|
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 ... |
852-1932 |
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: 1398.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 852 TRQEEEMGQKDEELKAAKEVAAKVETELKDITQKHTQLMEERAQLEMKLHAETELYAEAEEMRVRLEAKKQELEEVLHEM 931
Cdd:pfam01576 1 TRQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 932 ESRLEEEEDRSNALHNERKEMEQQLQLMEAHIAEEEDARQKLQMEKVSVEGKVKKLEEDILMMEDQNNKLQKERKLLEER 1011
Cdd:pfam01576 81 ESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1012 LADMSSNLAEEEEKSKNLSKLKTKHESMISELELRMKKEEKGRLDMEKAKRKVEAELGDLQEQHADLQAQLAELRAQLAA 1091
Cdd:pfam01576 161 ISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1092 KEEELQATQARLEEECNQRGAAVKRVRELEVLISELQEDLEAERAARGKVEAARRDLGEELNALRTELEDSLGTTAAQQE 1171
Cdd:pfam01576 241 KEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1172 LRAKREQEVSMLKKAMEDEGRSHEAQVQDLRQKHSQAVEELTEQLEQAKRVRAGLEKAKQALEKESADLSADLRSLASAK 1251
Cdd:pfam01576 321 LRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1252 QDVEHKKKKVEGQLNELNSRFNESERQRTELGERVSKLTTELDSVTGLLNEAEGKNIKLSKDVSSLSSQLQDAQELLSEE 1331
Cdd:pfam01576 401 QDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1332 TRQKLNLSGRLRQTEEDRNSLMEQLEEETEAKRAVERQVSSLNMQLSDSKKKLDEMSGTVEALEEGKKRLQRELEAANSD 1411
Cdd:pfam01576 481 TRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQ 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1412 YEEKASAYDKLEKSRGRMQQELEDVLMDLDSQRQLVSNLEKKQKKFDQMLAEERAVSCKFAEERDRAEAEAREKETRVLA 1491
Cdd:pfam01576 561 LEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALS 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1492 LARALEENQGALEEAEKTMKGLRADMEDLISSKDDVGKSVHDLEKAKRGLEAIVDEMRTQMEELEDELQVAEDAKLRLDV 1571
Cdd:pfam01576 641 LARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEV 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1572 NTQALRAQHERELHARDELGEEKRKQLLKQVRELEAELEEERKQRGQASGSKKKLEGELKDMEDQLEATSRGRDEAVKQL 1651
Cdd:pfam01576 721 NMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQL 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1652 RKIQGQVKDLQRDLEDSRAAQKEVLASARESERRSKAMEADIVQLHEMLAAVERARKQAEVERDELSEELASNSSGKSLM 1731
Cdd:pfam01576 801 KKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSAL 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1732 SDEKRRLDTKISQLEEELEEEQANVESLNDRLRKSQQLVEQLGAELAAERSTSQSREGSRQQLERQNRELKAKMQEMEGQ 1811
Cdd:pfam01576 881 QDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGT 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1812 GRSKLKASIAALEAKLREAEEQLEIESRERQANGKNLRQKEKKLKDLTIQMEDERKQAQQYKDQAEKGNVRVKQLKHQLE 1891
Cdd:pfam01576 961 VKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLE 1040
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|.
gi 1604784239 1892 EAEEEAQRMAAARRKLQRELDEATEANDTLSRDMASLRSKL 1932
Cdd:pfam01576 1041 EAEEEASRANAARRKLQRELDDATESNESMNREVSTLKSKL 1081
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
96-775 |
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: 1303.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 96 ASVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLPIYSEKIIEMYKGKKRHEVPPHIYSITDNAYRNMMQDREDQSILCTG 175
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 176 ESGAGKTENTKKVIQYLAVVASSHKGKKDATPQpqqagslaYGELEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKLN 255
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASSKKKKESGKK--------KGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIH 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 256 FDVTGYIVGANIDTYLLEKSRCIRQSMTERAFHIFYYMVAGAKDKLREELLLEDFSCYRFLVA-GHVEISGQEDDEMFIE 334
Cdd:cd01377 153 FGSTGKIAGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYFFLSqGELTIDGVDDAEEFKL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 335 TLEAMEIMGFTEEERMGMMKVVSTVLQLGNIKFEKERNSEQATMPDDTAAQKVCHLQGINITDFIRAILTPRIKVGREVV 414
Cdd:cd01377 233 TDEAFDILGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 415 QKAQTKQQADFAVEALAKAMYERLFRWILARVNKTLDKsKRQSSSFLGILDIAGFEIFEDNSFEQLCINYTNERLQQLFN 494
Cdd:cd01377 313 TKGQNKEQVVFSVGALAKALYERLFLWLVKRINKTLDT-KSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFN 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 495 HTMFVLEQEEYKREGIQWSFIDFGLDLQPCIELIERPNnpPGILALLDEECWFPKATDVSFVEKLLNTHTGHVK-FSKPK 573
Cdd:cd01377 392 HHMFVLEQEEYKKEGIEWTFIDFGLDLQPTIDLIEKPN--MGILSILDEECVFPKATDKTFVEKLYSNHLGKSKnFKKPK 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 574 QHKDKLMFTVLHYAGKVDYNAANWLTKNMDPLNDNVTALLNNSSSNFIQDLWKDADRvvgletitkMSESSAPPKSKKGM 653
Cdd:cd01377 470 PKKSEAHFILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEE---------SGGGGGKKKKKGGS 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 654 FRTVGQLYKESLGKLMTTLHNTQPNFVRCIIPNHEKRAGKMDSNLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 733
Cdd:cd01377 541 FRTVSQLHKEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYS 620
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1604784239 734 ILAANAIPKGFMDGKQACCLMVKHLDLDPNLYRIGQSKMFFR 775
Cdd:cd01377 621 ILAPNAIPKGFDDGKAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
96-775 |
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: 1175.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 96 ASVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLPIYSEKIIEMYKGKKRHEVPPHIYSITDNAYRNMMQDREDQSILCTG 175
Cdd:cd14920 1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 176 ESGAGKTENTKKVIQYLAVVASSHKGKKDATpqpqqagslAYGELEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKLN 255
Cdd:cd14920 81 ESGAGKTENTKKVIQYLAHVASSHKGRKDHN---------IPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRIN 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 256 FDVTGYIVGANIDTYLLEKSRCIRQSMTERAFHIFYYMVAGAKDKLREELLLEDFSCYRFLVAGHVEISGQEDDEMFIET 335
Cdd:cd14920 152 FDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQET 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 336 LEAMEIMGFTEEERMGMMKVVSTVLQLGNIKFEKERNSEQATMPDDTAAQKVCHLQGINITDFIRAILTPRIKVGREVVQ 415
Cdd:cd14920 232 MEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 416 KAQTKQQADFAVEALAKAMYERLFRWILARVNKTLDKSKRQSSSFLGILDIAGFEIFEDNSFEQLCINYTNERLQQLFNH 495
Cdd:cd14920 312 KAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNH 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 496 TMFVLEQEEYKREGIQWSFIDFGLDLQPCIELIERPNNPPGILALLDEECWFPKATDVSFVEKLLNTHTGHVKFSKPKQH 575
Cdd:cd14920 392 TMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQL 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 576 KDKLMFTVLHYAGKVDYNAANWLTKNMDPLNDNVTALLNNSSSNFIQDLWKDADRVVGLETITKMSESS--APPKSKKGM 653
Cdd:cd14920 472 KDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTETAfgSAYKTKKGM 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 654 FRTVGQLYKESLGKLMTTLHNTQPNFVRCIIPNHEKRAGKMDSNLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 733
Cdd:cd14920 552 FRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 631
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1604784239 734 ILAANAIPKGFMDGKQACCLMVKHLDLDPNLYRIGQSKMFFR 775
Cdd:cd14920 632 ILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
96-775 |
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: 1157.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 96 ASVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLPIYSEKIIEMYKGKKRHEVPPHIYSITDNAYRNMMQDREDQSILCTG 175
Cdd:cd14921 1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 176 ESGAGKTENTKKVIQYLAVVASSHKGKKDATpqpqqagslAYGELEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKLN 255
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVVASSHKGKKDTS---------ITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 256 FDVTGYIVGANIDTYLLEKSRCIRQSMTERAFHIFYYMVAGAKDKLREELLLEDFSCYRFLVAGHVEISGQEDDEMFIET 335
Cdd:cd14921 152 FDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDDEMFQET 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 336 LEAMEIMGFTEEERMGMMKVVSTVLQLGNIKFEKERNSEQATMPDDTAAQKVCHLQGINITDFIRAILTPRIKVGREVVQ 415
Cdd:cd14921 232 LEAMSIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 416 KAQTKQQADFAVEALAKAMYERLFRWILARVNKTLDKSKRQSSSFLGILDIAGFEIFEDNSFEQLCINYTNERLQQLFNH 495
Cdd:cd14921 312 KAQTKEQADFAIEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNH 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 496 TMFVLEQEEYKREGIQWSFIDFGLDLQPCIELIERPNNPPGILALLDEECWFPKATDVSFVEKLLNTHTGHVKFSKPKQH 575
Cdd:cd14921 392 TMFILEQEEYQREGIEWNFIDFGLDLQPCIELIERPNNPPGVLALLDEECWFPKATDKSFVEKLCTEQGNHPKFQKPKQL 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 576 KDKLMFTVLHYAGKVDYNAANWLTKNMDPLNDNVTALLNNSSSNFIQDLWKDADRVVGLETITKMSESSAP--PKSKKGM 653
Cdd:cd14921 472 KDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVGLDQMAKMTESSLPsaSKTKKGM 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 654 FRTVGQLYKESLGKLMTTLHNTQPNFVRCIIPNHEKRAGKMDSNLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 733
Cdd:cd14921 552 FRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 631
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1604784239 734 ILAANAIPKGFMDGKQACCLMVKHLDLDPNLYRIGQSKMFFR 775
Cdd:cd14921 632 ILAANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
96-775 |
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: 1135.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 96 ASVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLPIYSEKIIEMYKGKKRHEVPPHIYSITDNAYRNMMQDREDQSILCTG 175
Cdd:cd14932 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 176 ESGAGKTENTKKVIQYLAVVASSHKGKKDatpqpQQAGSLAYGELEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKLN 255
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVASSFKTKKD-----QSSIALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 256 FDVTGYIVGANIDTYLLEKSRCIRQSMTERAFHIFYYMVAGAKDKLREELLLEDFSCYRFLVAGHVEISGQEDDEMFIET 335
Cdd:cd14932 156 FDVNGYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNVTIPGQQDKELFAET 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 336 LEAMEIMGFTEEERMGMMKVVSTVLQLGNIKFEKERNSEQATMPDDTAAQKVCHLQGINITDFIRAILTPRIKVGREVVQ 415
Cdd:cd14932 236 MEAFRIMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQ 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 416 KAQTKQQADFAVEALAKAMYERLFRWILARVNKTLDKSKRQSSSFLGILDIAGFEIFEDNSFEQLCINYTNERLQQLFNH 495
Cdd:cd14932 316 KAQTQEQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNH 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 496 TMFVLEQEEYKREGIQWSFIDFGLDLQPCIELIERPNNPPGILALLDEECWFPKATDVSFVEKLLNTHTGHVKFSKPKQH 575
Cdd:cd14932 396 TMFILEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNGPPGILALLDEECWFPKATDKSFVEKVVQEQGNNPKFQKPKKL 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 576 KDKLMFTVLHYAGKVDYNAANWLTKNMDPLNDNVTALLNNSSSNFIQDLWKDADRVVGLETITKMSES-SAPPKSKKGMF 654
Cdd:cd14932 476 KDDADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVDRIVGLDKVAGMGESlHGAFKTRKGMF 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 655 RTVGQLYKESLGKLMTTLHNTQPNFVRCIIPNHEKRAGKMDSNLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 734
Cdd:cd14932 556 RTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 635
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 1604784239 735 LAANAIPKGFMDGKQACCLMVKHLDLDPNLYRIGQSKMFFR 775
Cdd:cd14932 636 LTPNAIPKGFMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
84-775 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 1069.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 84 VEDMAALTFLNEASVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLPIYSEKIIEMYKGKKRHEVPPHIYSITDNAYRNMM 163
Cdd:pfam00063 1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 164 QDREDQSILCTGESGAGKTENTKKVIQYLAVVASSHKGKKdatpqpqqagslaYGELEKQLLQANPILEAFGNAKTIKND 243
