273
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
851-1142 |
2.42e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 45.29 E-value: 2.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 851 EEEMQAKEDELQKTKERQQKAESELKELEQKHSQLTEEKNLLQEQLQAETELYAEAEEMRvrlaakKQELEEIlhemear 930
Cdd:COG1340 7 SSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKR------DELNEKV------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 931 leeeedrsQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDdiLVMDDQNNKLSKERkllEERISD 1010
Cdd:COG1340 74 --------KELKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIER--LEWRQQTEVLSPEE---EKELVE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1011 LTTNLAEEEEKAKNLTKLKNKhesmISELEVRLKKEEKSRQELEKLKRKLDGEASDLHEQIAELQAQIAELKMQLAKKEE 1090
Cdd:COG1340 141 KIKELEKELEKAKKALEKNEK----LKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHK 216
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 156120901 1091 ELQAALGRLDDEMAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKR 1142
Cdd:COG1340 217 EIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEK 268
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
978-1158 |
2.46e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 46.16 E-value: 2.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 978 AKIKKLEDDILVMDDQNNKLSKERKLLEERISDLTT----NLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKS---- 1049
Cdd:PHA02562 174 DKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKkngeNIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDiedp 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1050 -------RQELEKLKRKLDGEASDLH------------EQIAELQAQIAELK---MQLAKKEEELQAALGRLDDEMAQKN 1107
Cdd:PHA02562 254 saalnklNTAAAKIKSKIEQFQKVIKmyekggvcptctQQISEGPDRITKIKdklKELQHSLEKLDTAIDELEEIMDEFN 333
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 156120901 1108 NALKKIRELEGHISDLQEDLDSER-------AARNKAEKQKRDLGEELEALKTELEDT 1158
Cdd:PHA02562 334 EQSKKLLELKNKISTNKQSLITLVdkakkvkAAIEELQAEFVDNAEELAKLQDELDKI 391
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1446-1781 |
2.67e-04 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 45.44 E-value: 2.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1446 LEKKQKKFDQLLAEEKNISSKY-ADERDRAEAEAREKETKALSLARALEEALEAKEELERTnkmlkAEMEDLVSSKDDVG 1524
Cdd:pfam19220 57 LAQERAAYGKLRRELAGLTRRLsAAEGELEELVARLAKLEAALREAEAAKEELRIELRDKT-----AQAEALERQLAAET 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1525 KNVHELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKVQFER------DLQARDEQNEEKRRQLQRQL 1598
Cdd:pfam19220 132 EQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEqaaelaELTRRLAELETQLDATRARL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1599 HEYETELEDERKQRALAVAA-----------KKKLEGDLKDLELQADSAIKGREEAIKQLRKLQAQMKDFQRELEDARAS 1667
Cdd:pfam19220 212 RALEGQLAAEQAERERAEAQleeaveahraeRASLRMKLEALTARAAATEQLLAEARNQLRDRDEAIRAAERRLKEASIE 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1668 RDEIfatakenEKKAKSLEADLMQLQEDLAAAERARKQADLEKDELAEELASSVSGRNALQDEKRRLEARIAQLEEELEE 1747
Cdd:pfam19220 292 RDTL-------ERRLAGLEADLERRTQQFQEMQRARAELEERAEMLTKALAAKDAALERAEERIASLSDRIAELTKRFEV 364
|
330 340 350
....*....|....*....|....*....|....
gi 156120901 1748 EQGNTEAMSERVRkatqqaEQLSNELAtERSAAQ 1781
Cdd:pfam19220 365 ERAALEQANRRLK------EELQRERA-ERALAQ 391
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1088-1412 |
2.96e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 46.05 E-value: 2.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1088 KEEELQAALGRLDDEMAQKNNALKKIRELEGHISDlqedldseRAARNKAEKQKRDLGEELEALKTELEDTLDSTATQQE 1167
Cdd:PLN02939 71 ENGQLENTSLRTVMELPQKSTSSDDDHNRASMQRD--------EAIAAIDNEQQTNSKDGEQLSDFQLEDLVGMIQNAEK 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1168 ----LRAKREQEVTMLKKALDE-ETRSHESQVQEMRqkhtqvVEELTEQLEQFKRAKANLDKNKQALEKENAELAGELrv 1242
Cdd:PLN02939 143 nillLNQARLQALEDLEKILTEkEALQGKINILEMR------LSETDARIKLAAQEKIHVEILEEQLEKLRNELLIRG-- 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1243 lSQAKQEVEHKKKKLEVQLQELQSKYSDGEKVRAEL------NDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLGSQ 1316
Cdd:PLN02939 215 -ATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAELievaetEERVFKLEKERSLLDASLRELESKFIVAQEDVSKLSPL 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1317 LQDT--------QELLQEETRQKLNVSTKLRQ---LEDERNSLQEQLDEEMEAKQNLERhISTLNIQLSDSKKKLQ---- 1381
Cdd:PLN02939 294 QYDCwwekvenlQDLLDRATNQVEKAALVLDQnqdLRDKVDKLEASLKEANVSKFSSYK-VELLQQKLKLLEERLQasdh 372
|
330 340 350
....*....|....*....|....*....|.
gi 156120901 1382 DFASTVELLEEGKKKFQKEIESLTQQYEEKA 1412
Cdd:PLN02939 373 EIHSYIQLYQESIKEFQDTLSKLKEESKKRS 403
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
839-1379 |
3.01e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 45.97 E-value: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 839 TKVKPLLQVTRQEEEMQAKEDELQKTKERQQKAESELKELEQKHSQLTEEKNLLQEQLQAETELYAEAEEMRVRLAAKKQ 918
Cdd:pfam10174 259 LKTNGLLHTEDREEEIKQMEVYKSHSKFMKNKIDQLKQELSKKESELLALQTKLETLTNQNSDCKQHIEVLKESLTAKEQ 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 919 eleeilhemearleeeedRSQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDDILVMDDQNNKLS 998
Cdd:pfam10174 339 ------------------RAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQ 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 999 KERKLLEERISDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSrqeLEKLKRKLDGEASDLHEQIAELQAQI 1078
Cdd:pfam10174 401 KKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERI---IERLKEQREREDRERLEELESLKKEN 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1079 AELKMQLAKKEEELQaalgrlddemaqknnalkkirELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALKTE---L 1155
Cdd:pfam10174 478 KDLKEKVSALQPELT---------------------EKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEEcskL 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1156 EDTLdSTATQQELRAKREQEVTMLKKALDEETRSHesqvQEMRQKHTQVVEELTEQLEQFKRAKANLDKNKQALEKENAE 1235
Cdd:pfam10174 537 ENQL-KKAHNAEEAVRTNPEINDRIRLLEQEVARY----KEESGKAQAEVERLLGILREVENEKNDKDKKIAELESLTLR 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1236 LAGELRVLSQAKQEVEHKKKKLEVQLQElqskysDGEKVRAELNDKVHKLQnevesvtgmLNEAEGKAIKLAKDVASLGS 1315
Cdd:pfam10174 612 QMKEQNKKVANIKHGQQEMKKKGAQLLE------EARRREDNLADNSQQLQ---------LEELMGALEKTRQELDATKA 676
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1316 QLQDTQELLQEetrqklnvstKLRQLEDERNSLQEQLDEEMEAKQNL------ERHISTLNIQLSDSKKK 1379
Cdd:pfam10174 677 RLSSTQQSLAE----------KDGHLTNLRAERRKQLEEILEMKQEAllaaisEKDANIALLELSSSKKK 736
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1016-1382 |
3.14e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.28 E-value: 3.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1016 AEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKlkrkldgEASDLHEQIAELQAQIAELKMQLAKKEEELQAA 1095
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQE-------ELEQLREELEQAREELEQLEEELEQARSELEQL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1096 LGRLDDEMAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALKTELEDTLDSTATQQELRAKREQE 1175
Cdd:COG4372 79 EEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1176 VTMLKKALDEETRSHESQVQEMRQKHTQVVEELTEQLEQFKRAKANLDKNKQALEKENAELAGELRVLSQAKQEVEHKKK 1255
Cdd:COG4372 159 LESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSAL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1256 KLEVQLQELQSKYSDGEKVRAELNDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLGSQLQDTQELLQEETRQKLNVS 1335
Cdd:COG4372 239 LDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALL 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 156120901 1336 TKLRQLEDERNSLQEQLDEEMEAKQNLERHISTLNIQLSDSKKKLQD 1382
Cdd:COG4372 319 AALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEA 365
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
967-1519 |
3.24e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 46.20 E-value: 3.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 967 QKLQLEKVTAEAKIKKLEDdilVMDDQNNKLSKERKLLEERISDLTTNlaeEEEKAKNLTKLKNKHESMISelevrlKKE 1046
Cdd:TIGR01612 1229 EKIDEEKKKSEHMIKAMEA---YIEDLDEIKEKSPEIENEMGIEMDIK---AEMETFNISHDDDKDHHIIS------KKH 1296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1047 EKSRQELEKLKRKL---DGEASDLHEQIAELQAQIAELKmqlaKKEEELQAALGRLDD--EMAQKNNALKKIRELEGHIS 1121
Cdd:TIGR01612 1297 DENISDIREKSLKIiedFSEESDINDIKKELQKNLLDAQ----KHNSDINLYLNEIANiyNILKLNKIKKIIDEVKEYTK 1372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1122 DLQEDLDSERAARNKAEKQKRDLGEE--LEALKTELEDTLDSTATQQELRAKREQEVTMLKKALDEET-----RSHESQV 1194
Cdd:TIGR01612 1373 EIEENNKNIKDELDKSEKLIKKIKDDinLEECKSKIESTLDDKDIDECIKKIKELKNHILSEESNIDTyfknaDENNENV 1452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1195 Q------EMRQKHTQVV----------------EELTEQLEQFKRAKANLDKNKQALEKeNAELagelrvLSQAKQEVeh 1252
Cdd:TIGR01612 1453 LllfkniEMADNKSQHIlkikkdnatndhdfniNELKEHIDKSKGCKDEADKNAKAIEK-NKEL------FEQYKKDV-- 1523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1253 kkkklevqlQELQSKYSDgekvrAELNDKVHKLQNEVESVTGMLNEAEGKAIKLAkdvaslGSQLQDTQELLQEETRqkl 1332
Cdd:TIGR01612 1524 ---------TELLNKYSA-----LAIKNKFAKTKKDSEIIIKEIKDAHKKFILEA------EKSEQKIKEIKKEKFR--- 1580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1333 nvstklrqLEDERNSLQEQLDEEMEAKQNLErHISTLNIQLSDSKKKLQDFASTVELLEegkkkfqKEIESLTQQYEEKa 1412
Cdd:TIGR01612 1581 --------IEDDAAKNDKSNKAAIDIQLSLE-NFENKFLKISDIKKKINDCLKETESIE-------KKISSFSIDSQDT- 1643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1413 aaydKLEKTKNRLQQeLDDLVVDLDNQRQlvsNLEKKQKKFDQLLAEEKNISSKYADERDRAEAEAREKetkalslarAL 1492
Cdd:TIGR01612 1644 ----ELKENGDNLNS-LQEFLESLKDQKK---NIEDKKKELDELDSEIEKIEIDVDQHKKNYEIGIIEK---------IK 1706
|
570 580
....*....|....*....|....*..
gi 156120901 1493 EEALEAKEELERTNKMLKAEMEDLVSS 1519
Cdd:TIGR01612 1707 EIAIANKEEIESIKELIEPTIENLISS 1733
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1260-1482 |
3.30e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 45.45 E-value: 3.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1260 QLQELQSKYSDGEKvraelndKVHKLQNEVESVTGMLNEAEgkaiklaKDVASLGSQLQDTQELLQEETRQKLNVSTKLR 1339
Cdd:PRK11637 48 QLKSIQQDIAAKEK-------SVRQQQQQRASLLAQLKKQE-------EAISQASRKLRETQNTLNQLNKQIDELNASIA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1340 QLEDERN----SLQEQLD-----------------EEMEAKQNLERHISTLNIQLSDSKKKLQDFASTVEL---LEEGKK 1395
Cdd:PRK11637 114 KLEQQQAaqerLLAAQLDaafrqgehtglqlilsgEESQRGERILAYFGYLNQARQETIAELKQTREELAAqkaELEEKQ 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1396 KFQKEIesLTQQYEEKAaaydKLEKTKNRLQQELDdlvvdldnqrQLVSNLEKKQKKFDQLLAEEKNISSKYAD-ERD-- 1472
Cdd:PRK11637 194 SQQKTL--LYEQQAQQQ----KLEQARNERKKTLT----------GLESSLQKDQQQLSELRANESRLRDSIARaEREak 257
|
250
....*....|.
gi 156120901 1473 -RAEAEAREKE 1482
Cdd:PRK11637 258 aRAEREAREAA 268
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
850-1395 |
3.54e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 45.71 E-value: 3.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 850 QEEEMQAKEDELQKTKERQQKAESELKELEQKHSQ---LTEEKNLLQEQLQAETE-LYAEAEEMRVRLAAKKQELEEI-- 923
Cdd:COG3096 513 RLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQqldAAEELEELLAELEAQLEeLEEQAAEAVEQRSELRQQLEQLra 592
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 924 ----LHEMEARLEEEEDRSQQLQ-------AERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLE-------- 984
Cdd:COG3096 593 rikeLAARAPAWLAAQDALERLReqsgealADSQEVTAAMQQLLEREREATVERDELAARKQALESQIERLSqpggaedp 672
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 985 ------------------DDI------------------LVMDDqnnkLSKERKLLEERiSDLTTNL------------- 1015
Cdd:COG3096 673 rllalaerlggvllseiyDDVtledapyfsalygparhaIVVPD----LSAVKEQLAGL-EDCPEDLyliegdpdsfdds 747
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1016 ---AEEEEKAkNLTKLKNKH--ESMISELEV-----RLKKEEKSRQELEKLKRKLDGEASD------LHEQIAELQAQ-- 1077
Cdd:COG3096 748 vfdAEELEDA-VVVKLSDRQwrYSRFPEVPLfgraaREKRLEELRAERDELAEQYAKASFDvqklqrLHQAFSQFVGGhl 826
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1078 --------IAELKmQLAKKEEELQAALGRLDDEMAQKNNALKKIRE---------------LEGHISDLQEDLDSERAAR 1134
Cdd:COG3096 827 avafapdpEAELA-ALRQRRSELERELAQHRAQEQQLRQQLDQLKEqlqllnkllpqanllADETLADRLEELREELDAA 905
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1135 NKAEKQKRDLGEELEALKTELeDTLDSTATQQElrakreqevtmlkkALDEETRSHESQVQEMRQKhTQVVEELTEQLEQ 1214
Cdd:COG3096 906 QEAQAFIQQHGKALAQLEPLV-AVLQSDPEQFE--------------QLQADYLQAKEQQRRLKQQ-IFALSEVVQRRPH 969
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1215 FKRAKAnldknkQALEKENAELAGELRvlsQAKQEVEHKKKKLEVQLQELQSKYSDGEKVRAELnDKVHKLQNEvesvtg 1294
Cdd:COG3096 970 FSYEDA------VGLLGENSDLNEKLR---ARLEQAEEARREAREQLRQAQAQYSQYNQVLASL-KSSRDAKQQ------ 1033
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1295 MLNEAEgkaiklaKDVASLGSQLQDTQELLQEETRQKLNvsTKLRQLEDERNSLQEQLdeemeakQNLERHISTLNIQLs 1374
Cdd:COG3096 1034 TLQELE-------QELEELGVQADAEAEERARIRRDELH--EELSQNRSRRSQLEKQL-------TRCEAEMDSLQKRL- 1096
|
650 660
....*....|....*....|.