Cdd:pfam00063 81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAGN-------------VGRLEEQILQSNPILEAFGNAKTVRNN 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 244 NSSRFGKFIKLNFDVTGYIVGANIDTYLLEKSRCIRQSMTERAFHIFYYMVAGAKDKLREELLLEDFSCYRFLVA-GHVE 322
Cdd:pfam00063 148 NSSRFGKYIEIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYLSQsGCYT 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 323 ISGQEDDEMFIETLEAMEIMGFTEEERMGMMKVVSTVLQLGNIKFEKERNSEQATMPDDTAAQKVCHLQGINITDFIRAI 402
Cdd:pfam00063 228 IDGIDDSEEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKAL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 403 LTPRIKVGREVVQKAQTKQQADFAVEALAKAMYERLFRWILARVNKTLDKSKRQSSSFLGILDIAGFEIFEDNSFEQLCI 482
Cdd:pfam00063 308 CKRRIKTGRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTIEKASFIGVLDIYGFEIFEKNSFEQLCI 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 483 NYTNERLQQLFNHTMFVLEQEEYKREGIQWSFIDFGlDLQPCIELIERPnnPPGILALLDEECWFPKATDVSFVEKLLNT 562
Cdd:pfam00063 388 NYVNEKLQQFFNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEKK--PLGILSLLDEECLFPKATDQTFLDKLYST 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 563 HTGHVKFSKPKQhKDKLMFTVLHYAGKVDYNAANWLTKNMDPLNDNVTALLNNSSSNFIQDLWKDADRVVglETITKMSE 642
Cdd:pfam00063 465 FSKHPHFQKPRL-QGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAE--SAAANESG 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 643 SSAPPKSKKGMFRTVGQLYKESLGKLMTTLHNTQPNFVRCIIPNHEKRAGKMDSNLVLEQLRCNGVLEGIRICRQGFPNR 722
Cdd:pfam00063 542 KSTPKRTKKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNR 621
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 1604784239 723 IVFQEFRQRYEILAANAIPKGFMDGKQACCLMVKHLDLDPNLYRIGQSKMFFR 775
Cdd:pfam00063 622 ITFQEFVQRYRILAPKTWPKWKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
96-775 |
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: 1066.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 96 ASVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLPIYSEKIIEMYKGKKRHEVPPHIYSITDNAYRNMMQDREDQSILCTG 175
Cdd:cd14911 1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 176 ESGAGKTENTKKVIQYLAVVASSHKGKKDATPQPQQAGSLAYGELEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKLN 255
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVAASKPKGSGAVPHPAVNPAVLIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 256 FDVTGYIVGANIDTYLLEKSRCIRQSMTERAFHIFYYMVAGAKDKLREELLLEDFSCYRFLVAGHVEISGQEDDEMFIET 335
Cdd:cd14911 161 FDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVPGVDDYAEFQAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 336 LEAMEIMGFTEEERMGMMKVVSTVLQLGNIKFEKERNSEQATMPDDTAAQKVCHLQGINITDFIRAILTPRIKVGREVVQ 415
Cdd:cd14911 241 VKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFVT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 416 KAQTKQQADFAVEALAKAMYERLFRWILARVNKTLDKSKRQSSSFLGILDIAGFEIFEDNSFEQLCINYTNERLQQLFNH 495
Cdd:cd14911 321 KAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 496 TMFVLEQEEYKREGIQWSFIDFGLDLQPCIELIERPNnppGILALLDEECWFPKATDVSFVEKLLNTHTGHVKFSKpKQH 575
Cdd:cd14911 401 TMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPG---GIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMK-TDF 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 576 KDKLMFTVLHYAGKVDYNAANWLTKNMDPLNDNVTALLNNSSSNFIQDLWKDADrVVGLETITkMSESSAPPKSKKGMFR 655
Cdd:cd14911 477 RGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAE-IVGMAQQA-LTDTQFGARTRKGMFR 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 656 TVGQLYKESLGKLMTTLHNTQPNFVRCIIPNHEKRAGKMDSNLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 735
Cdd:cd14911 555 TVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELL 634
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 1604784239 736 AANAIPKGFMDGKQACCLMVKHLDLDPNLYRIGQSKMFFR 775
Cdd:cd14911 635 TPNVIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
96-775 |
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: 1063.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 96 ASVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLPIYSEKIIEMYKGKKRHEVPPHIYSITDNAYRNMMQDREDQSILCTG 175
Cdd:cd15896 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 176 ESGAGKTENTKKVIQYLAVVASSHKGKKDatpqpQQAGSLAYGELEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKLN 255
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVASSHKTKKD-----QNSLALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 256 FDVTGYIVGANIDTYLLEKSRCIRQSMTERAFHIFYYMVAGAKDKLREELLLEDFSCYRFLVAGHVEISGQEDDEMFIET 335
Cdd:cd15896 156 FDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYNNYRFLSNGNVTIPGQQDKDLFTET 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 336 LEAMEIMGFTEEERMGMMKVVSTVLQLGNIKFEKERNSEQATMPDDTAAQKVCHLQGINITDFIRAILTPRIKVGREVVQ 415
Cdd:cd15896 236 MEAFRIMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQ 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 416 KAQTKQQADFAVEALAKAMYERLFRWILARVNKTLDKSKRQSSSFLGILDIAGFEIFEDNSFEQLCINYTNERLQQLFNH 495
Cdd:cd15896 316 KAQTQEQAEFAVEALAKATYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNH 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 496 TMFVLEQEEYKREGIQWSFIDFGLDLQPCIELIERPNNPPGILALLDEECWFPKATDVSFVEKLLNTHTGHVKFSKPKQH 575
Cdd:cd15896 396 TMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIEKPASPPGILALLDEECWFPKATDKSFVEKVLQEQGTHPKFFKPKKL 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 576 KDKLMFTVLHYAGKVDYNAANWLTKNMDPLNDNVTALLNNSSSNFIQDLWKDADRVVGLETITKMSESSAPPKSKKGMFR 655
Cdd:cd15896 476 KDEADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVDRIVGLDKVSGMSEMPGAFKTRKGMFR 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 656 TVGQLYKESLGKLMTTLHNTQPNFVRCIIPNHEKRAGKMDSNLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 735
Cdd:cd15896 556 TVGQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 635
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 1604784239 736 AANAIPKGFMDGKQACCLMVKHLDLDPNLYRIGQSKMFFR 775
Cdd:cd15896 636 TPNAIPKGFMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
96-775 |
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: 1055.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 96 ASVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLPIYSEKIIEMYKGKKRHEVPPHIYSITDNAYRNMMQDREDQSILCTG 175
Cdd:cd14919 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 176 ESGAGKTENTKKVIQYLAVVASSHKGKKDAtpqpqqagslayGELEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKLN 255
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHVASSHKSKKDQ------------GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 256 FDVTGYIVGANIDTYLLEKSRCIRQSMTERAFHIFYYMVAGAKDKLREELLLEDFSCYRFLVAGHVEISGQEDDEMFIET 335
Cdd:cd14919 149 FDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQET 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 336 LEAMEIMGFTEEERMGMMKVVSTVLQLGNIKFEKERNSEQATMPDDTAAQKVCHLQGINITDFIRAILTPRIKVGREVVQ 415
Cdd:cd14919 229 MEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQ 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 416 KAQTKQQADFAVEALAKAMYERLFRWILARVNKTLDKSKRQSSSFLGILDIAGFEIFEDNSFEQLCINYTNERLQQLFNH 495
Cdd:cd14919 309 KAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNH 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 496 TMFVLEQEEYKREGIQWSFIDFGLDLQPCIELIERPNNPPGILALLDEECWFPKATDVSFVEKLLNTHTGHVKFSKPKQH 575
Cdd:cd14919 389 TMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAGPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKQL 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 576 KDKLMFTVLHYAGKVDYNAANWLTKNMDPLNDNVTALLNNSSSNFIQDLWKDADRVVGLETITKMSESSAPP--KSKKGM 653
Cdd:cd14919 469 KDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGMSETALPGafKTRKGM 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 654 FRTVGQLYKESLGKLMTTLHNTQPNFVRCIIPNHEKRAGKMDSNLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 733
Cdd:cd14919 549 FRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYE 628
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1604784239 734 ILAANAIPKGFMDGKQACCLMVKHLDLDPNLYRIGQSKMFFR 775
Cdd:cd14919 629 ILTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
96-775 |
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: 1002.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 96 ASVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLPIYSEKIIEMYKGKKRHEVPPHIYSITDNAYRNMMQDREDQSILCTG 175
Cdd:cd14930 1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 176 ESGAGKTENTKKVIQYLAVVASSHKGKKD-ATPqpqqagslayGELEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKL 254
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHVASSPKGRKEpGVP----------GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 255 NFDVTGYIVGANIDTYLLEKSRCIRQSMTERAFHIFYYMVAGAKDKLREELLLEDFSCYRFLVAGHVEISGQEDdEMFIE 334
Cdd:cd14930 151 NFDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQER-ELFQE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 335 TLEAMEIMGFTEEERMGMMKVVSTVLQLGNIKFEKERNSEQATMPDDTAAQKVCHLQGINITDFIRAILTPRIKVGREVV 414
Cdd:cd14930 230 TLESLRVLGFSHEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 415 QKAQTKQQADFAVEALAKAMYERLFRWILARVNKTLDKSKRQSSSFLGILDIAGFEIFEDNSFEQLCINYTNERLQQLFN 494
Cdd:cd14930 310 QKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFN 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 495 HTMFVLEQEEYKREGIQWSFIDFGLDLQPCIELIERPNNPPGILALLDEECWFPKATDVSFVEKLLNTHTGHVKFSKPKQ 574
Cdd:cd14930 390 HTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRH 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 575 HKDKLMFTVLHYAGKVDYNAANWLTKNMDPLNDNVTALLNNSSSNFIQDLWKDADRVVGLETITKMSESSAPPKSKKGMF 654
Cdd:cd14930 470 LRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDGPPGGRPRRGMF 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 655 RTVGQLYKESLGKLMTTLHNTQPNFVRCIIPNHEKRAGKMDSNLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 734
Cdd:cd14930 550 RTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEI 629
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 1604784239 735 LAANAIPKGFMDGKQACCLMVKHLDLDPNLYRIGQSKMFFR 775
Cdd:cd14930 630 LTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
77-787 |
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: 986.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 77 NPPKFSKVEDMAALTFLNEASVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLPIYSEKIIEMYKGKKRHEVPPHIYSITD 156
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 157 NAYRNMMQDREDQSILCTGESGAGKTENTKKVIQYLAVVASSHKGKkdatpqpqqagslayGELEKQLLQANPILEAFGN 236
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNTEV---------------GSVEDQILESNPILEAFGN 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 237 AKTIKNDNSSRFGKFIKLNFDVTGYIVGANIDTYLLEKSRCIRQSMTERAFHIFYYMVAGAKDKLREELLLEDFSCYRFL 316
Cdd:smart00242 146 AKTLRNNNSSRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSPEDYRYL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 317 -VAGHVEISGQEDDEMFIETLEAMEIMGFTEEERMGMMKVVSTVLQLGNIKFEKERNSEQATMPDDT-AAQKVCHLQGIN 394
Cdd:smart00242 226 nQGGCLTVDGIDDAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAASTVKDKeELSNAAELLGVD 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 395 ITDFIRAILTPRIKVGREVVQKAQTKQQADFAVEALAKAMYERLFRWILARVNKTLDKsKRQSSSFLGILDIAGFEIFED 474
Cdd:smart00242 306 PEELEKALTKRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSF-KDGSTYFIGVLDIYGFEIFEV 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 475 NSFEQLCINYTNERLQQLFNHTMFVLEQEEYKREGIQWSFIDFGlDLQPCIELIErpNNPPGILALLDEECWFPKATDVS 554
Cdd:smart00242 385 NSFEQLCINYANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIE--KKPPGILSLLDEECRFPKGTDQT 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 555 FVEKLLNTHTGHVKFSKPKQhKDKLMFTVLHYAGKVDYNAANWLTKNMDPLNDNVTALLNNSSSNFIQDLWkdadrvvgl 634
Cdd:smart00242 462 FLEKLNQHHKKHPHFSKPKK-KGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLF--------- 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 635 etitkmsESSAPPKSKKGMFRTVGQLYKESLGKLMTTLHNTQPNFVRCIIPNHEKRAGKMDSNLVLEQLRCNGVLEGIRI 714
Cdd:smart00242 532 -------PSGVSNAGSKKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRI 604
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1604784239 715 CRQGFPNRIVFQEFRQRYEILAANAIPKGFMDGKQACCLMVKHLDLDPNLYRIGQSKMFFRTGVLAQLEEERD 787
Cdd:smart00242 605 RRAGFPYRLPFDEFLQRYRVLLPDTWPPWGGDAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELRE 677
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
96-775 |
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: 882.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 96 ASVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLPIYSEKIIEMYKGKKRH-EVPPHIYSITDNAYRNMMQDREDQSILCT 174
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 175 GESGAGKTENTKKVIQYLAVVASSHKGKKDATpqpqqagslaYGELEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKL 254
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAALSGSGSSKSSSS----------ASSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIEL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 255 NFDVTGYIVGANIDTYLLEKSRCIRQSMTERAFHIFYYMVAGAKDKLREELLLEDFSCYRFLV-----AGHVEISGQEDD 329
Cdd:cd00124 151 QFDPTGRLVGASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYYYLNdylnsSGCDRIDGVDDA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 330 EMFIETLEAMEIMGFTEEERMGMMKVVSTVLQLGNIKFEKERNSE--QATMPDDTAAQKVCHLQGINITDFIRAILTPRI 407
Cdd:cd00124 231 EEFQELLDALDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDEdsSAEVADDESLKAAAKLLGVDAEDLEEALTTRTI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 408 KVGREVVQKAQTKQQADFAVEALAKAMYERLFRWILARVNKTLD-KSKRQSSSFLGILDIAGFEIFEDNSFEQLCINYTN 486
Cdd:cd00124 311 KVGGETITKPLTVEQAEDARDALAKALYSRLFDWLVNRINAALSpTDAAESTSFIGILDIFGFENFEVNSFEQLCINYAN 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 487 ERLQQLFNHTMFVLEQEEYKREGIQWSFIDFgLDLQPCIELIERPnnPPGILALLDEECWFPKATDVSFVEKLLNTHTGH 566
Cdd:cd00124 391 EKLQQFFNQHVFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEGK--PLGILSLLDEECLFPKGTDATFLEKLYSAHGSH 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 567 VKFSKPKQhKDKLMFTVLHYAGKVDYNAANWLTKNMDPLNDNVTALLNNSSSnfiqdlwkdadrvvgletitkmsessap 646
Cdd:cd00124 468 PRFFSKKR-KAKLEFGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSGSQ---------------------------- 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 647 pkskkgmfrtvgqlYKESLGKLMTTLHNTQPNFVRCIIPNHEKRAGKMDSNLVLEQLRCNGVLEGIRICRQGFPNRIVFQ 726
Cdd:cd00124 519 --------------FRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFD 584
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 1604784239 727 EFRQRYEILAANAIPKGFMDGKQACCLMVKHLDLDPNLYRIGQSKMFFR 775
Cdd:cd00124 585 EFLKRYRILAPGATEKASDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
34-1629 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 880.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 34 VWIPSEKEGFEAASIKEE---KGD-EVLVELSNGQKMTVNKDDIQ--KMNPPKFSKVEDMAALTFLNEASVLQNLRERYF 107
Cdd:COG5022 12 CWIPDEEKGWIWAEIIKEafnKGKvTEEGKKEDGESVSVKKKVLGndRIKLPKFDGVDDLTELSYLNEPAVLHNLEKRYN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 108 SSLIYTYSGLFCVVVNPYKMLPIYSEKIIEMYKGKKRHEVPPHIYSITDNAYRNMMQDREDQSILCTGESGAGKTENTKK 187
Cdd:COG5022 92 NGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTENAKR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 188 VIQYLAVVASSHkgkkdaTPQPQQagslaygeLEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKLNFDVTGYIVGANI 267
Cdd:COG5022 172 IMQYLASVTSSS------TVEISS--------IEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 268 DTYLLEKSRCIRQSMTERAFHIFYYMVAGAKDKLREELLLEDFSCYRFLVAGHV-EISGQEDDEMFIETLEAMEIMGFTE 346
Cdd:COG5022 238 ETYLLEKSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLSQGGCdKIDGIDDAKEFKITLDALKTIGIDE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 347 EERMGMMKVVSTVLQLGNIKFEKERNsEQATMPDDTAAQKVCHLQGINITDFIRAILTPRIKVGREVVQKAQTKQQADFA 426
Cdd:COG5022 318 EEQDQIFKILAAILHIGNIEFKEDRN-GAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALAI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 427 VEALAKAMYERLFRWILARVNKTLDKSKRQsSSFLGILDIAGFEIFEDNSFEQLCINYTNERLQQLFNHTMFVLEQEEYK 506
Cdd:COG5022 397 RDSLAKALYSNLFDWIVDRINKSLDHSAAA-SNFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYV 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 507 REGIQWSFIDFgLDLQPCIELIERpNNPPGILALLDEECWFPKATDVSFVEKL---LNTHTGHvKFSKPKQHKDKlmFTV 583
Cdd:COG5022 476 KEGIEWSFIDY-FDNQPCIDLIEK-KNPLGILSLLDEECVMPHATDESFTSKLaqrLNKNSNP-KFKKSRFRDNK--FVV 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 584 LHYAGKVDYNAANWLTKNMDPLNDNVTALLNNSSSNFIQDLWKDADRvvgletitkmsessappKSKKGMFRTVGQLYKE 663
Cdd:COG5022 551 KHYAGDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDEEN-----------------IESKGRFPTLGSRFKE 613
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 664 SLGKLMTTLHNTQPNFVRCIIPNHEKRAGKMDSNLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANA---- 739
Cdd:COG5022 614 SLNSLMSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSKswtg 693
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 740 IPKGFMDGKQACCLMVKHLDLDPNLYRIGQSKMFFRTGVLAQLEEERDLKLTVVIIAFQAQARGFLARKAFSKRQQQLTA 819
Cdd:COG5022 694 EYTWKEDTKNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKK 773
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 820 MKVIQRNCACYLKLKNWQWWRLFTKVKPLLQVTRQEEEMGQKDEELKaakevaaKVETELKDITQKHTQLMEERAQLEMK 899
Cdd:COG5022 774 IQVIQHGFRLRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACII-------KLQKTIKREKKLRETEEVEFSLKAEV 846
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 900 LHAETELYAEAEEmRVRLEAKKQELEEVLhemesrleeeedrsnalhnerkemeqqlqlmeahiAEEEDARQKLQMEKVS 979
Cdd:COG5022 847 LIQKFGRSLKAKK-RFSLLKKETIYLQSA-----------------------------------QRVELAERQLQELKID 890
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 980 VEgKVKKLEEdilmmedQNNKLQKErkLLEERLADMSSNLAEEEEKSKNLSKLK-TKHESMISELELRM--KKEEKGRLD 1056
Cdd:COG5022 891 VK-SISSLKL-------VNLELESE--IIELKKSLSSDLIENLEFKTELIARLKkLLNNIDLEEGPSIEyvKLPELNKLH 960
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1057 MEKAKrkveaeLGDLQEQHADLQAQLAELRAQLAAKEEELQATQARLEEECNQRGAAVKRVRELEVLISELQEDLEAERa 1136
Cdd:COG5022 961 EVESK------LKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQLKELPVEVAELQSASK- 1033
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1137 argkveaarrdlgeELNALRTELedslgttaaqqelraKREQEVSMLKKAMEDEGRSHEAQVQDLRQKHSQAVEELTeQL 1216
Cdd:COG5022 1034 --------------IISSESTEL---------------SILKPLQKLKGLLLLENNQLQARYKALKLRRENSLLDDK-QL 1083
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1217 EQAKRVRaGLEKAKQALEKESADLSADLRSLASAKQDVEHKKKKVEGQLNELNSRFNESERQRTelgERVSKLTTELDSV 1296
Cdd:COG5022 1084 YQLESTE-NLLKTINVKDLEVTNRNLVKPANVLQFIVAQMIKLNLLQEISKFLSQLVNTLEPVF---QKLSVLQLELDGL 1159
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1297 TGLLNEAEgkniKLSKDVSSLSSqlqdaQELLSEETRQKLNLSGRLrqteedrnSLMEQLEEETEAKRAVERQVSSLNMQ 1376
Cdd:COG5022 1160 FWEANLEA----LPSPPPFAALS-----EKRLYQSALYDEKSKLSS--------SEVNDLKNELIALFSKIFSGWPRGDK 1222
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1377 LSDSKKKLDEMSGTVEALEEGKKRLQRELEAANSDYEEKASAYDKLEKSrgRMQQELEDVLMDLdSQRQLVSNLekKQKK 1456
Cdd:COG5022 1223 LKKLISEGWVPTEYSTSLKGFNNLNKKFDTPASMSNEKLLSLLNSIDNL--LSSYKLEEEVLPA-TINSLLQYI--NVGL 1297
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1457 FDQMLAEERAVSCKFAEE--RDRAEAEAREKETRVLALARALEEnqgaLEEAEKTMKGLRADMEDLiSSKDDVGKSVHDL 1534
Cdd:COG5022 1298 FNALRTKASSLRWKSATEvnYNSEELDDWCREFEISDVDEELEE----LIQAVKVLQLLKDDLNKL-DELLDACYSLNPA 1372
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1535 EKAKRGLEaivDEMRTQMEELEDELQVAEDAKLRLDVNTQALRAQHERELHARDELGEEKRKQLLKqvreLEAELEEERK 1614
Cdd:COG5022 1373 EIQNLKSR---YDPADKENNLPKEILKKIEALLIKQELQLSLEGKDETEVHLSEIFSEEKSLISLD----RNSIYKEEVL 1445
|
1610
....*....|....*
gi 1604784239 1615 QRGQASGSKKKLEGE 1629
Cdd:COG5022 1446 SSLSALLTKEKIALL 1460
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
96-775 |
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: 789.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 96 ASVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLPIYSEKIIEMYKGKKRHEVPPHIYSITDNAYRNMMQDREDQSILCTG 175
Cdd:cd14927 1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 176 ESGAGKTENTKKVIQYLAVVASSHKGKKDATPQPqqaGSLAYGELEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKLN 255
Cdd:cd14927 81 ESGAGKTVNTKRVIQYFAIVAALGDGPGKKAQFL---ATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 256 FDVTGYIVGANIDTYLLEKSRCIRQSMTERAFHIFYYMVAGAKDKLREELLLEDFSC-YRFLVAGHVEISGQEDDEMFIE 334
Cdd:cd14927 158 FGPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLVSMNPYdYHFCSQGVTTVDNMDDGEELMA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 335 TLEAMEIMGFTEEERMGMMKVVSTVLQLGNIKFEKERNSEQATMPDDTAAQKVCHLQGINITDFIRAILTPRIKVGREVV 414
Cdd:cd14927 238 TDHAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 415 QKAQTKQQADFAVEALAKAMYERLFRWILARVNKTLDKS-KRQssSFLGILDIAGFEIFEDNSFEQLCINYTNERLQQLF 493
Cdd:cd14927 318 TKGQSVEQVVYAVGALAKATYDRMFKWLVSRINQTLDTKlPRQ--FFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFF 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 494 NHTMFVLEQEEYKREGIQWSFIDFGLDLQPCIELIERPNnppGILALLDEECWFPKATDVSFVEKLLNTHTGHV-KFSKP 572
Cdd:cd14927 396 NHHMFILEQEEYKREGIEWVFIDFGLDLQACIDLIEKPL---GILSILEEECMFPKASDASFKAKLYDNHLGKSpNFQKP 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 573 ---KQHKDKLMFTVLHYAGKVDYNAANWLTKNMDPLNDNVTALLNNSSSNFIQDLWKDadrVVGLETITKMSESSAPPKS 649
Cdd:cd14927 473 rpdKKRKYEAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYEN---YVGSDSTEDPKSGVKEKRK 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 650 KKGMFRTVGQLYKESLGKLMTTLHNTQPNFVRCIIPNHEKRAGKMDSNLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFR 729
Cdd:cd14927 550 KAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFK 629
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1604784239 730 QRYEILAANAIPK-GFMDGKQACCLMVKHLDLDPNLYRIGQSKMFFR 775
Cdd:cd14927 630 QRYRILNPSAIPDdKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
97-775 |
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: 767.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 97 SVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLPIYSEKIIEMYKGKKRHEVPPHIYSITDNAYRNMMQDREDQSILCTGE 176
Cdd:cd14913 2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 177 SGAGKTENTKKVIQYLAVVASSH--KGKKDATPQpqqagslayGELEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKL 254
Cdd:cd14913 82 SGAGKTVNTKRVIQYFATIAATGdlAKKKDSKMK---------GTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 255 NFDVTGYIVGANIDTYLLEKSRCIRQSMTERAFHIFYYMVAGAKDKLREELLLEDFSC-YRFLVAGHVEISGQEDDEMFI 333
Cdd:cd14913 153 HFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPYdYPFISQGEILVASIDDAEELL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 334 ETLEAMEIMGFTEEERMGMMKVVSTVLQLGNIKFEKERNSEQATmPDDT-AAQKVCHLQGINITDFIRAILTPRIKVGRE 412
Cdd:cd14913 233 ATDSAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKTAYLMGLNSSDLLKALCFPRVKVGNE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 413 VVQKAQTKQQADFAVEALAKAMYERLFRWILARVNKTLDkSKRQSSSFLGILDIAGFEIFEDNSFEQLCINYTNERLQQL 492
Cdd:cd14913 312 YVTKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLD-TKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQF 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 493 FNHTMFVLEQEEYKREGIQWSFIDFGLDLQPCIELIERPNnppGILALLDEECWFPKATDVSFVEKLLNTHTGH-VKFSK 571