gi 156120901 1375 dsKKKLQDFASTVELLEEGKK 1395
Cdd:COG3096 1097 --RKAERDYKQEREQVVQAKA 1115
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
1658-1930 |
3.90e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 45.84 E-value: 3.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1658 QRELEDARASRDEIFATAKENEKKAKSLEADLMQLQEDlaaaERARkqaDLEKDELAEELASSVSGRNALQDEKRRLEAR 1737
Cdd:COG5022 799 LQPLLSLLGSRKEYRSYLACIIKLQKTIKREKKLRETE----EVEF---SLKAEVLIQKFGRSLKAKKRFSLLKKETIYL 871
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1738 IAQleeeleeeqgnteamsERVRKATQQAEQLSNELATERSAAQKNENARQQLERQNKELRSKLQEmegavKSKFKSTIA 1817
Cdd:COG5022 872 QSA----------------QRVELAERQLQELKIDVKSISSLKLVNLELESEIIELKKSLSSDLIE-----NLEFKTELI 930
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1818 ALEAKI---AQLEEQVEQEAREKQATAKaLKQKDKKLKEALLQVEDERKMAEQYKEQAEKGNLRVKQLKRQLEEAEEESQ 1894
Cdd:COG5022 931 ARLKKLlnnIDLEEGPSIEYVKLPELNK-LHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYG 1009
|
250 260 270
....*....|....*....|....*....|....*.
gi 156120901 1895 RINANRRKLQRELDEATESNEAMGREVTALKSKLRR 1930
Cdd:COG5022 1010 ALQESTKQLKELPVEVAELQSASKIISSESTELSIL 1045
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1280-1485 |
3.90e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.21 E-value: 3.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1280 DKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLGSQLQDTQELLQEETRQKLNVSTKLRQLEDERNSLQEQLDEEMEAK 1359
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1360 QNLERHISTLNIQLSDskKKLQDFASTVELLE----------EGKKKFQKEIESLTQQYEEKAAAYDKLEKTKNRLQQEL 1429
Cdd:COG3883 96 YRSGGSVSYLDVLLGS--ESFSDFLDRLSALSkiadadadllEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 156120901 1430 DDLVvdlDNQRQLVSNLEKKQKKFDQLLAEEKNISSKYADERDRAEAEAREKETKA 1485
Cdd:COG3883 174 EAQQ---AEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAA 226
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1579-1740 |
4.12e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.15 E-value: 4.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1579 DLQARD---EQNEEKRRQLQRQLHEYETELEDERKQRALAVAAKKKLEGDLKDLELQADSAikgrEEAIKQLRKLQAQ-- 1653
Cdd:COG1579 11 DLQELDselDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEV----EARIKKYEEQLGNvr 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1654 ----MKDFQRELEDARASRDEIFATAKENEKKAKSLEADLMQLQEDLAAAERARKQadlEKDELAEELAssvsgrnALQD 1729
Cdd:COG1579 87 nnkeYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEE---KKAELDEELA-------ELEA 156
|
170
....*....|.
gi 156120901 1730 EKRRLEARIAQ 1740
Cdd:COG1579 157 ELEELEAEREE 167
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1004-1136 |
4.15e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 44.96 E-value: 4.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1004 LEERISDLTTNLAEEEEKAKNLtklknkhESMISELEVRLKKEEKSRQELEKLKRKLDGEASDLHEQIAEL--------- 1074
Cdd:PRK09039 58 LNSQIAELADLLSLERQGNQDL-------QDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELaqeldsekq 130
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156120901 1075 -----QAQIAELKMQLAKKEEELQAALGRLDDemaqknnALKKIRELEGHISDLQEDLDSERAARNK 1136
Cdd:PRK09039 131 vsaraLAQVELLNQQIAALRRQLAALEAALDA-------SEKRDRESQAKIADLGRRLNVALAQRVQ 190
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1527-1928 |
4.20e-04 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 45.40 E-value: 4.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1527 VHELEKSKRAletqMEEMKTQLEELE-DELQATED---AKLRLEvnmqalkvqfERDLQARDEQNEEKRrqlqrqlheye 1602
Cdd:pfam05701 69 LEELESTKRL----IEELKLNLERAQtEEAQAKQDselAKLRVE----------EMEQGIADEASVAAK----------- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1603 TELEDERKQRALAVAAKKKLEGDLKDLELQADSAIKGREEAIKQLRKLQAQMKDFQRELEDARAsrdEIFATAKENEK-K 1681
Cdd:pfam05701 124 AQLEVAKARHAAAVAELKSVKEELESLRKEYASLVSERDIAIKRAEEAVSASKEIEKTVEELTI---ELIATKESLESaH 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1682 AKSLEAD------LMQLQEDLAAAERARKQADLEKDELAEELASSvsgrnalQDEKRRLEARIAQLEEEleeeqgNTEAM 1755
Cdd:pfam05701 201 AAHLEAEehrigaALAREQDKLNWEKELKQAEEELQRLNQQLLSA-------KDLKSKLETASALLLDL------KAELA 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1756 SERVRKATQQAEQLSNELATERSAAQKNENARQQLERQNKELrsklqemegavkSKFKSTIAALEAKIAQLEEQVEqeaR 1835
Cdd:pfam05701 268 AYMESKLKEEADGEGNEKKTSTSIQAALASAKKELEEVKANI------------EKAKDEVNCLRVAAASLRSELE---K 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1836 EKQATAkALKQKDKKLKEALLQVEDE----RKMAEQYKEQAEKGNLRVKQLKRQLEEAEEESQRINANRRKLQRELDEAT 1911
Cdd:pfam05701 333 EKAELA-SLRQREGMASIAVSSLEAElnrtKSEIALVQAKEKEAREKMVELPKQLQQAAQEAEEAKSLAQAAREELRKAK 411
|
410
....*....|....*..
gi 156120901 1912 ESNEAMGREVTALKSKL 1928
Cdd:pfam05701 412 EEAEQAKAAASTVESRL 428
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
858-1105 |
4.26e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 45.07 E-value: 4.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 858 EDELQKTKE---RQQKAESELKELEQKHSQLTEEKNLLQEQLQaetELYAeaeemrvrLAAKKQELEEilhemearleee 934
Cdd:COG0497 154 EELLEEYREayrAWRALKKELEELRADEAERARELDLLRFQLE---ELEA--------AALQPGEEEE------------ 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 935 edrsqqLQAERKKMAQqmldLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDDILVMDDQNNKLSKERKLLEE---RISDL 1011
Cdd:COG0497 211 ------LEEERRRLSN----AEKLREALQEALEALSGGEGGALDLLGQALRALERLAEYDPSLAELAERLESaliELEEA 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1012 TTN--------------LAEEEEKAKNLTKLKNKHESMISELevrLKKEEKSRQELEKLkrkldgeaSDLHEQIAELQAQ 1077
Cdd:COG0497 281 ASElrryldslefdperLEEVEERLALLRRLARKYGVTVEEL---LAYAEELRAELAEL--------ENSDERLEELEAE 349
|
250 260 270
....*....|....*....|....*....|..
gi 156120901 1078 IAELKMQLAKKEEEL----QAALGRLDDEMAQ 1105
Cdd:COG0497 350 LAEAEAELLEAAEKLsaarKKAAKKLEKAVTA 381
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
967-1175 |
4.89e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.82 E-value: 4.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 967 QKLQLEKVTAEAKIKKLEDDILVMDDQNNKLSKERKLLEERISDLTTNLAEEEEK-AKNLTKLKN------KHESMISEL 1039
Cdd:COG3883 26 SELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEiEERREELGEraralyRSGGSVSYL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1040 EVRLKKEEKSR--QELEKLKRKLDGEASDLhEQIAELQAQIAELKMQLAKKEEELQAALGRLDDEMAqknnalkkirELE 1117
Cdd:COG3883 106 DVLLGSESFSDflDRLSALSKIADADADLL-EELKADKAELEAKKAELEAKLAELEALKAELEAAKA----------ELE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 156120901 1118 GHISDLQEDLDSERAARNKAEKQKRDLGEELEALKTELEDTLDSTATQQELRAKREQE 1175
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1231-1595 |
5.02e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 45.11 E-value: 5.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1231 KENAELAGELRVLSQAKQEVEHKKKKLEVQLQELQSKYsDGEKVRAELNDKVHKL-------------QNEVESVTGMLN 1297
Cdd:pfam17380 259 RYNGQTMTENEFLNQLLHIVQHQKAVSERQQQEKFEKM-EQERLRQEKEEKAREVerrrkleeaekarQAEMDRQAAIYA 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1298 EAEGKAIKLAKDVA--SLGSQLQDTQELLQEETRQKLNVSTKLRQLEDERNSLQEQLDEEMEAKQNLErhistlnIQLSD 1375
Cdd:pfam17380 338 EQERMAMERERELEriRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVK-------ILEEE 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1376 SKKKLQDFASTVELL-EEGKKKFQKEIESLTqqyEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQlvSNLEKKQKKFD 1454
Cdd:pfam17380 411 RQRKIQQQKVEMEQIrAEQEEARQREVRRLE---EERAREMERVRLEEQERQQQVERLRQQEEERKR--KKLELEKEKRD 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1455 QLLAEEKNisskyadeRDRAEAEAREKETKALslaraleealeakeELERTNKMLKAEMEDLvsskddvGKNVHELEKSK 1534
Cdd:pfam17380 486 RKRAEEQR--------RKILEKELEERKQAMI--------------EEERKRKLLEKEMEER-------QKAIYEEERRR 536
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 156120901 1535 RAletqmEEMKTQLEELEDELQATEDAKLRLEVNMQALKVQFERDLQARDEQNEEKRRQLQ 1595
Cdd:pfam17380 537 EA-----EEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAEYE 592
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
992-1901 |
5.14e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 45.43 E-value: 5.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 992 DQNNKLSKERKLLEERISDLTTNLAEEEEKAKNLTKLKNKHESMI---------SELEVRLKKEEKSRQELEKLKRKLDG 1062
Cdd:TIGR01612 486 DENSKQDNTVKLILMRMKDFKDIIDFMELYKPDEVPSKNIIGFDIdqnikaklyKEIEAGLKESYELAKNWKKLIHEIKK 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1063 EASDLHEQIAELQAQIAELKMQLAKKEEE------LQAALGRLDDEMAQKNNALKKIRELE-------GHISDLQ----- 1124
Cdd:TIGR01612 566 ELEEENEDSIHLEKEIKDLFDKYLEIDDEiiyinkLKLELKEKIKNISDKNEYIKKAIDLKkiiennnAYIDELAkispy 645
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1125 ---EDLDSERAARNKAEKQKRDLGE-ELEALKTEL-----EDTLDST---ATQQELRAKREQEVTMLKKALDEETRSHES 1192
Cdd:TIGR01612 646 qvpEHLKNKDKIYSTIKSELSKIYEdDIDALYNELssivkENAIDNTedkAKLDDLKSKIDKEYDKIQNMETATVELHLS 725
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1193 QVQEMRQK------------HTQVVEELTEQLEQFKRAKANLDKNKQALEKENAELAGELRVLSQ--------------- 1245
Cdd:TIGR01612 726 NIENKKNElldiiveikkhiHGEINKDLNKILEDFKNKEKELSNKINDYAKEKDELNKYKSKISEiknhyndqinidnik 805
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1246 ---AKQEVEHKK---KKLEVQLQELQSKYSDGEKVRAELNDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLGS--QL 1317
Cdd:TIGR01612 806 dedAKQNYDKSKeyiKTISIKEDEIFKIINEMKFMKDDFLNKVDKFINFENNCKEKIDSEHEQFAELTNKIKAEISddKL 885
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1318 QDTQELLQeETRQKLNVSTKLRQLEDERNSLQEQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFASTVELLEEGKKKF 1397
Cdd:TIGR01612 886 NDYEKKFN-DSKSLINEINKSIEEEYQNINTLKKVDEYIKICENTKESIEKFHNKQNILKEILNKNIDTIKESNLIEKSY 964
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1398 QKEIE-SLTQQYEE-----KAAAYDKLEKTKNRLQQELDDLVVDL------------DNQRQLVSNLEKKQKKFDQ---- 1455
Cdd:TIGR01612 965 KDKFDnTLIDKINEldkafKDASLNDYEAKNNELIKYFNDLKANLgknkenmlyhqfDEKEKATNDIEQKIEDANKnipn 1044
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1456 ----------LLAEE------KNISSKYADERDRAEAEAREKETKALSLARALEEALEAKEELERTNKMLKAEmEDLVSS 1519
Cdd:TIGR01612 1045 ieiaihtsiyNIIDEiekeigKNIELLNKEILEEAEINITNFNEIKEKLKHYNFDDFGKEENIKYADEINKIK-DDIKNL 1123
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1520 KDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQAT---EDAKlRLEVNMQALKVQFERDLQARDEQNeekrrQLQR 1596
Cdd:TIGR01612 1124 DQKIDHHIKALEEIKKKSENYIDEIKAQINDLEDVADKAisnDDPE-EIEKKIENIVTKIDKKKNIYDEIK-----KLLN 1197
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1597 QLHEYETELEDERKQRALAVAAKKKLEG----DLKDLELQADSAIKGREEAIKQLRKLQAQMKDFQRELEDARASRDEIF 1672
Cdd:TIGR01612 1198 EIAEIEKDKTSLEEVKGINLSYGKNLGKlfleKIDEEKKKSEHMIKAMEAYIEDLDEIKEKSPEIENEMGIEMDIKAEME 1277
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1673 ATAKENEKKAKsleadlmqlqEDLAAAERARKQADLEKDELaeELASSVSGRNALQDEKRRLEARIAQleeeleeEQGNT 1752
Cdd:TIGR01612 1278 TFNISHDDDKD----------HHIISKKHDENISDIREKSL--KIIEDFSEESDINDIKKELQKNLLD-------AQKHN 1338
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1753 EAMSERVRKATQQAEQLsnELATERSAAQKNENARQQLERQNKELRSKLQEMEGAVKsKFKSTIAALEAKiAQLEEQVEq 1832
Cdd:TIGR01612 1339 SDINLYLNEIANIYNIL--KLNKIKKIIDEVKEYTKEIEENNKNIKDELDKSEKLIK-KIKDDINLEECK-SKIESTLD- 1413
|
970 980 990 1000 1010 1020
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 156120901 1833 earekqatAKALKQKDKKLKEALLQVEDERKMAEQYKEQAEKGNLRVKQLKRQLEEAEEESQRINANRR 1901
Cdd:TIGR01612 1414 --------DKDIDECIKKIKELKNHILSEESNIDTYFKNADENNENVLLLFKNIEMADNKSQHILKIKK 1474
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
850-1114 |
5.55e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.01 E-value: 5.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 850 QEEEMQAKEDELQKT----KERQQKAESELKELEQKHSQLTEEKNL--LQEQLQAETELYAEAEEMRVRLAAKKQELEEi 923
Cdd:COG3206 162 LEQNLELRREEARKAleflEEQLPELRKELEEAEAALEEFRQKNGLvdLSEEAKLLLQQLSELESQLAEARAELAEAEA- 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 924 lhemearleeeedRSQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDDILVMDdqnnklskerkl 1003
Cdd:COG3206 241 -------------RLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIA------------ 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1004 LEERISDLTTNLAEEEEKAKNLTKlknkhesmiSELEVRLKKEEKSRQELEKLKRKLDgeasdlheQIAELQAQIAELKM 1083
Cdd:COG3206 296 LRAQIAALRAQLQQEAQRILASLE---------AELEALQAREASLQAQLAQLEARLA--------ELPELEAELRRLER 358
|
250 260 270
....*....|....*....|....*....|.