Cdd:cd14913 391 FNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYDQHLGKsNNFQK 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 572 PKQHKDK--LMFTVLHYAGKVDYNAANWLTKNMDPLNDNVTALLNNSSSNFIQDLWKDadrvvgLETITKMSESSAPPKS 649
Cdd:cd14913 468 PKVVKGRaeAHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYAT------FATADADSGKKKVAKK 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 650 KKGMFRTVGQLYKESLGKLMTTLHNTQPNFVRCIIPNHEKRAGKMDSNLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFR 729
Cdd:cd14913 542 KGSSFQTVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFK 621
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1604784239 730 QRYEILAANAIPKG-FMDGKQACCLMVKHLDLDPNLYRIGQSKMFFR 775
Cdd:cd14913 622 QRYRVLNASAIPEGqFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
96-775 |
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: 752.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 96 ASVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLPIYSEKIIEMYKGKKRHEVPPHIYSITDNAYRNMMQDREDQSILCTG 175
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 176 ESGAGKTENTKKVIQYLAVVASSHKGKKDATPQpqqagslayGELEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKLN 255
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGASKKTDEAAKSK---------GSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIH 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 256 FDVTGYIVGANIDTYLLEKSRCIRQSMTERAFHIFYYMVAGAKDKLREELLL-EDFSCYRFLVAGHVEISGQEDDEMFIE 334
Cdd:cd14909 152 FGPTGKLAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLsDNIYDYYIVSQGKVTVPNVDDGEEFSL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 335 TLEAMEIMGFTEEERMGMMKVVSTVLQLGNIKFEKERNSEQATMPDDTAAQKVCHLQGINITDFIRAILTPRIKVGREVV 414
Cdd:cd14909 232 TDQAFDILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 415 QKAQTKQQADFAVEALAKAMYERLFRWILARVNKTLD-KSKRQssSFLGILDIAGFEIFEDNSFEQLCINYTNERLQQLF 493
Cdd:cd14909 312 TQGRNVQQVTNSIGALCKGVFDRLFKWLVKKCNETLDtQQKRQ--HFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFF 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 494 NHTMFVLEQEEYKREGIQWSFIDFGLDLQPCIELIERPNnppGILALLDEECWFPKATDVSFVEKLLNTHTGH-VKFSKP 572
Cdd:cd14909 390 NHHMFVLEQEEYKREGIDWAFIDFGMDLLACIDLIEKPM---GILSILEEESMFPKATDQTFSEKLTNTHLGKsAPFQKP 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 573 KQHKDKLM---FTVLHYAGKVDYNAANWLTKNMDPLNDNVTALLNNSSSNFIQDLWKDADrvvgletitkmSESSAPPKS 649
Cdd:cd14909 467 KPPKPGQQaahFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHA-----------GQSGGGEQA 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 650 KKGM------FRTVGQLYKESLGKLMTTLHNTQPNFVRCIIPNHEKRAGKMDSNLVLEQLRCNGVLEGIRICRQGFPNRI 723
Cdd:cd14909 536 KGGRgkkgggFATVSSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRM 615
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 1604784239 724 VFQEFRQRYEILAANAIpKGFMDGKQACCLMVKHLDLDPNLYRIGQSKMFFR 775
Cdd:cd14909 616 MYPDFKMRYKILNPAGI-QGEEDPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
96-775 |
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: 743.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 96 ASVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLPIYSEKIIEMYKGKKRHEVPPHIYSITDNAYRNMMQDREDQSILCTG 175
Cdd:cd14934 1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 176 ESGAGKTENTKKVIQYLAVVASSHKGKKDATpqpqqagslayGELEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKLN 255
Cdd:cd14934 81 ESGAGKTENTKKVIQYFANIGGTGKQSSDGK-----------GSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIH 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 256 FDVTGYIVGANIDTYLLEKSRCIRQSMTERAFHIFYYMVAGAKDKLREELLL-EDFSCYRFLVAGHVEISGQEDDEMFIE 334
Cdd:cd14934 150 FGTTGKLAGADIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLLvPNPKEYHWVSQGVTVVDNMDDGEELQI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 335 TLEAMEIMGFTEEERMGMMKVVSTVLQLGNIKFEKERNSEQATMPDDTAAQKVCHLQGINITDFIRAILTPRIKVGREVV 414
Cdd:cd14934 230 TDVAFDVLGFSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 415 QKAQTKQQADFAVEALAKAMYERLFRWILARVNKTLDkSKRQSSSFLGILDIAGFEIFEDNSFEQLCINYTNERLQQLFN 494
Cdd:cd14934 310 QKGQNMEQCNNSIGALGKAVYDKMFKWLVVRINKTLD-TKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFN 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 495 HTMFVLEQEEYKREGIQWSFIDFGLDLQPCIELIERPNnppGILALLDEECWFPKATDVSFVEKLLNTHTGHV-KFSKPK 573
Cdd:cd14934 389 HHMFVLEQEEYKREGIEWVFIDFGLDLQACIDLLEKPM---GIFSILEEQCVFPKATDATFKAALYDNHLGKSsNFLKPK 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 574 QHKDK---LMFTVLHYAGKVDYNAANWLTKNMDPLNDNVTALLNNSSsnfiqdlwkdadrvVGLETITKMSESSA--PPK 648
Cdd:cd14934 466 GGKGKgpeAHFELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSS--------------LGLLALLFKEEEAPagSKK 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 649 SKKGM-FRTVGQLYKESLGKLMTTLHNTQPNFVRCIIPNHEKRAGKMDSNLVLEQLRCNGVLEGIRICRQGFPNRIVFQE 727
Cdd:cd14934 532 QKRGSsFMTVSNFYREQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPE 611
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 1604784239 728 FRQRYEILAANAIPKGFMDGKQACCLMVKHLDLDPNLYRIGQSKMFFR 775
Cdd:cd14934 612 FKQRYQVLNPNVIPQGFVDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
96-775 |
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: 705.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 96 ASVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLPIYSEKIIEMYKGKKRHEVPPHIYSITDNAYRNMMQDREDQSILCTG 175
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 176 ESGAGKTENTKKVIQYLAVVASSHKGKKDatpqpqqagslaYGELEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKLN 255
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAMIESKKK------------LGALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMH 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 256 FDVTGYIVGANIDTYLLEKSRCIRQSMTERAFHIFYYMVAGAKDkLREELLL-EDFSCYRFLVAGHVEISGQEDDEMFIE 334
Cdd:cd14929 149 FGARGMLSSADIDIYLLEKSRVIFQQPGERNYHIFYQILSGKKE-LRDLLLVsANPSDFHFCSCGAVAVESLDDAEELLA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 335 TLEAMEIMGFTEEERMGMMKVVSTVLQLGNIKFEKERNSEQATMPDDTAAQKVCHLQGINITDFIRAILTPRIKVGREVV 414
Cdd:cd14929 228 TEQAMDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 415 QKAQTKQQADFAVEALAKAMYERLFRWILARVNKTLDkSKRQSSSFLGILDIAGFEIFEDNSFEQLCINYTNERLQQLFN 494
Cdd:cd14929 308 TRSQNIEQVTYAVGALSKSIYERMFKWLVARINRVLD-AKLSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFN 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 495 HTMFVLEQEEYKREGIQWSFIDFGLDLQPCIELIERPNnppGILALLDEECWFPKATDVSFVEKLLNTHTGH-VKFSKPK 573
Cdd:cd14929 387 QHMFVLEQEEYRKEGIDWVSIDFGLDLQACIDLIEKPM---GIFSILEEECMFPKATDLTFKTKLFDNHFGKsVHFQKPK 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 574 QHKDKLM--FTVLHYAGKVDYNAANWLTKNMDPLNDNVTALLNNSSSNFIQDLWKDadrvvgletitKMSESSAPP---- 647
Cdd:cd14929 464 PDKKKFEahFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFEN-----------YISTDSAIQfgek 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 648 KSKKGM-FRTVGQLYKESLGKLMTTLHNTQPNFVRCIIPNHEKRAGKMDSNLVLEQLRCNGVLEGIRICRQGFPNRIVFQ 726
Cdd:cd14929 533 KRKKGAsFQTVASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYA 612
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 1604784239 727 EFRQRYEILAANAIPKG-FMDGKQACCLMVKHLDLDPNLYRIGQSKMFFR 775
Cdd:cd14929 613 DFKQRYCILNPRTFPKSkFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
97-775 |
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: 705.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 97 SVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLPIYSEKIIEMYKGKKRHEVPPHIYSITDNAYRNMMQDREDQSILCTGE 176
Cdd:cd14917 2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 177 SGAGKTENTKKVIQYLAVVAS-SHKGKKDATPqpqqagslAYGELEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKLN 255
Cdd:cd14917 82 SGAGKTVNTKRVIQYFAVIAAiGDRSKKDQTP--------GKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIH 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 256 FDVTGYIVGANIDTYLLEKSRCIRQSMTERAFHIFYYMVAGAKDKLREELLLEDFSC-YRFLVAGHVEISGQEDDEMFIE 334
Cdd:cd14917 154 FGATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYdYAFISQGETTVASIDDAEELMA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 335 TLEAMEIMGFTEEERMGMMKVVSTVLQLGNIKFEKERNSEQATmPDDT-AAQKVCHLQGINITDFIRAILTPRIKVGREV 413
Cdd:cd14917 234 TDNAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAE-PDGTeEADKSAYLMGLNSADLLKGLCHPRVKVGNEY 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 414 VQKAQTKQQADFAVEALAKAMYERLFRWILARVNKTLDkSKRQSSSFLGILDIAGFEIFEDNSFEQLCINYTNERLQQLF 493
Cdd:cd14917 313 VTKGQNVQQVIYATGALAKAVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFF 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 494 NHTMFVLEQEEYKREGIQWSFIDFGLDLQPCIELIERPNnppGILALLDEECWFPKATDVSFVEKLLNTHTGH-VKFSKP 572
Cdd:cd14917 392 NHHMFVLEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKATDMTFKAKLFDNHLGKsNNFQKP 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 573 KQHKDK--LMFTVLHYAGKVDYNAANWLTKNMDPLNDNVTALLNNSSSNFIQDLWKDadrVVGLETITKMSESsappKSK 650
Cdd:cd14917 469 RNIKGKpeAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFAN---YAGADAPIEKGKG----KAK 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 651 KG-MFRTVGQLYKESLGKLMTTLHNTQPNFVRCIIPNHEKRAGKMDSNLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFR 729
Cdd:cd14917 542 KGsSFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFR 621
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1604784239 730 QRYEILAANAIPKG-FMDGKQACCLMVKHLDLDPNLYRIGQSKMFFR 775
Cdd:cd14917 622 QRYRILNPAAIPEGqFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
97-775 |
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: 697.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 97 SVLQNLRERYF-SSLIYTYSGLFCVVVNPYKMLPIYSEKIIEMYKGKKRHEVPPHIYSITDNAYRNMMQDREDQSILCTG 175
Cdd:cd01380 2 AVLHNLKVRFCqRNAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 176 ESGAGKTENTKKVIQYLAVVASSHKGKKdatpqpqqagslaygELEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKLN 255
Cdd:cd01380 82 ESGAGKTVSAKYAMRYFATVGGSSSGET---------------QVEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEIL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 256 FDVTGYIVGANIDTYLLEKSRCIRQSMTERAFHIFYYMVAGAKDKLREELLLEDFSCYRFLVAG-HVEISGQEDDEMFIE 334
Cdd:cd01380 147 FDKNYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNQGgSPVIDGVDDAAEFEE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 335 TLEAMEIMGFTEEERMGMMKVVSTVLQLGNIKFEKERNSEQATMPDDTAAQKVCHLQGINITDFIRAILTPRIKVGREVV 414
Cdd:cd01380 227 TRKALTLLGISEEEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVI 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 415 QKAQTKQQADFAVEALAKAMYERLFRWILARVNKTLD-KSKRQSSSFLGILDIAGFEIFEDNSFEQLCINYTNERLQQLF 493
Cdd:cd01380 307 VKPLTLQQAIVARDALAKHIYAQLFDWIVDRINKALAsPVKEKQHSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQF 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 494 NHTMFVLEQEEYKREGIQWSFIDFgLDLQPCIELIErpnNPPGILALLDEECWFPKATDVSFVEKLLNTHTGHVK--FSK 571
Cdd:cd01380 387 NQHVFKLEQEEYVKEEIEWSFIDF-YDNQPCIDLIE---GKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKPNkhFKK 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 572 PKQHKDKlmFTVLHYAGKVDYNAANWLTKNMDPLNDNVTALLNNSssnfiqdlwkdadrvvgletitkmsessappKSKK 651
Cdd:cd01380 463 PRFSNTA--FIVKHFADDVEYQVEGFLEKNRDTVSEEHLNVLKAS-------------------------------KNRK 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 652 gmfRTVGQLYKESLGKLMTTLHNTQPNFVRCIIPNHEKRAGKMDSNLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQR 731
Cdd:cd01380 510 ---KTVGSQFRDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSR 586
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1604784239 732 YEILaanaIPKGF---MDGKQACCLMVKHLDLDPNLYRIGQSKMFFR 775
Cdd:cd01380 587 YRVL----LPSKEwlrDDKKKTCENILENLILDPDKYQFGKTKIFFR 629