gi 156120901 1084 QLAKKEEELQAALGRLDDEMAQKNNALKKIR 1114
Cdd:COG3206 359 EVEVARELYESLLQRLEEARLAEALTVGNVR 389
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1081-1235 |
5.88e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 44.19 E-value: 5.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1081 LKMQLAKKEEELQaalgRLDDEMAQKNNALKkireLE-GHISDLQEDLDSERAARNKAEkqkrdlgeeleALKTELEDTL 1159
Cdd:PRK09039 44 LSREISGKDSALD----RLNSQIAELADLLS----LErQGNQDLQDSVANLRASLSAAE-----------AERSRLQALL 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156120901 1160 DSTATQQELRAKREQEvtmLKKALDEE-TRSHESQVQemrqkhtqvVEELTEQLEQFKRAKANLDKNKQALEKENAE 1235
Cdd:PRK09039 105 AELAGAGAAAEGRAGE---LAQELDSEkQVSARALAQ---------VELLNQQIAALRRQLAALEAALDASEKRDRE 169
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1706-1874 |
5.92e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 43.76 E-value: 5.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1706 ADLEKDELAEELASSVSGRNALQDEKRRLEARIAQLEEELEEEQGNTEAMSERVRKATQQAEQLSNELATERSAAQKNEn 1785
Cdd:COG1579 1 AMPEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYE- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1786 ARQQLERQNKELRSKLQEMEGAvkskfKSTIAALEAKIAQLEEQVEQEAREKQATAKALKQKDKKLKEALLQVEDERKMA 1865
Cdd:COG1579 80 EQLGNVRNNKEYEALQKEIESL-----KRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAEL 154
|
....*....
gi 156120901 1866 EQYKEQAEK 1874
Cdd:COG1579 155 EAELEELEA 163
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
1129-1362 |
6.22e-04 |
|
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 trasnmembrane helices, followed by a C-terminal coiled-coil region. Macoilin is a highly conserved protein present in eukaryotes. Macoilin appears to be found in the ER and be involved in the function of neurons.
Pssm-ID: 462859 [Multi-domain] Cd Length: 670 Bit Score: 44.84 E-value: 6.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1129 SERAARNKAEKQKRDLGEELEALKTELEDTLDSTATQQELRAKR-EQEVTMLKKALdeetrshesqvqemrQKHTQVVEE 1207
Cdd:pfam09726 356 TSSSSSKNSKKQKGPGGKSGARHKDPAENCIPNNQLSKPDALVRlEQDIKKLKAEL---------------QASRQTEQE 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1208 LTEQLEQFKRAKANLDKNKQALEKENAELAGELRVLSQAKQEVEHKKKKLEVQLQELQSKYSDGEKVRAE---------- 1277
Cdd:pfam09726 421 LRSQISSLTSLERSLKSELGQLRQENDLLQTKLHNAVSAKQKDKQTVQQLEKRLKAEQEARASAEKQLAEekkrkkeeea 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1278 -------------------LNDKVHKLQNEVESVTG--MLNEAEGKAIKL-----------AKDVASLGSQLQDTQEL-- 1323
Cdd:pfam09726 501 taaravalaaasrgectesLKQRKRELESEIKKLTHdiKLKEEQIRELEIkvqelrkykesEKDTEVLMSALSAMQDKnq 580
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 156120901 1324 -----LQEETRQKLNVSTKL----RQLEDERNSLQEQLDEEMEAKQNL 1362
Cdd:pfam09726 581 hlensLSAETRIKLDLFSALgdakRQLEIAQGQIYQKDQEIKDLKQKI 628
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1319-1933 |
6.32e-04 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 44.74 E-value: 6.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1319 DTQELLQEETRQKLNVSTKLRQLedernslQEQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFASTVELLEEGKKKFQ 1398
Cdd:pfam07111 42 DGQGPGRRGRSLELEGSQALSQQ-------AELISRQLQELRRLEEEVRLLRETSLQQKMRLEAQAMELDALAVAEKAGQ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1399 KEIESLTQQYEEKAAAYDKLEKTKNRLQQELDDLvvdldNQRQLVSNLEKKQKKFDQLLAEEKNISSKYADERDRAEAEA 1478
Cdd:pfam07111 115 AEAEGLRAALAGAEMVRKNLEEGSQRELEEIQRL-----HQEQLSSLTQAHEEALSSLTSKAEGLEKSLNSLETKRAGEA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1479 REketkalsLARALEEALEAKEELERTNKMLKAEMEDLVSSKDDVGKNVHElekskralETQMEEMKTQLEELEDELQAT 1558
Cdd:pfam07111 190 KQ-------LAEAQKEAELLRKQLSKTQEELEAQVTLVESLRKYVGEQVPP--------EVHSQTWELERQELLDTMQHL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1559 EDAKLRLEVNMQALKVQFERDLQARDEQNEEKRRQLQRQlheYETELEDERKQRALAVAAKKK---LEGDLKDLELQADS 1635
Cdd:pfam07111 255 QEDRADLQATVELLQVRVQSLTHMLALQEEELTRKIQPS---DSLEPEFPKKCRSLLNRWREKvfaLMVQLKAQDLEHRD 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1636 AIKGREEAIKQLR-KLQAQMKD---FQRELEDarasrdeifatakenekKAKSLEADLMQ---LQEDLAAAERARKQADL 1708
Cdd:pfam07111 332 SVKQLRGQVAELQeQVTSQSQEqaiLQRALQD-----------------KAAEVEVERMSakgLQMELSRAQEARRRQQQ 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1709 EKDELAEELASSVSGRNALQDEKRRLEARIAQLEeeleeeqGNTEAMSERVRKATQQAEQLSNELATERSAAQknenarq 1788
Cdd:pfam07111 395 QTASAEEQLKFVVNAMSSTQIWLETTMTRVEQAV-------ARIPSLSNRLSYAVRKVHTIKGLMARKVALAQ------- 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1789 qlerqnkelrskLQEMEGAVKSKFKSTIAALEAKIAQLEEQVEQEAREKQATAKALKQKdkklkeallqvederkmAEQY 1868
Cdd:pfam07111 461 ------------LRQESCPPPPPAPPVDADLSLELEQLREERNRLDAELQLSAHLIQQE-----------------VGRA 511
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 156120901 1869 KEQAEKGNLRVKQLKRQLEEAEEESQRINANrrkLQRELDEATESNEAMGREVTALKSKLRRGNE 1933
Cdd:pfam07111 512 REQGEAERQQLSEVAQQLEQELQRAQESLAS---VGQQLEVARQGQQESTEEAASLRQELTQQQE 573
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1523-1688 |
6.49e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.38 E-value: 6.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1523 VGKNVHELEKSKRALETQmEEMKTQLEELEDELQATEDAKLrLEVN--MQALKVQFERDLQARDEQNEEKRRQLQRQLHE 1600
Cdd:PRK12704 20 IGYFVRKKIAEAKIKEAE-EEAKRILEEAKKEAEAIKKEAL-LEAKeeIHKLRNEFEKELRERRNELQKLEKRLLQKEEN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1601 YETELEDERKQRALAVAAKKKLEGDLKDLELQADSAIKGREEAIKQLRKLQAQMKDFQRE--LEDARA-SRDEIFATAKE 1677
Cdd:PRK12704 98 LDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEEAKEilLEKVEEeARHEAAVLIKE 177
|
170
....*....|.
gi 156120901 1678 NEKKAKsLEAD 1688
Cdd:PRK12704 178 IEEEAK-EEAD 187
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1597-1841 |
6.51e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 6.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1597 QLHEYETELEDERKQRALAVAAKKKLEGDLKDLELQADSAIKGREEAIKQLRKLQAQMKDFQRELEDARASRDEIFATAK 1676
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1677 ENEKKAKSLEADLMQ--LQEDLAAAERARKQADLEKDELaeelassvsgrNALQDEKRRLEARIAQLEEELEEEQGNTEA 1754
Cdd:COG3883 97 RSGGSVSYLDVLLGSesFSDFLDRLSALSKIADADADLL-----------EELKADKAELEAKKAELEAKLAELEALKAE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1755 MSERVRKATQQAEQLSNELATERSAAQKNENARQQLERQNKELRSKLQEMEGAVKSKFKSTIAALEAKIAQLEEQVEQEA 1834
Cdd:COG3883 166 LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAS 245
|
....*..
gi 156120901 1835 REKQATA 1841
Cdd:COG3883 246 AAGAGAA 252
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1389-1928 |
6.71e-04 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 44.63 E-value: 6.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1389 LLEEGKKKFQKEIESLTQQYEE----KAAAYDKLEKTKNrlqqELDDLVVDLDNqrqlvSNLEKKQKKFDQLLAE----- 1459
Cdd:pfam05701 39 LVELELEKVQEEIPEYKKQSEAaeaaKAQVLEELESTKR----LIEELKLNLER-----AQTEEAQAKQDSELAKlrvee 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1460 -EKNISSkyaDERDRAEAE---AREKETKALSLARALEEALeakeelertnKMLKAEMEDLVSSKDDVGKNVHELEKSKR 1535
Cdd:pfam05701 110 mEQGIAD---EASVAAKAQlevAKARHAAAVAELKSVKEEL----------ESLRKEYASLVSERDIAIKRAEEAVSASK 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1536 ALETQMEEMKTQLEELEDELQATEDAklRLEVNMQALKVQFERdlqardeqnEEKRRQLQRQLHEYETELEDERKQRALA 1615
Cdd:pfam05701 177 EIEKTVEELTIELIATKESLESAHAA--HLEAEEHRIGAALAR---------EQDKLNWEKELKQAEEELQRLNQQLLSA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1616 VAAKKKLEG------DLKDlELQADSAIKGREEAIKQL------RKLQAQMKDFQRELEDARASRDEIFATAKENEKKAK 1683
Cdd:pfam05701 246 KDLKSKLETasalllDLKA-ELAAYMESKLKEEADGEGnekktsTSIQAALASAKKELEEVKANIEKAKDEVNCLRVAAA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1684 SLEADL---------MQLQEDLAAAERARKQADLEKdeLAEELASSVSGRNALQDEKRRLEARIAQLEEELEEEQGNTEA 1754
Cdd:pfam05701 325 SLRSELekekaelasLRQREGMASIAVSSLEAELNR--TKSEIALVQAKEKEAREKMVELPKQLQQAAQEAEEAKSLAQA 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1755 MSERVRKATQQAEQLSNELATERSaaqknenarqqlerqnkELRSKLQEMEgAVKSKFKSTIAALEAkiaqLEEQveqea 1834
Cdd:pfam05701 403 AREELRKAKEEAEQAKAAASTVES-----------------RLEAVLKEIE-AAKASEKLALAAIKA----LQES----- 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1835 rekQATAKALKQKDKKlKEALLQVEDERKMAEQYKEQAEKGNLRVKQLKRQLEEAEEESQRINANRRKLQRELDEATES- 1913
Cdd:pfam05701 456 ---ESSAESTNQEDSP-RGVTLSLEEYYELSKRAHEAEELANKRVAEAVSQIEEAKESELRSLEKLEEVNREMEERKEAl 531
|
570
....*....|....*
gi 156120901 1914 NEAMGREVTALKSKL 1928
Cdd:pfam05701 532 KIALEKAEKAKEGKL 546
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
846-1136 |
7.34e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.12 E-value: 7.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 846 QVTRQEEEMQAKEDELQKTKERQQKAESELKELEQKHSQLTEEKNLLQEQLQAETELYAEAEEMRVRLAAKKQELEEILH 925
Cdd:COG4372 53 ELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRK 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 926 EMEARLEEEEDRSQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDDILVMDDQNNKLSKERKLLE 1005
Cdd:COG4372 133 QLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESL 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1006 ERISDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLDGEASDLHEQIAELQAQIAELKMQL 1085
Cdd:COG4372 213 PRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAA 292
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 156120901 1086 AKKEEELQAALGRLDDEMAQKNNALKKIRELEGHISDLQEDLDSERAARNK 1136
Cdd:COG4372 293 LELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLL 343
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1413-1640 |
7.44e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 44.62 E-value: 7.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1413 AAYDKLEKTKNR-LQQELDDLVVDLDN-------QRQLVSNLEK--------KQKKFDQLLAEEKNISSKYADERDRAEA 1476
Cdd:PHA02562 166 SEMDKLNKDKIReLNQQIQTLDMKIDHiqqqiktYNKNIEEQRKkngeniarKQNKYDELVEEAKTIKAEIEELTDELLN 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1477 EAREKETKALSLARALEEALEAKEELERTNKMLK---------AEMEDLVSSKDDVGK---NVHELEKSKRALETQMEEm 1544
Cdd:PHA02562 246 LVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKmyekggvcpTCTQQISEGPDRITKikdKLKELQHSLEKLDTAIDE- 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1545 ktqLEELEDELQATEDAKLRLEVNMQALKVQFER-DLQARDEQNEEKRRQLQRQLHEYETELEDERKQRALAVAAKKKLE 1623
Cdd:PHA02562 325 ---LEEIMDEFNEQSKKLLELKNKISTNKQSLITlVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKE 401
|
250
....*....|....*....
gi 156120901 1624 GDLKDL--ELQADSAIKGR 1640
Cdd:PHA02562 402 KYHRGIvtDLLKDSGIKAS 420
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1336-1484 |
7.83e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 43.37 E-value: 7.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1336 TKLRQLEDERNSLQEQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFASTVELLEEGKKKFQ---------KEIESLTQ 1406
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEeqlgnvrnnKEYEALQK 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 156120901 1407 QYEEKAAAYDKLEKTKNRLQQELDDLVVDLDnqrQLVSNLEKKQKKFDQLLAEEKNISSKYADERDRAEAEAREKETK 1484
Cdd:COG1579 97 EIESLKRRISDLEDEILELMERIEELEEELA---ELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1601-1740 |
8.10e-04 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 43.95 E-value: 8.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1601 YETELEDERKQRALAVAAKKKLEGDLKDLE-LQADSAI--KGREEAIKQLRKLQAQMKDFQRELEDARASRDEIFATAKE 1677
Cdd:pfam00529 56 YQAALDSAEAQLAKAQAQVARLQAELDRLQaLESELAIsrQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPI 135
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156120901 1678 N---EKKAKSLEADLMQLQEDLAAAERARKQADLEKDELAEELASSV-SGRNALQDEKRRLEARIAQ 1740
Cdd:pfam00529 136 GgisRESLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVrSELSGAQLQIAEAEAELKL 202
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1505-1650 |
9.14e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.08 E-value: 9.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1505 TNKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEvnmqaLKVQFERDLQARD 1584
Cdd:COG2433 386 IEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLE-----RELSEARSEERRE 460
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156120901 1585 EQNEEKRRQLQRQLHEYETELEDERKQRalavaakKKLEGDLKDLELQADSAIKGREEAIKQLRKL 1650
Cdd:COG2433 461 IRKDREISRLDREIERLERELEEERERI-------EELKRKLERLKELWKLEHSGELVPVKVVEKF 519
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1585-1901 |
9.20e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.74 E-value: 9.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1585 EQNEEKRRQLQRQLHEYETELEDERKQRALAVAAKKKLEGDLKDLELQADSAIKGREEAIKQLRKLQAQMKDFQRELEDA 1664
Cdd:COG4372 34 RKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEEL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1665 RASRDEIFATAKENEKKAKSLEADLMQLQEDLAAAERARKQADLEKDELAEELASSVSGRNALQDEK--RRLEARIAQLE 1742
Cdd:COG4372 114 QEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEaeQALDELLKEAN 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1743 EELEEEQGNTEAMSERVRKATQQAEQLSNELATERSAAQKNENARQQLERQNKELRSKLQEMEGAVKSKFKSTIAALEAK 1822
Cdd:COG4372 194 RNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDT 273
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 156120901 1823 IAQLEEQVEQEAREKQATAKALKQKDKKLKEALLQVEDERKMAEQYKEQAEKGNLRVKQLKRQLEEAEEESQRINANRR 1901
Cdd:COG4372 274 EEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLD 352
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
846-1080 |
1.04e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.24 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 846 QVTRQEEEMQAKEDELQKTKERQQ--KAESELKELEQKHSQLTEEKNLLQEQLQaetELYAEAEEMRVRLAAKKQELEEI 923
Cdd:COG3206 183 QLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEARAELA---EAEARLAALRAQLGSGPDALPEL 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 924 LhemearleeEEDRSQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDDILVmddqnnKLSKERKL 1003
Cdd:COG3206 260 L---------QSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILA------SLEAELEA 324
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156120901 1004 LEERISDLTTNLAEEEEKAKNLTKLKNKHESMISELEVrlkkeekSRQELEKLKRKLdgEASDLHEQIAELQAQIAE 1080
Cdd:COG3206 325 LQAREASLQAQLAQLEARLAELPELEAELRRLEREVEV-------ARELYESLLQRL--EEARLAEALTVGNVRVID 392
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
997-1122 |
1.07e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 43.42 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 997 LSKERKL-LEERISDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLDGEASDLHEQIAELQ 1075
Cdd:PRK09039 71 LERQGNQdLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDSEKQVSARALAQVELLNQQIAALR 150
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 156120901 1076 AQIAELKMQLAKKEEELQAALGRLDDEMAQKNNAL-KKIRELEGHISD 1122
Cdd:PRK09039 151 RQLAALEAALDASEKRDRESQAKIADLGRRLNVALaQRVQELNRYRSE 198
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1712-1826 |
1.11e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 43.42 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1712 ELAEELASSVSGRNALQDEKRRLEARIAQLEEELEEEQGNTEAMSERVRKATQQAEQLSNELATERsaaQKNENARQQLE 1791
Cdd:PRK09039 64 ELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDSEK---QVSARALAQVE 140
|
90 100 110
....*....|....*....|....*....|....*...
gi 156120901 1792 RQNKE---LRSKLQEMEGAVKSkFKSTIAALEAKIAQL 1826
Cdd:PRK09039 141 LLNQQiaaLRRQLAALEAALDA-SEKRDRESQAKIADL 177
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1415-1859 |
1.13e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 43.74 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1415 YDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQKKFDQLLAEEKNISSKYADERDRAEAEAREKETKALSLARALEE 1494
Cdd:COG5278 81 YEEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1495 ALEAKEELERTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKV 1574
Cdd:COG5278 161 LALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALAL 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1575 QFERDLQARDEQNEEKRRQLQRQLHEYETELEDERKQRALAVAAKKKLEGDLKDLELQADSAIKGREEAIKQLRKLQAQM 1654
Cdd:COG5278 241 ALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAA 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1655 KDFQRELEDARASRDEIFATAKENEKKAKSLEADLMQLQEDLAAAERARKQADLEKDELAEELASSVSGRNALQDEKRRL 1734
Cdd:COG5278 321 AAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAA 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1735 EARIAQLEEELEEEQGNTEAMSERVRKATQQAEQLSNELATERSAAQKNENARQQLERQNKELRSKLQEMEGAVKSKFKS 1814
Cdd:COG5278 401 AAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAA 480
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 156120901 1815 TIAALEAKIAQLEEQVEQEAREKQATAKALKQKDKKLKEALLQVE 1859
Cdd:COG5278 481 AAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAAL 525
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1016-1693 |
1.31e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 43.66 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1016 AEEEEKAKNLTKLKNKHESMISELEVRLK----KEEKSRQELEKLK-----RKLDGEASDLHEQIAELQAQIAELKMQLA 1086
Cdd:pfam10174 123 SEHERQAKELFLLRKTLEEMELRIETQKQtlgaRDESIKKLLEMLQskglpKKSGEEDWERTRRIAEAEMQLGHLEVLLD 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1087 KKEEELQAalgrLDDEMAQKNNALKKIREleghISDLQEDLDSERAARNKAEKQKRDLGEELEALKTELEdtldstatqq 1166
Cdd:pfam10174 203 QKEKENIH----LREELHRRNQLQPDPAK----TKALQTVIEMKDTKISSLERNIRDLEDEVQMLKTNGL---------- 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1167 elrakreqevtmlkkaLDEETRSHESQVQEMRQKHTQVVEELTEQLeqfkrakanldknKQALEKENAELAGELRVLSQA 1246
Cdd:pfam10174 265 ----------------LHTEDREEEIKQMEVYKSHSKFMKNKIDQL-------------KQELSKKESELLALQTKLETL 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1247 KQEVEHKKKKLEVQLQELQSKysdgEKVRAELNDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLGSQLQDTQELLQE 1326
Cdd:pfam10174 316 TNQNSDCKQHIEVLKESLTAK----EQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDV 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1327 ETRQKLNVSTKLRQLEDERNSLQEQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFASTVELLEEGK----KKFQKEIE 1402
Cdd:pfam10174 392 KERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQReredRERLEELE 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1403 SLTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQKKFDQLLAEEKNISSKYADERDRAEAEAREKE 1482
Cdd:pfam10174 472 SLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVR 551
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1483 TKALSLARALEEALEAKEELERTNKMlKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQleeledelQATEDAK 1562
Cdd:pfam10174 552 TNPEINDRIRLLEQEVARYKEESGKA-QAEVERLLGILREVENEKNDKDKKIAELESLTLRQMKE--------QNKKVAN 622
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1563 LRLeVNMQALKVQFERDLQARDEQNEEKRRQLQRQLHEYETELEderKQRALAVAAKKKLEGDLKDLELQADSAIKGREE 1642
Cdd:pfam10174 623 IKH-GQQEMKKKGAQLLEEARRREDNLADNSQQLQLEELMGALE---KTRQELDATKARLSSTQQSLAEKDGHLTNLRAE 698
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 156120901 1643 AIKQLRKLqAQMKdfQRELEDARASRDEIFATAKENEKKAKSLEADLMQLQ 1693
Cdd:pfam10174 699 RRKQLEEI-LEMK--QEALLAAISEKDANIALLELSSSKKKKTQEEVMALK 746
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1529-1649 |
1.31e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.60 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1529 ELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKVQFERD---------------LQARDEQNEEKRRQ 1593
Cdd:COG1579 28 ELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYeeqlgnvrnnkeyeaLQKEIESLKRRISD 107
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 156120901 1594 LQRQLHEYETELEDERKQRALAVAAKKKLEGDLKDLELQADSAIKGREEAIKQLRK 1649
Cdd:COG1579 108 LEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEA 163
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1216-1396 |
1.38e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 43.66 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1216 KRAKANLDKNKQALEKENAELAGELRVLSQAKQEVEHKKKKLEVQLQELQSKYsdgEKVRAELNDKVHKLQNEVEsvtgm 1295
Cdd:PRK00409 505 EEAKKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKK---EKLQEEEDKLLEEAEKEAQ----- 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1296 lneaegKAIKLAKDVASlgSQLQDTQELLQEETRqklnvSTKLRQLEDERNSLQEQLdEEMEAKQNLERHISTlNIQLSD 1375
Cdd:PRK00409 577 ------QAIKEAKKEAD--EIIKELRQLQKGGYA-----SVKAHELIEARKRLNKAN-EKKEKKKKKQKEKQE-ELKVGD 641
|
170 180
....*....|....*....|.
gi 156120901 1376 sKKKLQDFASTVELLEEGKKK 1396
Cdd:PRK00409 642 -EVKYLSLGQKGEVLSIPDDK 661
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
939-1110 |
1.48e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.22 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 939 QQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDDIlvmddQNNKLSKERKLLEERISDLTTNLAEE 1018
Cdd:COG1579 34 AELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQL-----GNVRNNKEYEALQKEIESLKRRISDL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1019 EEKAKNLTKLKNKHESMISELEvrlkkeeksrQELEKLKRKLDGEASDLHEQIAELQAQIAELKMQLAKKEEELQAALGR 1098
Cdd:COG1579 109 EDEILELMERIEELEEELAELE----------AELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPPELLA 178
|
170
....*....|..
gi 156120901 1099 LDDEMAQKNNAL 1110
Cdd:COG1579 179 LYERIRKRKNGL 190
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1543-1907 |
1.58e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 43.58 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1543 EMKTQLEELEDELQATEDAKLRLEVNMQALKVQFERDLQARDEQNEEKRRQLqRQLHEYETELEDERKQRALAVAAKKKL 1622
Cdd:pfam05557 6 ESKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRI-RLLEKREAEAEEALREQAELNRLKKKY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1623 EGDLKDLELQADSAIKGREEAI----KQLRKLQAQMKDFQRELEDARASRDEIFATAKENEKKAKSLEadlmQLQEDLAA 1698
Cdd:pfam05557 85 LEALNKKLNEKESQLADAREVIsclkNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAE----QLRQNLEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1699 AERARKQADLEKDELAEELASSVSGRNALQDEKRRLeARIAQLEEELEEEqgntEAMSERVRKATQQAEQLSNELATERS 1778
Cdd:pfam05557 161 QQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSKSEL-ARIPELEKELERL----REHNKHLNENIENKLLLKEEVEDLKR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1779 AAQKNENARQQ---LERQNKELRSKLQEMEGAVKSKFKS--TIAALEAKIAQLeeqveqearekQATAKALKQKDKKLKE 1853
Cdd:pfam05557 236 KLEREEKYREEaatLELEKEKLEQELQSWVKLAQDTGLNlrSPEDLSRRIEQL-----------QQREIVLKEENSSLTS 304
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 156120901 1854 ALLQVEDERKMAEQykeqaekgnlRVKQLKRQLEEAEEESQRINANRRKLQREL 1907
Cdd:pfam05557 305 SARQLEKARRELEQ----------ELAQYLKKIEDLNKKLKRHKALVRRLQRRV 348
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
960-1427 |
1.74e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 43.35 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 960 EEEEAARQKLQLEKVTAEAKIKKLEDDILVMDDQNNKLS---KERKLLEERISDLTTNLAEEEEKAKNLTKLKNKHESMI 1036
Cdd:PRK01156 207 ADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSsleDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKII 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1037 SELEVRLKKE-------EKSRQELEKLKRKLDGEAS---DLHEQIAELQAQIAE-LKMQlaKKEEELQAALGRLDDEMAQ 1105
Cdd:PRK01156 287 NDPVYKNRNYindyfkyKNDIENKKQILSNIDAEINkyhAIIKKLSVLQKDYNDyIKKK--SRYDDLNNQILELEGYEMD 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1106 KNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALKTELEDTLDSTAT-----QQELRAKREQEVTMLK 1180
Cdd:PRK01156 365 YNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSkvsslNQRIRALRENLDELSR 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1181 KALDEETRS---------HESQVQEMRQKHTQVVEELTEQLEQFKRAKANLDKNKQALEKENAELAGE--------LRVL 1243
Cdd:PRK01156 445 NMEMLNGQSvcpvcgttlGEEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEeinksineYNKI 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1244 SQAKQEVEHKKKKL------------------EVQLQELQSKYSDGEKVRAEL-NDKVHKLQNEVESVTGMLNEAEGKAI 1304
Cdd:PRK01156 525 ESARADLEDIKIKInelkdkhdkyeeiknrykSLKLEDLDSKRTSWLNALAVIsLIDIETNRSRSNEIKKQLNDLESRLQ 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1305 KLAKDVASLGSQLQDTQELLQEETRQKLNVSTKLRQLEDERNSLQEQLD---EEMEAKQNLERHISTLNIQLSDSKKKLQ 1381
Cdd:PRK01156 605 EIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIEKLRGKIDnykKQIAEIDSIIPDLKEITSRINDIEDNLK 684
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 156120901 1382 DFASTVELLEEGKKKFQKEIESLTQQYEEKAAAYDKLEKTKNRLQQ 1427
Cdd:PRK01156 685 KSRKALDDAKANRARLESTIEILRTRINELSDRINDINETLESMKK 730
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1545-1740 |
1.76e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 42.91 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1545 KTQLEELEDELQATEDAKLRLEVNMQALKVQFERDLQARDEQNEEKRRQLQRQLHEYETEL----EDERKQRALAVAAKK 1620
Cdd:TIGR02794 64 KKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAkakqAAEAKAKAEAEAERK 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1621 KLEGDLKDLELQADSAIKGREEAIKQLRKLQAQMKDFQRELEDARASRDEIFATAKENEKKAKSLEADLMQLQEDLAAAE 1700
Cdd:TIGR02794 144 AKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAA 223
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 156120901 1701 RARKQADLEKDELAEELASSVSGRNALQDEKRRLEARIAQ 1740
Cdd:TIGR02794 224 EAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDK 263
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1509-1656 |
1.79e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 43.09 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1509 LKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRL---EVNMQALKVQFE---RDLQA 1582
Cdd:pfam05667 340 LQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEELEKQYKVKKKTLDLLpdaEENIAKLQALVDasaQRLVE 419
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156120901 1583 RDEQNEEKRRQLqrqLHEYEtELEDERKQRALavAAKKKLE--GDLKDLELQADSAIKGREEAIKQlrkLQAQMKD 1656
Cdd:pfam05667 420 LAGQWEKHRVPL---IEEYR-ALKEAKSNKED--ESQRKLEeiKELREKIKEVAEEAKQKEELYKQ---LVAEYER 486
|
|
| TOPEUc |
smart00435 |
DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina ... |
991-1097 |
1.80e-03 |
|
DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina virus topoisomerase, Variola virus topoisomerase, Shope fibroma virus topoisomeras
Pssm-ID: 214661 [Multi-domain] Cd Length: 391 Bit Score: 42.72 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 991 DDQNNKLSKERKLLEERISDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRkldgeasdlheQ 1070
Cdd:smart00435 276 EKSMEKLQEKIKALKYQLKRLKKMILLFEMISDLKRKLKSKFERDNEKLDAEVKEKKKEKKKEEKKKK-----------Q 344
|
90 100
....*....|....*....|....*..
gi 156120901 1071 IAELQAQIAELKMQLAKKEEELQAALG 1097
Cdd:smart00435 345 IERLEERIEKLEVQATDKEENKTVALG 371
|
|
| PRK12472 |
PRK12472 |
hypothetical protein; Provisional |
1659-1825 |
1.84e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237110 [Multi-domain] Cd Length: 508 Bit Score: 42.94 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1659 RELEDARASRDEIFATAKENEKKAKSLEADLMQLQEDLAAAERARKQADlekdelaEELASSVSgrnalQDEKRRLEari 1738
Cdd:PRK12472 197 REAEDAARAADEAKTAAAAAAREAAPLKASLRKLERAKARADAELKRAD-------KALAAAKT-----DEAKARAE--- 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1739 aqleeeleeeqgnteamsERVRKATQQAEQLSNELATERSAAQKNENArqqlerqnkeLRSKLQEMEGAVKSKFKSTIAA 1818
Cdd:PRK12472 262 ------------------ERQQKAAQQAAEAATQLDTAKADAEAKRAA----------AAATKEAAKAAAAKKAETAKAA 313
|
....*..
gi 156120901 1819 LEAKIAQ 1825
Cdd:PRK12472 314 TDAKLAL 320
|
|
| HAP1_N |
pfam04849 |
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ... |
977-1200 |
1.85e-03 |
|
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found in several huntingtin-associated protein 1 (HAP1) homologs. HAP1 binds to huntingtin in a polyglutamine repeat-length-dependent manner. However, its possible role in the pathogenesis of Huntington's disease is unclear. This family also includes a similar N-terminal conserved region from hypothetical protein products of ALS2CR3 genes found in the human juvenile amyotrophic lateral sclerosis critical region 2q33-2q34.