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
98-775 |
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: 694.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 98 VLQNLRERYFSSLIYTYSGLFCVVVNPYKMLPIYSEKIIEMYKGKKRHEVPPHIYSITDNAYRNMMQDREDQSILCTGES 177
Cdd:cd14918 3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 178 GAGKTENTKKVIQYLAVVASSHKGKKDATPQPQqagslayGELEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKLNFD 257
Cdd:cd14918 83 GAGKTVNTKRVIQYFATIAVTGEKKKEESGKMQ-------GTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 258 VTGYIVGANIDTYLLEKSRCIRQSMTERAFHIFYYMVAGAKDKLREELLLEDFSC-YRFLVAGHVEISGQEDDEMFIETL 336
Cdd:cd14918 156 TTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYdYAFVSQGEITVPSIDDQEELMATD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 337 EAMEIMGFTEEERMGMMKVVSTVLQLGNIKFEKERNSEQATmPDDT-AAQKVCHLQGINITDFIRAILTPRIKVGREVVQ 415
Cdd:cd14918 236 SAIDILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLQSLNSADLLKALCYPRVKVGNEYVT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 416 KAQTKQQADFAVEALAKAMYERLFRWILARVNKTLDkSKRQSSSFLGILDIAGFEIFEDNSFEQLCINYTNERLQQLFNH 495
Cdd:cd14918 315 KGQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNH 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 496 TMFVLEQEEYKREGIQWSFIDFGLDLQPCIELIERpnnPPGILALLDEECWFPKATDVSFVEKLLNTHTGH-VKFSKPK- 573
Cdd:cd14918 394 HMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEK---PLGIFSILEEECMFPKATDTSFKNKLYDQHLGKsANFQKPKv 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 574 -QHKDKLMFTVLHYAGKVDYNAANWLTKNMDPLNDNVTALLNNSSSNFIQDLWKdadrvvglETITKMSESSAPPKSKK- 651
Cdd:cd14918 471 vKGKAEAHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFS--------TYASAEADSGAKKGAKKk 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 652 -GMFRTVGQLYKESLGKLMTTLHNTQPNFVRCIIPNHEKRAGKMDSNLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQ 730
Cdd:cd14918 543 gSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQ 622
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 1604784239 731 RYEILAANAIPKG-FMDGKQACCLMVKHLDLDPNLYRIGQSKMFFR 775
Cdd:cd14918 623 RYKVLNASAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
97-775 |
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: 693.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 97 SVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLPIYSEKIIEMYKGKKRHEVPPHIYSITDNAYRNMMQDREDQSILCTGE 176
Cdd:cd14923 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 177 SGAGKTENTKKVIQYLAVVASSHKGKKDATPQPQQagslayGELEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKLNF 256
Cdd:cd14923 82 SGAGKTVNTKRVIQYFATIAVTGDKKKEQQPGKMQ------GTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 257 DVTGYIVGANIDTYLLEKSRCIRQSMTERAFHIFYYMVAGAKDKLREELLLE----DFScyrFLVAGHVEISGQEDDEMF 332
Cdd:cd14923 156 GATGKLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLIStnpfDFP---FVSQGEVTVASIDDSEEL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 333 IETLEAMEIMGFTEEERMGMMKVVSTVLQLGNIKFEKERNSEQATmPDDT-AAQKVCHLQGINITDFIRAILTPRIKVGR 411
Cdd:cd14923 233 LATDNAIDILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAGYLMGLNSAEMLKGLCCPRVKVGN 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 412 EVVQKAQTKQQADFAVEALAKAMYERLFRWILARVNKTLDkSKRQSSSFLGILDIAGFEIFEDNSFEQLCINYTNERLQQ 491
Cdd:cd14923 312 EYVTKGQNVQQVTNSVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQ 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 492 LFNHTMFVLEQEEYKREGIQWSFIDFGLDLQPCIELIERPNnppGILALLDEECWFPKATDVSFVEKLLNTHTGHV-KFS 570
Cdd:cd14923 391 FFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYDQHLGKSnNFQ 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 571 KPKQHKDK--LMFTVLHYAGKVDYNAANWLTKNMDPLNDNVTALLNNSSSNFIQDLWKDADRVVGLETitkmSESSAPPK 648
Cdd:cd14923 468 KPKPAKGKaeAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYAGAEAGDS----GGSKKGGK 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 649 SKKGMFRTVGQLYKESLGKLMTTLHNTQPNFVRCIIPNHEKRAGKMDSNLVLEQLRCNGVLEGIRICRQGFPNRIVFQEF 728
Cdd:cd14923 544 KKGSSFQTVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADF 623
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 1604784239 729 RQRYEILAANAIPKG-FMDGKQACCLMVKHLDLDPNLYRIGQSKMFFR 775
Cdd:cd14923 624 KQRYRILNASAIPEGqFIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
97-775 |
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: 690.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 97 SVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLPIYSEKIIEMYKGKKRHEVPPHIYSITDNAYRNMMQDREDQSILCTGE 176
Cdd:cd14910 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 177 SGAGKTENTKKVIQYLAVVASSHKGKKDATPQPQQAGSlaygeLEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKLNF 256
Cdd:cd14910 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEATSGKMQGT-----LEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 257 DVTGYIVGANIDTYLLEKSRCIRQSMTERAFHIFYYMVAGAKDKLREELLLEDFSC-YRFLVAGHVEISGQEDDEMFIET 335
Cdd:cd14910 157 GTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYdYAFVSQGEITVPSIDDQEELMAT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 336 LEAMEIMGFTEEERMGMMKVVSTVLQLGNIKFEKERNSEQATmPDDT-AAQKVCHLQGINITDFIRAILTPRIKVGREVV 414
Cdd:cd14910 237 DSAIEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLQNLNSADLLKALCYPRVKVGNEYV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 415 QKAQTKQQADFAVEALAKAMYERLFRWILARVNKTLDkSKRQSSSFLGILDIAGFEIFEDNSFEQLCINYTNERLQQLFN 494
Cdd:cd14910 316 TKGQTVQQVYNAVGALAKAVYDKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFN 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 495 HTMFVLEQEEYKREGIQWSFIDFGLDLQPCIELIERPNnppGILALLDEECWFPKATDVSFVEKLLNTHTGHV-KFSKPK 573
Cdd:cd14910 395 HHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHLGKSnNFQKPK 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 574 QHKDKL--MFTVLHYAGKVDYNAANWLTKNMDPLNDNVTALLNNSSSNFIQDLWKDADRVVGletitKMSESSAPPKSKK 651
Cdd:cd14910 472 PAKGKVeaHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGAAAAEA-----EEGGGKKGGKKKG 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 652 GMFRTVGQLYKESLGKLMTTLHNTQPNFVRCIIPNHEKRAGKMDSNLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQR 731
Cdd:cd14910 547 SSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQR 626
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 1604784239 732 YEILAANAIPKG-FMDGKQACCLMVKHLDLDPNLYRIGQSKMFFR 775
Cdd:cd14910 627 YKVLNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
97-775 |
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: 690.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 97 SVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLPIYSEKIIEMYKGKKRHEVPPHIYSITDNAYRNMMQDREDQSILCTGE 176
Cdd:cd14916 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 177 SGAGKTENTKKVIQYLAVVAS-SHKGKKDATPQPQqagslayGELEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKLN 255
Cdd:cd14916 82 SGAGKTVNTKRVIQYFASIAAiGDRSKKENPNANK-------GTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIH 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 256 FDVTGYIVGANIDTYLLEKSRCIRQSMTERAFHIFYYMVAGAKDKLREELLLEDFSC-YRFLVAGHVEISGQEDDEMFIE 334
Cdd:cd14916 155 FGATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYdYAFVSQGEVSVASIDDSEELLA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 335 TLEAMEIMGFTEEERMGMMKVVSTVLQLGNIKFEKERNSEQATmPDDTA-AQKVCHLQGINITDFIRAILTPRIKVGREV 413
Cdd:cd14916 235 TDSAFDVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAE-PDGTEdADKSAYLMGLNSADLLKGLCHPRVKVGNEY 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 414 VQKAQTKQQADFAVEALAKAMYERLFRWILARVNKTLDkSKRQSSSFLGILDIAGFEIFEDNSFEQLCINYTNERLQQLF 493
Cdd:cd14916 314 VTKGQSVQQVYYSIGALAKSVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFF 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 494 NHTMFVLEQEEYKREGIQWSFIDFGLDLQPCIELIERPNnppGILALLDEECWFPKATDVSFVEKLLNTHTGH-VKFSKP 572
Cdd:cd14916 393 NHHMFVLEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKASDMTFKAKLYDNHLGKsNNFQKP 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 573 KQHKDK--LMFTVLHYAGKVDYNAANWLTKNMDPLNDNVTALLNNSSSNFIQDLWKD---ADrvvgletiTKMSESSAPP 647
Cdd:cd14916 470 RNVKGKqeAHFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTyasAD--------TGDSGKGKGG 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 648 KSKKGMFRTVGQLYKESLGKLMTTLHNTQPNFVRCIIPNHEKRAGKMDSNLVLEQLRCNGVLEGIRICRQGFPNRIVFQE 727
Cdd:cd14916 542 KKKGSSFQTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGD 621
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 1604784239 728 FRQRYEILAANAIPKG-FMDGKQACCLMVKHLDLDPNLYRIGQSKMFFR 775
Cdd:cd14916 622 FRQRYRILNPAAIPEGqFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
97-775 |
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: 688.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 97 SVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLPIYSEKIIEMYKGKKRHEVPPHIYSITDNAYRNMMQDREDQSILCTGE 176
Cdd:cd14912 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 177 SGAGKTENTKKVIQYLAVVASSHKGKKDATPQPQQAGSlaygeLEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKLNF 256
Cdd:cd14912 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEITSGKMQGT-----LEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 257 DVTGYIVGANIDTYLLEKSRCIRQSMTERAFHIFYYMVAGAKDKLREELLLEDFSC-YRFLVAGHVEISGQEDDEMFIET 335
Cdd:cd14912 157 GTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYdYPFVSQGEISVASIDDQEELMAT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 336 LEAMEIMGFTEEERMGMMKVVSTVLQLGNIKFEKERNSEQATmPDDT-AAQKVCHLQGINITDFIRAILTPRIKVGREVV 414
Cdd:cd14912 237 DSAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAE-PDGTeVADKAAYLQSLNSADLLKALCYPRVKVGNEYV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 415 QKAQTKQQADFAVEALAKAMYERLFRWILARVNKTLDkSKRQSSSFLGILDIAGFEIFEDNSFEQLCINYTNERLQQLFN 494
Cdd:cd14912 316 TKGQTVEQVTNAVGALAKAVYEKMFLWMVARINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFN 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 495 HTMFVLEQEEYKREGIQWSFIDFGLDLQPCIELIERPNnppGILALLDEECWFPKATDVSFVEKLLNTHTGH-VKFSKPK 573
Cdd:cd14912 395 HHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHLGKsANFQKPK 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 574 --QHKDKLMFTVLHYAGKVDYNAANWLTKNMDPLNDNVTALLNNSSSNFIQDLWKDADRVVGLETITKMSESSappKSKK 651
Cdd:cd14912 472 vvKGKAEAHFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSGAQTAEGASAGGGAKKGG---KKKG 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 652 GMFRTVGQLYKESLGKLMTTLHNTQPNFVRCIIPNHEKRAGKMDSNLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQR 731
Cdd:cd14912 549 SSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQR 628
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 1604784239 732 YEILAANAIPKG-FMDGKQACCLMVKHLDLDPNLYRIGQSKMFFR 775
Cdd:cd14912 629 YKVLNASAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
97-775 |
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: 676.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 97 SVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLPIYSEKIIEMYKGKKRHEVPPHIYSITDNAYRNMMQDREDQSILCTGE 176
Cdd:cd14915 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 177 SGAGKTENTKKVIQYLAVVA-SSHKGKKDATPQPQQagslayGELEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKLN 255
Cdd:cd14915 82 SGAGKTVNTKRVIQYFATIAvTGEKKKEEAASGKMQ------GTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 256 FDVTGYIVGANIDTYLLEKSRCIRQSMTERAFHIFYYMVAGAKDKLREELLLE----DFScyrFLVAGHVEISGQEDDEM 331
Cdd:cd14915 156 FGATGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITtnpyDFA---FVSQGEITVPSIDDQEE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 332 FIETLEAMEIMGFTEEERMGMMKVVSTVLQLGNIKFEKERNSEQATmPDDT-AAQKVCHLQGINITDFIRAILTPRIKVG 410