Pssm-ID: 461455 [Multi-domain] Cd Length: 309 Bit Score: 42.71 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 977 EAKIKKLEDDILVMDDQNNKLSKERKLLEERISDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKL 1056
Cdd:pfam04849 100 TERNEALEEQLGSAREEILQLRHELSKKDDLLQIYSNDAEESETESSCSTPLRRNESFSSLHGCVQLDALQEKLRGLEEE 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1057 KRKLDGEASDLHEQIAELQAQIAELKMQLAKKEEELQAALGRLDDEMAQKNNALKKIRE----LEGHISDLQEDLdsera 1132
Cdd:pfam04849 180 NLKLRSEASHLKTETDTYEEKEQQLMSDCVEQLSEANQQMAELSEELARKMEENLRQQEeitsLLAQIVDLQHKC----- 254
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156120901 1133 arnkaekqkRDLGEELEALKTELEDTLDS----TATQQELRAKREQEVTMLkkaldeetrsHESQ--VQEMRQK 1200
Cdd:pfam04849 255 ---------KELGIENEELQQHLQASKEAqrqlTSELQELQDRYAECLGML----------HEAQeeLKELRKK 309
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1205-1452 |
1.93e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.59 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1205 VEELTEQLEQFKRAKANLDKNKQALEKENAELAGELRVLSQAKQEVEHKKKKLEVQLQELQSKYSDGEKVRAELNDKVHK 1284
Cdd:COG1340 10 LEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1285 LQNEVESVTGMLNEAEGKAI---KLAKDVASLGSQLQdTQELLQEETRQKLNvstKLRQLEDERNSLQEQLDEEMEAKQN 1361
Cdd:COG1340 90 LREELDELRKELAELNKAGGsidKLRKEIERLEWRQQ-TEVLSPEEEKELVE---KIKELEKELEKAKKALEKNEKLKEL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1362 LERhISTLNIQLSDSKKKLQDFA----STVELLEEGKKK---FQKEIESLTQQYEEKAAAYDKLEKTKNRLQQELDDLVV 1434
Cdd:COG1340 166 RAE-LKELRKEAEEIHKKIKELAeeaqELHEEMIELYKEadeLRKEADELHKEIVEAQEKADELHEEIIELQKELRELRK 244
|
250
....*....|....*...
gi 156120901 1435 DLDNQRQLVSNLEKKQKK 1452
Cdd:COG1340 245 ELKKLRKKQRALKREKEK 262
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
869-1055 |
1.93e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.83 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 869 QKAESELKELEQKHSQLTEEKNLLQEQLQAETELYAEAEEMRVRLAAKKQELEEILhemearleeeedrsQQLQAERKKM 948
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEI--------------EEVEARIKKY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 949 AQQMLDLEEQLEEeeaarQKLQLEKVTAEAKIKKLEDDILVMDDQNNKLSKERKLLEERISDLTTNLAEEeekaknltkl 1028
Cdd:COG1579 79 EEQLGNVRNNKEY-----EALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEK---------- 143
|
170 180
....*....|....*....|....*..
gi 156120901 1029 KNKHESMISELEVRLKKEEKSRQELEK 1055
Cdd:COG1579 144 KAELDEELAELEAELEELEAEREELAA 170
|
|
| ASY3-like |
pfam20435 |
Meiosis-specific protein ASY3-like; This entry represents a group of plant meiosis-specific ... |
1008-1113 |
2.12e-03 |
|
Meiosis-specific protein ASY3-like; This entry represents a group of plant meiosis-specific proteins, such as AtASY3 from Arabidopsis and PAIR3 from rice. They are coiled-coil domain proteins required for normal meiosis. PAIR3 is an axial element and part of the synaptonemal complex (SC) that forms between homologous chromosomes during meiosis. Members of this family are homologs of SCYP2 from vertebrates and fungal Red1/Rec10.
Pssm-ID: 466584 [Multi-domain] Cd Length: 793 Bit Score: 42.95 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1008 ISDLTTNLAEEEEKAKNLTKLKNKHEsmiselEVRLK-KEEKSRQELEKLKRKLDGEASDLHEQIAELQAQIAELKMQLA 1086
Cdd:pfam20435 667 LENIKSHIITEAGKTSNLAKTKRKHA------ETRLQeQEEKMRMIHEKFKDDVSHHLEDFKSTIEELEANQSELKGSIK 740
|
90 100
....*....|....*....|....*...
gi 156120901 1087 KKEEELQAALGRLDDEMAQK-NNALKKI 1113
Cdd:pfam20435 741 KQRTSHQKLIAHFEGGIETKlDDATKRI 768
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1671-1912 |
2.65e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 42.71 E-value: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1671 IFATAKENEKkakslEADLMQLQEDLAAAE-RARKQADLEKDeLAEELASSVSGRNALQDEKRRLEARIAQLEEELEEEQ 1749
Cdd:pfam05667 215 ELAAAQEWEE-----EWNSQGLASRLTPEEyRKRKRTKLLKR-IAEQLRSAALAGTEATSGASRSAQDLAELLSSFSGSS 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1750 GNTEAMSERVRKATQQAEQLSNELATERS----AAQKNENARQQLERQNKELRSKLQEMEgAVKSKFKSTIAALEAKIAQ 1825
Cdd:pfam05667 289 TTDTGLTKGSRFTHTEKLQFTNEAPAATSspptKVETEEELQQQREEELEELQEQLEDLE-SSIQELEKEIKKLESSIKQ 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1826 LEEQVEQEAREKQATAKALKQKDKKLKE--------ALLQVEDER------KMAEQYKEQAEKGNLRVKQLKRQLEEAEE 1891
Cdd:pfam05667 368 VEEELEELKEQNEELEKQYKVKKKTLDLlpdaeeniAKLQALVDAsaqrlvELAGQWEKHRVPLIEEYRALKEAKSNKED 447
|
250 260
....*....|....*....|.
gi 156120901 1892 ESQRINANRRKLQRELDEATE 1912
Cdd:pfam05667 448 ESQRKLEEIKELREKIKEVAE 468
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1766-1905 |
2.71e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.54 E-value: 2.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1766 AEQLSNELATERSAAQKNENARQQLERQNKELRSKLQEMEGAVKSkFKSTIAALEAKIAQLEEQVEQEAREKQATAKalk 1845
Cdd:COG2433 387 EKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEE-LEAELEEKDERIERLERELSEARSEERREIR--- 462
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1846 qKDKKLkeallqvedeRKMAEqykeqaekgnlRVKQLKRQLEEAEEesqRINANRRKLQR 1905
Cdd:COG2433 463 -KDREI----------SRLDR-----------EIERLERELEEERE---RIEELKRKLER 497
|
|
| COG5283 |
COG5283 |
Phage-related tail protein [Mobilome: prophages, transposons]; |
1801-1917 |
2.84e-03 |
|
Phage-related tail protein [Mobilome: prophages, transposons];
Pssm-ID: 444094 [Multi-domain] Cd Length: 747 Bit Score: 42.53 E-value: 2.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1801 LQEMEGAVKSKFKSTIAALEAKIAQLEEQVEQEAREKQATAKALKQKDKKLKEALLQVEDERKMAEQYKEQAEKGNLRVK 1880
Cdd:COG5283 1 LQVILGAVDKPFKSALESAKQRVAALAQALKALEAPTRALARALERAKQAAARLQTKYNKLRQSLQRLRQALDQAGIDTR 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 156120901 1881 QLKRQLEEAEEESQRINANRRKLQRELDEATESNEAM 1917
Cdd:COG5283 81 QLSAAQRRLRSSLEQTNRQLERQQQRLARLGARQDRL 117
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1781-1929 |
2.98e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.45 E-value: 2.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1781 QKNENARQQLERQNKELRSKLQEMEGAVKsKFKSTIAALEAKIAQLEEQVeqeaREKQATAKALKQKDKKLKEALLQVED 1860
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELA-ALEARLEAAKTELEDLEKEI----KRLELEIEEVEARIKKYEEQLGNVRN 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 156120901 1861 ERKMA------EQYKEQAEKGNLRVKQLKRQLEEAEEESQRINANRRKLQRELDEATESNEAMGREVTALKSKLR 1929
Cdd:COG1579 88 NKEYEalqkeiESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELE 162
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1750-1916 |
3.05e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 42.10 E-value: 3.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1750 GNTEAMSERVRKATQQAEQLSNELATERSAAQKNENARQQLERQNKelrsklQEMEGAVKSKFKSTIAALEAKIAQLEEQ 1829
Cdd:PRK09510 73 SAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKK------QAEEAAKQAALKQKQAEEAAAKAAAAAK 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1830 VEQEAREKQATAKALKQKDKKLKEAllQVEDERKMAEQYKEQAE-KGNLRVKQLKRQLEEAEEESQRINANRRKLQRELD 1908
Cdd:PRK09510 147 AKAEAEAKRAAAAAKKAAAEAKKKA--EAEAAKKAAAEAKKKAEaEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAK 224
|
....*...
gi 156120901 1909 EATESNEA 1916
Cdd:PRK09510 225 AAAAKAAA 232
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
856-1152 |
3.28e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.20 E-value: 3.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 856 AKEDELQKTKERQQKAESELKELEQKHSQLTEEKNLLQEQLQAETELYAEAEEMRVRLAAKKQELEEILHEMEARLEEEE 935
Cdd:COG4372 28 ALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 936 DRSQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDDILVMDDQNNKLSKERKLLEERISDLTTNL 1015
Cdd:COG4372 108 EEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDE 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1016 AEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLDGEASDLHEQIAELQAQIAELKMQLAKKEEELQAA 1095
Cdd:COG4372 188 LLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAI 267
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 156120901 1096 LGRLDDEMAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALK 1152
Cdd:COG4372 268 LVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLEL 324
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
964-1093 |
3.71e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 42.38 E-value: 3.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 964 AARQKLQLEKVTAEakIKKLEDDILVMDDQNNKLSKERKLL-EERISDLTTNLAEEEEKaknltklknkhesmISELEVR 1042
Cdd:COG0542 399 AARVRMEIDSKPEE--LDELERRLEQLEIEKEALKKEQDEAsFERLAELRDELAELEEE--------------LEALKAR 462
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 156120901 1043 LKKEEKSRQELEKLKRKLDgeasDLHEQIAELQAQIAELKMQLAKKEEELQ 1093
Cdd:COG0542 463 WEAEKELIEEIQELKEELE----QRYGKIPELEKELAELEEELAELAPLLR 509
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
1002-1173 |
3.73e-03 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 41.76 E-value: 3.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1002 KLLEERISDLTTNLAEEeekaknltKLKNKHESMiSELEVRLKKeekSRQELEKLKRK---LDGEAsdlheQIAELQAQI 1078
Cdd:COG3524 161 AESEELVNQLSERARED--------AVRFAEEEV-ERAEERLRD---AREALLAFRNRngiLDPEA-----TAEALLQLI 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1079 AELKMQLAKKEEELQAALGRLDDEMAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQkrdlgEELEALKTEL--- 1155
Cdd:COG3524 224 ATLEGQLAELEAELAALRSYLSPNSPQVRQLRRRIAALEKQIAAERARLTGASGGDSLASLL-----AEYERLELERefa 298
|
170
....*....|....*...
gi 156120901 1156 EDTLDSTATQQElRAKRE 1173
Cdd:COG3524 299 EKAYTSALAALE-QARIE 315
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1305-1638 |
3.87e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 3.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1305 KLAKDVASLGSQLQDTQELLQEETRQKLNVSTKLRQLEDERNSLQEQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFA 1384
Cdd:COG4372 42 KLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1385 STVELLEEGKKKFQKEIESLTQQYEEKAAAYDKLEKTKNRLQQELDDLvvdldNQRQLVSNLEKKQKKFDQLLAEEKNIs 1464
Cdd:COG4372 122 KERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAAL-----EQELQALSEAEAEQALDELLKEANRN- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1465 sKYADERDRAEAEAREKETKALSLARALEEALEAKEELERTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEM 1544
Cdd:COG4372 196 -AEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTE 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1545 KTQLEELEDELQATEDAKLRLEVNMQALKVQFERDLQARDEQNEEKRRQLQRQLHEYETELEDERKQRALAVAAKKKLEG 1624
Cdd:COG4372 275 EEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDND 354
|
330
....*....|....
gi 156120901 1625 DLKDLELQADSAIK 1638
Cdd:COG4372 355 VLELLSKGAEAGVA 368
|
|
| CagA_N |
pfam18971 |
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ... |
1359-1679 |
3.87e-03 |
|
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial virulence determinant and critical for gastric carcinogenesis. X-ray crystallographic analysis of the N-terminal CagA fragment (residues 1-876) revealed that the region has a structure comprised of three discrete domains. Domain I constitutes a mobile CagA N terminus, while Domain II tethers CagA to the plasma membrane by interacting with membrane phosphatidylserine. Domain III interacts intramolecularly with the intrinsically disordered C-terminal region, and this interaction potentiates the pathogenic scaffold/hub function of CagA.