Cdd:cd14915 233 LMATDSAVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLTSLNSADLLKALCYPRVKVG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 411 REVVQKAQTKQQADFAVEALAKAMYERLFRWILARVNKTLDkSKRQSSSFLGILDIAGFEIFEDNSFEQLCINYTNERLQ 490
Cdd:cd14915 312 NEYVTKGQTVQQVYNSVGALAKAIYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQ 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 491 QLFNHTMFVLEQEEYKREGIQWSFIDFGLDLQPCIELIERPNnppGILALLDEECWFPKATDVSFVEKLLNTHTGHV-KF 569
Cdd:cd14915 391 QFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHLGKSnNF 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 570 SKPKQHKDK--LMFTVLHYAGKVDYNAANWLTKNMDPLNDNVTALLNNSSSNFIQDLWKDadrvvGLETITKMSESSAPP 647
Cdd:cd14915 468 QKPKPAKGKaeAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFSG-----GQTAEAEGGGGKKGG 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 648 KSKKGMFRTVGQLYKESLGKLMTTLHNTQPNFVRCIIPNHEKRAGKMDSNLVLEQLRCNGVLEGIRICRQGFPNRIVFQE 727
Cdd:cd14915 543 KKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYAD 622
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 1604784239 728 FRQRYEILAANAIPKG-FMDGKQACCLMVKHLDLDPNLYRIGQSKMFFR 775
Cdd:cd14915 623 FKQRYKVLNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
97-775 |
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: 640.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 97 SVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLPIYSEKIIEMYKGKKRHEVPPHIYSITDNAYRNMMQDREDQSILCTGE 176
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 177 SGAGKTENTKKVIQYLAVVASSHKgkkdatpqpqqagslaygELEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKLNF 256
Cdd:cd14883 82 SGAGKTETTKLILQYLCAVTNNHS------------------WVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCF 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 257 DVTGYIVGANIDTYLLEKSRCIRQSMTERAFHIFYYMVAGAK--DKLREELLLEDFSCYRFL-VAGHVEISGQEDDEMFI 333
Cdd:cd14883 144 DASGHIKGAIIQDYLLEQSRITFQAPGERNYHVFYQLLAGAKhsKELKEKLKLGEPEDYHYLnQSGCIRIDNINDKKDFD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 334 ETLEAMEIMGFTEEERMGMMKVVSTVLQLGNIKFEKERNSEQATMPDDTAAQK-VCHLQGINITDFIRAILTPRIKVGRE 412
Cdd:cd14883 224 HLRLAMNVLGIPEEMQEGIFSVLSAILHLGNLTFEDIDGETGALTVEDKEILKiVAKLLGVDPDKLKKALTIRQINVRGN 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 413 VVQKAQTKQQADFAVEALAKAMYERLFRWILARVNKTLDKSkRQSSSFLGILDIAGFEIFEDNSFEQLCINYTNERLQQL 492
Cdd:cd14883 304 VTEIPLKVQEARDNRDAMAKALYSRTFAWLVNHINSCTNPG-QKNSRFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKF 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 493 FNHTMFVLEQEEYKREGIQWSFIDFGlDLQPCIELIERPnnPPGILALLDEECWFPKATDVSFVEKLLNTHTGHVKFSKP 572
Cdd:cd14883 383 FNHYVFKLEQEEYEKEGINWSHIVFT-DNQECLDLIEKP--PLGILKLLDEECRFPKGTDLTYLEKLHAAHEKHPYYEKP 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 573 KQHKDKLMFTVLHYAGKVDYNAANWLTKNMDPLNDNVTALLNNSSSNFIQDLWKDADRVVGLETITKMSESSAPPKSKKG 652
Cdd:cd14883 460 DRRRWKTEFGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFTYPDLLALTGLSISLGGDTTSRGTSKG 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 653 MfRTVGQLYKESLGKLMTTLHNTQPNFVRCIIPNHEKRAGKMDSNLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 732
Cdd:cd14883 540 K-PTVGDTFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRY 618
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1604784239 733 EILAANAIPKGFMDGKQACCLMVKHLDLDPNLYRIGQSKMFFR 775
Cdd:cd14883 619 LCLDPRARSADHKETCGAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
97-775 |
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: 637.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 97 SVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLPIYSEKIIEMYKGKKRHEVPPHIYSITDNAYRNMMQDREDQSILCTGE 176
Cdd:cd01378 2 AINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 177 SGAGKTENTKKVIQYLAVVASSHKGKKDATpqpqqagslaygelEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKLNF 256
Cdd:cd01378 82 SGAGKTEASKRIMQYIAAVSGGSESEVERV--------------KDMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQF 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 257 DVTGYIVGANIDTYLLEKSRCIRQSMTERAFHIFYYMVAGAKDKLREELLLE-DFSCYRFLVAGHVEISGQEDDEMFIET 335
Cdd:cd01378 148 DFKGEPVGGHITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQrPEQYYYYSKSGCFDVDGIDDAADFKEV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 336 LEAMEIMGFTEEERMGMMKVVSTVLQLGNIKFeKERNSEQATMPDDTAAQKVCHLQGINITDFIRAILTPRIKVG---RE 412
Cdd:cd01378 228 LNAMKVIGFTEEEQDSIFRILAAILHLGNIQF-AEDEEGNAAISDTSVLDFVAYLLGVDPDQLEKALTHRTIETGgggRS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 413 VVQKAQTKQQADFAVEALAKAMYERLFRWILARVNKTLDKSKRQSSSFLGILDIAGFEIFEDNSFEQLCINYTNERLQQL 492
Cdd:cd01378 307 VYEVPLNVEQAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKKKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQI 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 493 FnhTMFVL--EQEEYKREGIQWSFIDFgLDLQPCIELIErpNNPPGILALLDEECWFP-KATDVSFVEKLLNTHTGHVKF 569
Cdd:cd01378 387 F--IELTLkaEQEEYVREGIEWTPIKY-FNNKIICDLIE--EKPPGIFAILDDACLTAgDATDQTFLQKLNQLFSNHPHF 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 570 SKPKQHKDKLM--FTVLHYAGKVDYNAANWLTKNMDPLNDNVTALLNNSSSNFIQDLWKDADrvvgletitkmsessaPP 647
Cdd:cd01378 462 ECPSGHFELRRgeFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEGV----------------DL 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 648 KSKKgmfR--TVGQLYKESLGKLMTTLHNTQPNFVRCIIPNHEKRAGKMDSNLVLEQLRCNGVLEGIRICRQGFPNRIVF 725
Cdd:cd01378 526 DSKK---RppTAGTKFKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTY 602
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 1604784239 726 QEFRQRYEILAANAIPKGFMDGKQACCLMVKHLDLDPNLYRIGQSKMFFR 775
Cdd:cd01378 603 EKFLERYKLLSPKTWPAWDGTWQGGVESILKDLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
97-775 |
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: 635.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 97 SVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLPIYSEKIIEMYKgkKRHEVPPHIYSITDNAYRNMMQDREDQSILCTGE 176
Cdd:cd01383 2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYR--QKLLDSPHVYAVADTAYREMMRDEINQSIIISGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 177 SGAGKTENTKKVIQYLAVVASSHKGkkdatpqpqqagslaygeLEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKLNF 256
Cdd:cd01383 80 SGAGKTETAKIAMQYLAALGGGSSG------------------IENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHF 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 257 DVTGYIVGANIDTYLLEKSRCIRQSMTERAFHIFYYMVAGAKDKLREELLLEDFSCYRFLV-AGHVEISGQEDDEMFIET 335
Cdd:cd01383 142 DAAGKICGAKIQTYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKSASEYKYLNqSNCLTIDGVDDAKKFHEL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 336 LEAMEIMGFTEEERMGMMKVVSTVLQLGNIKFEKERNSEQATMPDDTAAQKVCHLQGINITDFIRAILTPRIKVGREVVQ 415
Cdd:cd01383 222 KEALDTVGISKEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIV 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 416 KAQTKQQADFAVEALAKAMYERLFRWILARVNKTLDKSKRQSSSFLGILDIAGFEIFEDNSFEQLCINYTNERLQQLFNH 495
Cdd:cd01383 302 KKLTLQQAIDARDALAKAIYASLFDWLVEQINKSLEVGKRRTGRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNR 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 496 TMFVLEQEEYKREGIQWSFIDFgLDLQPCIELIERpnNPPGILALLDEECWFPKATDVSFVEKLLNTHTGHVKFskpKQH 575
Cdd:cd01383 382 HLFKLEQEEYELDGIDWTKVDF-EDNQECLDLIEK--KPLGLISLLDEESNFPKATDLTFANKLKQHLKSNSCF---KGE 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 576 KDKLmFTVLHYAGKVDYNAANWLTKNMDPLNDNVTALLNNSSSNFIQDLWK---DADRVVGLETITKMSESsappkskkg 652
Cdd:cd01383 456 RGGA-FTIRHYAGEVTYDTSGFLEKNRDLLHSDLIQLLSSCSCQLPQLFASkmlDASRKALPLTKASGSDS--------- 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 653 MFRTVGQLYKESLGKLMTTLHNTQPNFVRCIIPNHEKRAGKMDSNLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 732
Cdd:cd01383 526 QKQSVATKFKGQLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRY 605
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1604784239 733 EILAANAIpKGFMDGKQACCLMVKHLDLDPNLYRIGQSKMFFR 775
Cdd:cd01383 606 GFLLPEDV-SASQDPLSTSVAILQQFNILPEMYQVGYTKLFFR 647
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
96-775 |
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: 614.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 96 ASVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLPIYSEKIIEMYKGKKRHEVPPHIYSITDNAYRNMMQDREDQSILCTG 175
Cdd:cd01381 1 AGILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 176 ESGAGKTENTKKVIQYLAVVASSHKgkkdatpqpqqagslaygELEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKLN 255
Cdd:cd01381 81 ESGAGKTESTKLILQYLAAISGQHS------------------WIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIH 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 256 FDVTGYIVGANIDTYLLEKSRCIRQSMTERAFHIFYYMVAGAKDKLREELLLEDFSCYRFLVAGH-VEISGQEDDEMFIE 334
Cdd:cd01381 143 FNKNGVIEGAKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDASDYYYLTQGNcLTCEGRDDAAEFAD 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 335 TLEAMEIMGFTEEERMGMMKVVSTVLQLGNIKFEK--ERNSEQATMPDDTAAQKVCHLQGINITDFIRAILTPRIKVGRE 412
Cdd:cd01381 223 IRSAMKVLMFTDEEIWDIFKLLAAILHLGNIKFEAtvVDNLDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGE 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 413 VVQKAQTKQQADFAVEALAKAMYERLFRWILARVNKTLDKSKRQSSS--FLGILDIAGFEIFEDNSFEQLCINYTNERLQ 490
Cdd:cd01381 303 TVVSPLSAEQALDVRDAFVKGIYGRLFIWIVNKINSAIYKPRGTDSSrtSIGVLDIFGFENFEVNSFEQLCINFANENLQ 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 491 QLFNHTMFVLEQEEYKREGIQWSFIDFgLDLQPCIELI-ERPNNppgILALLDEECWFPKATDVSFVEKLLNTHTGHVKF 569
Cdd:cd01381 383 QFFVRHIFKLEQEEYDKEGINWQHIEF-VDNQDVLDLIaLKPMN---IMSLIDEESKFPKGTDQTMLEKLHSTHGNNKNY 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 570 SKPKQHKDKLmFTVLHYAGKVDYNAANWLTKNMDPLNDNVTALLNNSSSNFIQDLWkDADRVVGLETITKmsessaPPks 649
Cdd:cd01381 459 LKPKSDLNTS-FGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLF-NEDISMGSETRKK------SP-- 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 650 kkgmfrTVGQLYKESLGKLMTTLHNTQPNFVRCIIPNHEKRAGKMDSNLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFR 729
Cdd:cd01381 529 ------TLSSQFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFV 602
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 1604784239 730 QRYEILAANAIPKGFMDGKQACCLMVKHLDLDPNLYRIGQSKMFFR 775
Cdd:cd01381 603 ERYRVLVPGIPPAHKTDCRAATRKICCAVLGGDADYQLGKTKIFLK 648
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
96-775 |
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: 610.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 96 ASVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLP-IYSEKIIEMYKGKKRHEVPPHIYSITDNAYRNMMQDREDQSILCT 174
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 175 GESGAGKTENTKKVIQYLAvvassHKGKKDATPQPQqagslaygeLEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKL 254
Cdd:cd01384 81 GESGAGKTETTKMLMQYLA-----YMGGRAVTEGRS---------VEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 255 NFDVTGYIVGANIDTYLLEKSRCIRQSMTERAFHIFYYMVAGAKDKLREELLLEDFSCYRFLVAGH-VEISGQEDDEMFI 333
Cdd:cd01384 147 QFDDAGRISGAAIRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKDPKQFHYLNQSKcFELDGVDDAEEYR 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 334 ETLEAMEIMGFTEEERMGMMKVVSTVLQLGNIKFEKERNSEQATMPDDTAAQ--KVC-HLQGINiTDFIRAILTPRIKVG 410
Cdd:cd01384 227 ATRRAMDVVGISEEEQDAIFRVVAAILHLGNIEFSKGEEDDSSVPKDEKSEFhlKAAaELLMCD-EKALEDALCKRVIVT 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 411 R-EVVQKAQTKQQADFAVEALAKAMYERLFRWILARVNKTLDKSKRqSSSFLGILDIAGFEIFEDNSFEQLCINYTNERL 489
Cdd:cd01384 306 PdGIITKPLDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPN-SKRLIGVLDIYGFESFKTNSFEQFCINLANEKL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 490 QQLFNHTMFVLEQEEYKREGIQWSFIDFgLDLQPCIELIERpnNPPGILALLDEECWFPKATDVSFVEKLLNTHTGHVKF 569
Cdd:cd01384 385 QQHFNQHVFKMEQEEYTKEEIDWSYIEF-VDNQDVLDLIEK--KPGGIIALLDEACMFPRSTHETFAQKLYQTLKDHKRF 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 570 SKPKqhKDKLMFTVLHYAGKVDYNAANWLTKNMDPLNDNVTALLNNSSSNFIQDLWkdadrvvgletitkmsESSAPPKS 649
Cdd:cd01384 462 SKPK--LSRTDFTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLF----------------PPLPREGT 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 650 KKGM-FRTVGQLYKESLGKLMTTLHNTQPNFVRCIIPNHEKRAGKMDSNLVLEQLRCNGVLEGIRICRQGFPNRIVFQEF 728
Cdd:cd01384 524 SSSSkFSSIGSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEF 603
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1604784239 729 RQRYEILAANAiPKGFMDGKQACCLMVKHLDLDPnlYRIGQSKMFFR 775
Cdd:cd01384 604 LDRFGLLAPEV-LKGSDDEKAACKKILEKAGLKG--YQIGKTKVFLR 647
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
96-775 |
2.44e-179 |
|
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: 558.40 E-value: 2.44e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 96 ASVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLP-IYSEKIIEMYKGKKRHEVPPHIYSITDNAYRNMMQDREDQSILCT 174
Cdd:cd01382 1 ATLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 175 GESGAGKTENTKKVIQYLAvvaSSHkgkkdatpqpqqaGSLAyGELEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKL 254
Cdd:cd01382 81 GESGAGKTESTKYILRYLT---ESW-------------GSGA-GPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 255 NFDVTGYIVGANIDTYLLEKSRCIRQSMTERAFHIFYYMVAGAKDKLREELLLEDFscyrflvaghveISGQEDdemFIE 334
Cdd:cd01382 144 HFNEKSSVVGGFVSHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLLKDPL------------LDDVGD---FIR 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 335 TLEAMEIMGFTEEERMGMMKVVSTVLQLGNIKFEKERN-----------SEQATMpddTAAQkvchLQGINITDFI---- 399
Cdd:cd01382 209 MDKAMKKIGLSDEEKLDIFRVVAAVLHLGNIEFEENGSdsgggcnvkpkSEQSLE---YAAE----LLGLDQDELRvslt 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 400 -RAILTPRIKVGREVVQKAQTKQQADFAVEALAKAMYERLFRWILARVNKTLDKSKrqSSSFLGILDIAGFEIFEDNSFE 478
Cdd:cd01382 282 tRVMQTTRGGAKGTVIKVPLKVEEANNARDALAKAIYSKLFDHIVNRINQCIPFET--SSYFIGVLDIAGFEYFEVNSFE 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 479 QLCINYTNERLQQLFNHTMFVLEQEEYKREGIQWSFIDFgLDLQPCIELIERPNNppGILALLDEECWFPKATDVSFVEK 558
Cdd:cd01382 360 QFCINYCNEKLQQFFNERILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEAKLV--GILDLLDEESKLPKPSDQHFTSA 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 559 LLNTHTGHVKF-----SKPKQHK---DKLMFTVLHYAGKVDYNAANWLTKNMDPLNDNVTALLNNSSSNFIQDLWKDADR 630
Cdd:cd01382 437 VHQKHKNHFRLsiprkSKLKIHRnlrDDEGFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFESSTN 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 631 vvgletitkmSESSAPPKSKKGMFRTVGQLYKESLGKLMTTLHNTQPNFVRCIIPNHEKRAGKMDSNLVLEQLRCNGVLE 710
Cdd:cd01382 517 ----------NNKDSKQKAGKLSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVS 586
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1604784239 711 GIRICRQGFPNRIVFQEFRQRYEILAANAIPKgfMDGKQACCLMVKHLDLDPNLYRIGQSKMFFR 775
Cdd:cd01382 587 VLDLMQGGFPSRTSFHDLYNMYKKYLPPKLAR--LDPRLFCKALFKALGLNENDFKFGLTKVFFR 649
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
96-775 |
1.91e-177 |
|
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: 554.00 E-value: 1.91e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 96 ASVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLP-IYSEKIIEMYKGKKRHEVPPHIYSITDNAYRNMMQ----DREDQS 170
Cdd:cd14890 1 ASLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQsgvlDPSNQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 171 ILCTGESGAGKTENTKKVIQYLAVVASSHK-GKKDATPQPQQAGSLAYGELEKQLLQANPILEAFGNAKTIKNDNSSRFG 249
Cdd:cd14890 81 IIISGESGAGKTEATKIIMQYLARITSGFAqGASGEGEAASEAIEQTLGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 250 KFIKLNFDVTGYIVGANIDTYLLEKSRCIRQSMTERAFHIFYYMVAGAKDKLREELLLEDFSCYRFLVAGHVEISGQEDD 329
Cdd:cd14890 161 KFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPVEYFYLRGECSSIPSCDDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 330 EMFIETLEAMEIMGFTEEERMGMMKVVSTVLQLGNIKFEKERNSEQATmpDDTAAQ---KVCHLQGINITDFIRAILTPR 406
Cdd:cd14890 241 KAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTVLE--DATTLQslkLAAELLGVNEDALEKALLTRQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 407 IKVGREVVQKAQTKQQADFAVEALAKAMYERLFRWILARVNKTLdKSKRQSSSFLGILDIAGFEIFEDNSFEQLCINYTN 486
Cdd:cd14890 319 LFVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTI-SSPDDKWGFIGVLDIYGFEKFEWNTFEQLCINYAN 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 487 ERLQQLFNHTMFVLEQEEYKREGIQWSFIDFGlDLQPCIELIE-RPNNPPGILALLDEeCWFPKAT--DVSFVEKLLNTH 563
Cdd:cd14890 398 EKLQRHFNQHMFEVEQVEYSNEGIDWQYITFN-DNQACLELIEgKVNGKPGIFITLDD-CWRFKGEeaNKKFVSQLHASF 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 564 -------------TGHVKFSKPKQHKDKLmFTVLHYAGKVDYNAANWLTKNMDPLNDNVTALLNNSSSNfiqdlwkdadr 630
Cdd:cd14890 476 grksgsggtrrgsSQHPHFVHPKFDADKQ-FGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSRRS----------- 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 631 vvgletitkMSESSappkskkgmfrtVGQLYKESLGKLMTTLHNTQPNFVRCIIPNHEKRAGKMDSNLVLEQLRCNGVLE 710
Cdd:cd14890 544 ---------IREVS------------VGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGMME 602
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1604784239 711 GIRICRQGFPNRIVFQEFRQRYEILAANAipkgfMDGKQACCLMVKHLDLDPNLYRIGQSKMFFR 775
Cdd:cd14890 603 AIQIRQQGFALREEHDSFFYDFQVLLPTA-----ENIEQLVAVLSKMLGLGKADWQIGSSKIFLK 662
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
96-775 |
6.86e-174 |
|
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: 543.60 E-value: 6.86e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 96 ASVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLPIYSEKIIEMYKGKKRHEVPPHIYSITDNAYRNMMQDREDQSILCTG 175
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 176 ESGAGKTENTKKVIQYLAVVASSHKGkkdatpqpqqagslaygeLEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKLN 255
Cdd:cd14872 81 ESGAGKTEATKQCLSFFAEVAGSTNG------------------VEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIH 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 256 FDVTGYIVGANIDTYLLEKSRCIRQSMTERAFHIFYYMVAGAKdkLREELLLEDFSCYRFLVAGH-VEISGQEDDEMFIE 334
Cdd:cd14872 143 FDNRGRICGASTENYLLEKSRVVYQIKGERNFHIFYQLLASPD--PASRGGWGSSAAYGYLSLSGcIEVEGVDDVADFEE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 335 TLEAMEIMGFTEEERMGMMKVVSTVLQLGNIKFEKE---RNSEQATMPDDTAAQKVCHLQGINITDFIRAILTPRIKV-G 410
Cdd:cd14872 221 VVLAMEQLGFDDADINNVMSLIAAILKLGNIEFASGggkSLVSGSTVANRDVLKEVATLLGVDAATLEEALTSRLMEIkG 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 411 REVVQKAQTKQQADFAVEALAKAMYERLFRWILARVNKTLDKSKRQSSSFLGILDIAGFEIFEDNSFEQLCINYTNERLQ 490
Cdd:cd14872 301 CDPTRIPLTPAQATDACDALAKAAYSRLFDWLVKKINESMRPQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEKLQ 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 491 QLFNHTMFVLEQEEYKREGIQWSFIDFgLDLQPCIELIErpNNPPGILALLDEECWFPKATDVSFVEKLLNTHTGHVKFS 570
Cdd:cd14872 381 QHFNQYTFKLEEALYQSEGVKFEHIDF-IDNQPVLDLIE--KKQPGLMLALDDQVKIPKGSDATFMIAANQTHAAKSTFV 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 571 KPKQHKDKLMFTVLHYAGKVDYNAANWLTKNMDPLNDNVTALLNNSSSNFIQDLWkdadrvvgletitkmsessaPPK-- 648
Cdd:cd14872 458 YAEVRTSRTEFIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLF--------------------PPSeg 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 649 SKKGMFRTVGQLYKESLGKLMTTLHNTQPNFVRCIIPNHEKRAGKMDSNLVLEQLRCNGVLEGIRICRQGFPNRIVFQEF 728
Cdd:cd14872 518 DQKTSKVTLGGQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERF 597
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 1604784239 729 RQRYEILAAnAIPKGFM-DGKQACCLMVKHLDLDPNLYRIGQSKMFFR 775
Cdd:cd14872 598 LKRYRFLVK-TIAKRVGpDDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
96-775 |
6.30e-172 |
|
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: 540.04 E-value: 6.30e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 96 ASVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLPIYSEKIIEMYKGKKRHEVPPHIYSITDNAYRNMMQDREDQSILCTG 175
Cdd:cd01385 1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 176 ESGAGKTENTKKVIQYLavVASSHKGkkdatpqpqqAGSlaygELEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKLN 255
Cdd:cd01385 81 ESGSGKTESTNFLLHHL--TALSQKG----------YGS----GVEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVN 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 256 FDVTGYIVGANIDTYLLEKSRCIRQSMTERAFHIFYYMVAGAKDKLREELLLEDFSCYRFLVAGHVEISGQEDDEMFIET 335
Cdd:cd01385 145 YRENGMVRGAVVEKYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHYLNQSDCYTLEGEDEKYEFER 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 336 L-EAMEIMGFTEEERMGMMKVVSTVLQLGNIKFEKER--NSEQATMPDDTAAQKVCHLQGINITDFIRAILTPRIKVGRE 412
Cdd:cd01385 225 LkQAMEMVGFLPETQRQIFSVLSAVLHLGNIEYKKKAyhRDESVTVGNPEVLDIISELLRVKEETLLEALTTKKTVTVGE 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 413 VVQKAQTKQQADFAVEALAKAMYERLFRWILARVNKTLDKSKRQSSS---FLGILDIAGFEIFEDNSFEQLCINYTNERL 489
Cdd:cd01385 305 TLILPYKLPEAIATRDAMAKCLYSALFDWIVLRINHALLNKKDLEEAkglSIGVLDIFGFEDFGNNSFEQFCINYANEHL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 490 QQLFNHTMFVLEQEEYKREGIQWSFIDFgLDLQPCIELIERpnNPPGILALLDEECWFPKATDVSFVEKLLNTHTGHVKF 569
Cdd:cd01385 385 QYYFNQHIFKLEQEEYKKEGISWHNIEY-TDNTGCLQLISK--KPTGLLCLLDEESNFPGATNQTLLAKFKQQHKDNKYY 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 570 SKPKqhKDKLMFTVLHYAGKVDYNAANWLTKNMDPLNDNVTALLNNSSSNFIQDL----------W-------------K 626
Cdd:cd01385 462 EKPQ--VMEPAFIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVRELigidpvavfrWavlrafframaafR 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 627 DADR------VVGLETITKMSESSAPPKSKKGMFRTVGQLYKESLGKLMTTLHNTQPNFVRCIIPNHEKRAGKMDSNLVL 700
Cdd:cd01385 540 EAGRrraqrtAGHSLTLHDRTTKSLLHLHKKKKPPSVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVL 619
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1604784239 701 EQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILaanaIPKGFMDGKQACCLMVKHLDLDPNLYRIGQSKMFFR 775
Cdd:cd01385 620 RQLRYTGMLETVRIRRSGYSVRYTFQEFITQFQVL----LPKGLISSKEDIKDFLEKLNLDRDNYQIGKTKVFLK 690
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
96-775 |
1.69e-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: 536.58 E-value: 1.69e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 96 ASVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLPIYSEKIIEMYKGKK-RHEVPPHIYSITDNAYRNMMQDREDQSILCT 174
Cdd:cd14897 1 NTIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 175 GESGAGKTENTKKVIQYLAVVASShkgkkdatpqpqqagslAYGELEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKL 254
Cdd:cd14897 81 GESGAGKTESTKYMIKHLMKLSPS-----------------DDSDLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIEL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 255 NFDVTGYIVGANIDTYLLEKSRCIRQSMTERAFHIFYYMVAGA-KDKLReELLLEDFSCYRFLVAGHVEISGQEDDE--- 330
Cdd:cd14897 144 HFTENGQLLGAKIDDYLLEKSRVVHRGNGEKNFHIFYALFAGMsRDRLL-YYFLEDPDCHRILRDDNRNRPVFNDSEele 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 331 ----MFIETLEAMEIMGFTEEERMGMMKVVSTVLQLGNIKFEKERNSEQATMPDDTAAQKVCHLQGINITDFIRAILTPR 406
Cdd:cd14897 223 yyrqMFHDLTNIMKLIGFSEEDISVIFTILAAILHLTNIVFIPDEDTDGVTVADEYPLHAVAKLLGIDEVELTEALISNV 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 407 IKVGREVVQKAQTKQQADFAVEALAKAMYERLFRWILARVNKTL----DKSKRQSSSFLGILDIAGFEIFEDNSFEQLCI 482
Cdd:cd14897 303 NTIRGERIQSWKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLwpdkDFQIMTRGPSIGILDMSGFENFKINSFDQLCI 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 483 NYTNERLQQLFNHTMFVLEQEEYKREGIQWSFIDFGlDLQPCIELIERpnNPPGILALLDEECWFPKATDVSFVEKLLNT 562