Pssm-ID: 408741 [Multi-domain] Cd Length: 876 Bit Score: 42.45 E-value: 3.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1359 KQNLERHISTLNIQLSDSKKKLQDFASTVELLEEGKKKFQKEIESltqqyEEKAAAYDKLEKTKNrlqqelddlvvdldn 1438
Cdd:pfam18971 558 RRNLENKLTAKGLSLQEANKLIKDFLSSNKELAGKALNFNKAVAE-----AKSTGNYDEVKKAQK--------------- 617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1439 qrqlvsNLEKKQKKFDQLLAE-EKNISSKYADE-RDRAEAEAREKETKALSLARALEEALEAKEELERTNKMLKAEMEDL 1516
Cdd:pfam18971 618 ------DLEKSLRKREHLEKEvEKKLESKSGNKnKMEAKAQANSQKDEIFALINKEANRDARAIAYTQNLKGIKRELSDK 691
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1517 VS--SKD--DVGKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEvNMQALKVQFerdlqaRDEQNEEKRR 1592
Cdd:pfam18971 692 LEkiSKDlkDFSKSFDEFKNGKNKDFSKAEETLKALKGSVKDLGINPEWISKVE-NLNAALNEF------KNGKNKDFSK 764
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1593 QLQRQlheyeTELEDERKQralaVAAKKKLEGDLKDLElQADSAIKGREEaIKQLRKLQAQMKDFQRELEDARASRDEIF 1672
Cdd:pfam18971 765 VTQAK-----SDLENSVKD----VIINQKVTDKVDNLN-QAVSVAKAMGD-FSRVEQVLADLKNFSKEQLAQQAQKNEDF 833
|
....*..
gi 156120901 1673 ATAKENE 1679
Cdd:pfam18971 834 NTGKNSE 840
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
844-1138 |
3.97e-03 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 41.98 E-value: 3.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 844 LLQVTRQEEEMQAKEDELQKTKERQQKAESELKELEQKHSQLTEEKNLLQEQLQAETELYAEAEEMRVRLAAKKQELEEI 923
Cdd:pfam19220 75 TRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDKTAQAEALERQLAAETEQNRALEEENKALREEAQAAEKA 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 924 LHEMEARLEEEEDRSQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDDILVM-----------DD 992
Cdd:pfam19220 155 LQRAEGELATARERLALLEQENRRLQALSEEQAAELAELTRRLAELETQLDATRARLRALEGQLAAEqaereraeaqlEE 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 993 QNNKLSKERKLLEERISDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLDGEASDLHEQIA 1072
Cdd:pfam19220 235 AVEAHRAERASLRMKLEALTARAAATEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQFQ 314
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156120901 1073 ELQAQIAELKMQ-------LAKKEEELQAALGR---LDDEMAQKNNALKKIRE-LEGHISDLQEDLDSERAARNKAE 1138
Cdd:pfam19220 315 EMQRARAELEERaemltkaLAAKDAALERAEERiasLSDRIAELTKRFEVERAaLEQANRRLKEELQRERAERALAQ 391
|
|
| V_HD-PTP_like |
cd09234 |
Protein-interacting V-domain of mammalian His-Domain type N23 protein tyrosine phosphatase and ... |
1020-1292 |
4.46e-03 |
|
Protein-interacting V-domain of mammalian His-Domain type N23 protein tyrosine phosphatase and related domains; This family contains the V-shaped (V) domain of mammalian His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23) and related domains. It belongs to the V_Alix_like superfamily which includes the V domains of Bro1 and Rim20 (also known as PalA) from Saccharomyces cerevisiae, mammalian Alix (apoptosis-linked gene-2 interacting protein X/ also known as apoptosis-linked gene-2 interacting protein 1, AIP1), and related domains. HD_PTP interacts with the ESCRT (Endosomal Sorting Complexes Required for Transport) system, and participates in cell migration and endosomal trafficking. The related Alix V-domain (belonging to a different family in this superfamily) contains a binding site, partially conserved in the superfamily, for the retroviral late assembly (L) domain YPXnL motif. The Alix V-domain is also a dimerization domain. In addition to the V-domain, HD_PTP also has an N-terminal Bro1-like domain, a proline-rich region (PRR), a catalytically inactive tyrosine phosphatase domain, and a region containing a PEST motif. Bro1-like domains bind components of the ESCRT-III complex, specifically to CHMP4 in the case of HD-PTP. The Bro1-like domain of HD-PTP can also bind human immunodeficiency virus type 1 (HIV-1) nucleocapsid. HD-PTP is encoded by the PTPN23 gene, a tumor suppressor gene candidate frequently absent in human kidney, breast, lung, and cervical tumors. This family also contains Drosophila Myopic, which promotes epidermal growth factor receptor (EGFR) signaling, and Caenorhabditis elegans (enhancer of glp-1) EGO-2 which promotes Notch signaling.
Pssm-ID: 185747 [Multi-domain] Cd Length: 337 Bit Score: 41.51 E-value: 4.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1020 EKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEklkrkldgeasDLHEQIAELQAQIAELKMQLAKKEEELQAAlgrl 1099
Cdd:cd09234 79 EAMGELSDVYQDVEAMLNEIESLLEEEELQEKEFQ-----------EAVGKRGSSIAHVTELKRELKKYKEAHEKA---- 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1100 ddemAQKNNALKKIRELegHISDLQEDLDSERAARNKAEKQKRDLGEELEALKTELEDTLDSTatqQELRAKREQEVTML 1179
Cdd:cd09234 144 ----SQSNTELHKAMNL--HIANLKLLAGPLDELQKKLPSPSLLDRPEDEAIEKELKRILNKV---NEMRKQRRSLEQQL 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1180 KKALDEE-------TRSHESQ---VQEMRQKHTQvveeLTEQLEQFKRAKANLDKnkqALEKENAELAGELRVLSQAKQE 1249
Cdd:cd09234 215 RDAIHEDditsklvTTTGGDMedlFKEELKKHDQ----LVNLIEQNLAAQENILK---ALTEANAKYAPVRKALSETKQK 287
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 156120901 1250 VEHKKKKL----EVqLQELQSKYSDGEKVRAELNDKVHKLQNEVESV 1292
Cdd:cd09234 288 RESTISSLiasyEA-YEDLLKKSQKGIDFYKKLEGNVSKLLQRIKSV 333
|
|
| PRK05431 |
PRK05431 |
seryl-tRNA synthetase; Provisional |
1638-1717 |
4.49e-03 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 235461 [Multi-domain] Cd Length: 425 Bit Score: 41.59 E-value: 4.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1638 KGREEAIKQLRKLQAQMKDFQRELEDARASRDEI---FATAKENEKKAKSLEADLMQLQEDLAAAERARKQADLEKDELA 1714
Cdd:PRK05431 21 RGFPLDVDELLELDEERRELQTELEELQAERNALskeIGQAKRKGEDAEALIAEVKELKEEIKALEAELDELEAELEELL 100
|
...
gi 156120901 1715 EEL 1717
Cdd:PRK05431 101 LRI 103
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1628-1792 |
4.49e-03 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 41.25 E-value: 4.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1628 DLELQADSAIKGREEAIKQLRKLQAQMKDFQ---RELEDARASRDEIFATAKENEKKAKSLEADLMQLQEDLAAAERARK 1704
Cdd:pfam00529 55 DYQAALDSAEAQLAKAQAQVARLQAELDRLQaleSELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAP 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1705 QADLEKDELAEElassvsgRNALQDEKRRLEARIAQLEEELEEEQGNTEAMSERVRKATQQAEQLSNELATERsaaqknE 1784
Cdd:pfam00529 135 IGGISRESLVTA-------GALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSGAQLQIAEAEAEL------K 201
|
....*...
gi 156120901 1785 NARQQLER 1792
Cdd:pfam00529 202 LAKLDLER 209
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
873-1472 |
4.53e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 42.35 E-value: 4.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 873 SELKELEQKHSQLTEEKNLLQEQLQAETELYAEAeemrvrlaakKQELEEILHEMEARleeeedrsqqlqAERKKMAQQM 952
Cdd:TIGR01612 1486 NELKEHIDKSKGCKDEADKNAKAIEKNKELFEQY----------KKDVTELLNKYSAL------------AIKNKFAKTK 1543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 953 LDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDDILVMDDQ---NNKLSK------------ERKLLeeRISDLTTN--- 1014
Cdd:TIGR01612 1544 KDSEIIIKEIKDAHKKFILEAEKSEQKIKEIKKEKFRIEDDaakNDKSNKaaidiqlslenfENKFL--KISDIKKKind 1621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1015 -LAEEEEKAKNLTKLK-NKHESMISELEVRLKKEEKSRQELEKLKRKLDgeasDLHEQIAELQAQIAELKMQLAKKEEEL 1092
Cdd:TIGR01612 1622 cLKETESIEKKISSFSiDSQDTELKENGDNLNSLQEFLESLKDQKKNIE----DKKKELDELDSEIEKIEIDVDQHKKNY 1697
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1093 QAALGRLDDEMAQKN-NALKKIRELeghisdLQEDLDSERAARNKAEKQKRDLGEELEALKTELEDTLDSTATQQELrak 1171
Cdd:TIGR01612 1698 EIGIIEKIKEIAIANkEEIESIKEL------IEPTIENLISSFNTNDLEGIDPNEKLEEYNTEIGDIYEEFIELYNI--- 1768
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1172 reqeVTMLKKALDEETRSHEsqvqEMRQKHTQVVEELTEQLEQFKRAKANLDknkqalekeNAELAGELRVLSQAKQEVE 1251
Cdd:TIGR01612 1769 ----IAGCLETVSKEPITYD----EIKNTRINAQNEFLKIIEIEKKSKSYLD---------DIEAKEFDRIINHFKKKLD 1831
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1252 HKKKKLEVQLQELQ------SKYSDGEKVRAELNDKVHKLQNEVESVTGMLN--------EAEGKAIKLAKDVASLGSQL 1317
Cdd:TIGR01612 1832 HVNDKFTKEYSKINegfddiSKSIENVKNSTDENLLFDILNKTKDAYAGIIGkkyysykdEAEKIFINISKLANSINIQI 1911
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1318 QDTQEL-------------LQEETRQKLN----------VSTKLR-----------QLEDERNSLQEQLDEEMEAKQNLE 1363
Cdd:TIGR01612 1912 QNNSGIdlfdniniailssLDSEKEDTLKfipspekepeIYTKIRdsydtlldifkKSQDLHKKEQDTLNIIFENQQLYE 1991
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1364 --RHISTLNIQLSDSKKKLQDFASTVELLEEGKKKFQKeIESLTQQYEE--KAAAYDKLEKTKNRLQQELDDLVVDLDNQ 1439
Cdd:TIGR01612 1992 kiQASNELKDTLSDLKYKKEKILNDVKLLLHKFDELNK-LSCDSQNYDTilELSKQDKIKEKIDNYEKEKEKFGIDFDVK 2070
|
650 660 670
....*....|....*....|....*....|....*
gi 156120901 1440 --RQLVSNLEKKQKKFDQLLAEEKNISSKYADERD 1472
Cdd:TIGR01612 2071 amEEKFDNDIKDIEKFENNYKHSEKDNHDFSEEKD 2105
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1159-1379 |
4.58e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 41.80 E-value: 4.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1159 LDSTATQQELRAKREQEVTML---KKALDEETRSHESQVQ--EMRQKHTQVVEELTEQLEQFKRAKANLDKNKQALEKEN 1233
Cdd:pfam07888 3 LDELVTLEEESHGEEGGTDMLlvvPRAELLQNRLEECLQEraELLQAQEAANRQREKEKERYKRDREQWERQRRELESRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1234 AELAGELRVLSQAKQEVEHKKKKLEVQLQELQSKYSDGEKVRAELNDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASL 1313
Cdd:pfam07888 83 AELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156120901 1314 GSQLQDTQELLQEETRQKLNVSTKLRQLEDERNSLQEQLDEEMEAKQNLERHISTLNIQLSDSKKK 1379
Cdd:pfam07888 163 GAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRK 228
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
846-982 |
4.65e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 41.72 E-value: 4.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 846 QVTRQEEEMQAKEDELQktkERQQKAESE-LKELEQKHSQLTEEKNLLQEQLQAETE---------LYAEAEEMRVRLAA 915
Cdd:PRK09510 84 KEQQQAEELQQKQAAEQ---ERLKQLEKErLAAQEQKKQAEEAAKQAALKQKQAEEAaakaaaaakAKAEAEAKRAAAAA 160
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 156120901 916 KKQELE-EILHEMEARLEEEEDRSQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQlEKVTAEAKIKK 982
Cdd:PRK09510 161 KKAAAEaKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAK-KKAAAEAKAAA 227
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1507-1700 |
4.84e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 41.20 E-value: 4.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1507 KMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDAKLrlevnmQALKVQFERDLQAR-DE 1585
Cdd:cd22656 117 KTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDLLTDEG------GAIARKEIKDLQKElEK 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1586 QNEEKRRQLQRQLHEYETELEDERKQralaVAAKKKLEGDLKDLELQADSAIKGREEAIKQLRKLQAQMKDFQRELEDAR 1665
Cdd:cd22656 191 LNEEYAAKLKAKIDELKALIADDEAK----LAAALRLIADLTAADTDLDNLLALIGPAIPALEKLQGAWQAIATDLDSLK 266
|
170 180 190
....*....|....*....|....*....|....*
gi 156120901 1666 asrdeifATAKENEKKAKSleADLMQLQEDLAAAE 1700
Cdd:cd22656 267 -------DLLEDDISKIPA--AILAKLELEKAIEK 292
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1800-1929 |
4.99e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.68 E-value: 4.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1800 KLQEMEGAVKsKFKSTIAALEAKIAQLEEQVEQEAREKQATAKALKQKDKKLKEALLQVEDERKMAEQYKEQAEKG---- 1875
Cdd:COG1579 11 DLQELDSELD-RLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnnk 89
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 156120901 1876 -----NLRVKQLKRQLEEAEEESQRINANRRKLQRELDEATESNEAMGREVTALKSKLR 1929
Cdd:COG1579 90 eyealQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELD 148
|
|
| COG4223 |
COG4223 |
Uncharacterized conserved protein [Function unknown]; |
1752-1844 |
5.03e-03 |
|
Uncharacterized conserved protein [Function unknown];
Pssm-ID: 443367 [Multi-domain] Cd Length: 259 Bit Score: 40.80 E-value: 5.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1752 TEAMSERVRKATQQAEQLSNELATERSAAqKNENARQQLERQNKELRSKLQEMEGAVKSkfkSTIAALEAKIAQLEEQVE 1831
Cdd:COG4223 2 IAALEAAVAELPAQLTALEQRLAALEAAP-AAAAATAALEARLAALRAALAAAREAVAA---AAAAALEARLAALEAKAA 77
|
90
....*....|...
gi 156120901 1832 QEAREKQATAKAL 1844
Cdd:COG4223 78 APEAEAAAAARAA 90
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1146-1831 |
5.06e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 42.09 E-value: 5.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1146 EELEALKTELEdTLDSTATQQEL--RAKREQEVTMLKKALDEETRSHESQVQEmrQKHTQVVEELTEQLEQFKRAKANLD 1223
Cdd:PRK10246 191 EQHKSARTELE-KLQAQASGVALltPEQVQSLTASLQVLTDEEKQLLTAQQQQ--QQSLNWLTRLDELQQEASRRQQALQ 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1224 KNKQALEK--------ENAELAGELRVLSQAKQEVEHKKKKLEVQLQE----LQSKYSDGEKVRAELNDKVHKLQNEVES 1291
Cdd:PRK10246 268 QALAAEEKaqpqlaalSLAQPARQLRPHWERIQEQSAALAHTRQQIEEvntrLQSTMALRARIRHHAAKQSAELQAQQQS 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1292 VTGMLNEAEGKAIklakdvasLGSQLQDTQELLQEETRQKlnvsTKLRQLEDERNSLQEQLDEEMEAKQNLERhistlni 1371
Cdd:PRK10246 348 LNTWLAEHDRFRQ--------WNNELAGWRAQFSQQTSDR----EQLRQWQQQLTHAEQKLNALPAITLTLTA------- 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1372 qlsdskkklQDFASTVELLEEGKKKFQKeIESLTQQYEEKAAAYDKLEKTKNRLQQElddlvvdldnQRQLVSNLEKKQK 1451
Cdd:PRK10246 409 ---------DEVAAALAQHAEQRPLRQR-LVALHGQIVPQQKRLAQLQVAIQNVTQE----------QTQRNAALNEMRQ 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1452 KFdqllaEEKNisSKYADERDRAEAEARekeTKALSLARALEEALEAKEELERTNKMLKAEMEDLvsSKDDVGKNVHELE 1531
Cdd:PRK10246 469 RY-----KEKT--QQLADVKTICEQEAR---IKDLEAQRAQLQAGQPCPLCGSTSHPAVEAYQAL--EPGVNQSRLDALE 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1532 KSKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKVQFE-------------RDLQARDEQNEEKRRQLQ--R 1596
Cdd:PRK10246 537 KEVKKLGEEGAALRGQLDALTKQLQRDESEAQSLRQEEQALTQQWQavcaslnitlqpqDDIQPWLDAQEEHERQLRllS 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1597 QLHEYETELEDERKQRALAVAA----KKKLEGDLKDLELQA------DSAIKGREEAIKQLRKLQAQMKDFQRELEDARA 1666
Cdd:PRK10246 617 QRHELQGQIAAHNQQIIQYQQQieqrQQQLLTALAGYALTLpqedeeASWLATRQQEAQSWQQRQNELTALQNRIQQLTP 696
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1667 SRDEIFATAKENEKKAK--------------SLEADL--MQLQEDLAAAERARKQADLEKDELAEELASSVSGRNALQDE 1730
Cdd:PRK10246 697 LLETLPQSDDLPHSEETvaldnwrqvheqclSLHSQLqtLQQQDVLEAQRLQKAQAQFDTALQASVFDDQQAFLAALLDE 776
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1731 KRRleARIAQLEEELEEEQGNTEAMSERVRKATQQAEQLSNELATERSAAQKNENARQQLERQNKELRSKLQEMEGAVK- 1809
Cdd:PRK10246 777 ETL--TQLEQLKQNLENQRQQAQTLVTQTAQALAQHQQHRPDGLDLTVTVEQIQQELAQLAQQLRENTTRQGEIRQQLKq 854
|
730 740
....*....|....*....|...
gi 156120901 1810 -SKFKSTIAALEAKIAQLEEQVE 1831
Cdd:PRK10246 855 dADNRQQQQALMQQIAQATQQVE 877
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
859-1091 |
5.33e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.54 E-value: 5.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 859 DELQKTKERQQKAESELKELEQKH--SQLTEEKNLLQEQLQAETELYAEAEEMRVRLAAK----KQELEEILHEMEARLE 932
Cdd:PHA02562 169 DKLNKDKIRELNQQIQTLDMKIDHiqQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEaktiKAEIEELTDELLNLVM 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 933 EEEDRSQQLQAERKKmaqqmldleeqleeeeAARQKLQLEKVTAEAK--------------IKKLEDDILVMDDQNNKLS 998
Cdd:PHA02562 249 DIEDPSAALNKLNTA----------------AAKIKSKIEQFQKVIKmyekggvcptctqqISEGPDRITKIKDKLKELQ 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 999 KERKLLEERISDLTTNLAEEEEKAKNLTKLKNKhesmISELEVRLKKEEKSRQELEKLKRKLDGEASDLHEQIAELQAQI 1078
Cdd:PHA02562 313 HSLEKLDTAIDELEEIMDEFNEQSKKLLELKNK----ISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDEL 388
|
250
....*....|...
gi 156120901 1079 AELKMQLAKKEEE 1091
Cdd:PHA02562 389 DKIVKTKSELVKE 401
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
1506-1636 |
5.53e-03 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 41.97 E-value: 5.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1506 NKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKVQFErDLQARDE 1585
Cdd:pfam05911 683 NKRLKEEFEQLKSEKENLEVELASCTENLESTKSQLQESEQLIAELRSELASLKESNSLAETQLKCMAESYE-DLETRLT 761
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 156120901 1586 QNEEKRRQLQRQLHEYETELEDERKqralavaAKKKLEGDLKDLELQADSA 1636
Cdd:pfam05911 762 ELEAELNELRQKFEALEVELEEEKN-------CHEELEAKCLELQEQLERN 805
|
|
| PRK03598 |
PRK03598 |
putative efflux pump membrane fusion protein; Provisional |
1601-1708 |
5.69e-03 |
|
putative efflux pump membrane fusion protein; Provisional
Pssm-ID: 235136 [Multi-domain] Cd Length: 331 Bit Score: 41.10 E-value: 5.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1601 YETELEDERKQRALAVAAKKKLEGDLKDLEL-QADSAIKGREEAI-------KQLRKLQAQMKDFQRELEDARASRDEIF 1672
Cdd:PRK03598 79 YENALMQAKANVSVAQAQLDLMLAGYRDEEIaQARAAVKQAQAAYdyaqnfyNRQQGLWKSRTISANDLENARSSRDQAQ 158
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 156120901 1673 ATAKENEKKAKSLEA-----DLMQLQEDLAAAERARKQADL 1708
Cdd:PRK03598 159 ATLKSAQDKLSQYREgnrpqDIAQAKASLAQAQAALAQAEL 199
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1392-1728 |
5.74e-03 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 41.74 E-value: 5.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1392 EGKKKFQKEIESLTQQYEEKAAAYDK--LEKTKNRLQQELDdlvvdldNQRQLVSNLEKKQKKFDQLlAEEKNISskyaD 1469
Cdd:NF012221 1539 ESSQQADAVSKHAKQDDAAQNALADKerAEADRQRLEQEKQ-------QQLAAISGSQSQLESTDQN-ALETNGQ----A 1606
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1470 ERDRAEAEARE------KETKALSLARALEEALEAKEELERTN---KMLKAEMEDLVSSKDDVGKnvhELEKSKRALETQ 1540
Cdd:NF012221 1607 QRDAILEESRAvtkeltTLAQGLDALDSQATYAGESGDQWRNPfagGLLDRVQEQLDDAKKISGK---QLADAKQRHVDN 1683
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1541 MEEMKTQLEELEDELQATEDAKLRLEVNMQALKVQFE-RDLQARDEQNEEKRRqlqrqlheyeteledERKQRALAVAAK 1619
Cdd:NF012221 1684 QQKVKDAVAKSEAGVAQGEQNQANAEQDIDDAKADAEkRKDDALAKQNEAQQA---------------ESDANAAANDAQ 1748
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1620 KKLEGDLKDLELQADSAikgreeaikqlrklQAQMKDFQRElEDARASRDEifATAKENEKKAKSLEAD---LMQLQEDL 1696
Cdd:NF012221 1749 SRGEQDASAAENKANQA--------------QADAKGAKQD-ESDKPNRQG--AAGSGLSGKAYSVEGVaepGSHINPDS 1811
|
330 340 350
....*....|....*....|....*....|..
gi 156120901 1697 AAAERARKQADLEKDELaEELASSVSGRNALQ 1728
Cdd:NF012221 1812 PAAADGRFSEGLTEQEQ-EALEGATNAVNRLQ 1842
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1641-1808 |
6.02e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.29 E-value: 6.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1641 EEAIKQLRKLQaqmkDFQRELEDARASRDEIFATAKENEKKAKSLEADLMQLQEDLAAAERARKQADLEKDELAEELASS 1720
Cdd:COG1579 3 PEDLRALLDLQ----ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1721 ----VSGRN-----ALQDEKRRLEARIAQLEEELEEEQGNTEAMSERVRKATQQAEQLSNELATERsaaQKNENARQQLE 1791
Cdd:COG1579 79 eeqlGNVRNnkeyeALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKK---AELDEELAELE 155
|
170
....*....|....*..
gi 156120901 1792 RQNKELRSKLQEMEGAV 1808
Cdd:COG1579 156 AELEELEAEREELAAKI 172
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1532-1882 |
6.47e-03 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 41.28 E-value: 6.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1532 KSKRALETQMEEMKTQLEE-LEDELQATEDAKLRLE---------VNMQALKVQFERDlqaRDEQNEEKRRQLQRQLHEY 1601
Cdd:pfam09731 114 EAKAQLPKSEQEKEKALEEvLKEAISKAESATAVAKeakddaiqaVKAHTDSLKEASD---TAEISREKATDSALQKAEA 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1602 ETELEDERKQRALAVAAKKKLEGDLKDLELQADS-----AIKGREEAIKQLRKLQAQMKD--------FQRELEdarASR 1668
Cdd:pfam09731 191 LAEKLKEVINLAKQSEEEAAPPLLDAAPETPPKLpehldNVEEKVEKAQSLAKLVDQYKElvaserivFQQELV---SIF 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1669 DEIFATAKENEKKAKS-LEADLMQLQEDLAAAERarKQADLEKDELAEELASSVSGRNALQDEKRRLEARIaqleeelee 1747
Cdd:pfam09731 268 PDIIPVLKEDNLLSNDdLNSLIAHAHREIDQLSK--KLAELKKREEKHIERALEKQKEELDKLAEELSARL--------- 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1748 eqgnteamsERVRKATQQAEQLSNELATERSAAQKNENARQQLERQNKELRSKLQEMegavkskfkstiaaLEAKIAQLE 1827
Cdd:pfam09731 337 ---------EEVRAADEAQLRLEFEREREEIRESYEEKLRTELERQAEAHEEHLKDV--------------LVEQEIELQ 393
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 156120901 1828 EQVEQEAREKQATAKALKQkdKKLKEALLQVEDERKMAEQYKeQAEKGNLRVKQL 1882
Cdd:pfam09731 394 REFLQDIKEKVEEERAGRL--LKLNELLANLKGLEKATSSHS-EVEDENRKAQQL 445
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1048-1264 |
6.53e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 41.21 E-value: 6.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1048 KSRQELEKLKRkldgEASDLHEQIAELQAQIAEL-KMQLAKKEEE------------------LQAALGRLDDEmaqKNN 1108
Cdd:COG0497 169 ALKKELEELRA----DEAERARELDLLRFQLEELeAAALQPGEEEeleeerrrlsnaeklreaLQEALEALSGG---EGG 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1109 ALKKIRELEGHISDLQEdLDSERAarnkaekqkrDLGEELEALKTELED---TLDSTATQQELRAKREQEVTMLKKALDE 1185
Cdd:COG0497 242 ALDLLGQALRALERLAE-YDPSLA----------ELAERLESALIELEEaasELRRYLDSLEFDPERLEEVEERLALLRR 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1186 ETRSHESQVQEMRQKHtqvvEELTEQLEQFKRAKANLDKNKQALEKENAELAGELRVLSQAKQEVEHK-KKKLEVQLQEL 1264
Cdd:COG0497 311 LARKYGVTVEELLAYA----EELRAELAELENSDERLEELEAELAEAEAELLEAAEKLSAARKKAAKKlEKAVTAELADL 386
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1763-1927 |
6.53e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 40.98 E-value: 6.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1763 TQQAEQLSNELATERSAAQKNENARQQLERQNKELRSKLQEMEGAVKSKFKSTIAALEAKIAQLEEQVEQEAREKQATAK 1842
Cdd:TIGR02794 45 PGAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1843 ALKQKDKKLKEAllQVEDERKMAEQYKEQAEKgnlrvkqlKRQLEEAEEESQRINANRRKLQRELDEATESNEAMGREVT 1922
Cdd:TIGR02794 125 KAKQAAEAKAKA--EAEAERKAKEEAAKQAEE--------EAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEA 194
|
....*
gi 156120901 1923 ALKSK 1927
Cdd:TIGR02794 195 KAKAE 199
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1027-1132 |
6.89e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.61 E-value: 6.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1027 KLKNKHESMISELEVRLKKEEKSRQELEKLKRKLDG----EASDLHEQIAELQAQIAELKMQLaKKEEELQAALGRLDDE 1102
Cdd:COG0542 401 RVRMEIDSKPEELDELERRLEQLEIEKEALKKEQDEasfeRLAELRDELAELEEELEALKARW-EAEKELIEEIQELKEE 479
|
90 100 110
....*....|....*....|....*....|
gi 156120901 1103 MAQKNNalkKIRELEGHISDLQEDLDSERA 1132
Cdd:COG0542 480 LEQRYG---KIPELEKELAELEEELAELAP 506
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1115-1280 |
6.97e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.35 E-value: 6.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1115 ELEGHISDLQE---DLDSERAARNKAEKQKRDLGEELEALKTELEDTLDSTATQQELRAKreQEVTMLKKALDEETRSHE 1191
Cdd:PRK00409 517 KLNELIASLEElerELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQ--QAIKEAKKEADEIIKELR 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1192 sqvQEMRQKHTQVVE-ELTEQLEQFKRAKANLDKNKQALEKENAEL-AG-ELRVLS-QAKQEVEHKKKKLEVQLQelqsk 1267
Cdd:PRK00409 595 ---QLQKGGYASVKAhELIEARKRLNKANEKKEKKKKKQKEKQEELkVGdEVKYLSlGQKGEVLSIPDDKEAIVQ----- 666
|
170
....*....|...
gi 156120901 1268 ySDGEKVRAELND 1280
Cdd:PRK00409 667 -AGIMKMKVPLSD 678
|
|
| ALIX_LYPXL_bnd |
pfam13949 |
ALIX V-shaped domain binding to HIV; The binding of the LYPxL motif of late HIV p6Gag and EIAV ... |
1023-1291 |
6.99e-03 |
|
ALIX V-shaped domain binding to HIV; The binding of the LYPxL motif of late HIV p6Gag and EIAV p9Gag to this domain is necessary for viral budding.This domain is generally central between an N-terminal Bro1 domain, pfam03097 and a C-terminal proline-rich domain. The retroviruses thus used this domain to hijack the ESCRT system of the cell.
Pssm-ID: 464053 [Multi-domain] Cd Length: 294 Bit Score: 40.68 E-value: 6.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1023 KNLTKLKNKHESMISELEVRLKKEEKSRQEL-EKLKRKLDGEASdlHEQIAELQAQIAELKmqlakkeeELQAALGRLDD 1101
Cdd:pfam13949 27 DDLPKLKQRNREILDEAEKLLDEEESEDEQLrAKYGTRWTRPPS--SELTATLRAEIRKYR--------EILEQASESDS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1102 EMAQK-NNALKKIRELEGHISDLQEDLDSERAARNKAEKQK-----RDLGEELEALKTELEDTLdstatqQELRAKREQ- 1174
Cdd:pfam13949 97 QVRSKfREHEEDLELLSGPDEDLEAFLPSSRRAKNSPSVEEqvaklRELLNKLNELKREREQLL------KDLKEKARNd 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1175 ---EVTMLKKALDEETRSHESQVQEMRQKHtqvvEELTEQLEQFKRAKANLdknKQALEKENAELAGELRVLSQAKQEVE 1251
Cdd:pfam13949 171 disPKLLLEKARLIAPNQEEQLFEEELEKY----DPLQNRLEQNLHKQEEL---LKEITEANNEFLQDKRVDSEKQRQRE 243
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 156120901 1252 HKKKKLEVQLQ---ELQSKYSDGEKVRAELNDKVHKLQNEVES 1291
Cdd:pfam13949 244 EALQKLENAYDkykELVSNLQEGLKFYNDLTEILEKLLKKVKD 286
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1764-1909 |
7.04e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 41.23 E-value: 7.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1764 QQAEQLSNELATERSAAQKN-ENARQQLERQNKELRSKLQEMEGAVKSKFKSTIAALEAKIAQLEEQVEQEAREKQATAK 1842
Cdd:PRK12705 26 KKRQRLAKEAERILQEAQKEaEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLEN 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 156120901 1843 ALKQKDKKLKEALLQVEDERKMAEQYKEQAEkgNLRVKQLKRQL------EEAEEESQRINANRRKLQRELDE 1909
Cdd:PRK12705 106 QLEEREKALSARELELEELEKQLDNELYRVA--GLTPEQARKLLlklldaELEEEKAQRVKKIEEEADLEAER 176
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1702-1894 |
7.90e-03 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 41.36 E-value: 7.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1702 ARKQADLEKDELAEELASSVSGRNALQDEKR------RLEARIAQLEEELEEEQGNTE----------------AMSERV 1759
Cdd:NF012221 1536 ATSESSQQADAVSKHAKQDDAAQNALADKERaeadrqRLEQEKQQQLAAISGSQSQLEstdqnaletngqaqrdAILEES 1615
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1760 RKATQQAEQLSNELATERSAAQKNENARQQLERQNKE-LRSKLQEMEGAVKSKFKSTIAALEAKIAQLEEQVeQEAREKQ 1838
Cdd:NF012221 1616 RAVTKELTTLAQGLDALDSQATYAGESGDQWRNPFAGgLLDRVQEQLDDAKKISGKQLADAKQRHVDNQQKV-KDAVAKS 1694
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 156120901 1839 ATAKAlkQKDKKLKEALLQVEDERKMAEQYKEQAEKGNLRVKQLKRQLEEAEEESQ 1894
Cdd:NF012221 1695 EAGVA--QGEQNQANAEQDIDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQ 1748
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1816-1923 |
8.16e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.22 E-value: 8.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1816 IAALEAKIAQLEEQVEQEAREKQAtakALKQKDKKLKEALLQVEDERKMAEQYKEQAEKGNLRVKQLKRQLEEAEEESQR 1895
Cdd:COG0542 406 IDSKPEELDELERRLEQLEIEKEA---LKKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQ 482
|
90 100 110
....*....|....*....|....*....|..
gi 156120901 1896 INANRRKLQRELDEATESNEAMGR----EVTA 1923
Cdd:COG0542 483 RYGKIPELEKELAELEEELAELAPllreEVTE 514
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1116-1482 |
8.26e-03 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 41.15 E-value: 8.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1116 LEGHISDLQEDLDSERaarnkaEKQKRDLGEELEALKTEL--EDTLDSTATQQELRAKREQEVTMLKKALDEETRSHESQ 1193
Cdd:NF033838 67 LEKILSEIQKSLDKRK------HTQNVALNKKLSDIKTEYlyELNVLKEKSEAELTSKTKKELDAAFEQFKKDTLEPGKK 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1194 VQEMRQKHTQVVEELTEQLEQFKR--------------AKANLDKNKQALE--KENAELAGELRVLSQAKQEVEHKKKKL 1257
Cdd:NF033838 141 VAEATKKVEEAEKKAKDQKEEDRRnyptntyktleleiAESDVEVKKAELElvKEEAKEPRDEEKIKQAKAKVESKKAEA 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1258 eVQLQELQSkysdgEKVRAELNDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLGSQ-LQDTQE--------LLQEET 1328
Cdd:NF033838 221 -TRLEKIKT-----DREKAEEEAKRRADAKLKEAVEKNVATSEQDKPKRRAKRGVLGEPaTPDKKEndakssdsSVGEET 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1329 RQKLNVSTKLRQLEDERNSLQEQL---DEEMEAKQNLERHI-STLNIQLSDSKKKLQDfaSTVELLEEGKKKFQKE--IE 1402
Cdd:NF033838 295 LPSPSLKPEKKVAEAEKKVEEAKKkakDQKEEDRRNYPTNTyKTLELEIAESDVKVKE--AELELVKEEAKEPRNEekIK 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1403 SLTQQYEEKAAAYDKLEKTKnrlqqelddlvvdldnqrqlvSNLEKKQKKFDQLLAEEKNISSKYADERDRAEAEAREKE 1482
Cdd:NF033838 373 QAKAKVESKKAEATRLEKIK---------------------TDRKKAEEEAKRKAAEEDKVKEKPAEQPQPAPAPQPEKP 431
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1589-1875 |
8.37e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.28 E-value: 8.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1589 EKRRQLQRQLHEYETELEDERKQRALAVAAKKKLEGDLKDLELQADSAIKGREEAIKQLRKLQAQMKDFQRELEDARASR 1668
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1669 DEIFATAKENEKKAKSLEADLMQLQEDLAAAERARKQ-ADLEKDELAEELasSVSGRNALQDEKRRLEARIAQLEEELEE 1747
Cdd:COG1340 81 DELNEKLNELREELDELRKELAELNKAGGSIDKLRKEiERLEWRQQTEVL--SPEEEKELVEKIKELEKELEKAKKALEK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1748 EQGNTEaMSERVRKATQQAEQLSNELATERSAAQKNENARQQLERQNKELRSKLQEMegavkskfKSTIAALEAKIAQLE 1827
Cdd:COG1340 159 NEKLKE-LRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADEL--------HKEIVEAQEKADELH 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 156120901 1828 EQVEQEAREKQATAKALKQKDKKLKEALLQVEDE--RKMAEQYKEQAEKG 1875
Cdd:COG1340 230 EEIIELQKELRELRKELKKLRKKQRALKREKEKEelEEKAEEIFEKLKKG 279
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
1831-1925 |
8.71e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 40.25 E-value: 8.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1831 EQEAREKQATAKALKQKDKKLKEAllQVEDERKMAEQYKEQAEKGNLRVKQLKRQLEEAEEESQRINANRRKLQREL--D 1908
Cdd:cd16269 197 EKEIEAERAKAEAAEQERKLLEEQ--QRELEQKLEDQERSYEEHLRQLKEKMEEERENLLKEQERALESKLKEQEALleE 274
|
90
....*....|....*..
gi 156120901 1909 EATESNEAMGREVTALK 1925
Cdd:cd16269 275 GFKEQAELLQEEIRSLK 291
|
|
| SHE3 |
pfam17078 |
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ... |
1256-1437 |
8.83e-03 |
|
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an RNA-binding protein that binds specific mRNAs, including the mRNA of Ash1, which is invalid in cell-fate determination. She3 acts as an adapter protein that docks the myosin motor Myo4p onto an Ash1-She2p ribonucleoprotein complex. She3 seems to bind to Myo4p and Shep2p via different domains.
Pssm-ID: 293683 [Multi-domain] Cd Length: 228 Bit Score: 39.72 E-value: 8.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1256 KLEVQLQELQSKYSDGEKVRAELNDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLGSQLQDTQELLQEETRQKLNVS 1335
Cdd:pfam17078 21 QLTVQSQNLLSKLEIAQQKESKFLENLASLKHENDNLSSMLNRKERRLKDLEDQLSELKNSYEELTESNKQLKKRLENSS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1336 TKLRQLEDERNSLQEQ----LDEEMEAKQNLERHISTLNIQLSDSKKKLQDFASTvelLEEGKKKFQKEIESLTQQYEEK 1411
Cdd:pfam17078 101 ASETTLEAELERLQIQydalVDSQNEYKDHYQQEINTLQESLEDLKLENEKQLEN---YQQRISSNDKDIDTKLDSYNNK 177
|
170 180
....*....|....*....|....*..
gi 156120901 1412 AAAYDKLEKTKN-RLQQELDDLVVDLD 1437
Cdd:pfam17078 178 FKNLDNIYVNKNnKLLTKLDSLAQLLD 204
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
1641-1797 |
9.34e-03 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 40.60 E-value: 9.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1641 EEAIKQL--RKLQAQMKDFQRELEDA----RASRDEIfaTAKENEKKAKSLEADLMQLQEDLAA--AERARKQADLekDE 1712
Cdd:COG3524 164 EELVNQLseRAREDAVRFAEEEVERAeerlRDAREAL--LAFRNRNGILDPEATAEALLQLIATleGQLAELEAEL--AA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1713 LAEELASSVSGRNALQDEKRRLEARIAQLEEELEEEQGNtEAMSERVrkATQQAEQLSNELATER--SAAQKNENARQQL 1790
Cdd:COG3524 240 LRSYLSPNSPQVRQLRRRIAALEKQIAAERARLTGASGG-DSLASLL--AEYERLELEREFAEKAytSALAALEQARIEA 316
|
....*..
gi 156120901 1791 ERQNKEL 1797
Cdd:COG3524 317 ARQQRYL 323
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1529-1888 |
9.45e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 41.11 E-value: 9.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1529 ELEKSKRALETQMEEMKTQLEELEDELQATEDAklrlevnmQALKVQFERDLQARDEQNEEkRRQLQRQLHEYETELEDE 1608
Cdd:TIGR00618 202 RSQLLTLCTPCMPDTYHERKQVLEKELKHLREA--------LQQTQQSHAYLTQKREAQEE-QLKKQQLLKQLRARIEEL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1609 RKQRALAVAAKKKLEGDLKDLELQADSaikgreEAIKQLRKlqaQMKDFQRELEDARASRDEIFATAKENEKKAKSLEAD 1688
Cdd:TIGR00618 273 RAQEAVLEETQERINRARKAAPLAAHI------KAVTQIEQ---QAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQ 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1689 LMQLQEDLAAAERARKQADLEKdelaeelassvsGRNALQDEKRRLEARIAQLeeeleeeQGNTEAMSERVRKATQQAEQ 1768
Cdd:TIGR00618 344 RRLLQTLHSQEIHIRDAHEVAT------------SIREISCQQHTLTQHIHTL-------QQQKTTLTQKLQSLCKELDI 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1769 LSNELATERSAAQKNENARQQLERQNKELRSKLQEMEgavkskfksTIAALEAKIAQLEEQVEQEAREKQATAKALKQKD 1848
Cdd:TIGR00618 405 LQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAE---------LCAAAITCTAQCEKLEKIHLQESAQSLKEREQQL 475
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 156120901 1849 KKLKEALlqvederkmaEQYKeqaEKGNLRVKQLKRQLEE 1888
Cdd:TIGR00618 476 QTKEQIH----------LQET---RKKAVVLARLLELQEE 502
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1345-1575 |
9.69e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.77 E-value: 9.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1345 RNSLQEQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFASTVEL--LEEGKKKFQKEIESLTQQYEEKAAAYDKLEKTK 1422
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLvdLSEEAKLLLQQLSELESQLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1423 NRLQQELDDLVVDLDNQRQlVSNLEKKQKKFDQLLAEEKNISSKYADE-RDRAEAEAREKETKALSLARALEEALEakee 1501
Cdd:COG3206 243 AALRAQLGSGPDALPELLQ-SPVIQQLRAQLAELEAELAELSARYTPNhPDVIALRAQIAALRAQLQQEAQRILAS---- 317
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156120901 1502 lertnkmLKAEMEDLVSskddvgkNVHELEKSKRALETQMEEMK---TQLEELEDELQATEDAKLRLEVNMQALKVQ 1575
Cdd:COG3206 318 -------LEAELEALQA-------REASLQAQLAQLEARLAELPeleAELRRLEREVEVARELYESLLQRLEEARLA 380
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
1096-1472 |
9.72e-03 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 41.19 E-value: 9.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1096 LGRLDDEMAQKNNALKKIREL-EGHI-------SDLQEDLDSERAARNKAEKQKRDLGEELEALKTELEDTLDSTATQQE 1167
Cdd:PTZ00108 1001 LGKLERELARLSNKVRFIKHViNGELvitnakkKDLVKELKKLGYVRFKDIIKKKSEKITAEEEEGAEEDDEADDEDDEE 1080
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1168 LRAKREQEVTMLKKALDEETRSH----ESQVQEMRQKHTQVVEELTEQLeqfkrAKANLDKNKQALEKENAELAGELRVL 1243
Cdd:PTZ00108 1081 ELGAAVSYDYLLSMPIWSLTKEKveklNAELEKKEKELEKLKNTTPKDM-----WLEDLDKFEEALEEQEEVEEKEIAKE 1155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1244 SQAKQevehKKKKLEVQLQELQSKYSDGEKVRAELNDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLGSQLQD---- 1319
Cdd:PTZ00108 1156 QRLKS----KTKGKASKLRKPKLKKKEKKKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSDQEDdeeq 1231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1320 -TQELLQEETRQKLNVSTKLRQLEDERNSLQEQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFASTVELLEEGKKKFQ 1398
Cdd:PTZ00108 1232 kTKPKKSSVKRLKSKKNNSSKSSEDNDEFSSDDLSKEGKPKNAPKRVSAVQYSPPPPSKRPDGESNGGSKPSSPTKKKVK 1311
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156120901 1399 KEIESLTQQYEEKaaaydKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQKKFDQLLAEEKNISSKYADERD 1472
Cdd:PTZ00108 1312 KRLEGSLAALKKK-----KKSEKKTARKKKSKTRVKQASASQSSRLLRRPRKKKSDSSSEDDDDSEVDDSEDED 1380
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1211-1367 |
9.79e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.91 E-value: 9.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1211 QLEQFKRAKANLDKNKQALEKENAELAGELRVLSQAKQEVEHKKKKLEVQLQELQSKYsdgEKVRAEL-----NDKVHKL 1285
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARI---KKYEEQLgnvrnNKEYEAL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120901 1286 QNEVESVTGMLNEAEGKAIKLAKDVASLGSQLQDTQELLQEETRQklnVSTKLRQLEDERNSLQEQLDEEMEAKQNLERH 1365
Cdd:COG1579 95 QKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAE---LEEKKAELDEELAELEAELEELEAEREELAAK 171
|
..
gi 156120901 1366 IS 1367
Cdd:COG1579 172 IP 173
|
|
| |