Cdd:cd14897 383 NLSNERLQQYFNDYVFPRERSEYEIEGIEWRDIEYH-DNDDVLELFFK--KPLGILPLLDEESTFPQSTDSSLVQKLNKY 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 563 HTGHVKFSKPKqhKDKLMFTVLHYAGKVDYNAANWLTKNMDPLNDNVTALLNNSSSNFIQDLWKdadrvvgletitkmse 642
Cdd:cd14897 460 CGESPRYVASP--GNRVAFGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLFT---------------- 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 643 ssappkskkgmfrtvgQLYKESLGKLMTTLHNTQPNFVRCIIPNHEKRAGKMDSNLVLEQLRCNGVLEGIRICRQGFPNR 722
Cdd:cd14897 522 ----------------SYFKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIR 585
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 1604784239 723 IVFQEFRQRYEILAANAiPKGFMDGKQACCLMVKHLDLDPnlYRIGQSKMFFR 775
Cdd:cd14897 586 IKYEDFVKRYKEICDFS-NKVRSDDLGKCQKILKTAGIKG--YQFGKTKVFLK 635
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
96-775 |
3.46e-170 |
|
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: 533.95 E-value: 3.46e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 96 ASVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLPIYSEKIIEMYKGKKRHEVPPHIYSITDNAYRNMMQDREDQSILCTG 175
Cdd:cd01387 1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 176 ESGAGKTENTKKVIQYLAVVASShkgkkdaTPQPQQagslaygeleKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKLN 255
Cdd:cd01387 81 ESGSGKTEATKLIMQYLAAVNQR-------RNNLVT----------EQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVF 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 256 FDvTGYIVGANIDTYLLEKSRCIRQSMTERAFHIFYYMVAGAKDKLREELLLEDFSCYRFL-VAGHVEISGQEDDEMFIE 334
Cdd:cd01387 144 FE-GGVIVGAITSQYLLEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQEAEKYFYLnQGGNCEIAGKSDADDFRR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 335 TLEAMEIMGFTEEERMGMMKVVSTVLQLGNIKFEK---ERNSEQATMPDDTAAQKVCHLQGINITDFIRAILTPRIKVGR 411
Cdd:cd01387 223 LLAAMQVLGFSSEEQDSIFRILASVLHLGNVYFHKrqlRHGQEGVSVGSDAEIQWVAHLLQISPEGLQKALTFKVTETRR 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 412 EVVQKAQTKQQADFAVEALAKAMYERLFRWILARVNKTLDKSKRQSSSfLGILDIAGFEIFEDNSFEQLCINYTNERLQQ 491
Cdd:cd01387 303 ERIFTPLTIDQALDARDAIAKALYALLFSWLVTRVNAIVYSGTQDTLS-IAILDIFGFEDLSENSFEQLCINYANENLQY 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 492 LFNHTMFVLEQEEYKREGIQWSFIDFgLDLQPCIELIERpnNPPGILALLDEECWFPKATDVSFVEKLLNTHTGHVKFSK 571
Cdd:cd01387 382 YFNKHVFKLEQEEYIREQIDWTEIAF-ADNQPVINLISK--KPVGILHILDDECNFPQATDHSFLEKCHYHHALNELYSK 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 572 PKQHKDKlmFTVLHYAGKVDYNAANWLTKNMDPLNDNVTALLNNSSSNFIQDLWKDadrvVGLETITKmsessaPPKSKK 651
Cdd:cd01387 459 PRMPLPE--FTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSS----HRAQTDKA------PPRLGK 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 652 GMF-------RTVGQLYKESLGKLMTTLHNTQPNFVRCIIPNHEKRAGKMDSNLVLEQLRCNGVLEGIRICRQGFPNRIV 724
Cdd:cd01387 527 GRFvtmkprtPTVAARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLP 606
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 1604784239 725 FQEFRQRYEILAANAIPKGfMDGKQACCLMVKHLDLDP-NLYRIGQSKMFFR 775
Cdd:cd01387 607 FQVFIDRYRCLVALKLPRP-APGDMCVSLLSRLCTVTPkDMYRLGATKVFLR 657
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
96-775 |
4.62e-168 |
|
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: 528.19 E-value: 4.62e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 96 ASVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLP-IYSEKIIEMYKGKKRHEVPPHIYSITDNAYRNMMQDREDQSILCT 174
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 175 GESGAGKTENTKKVIQYLAVVASshkGKKDATPqpqqagslaygeleKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKL 254
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIAG---GLNDSTI--------------KKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 255 NFDVTGYIVGANIDTYLLEKSRCIRQSMTERAFHIFYYMVAGAKDKlrEELLLEDFSCYRFLVAGHV-EISGQEDDEMFI 333
Cdd:cd14903 144 QFDKNGTLVGAKCRTYLLEKTRVISHERPERNYHIFYQLLASPDVE--ERLFLDSANECAYTGANKTiKIEGMSDRKHFA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 334 ETLEAMEIMGFTEEERMGMMKVVSTVLQLGNIKFEKERNSEQATM--PDDTAAQKVCHLQGINITDFIRAILTPRIKVGR 411
Cdd:cd14903 222 RTKEALSLIGVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSAiaPGDQGAVYATKLLGLSPEALEKALCSRTMRAAG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 412 EVVQKAQTKQQADFAVEALAKAMYERLFRWILARVNKTLDKSKRQSSSfLGILDIAGFEIFEDNSFEQLCINYTNERLQQ 491
Cdd:cd14903 302 DVYTVPLKKDQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKMANH-IGVLDIFGFEHFKHNSFEQFCINYANEKLQQ 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 492 LFNHTMFVLEQEEYKREGIQWSFIDFgLDLQPCIELIErpnNPPGILALLDEECWFPKATDVSFVEKLLNTHTGH---VK 568
Cdd:cd14903 381 KFTQDVFKTVQIEYEEEGIRWAHIDF-ADNQDVLAVIE---DRLGIISLLNDEVMRPKGNEESFVSKLSSIHKDEqdvIE 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 569 FSKpkqhKDKLMFTVLHYAGKVDYNAANWLTKNMDPLNDNVTALLNNSSSNFIQDLWKDADRVVGlETITKMSESSAPPK 648
Cdd:cd14903 457 FPR----TSRTQFTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKEKVESPA-AASTSLARGARRRR 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 649 SKKGMFRTVGQLYKESLGKLMTTLHNTQPNFVRCIIPNHEKRAGKMDSNLVLEQLRCNGVLEGIRICRQGFPNRIVFQEF 728
Cdd:cd14903 532 GGALTTTTVGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEF 611
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 1604784239 729 RQRYEILAANAiPKGFMDGKQACCLMVKHLDLD-PNLYRIGQSKMFFR 775
Cdd:cd14903 612 LDKFWLFLPEG-RNTDVPVAERCEALMKKLKLEsPEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
96-736 |
3.41e-166 |
|
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: 523.49 E-value: 3.41e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 96 ASVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLP-IYSEKIIEMYKgKKRHEVPPHIYSITDNAYRNMMQDREDQSILCT 174
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 175 GESGAGKTENTKKVIQYLAVVASSHKGKKDatpqpqqagslaygELEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKL 254
Cdd:cd14888 80 GESGAGKTESTKYVMKFLACAGSEDIKKRS--------------LVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIEL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 255 NFDVT---------GYIVGANIDTYLLEKSRCIRQSMTERAFHIFYYMVAGAKDKLREELLLEDFSCYRFL--------- 316
Cdd:cd14888 146 QFSKLkskrmsgdrGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAREAKNTGLSYEENDEKLAKgadakpisi 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 317 ---------------VAGHVEISGQEDDEMFIETLEAMEIMGFTEEERMGMMKVVSTVLQLGNIKFEKERNSEQATMPDD 381
Cdd:cd14888 226 dmssfephlkfryltKSSCHELPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFENNEACSEGAVVSA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 382 TAAQ---KVCHLQGINITDFIRAILTPRIKVGREVVQKAQTKQQADFAVEALAKAMYERLFRWILARVNKTLDKSKRQSS 458
Cdd:cd14888 306 SCTDdleKVASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGYSKDNSL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 459 SFLGILDIAGFEIFEDNSFEQLCINYTNERLQQLFNHTMFVLEQEEYKREGIQWSFIDFGlDLQPCIELIErpNNPPGIL 538
Cdd:cd14888 386 LFCGVLDIFGFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVDLLQ--EKPLGIF 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 539 ALLDEECWFPKATDVSFVEKLLNTHTGHVKFSKPKqhKDKLMFTVLHYAGKVDYNAANWLTKNMDPLNDNVTALLNNSSS 618
Cdd:cd14888 463 CMLDEECFVPGGKDQGLCNKLCQKHKGHKRFDVVK--TDPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKN 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 619 NFIQDLWKdadrvvgletitKMSESSAPPKSKKGMFRTVGQLYKESLGKLMTTLHNTQPNFVRCIIPNHEKRAGKMDSNL 698
Cdd:cd14888 541 PFISNLFS------------AYLRRGTDGNTKKKKFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRIS 608
|
650 660 670
....*....|....*....|....*....|....*...
gi 1604784239 699 VLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILA 736
Cdd:cd14888 609 VNEQLKYGGVLQAVQVSRAGYPVRLSHAEFYNDYRILL 646
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
97-775 |
5.18e-165 |
|
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: 519.14 E-value: 5.18e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 97 SVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLPIYSEKIIEMYKGKKRHEVPPHIYSITDNAYRNMMQDREDQSILCTGE 176
Cdd:cd01379 2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 177 SGAGKTENTKKVIQYLAVVasshkgkkdatpqpqqaGSLAYGELEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKLNF 256
Cdd:cd01379 82 SGAGKTESANLLVQQLTVL-----------------GKANNRTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKF 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 257 DVTGYIVGANIDTYLLEKSRCIRQSMTERAFHIFYYMVAG-AKDKLREELLLEDFSCYRFLVAGHVEISGQEDDEMFIET 335
Cdd:cd01379 145 TSTGAVTGARISEYLLEKSRVVHQAIGERNFHIFYYIYAGlAEDKKLAKYKLPENKPPRYLQNDGLTVQDIVNNSGNREK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 336 LEAME----IMGFTEEERMGMMKVVSTVLQLGNIKFE----KERNSEQATMPDDTAAQKVCHLQGINITDFIRAiLTPRI 407
Cdd:cd01379 225 FEEIEqcfkVIGFTKEEVDSVYSILAAILHIGDIEFTevesNHQTDKSSRISNPEALNNVAKLLGIEADELQEA-LTSHS 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 408 KVGR-EVVQKAQTKQQADFAVEALAKAMYERLFRWILARVNKTLDKSKRQSSSFL--GILDIAGFEIFEDNSFEQLCINY 484
Cdd:cd01379 304 VVTRgETIIRNNTVEEATDARDAMAKALYGRLFSWIVNRINSLLKPDRSASDEPLsiGILDIFGFENFQKNSFEQLCINI 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 485 TNERLQQLFNHTMFVLEQEEYKREGIQWSFIDFG-----LDLqpcieLIERPNnppGILALLDEECWFPKATDVSFVEKL 559
Cdd:cd01379 384 ANEQIQYYFNQHIFAWEQQEYLNEGIDVDLIEYEdnrplLDM-----FLQKPM---GLLALLDEESRFPKATDQTLVEKF 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 560 LNTHTGHVkFSKPKqhKDKLMFTVLHYAGKVDYNAANWLTKNMDPLNDNVTALLNNSSSNFIQdlwkdadrvvgletitk 639
Cdd:cd01379 456 HNNIKSKY-YWRPK--SNALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVR----------------- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 640 msessappkskkgmfRTVGQLYKESLGKLMTTLHNTQPNFVRCIIPNHEKRAGKMDSNLVLEQLRCNGVLEGIRICRQGF 719
Cdd:cd01379 516 ---------------QTVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGF 580
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 1604784239 720 PNRIVFQEFRQRYEILA--ANAIPKGfmdGKQACCLMVKHLDLDPnlYRIGQSKMFFR 775
Cdd:cd01379 581 SHRILFADFLKRYYFLAfkWNEEVVA---NRENCRLILERLKLDN--WALGKTKVFLK 633
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
96-775 |
2.27e-163 |
|
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: 515.46 E-value: 2.27e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 96 ASVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLPIYSEKIIEMYKGKKRHEV---PPHIYSITDNAYRNMMQDR----ED 168
Cdd:cd14892 1 APLLDVLRRRYERDAIYTFTADILISINPYKSIPLLYDVPGFDSQRKEEATAsspPPHVFSIAERAYRAMKGVGkgqgTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 169 QSILCTGESGAGKTENTKKVIQYLAVvASSHKgkKDATPQPQQAGslAYGELEKQLLQANPILEAFGNAKTIKNDNSSRF 248
Cdd:cd14892 81 QSIVVSGESGAGKTEASKYIMKYLAT-ASKLA--KGASTSKGAAN--AHESIEECVLLSNLILEAFGNAKTIRNDNSSRF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 249 GKFIKLNFDVTGYIVGANIDTYLLEKSRCIRQSMTERAFHIFYYMVAGAKDKLREELLLEDFSCYRFLVAGH-VEISGQE 327
Cdd:cd14892 156 GKYIQIHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAESFLFLNQGNcVEVDGVD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 328 DDEMFIETLEAMEIMGFTEEERMGMMKVVSTVLQLGNIKFEK----ERNSEQATMPDDTAaqKVCHLQGINITDFIRAIL 403
Cdd:cd14892 236 DATEFKQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEEnaddEDVFAQSADGVNVA--KAAGLLGVDAAELMFKLV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 404 TPRIKVGR-EVVQKAQTKQQADFAVEALAKAMYERLFRWILARVNK---------TLDKSKRQSSSFLGILDIAGFEIFE 473
Cdd:cd14892 314 TQTTSTARgSVLEIKLTAREAKNALDALCKYLYGELFDWLISRINAchkqqtsgvTGGAASPTFSPFIGILDIFGFEIMP 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 474 DNSFEQLCINYTNERLQQLFNHTMFVLEQEEYKREGIQWSFIDFGlDLQPCIELIERPnnPPGILALLDEECWFP-KATD 552
Cdd:cd14892 394 TNSFEQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQ-DNQDCLDLIQKK--PLGLLPLLEEQMLLKrKTTD 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 553 VSFVEKLLNTHTG-HVKFSKPKQHKDKlmFTVLHYAGKVDYNAANWLTKNMDPLNDNVTALLNNSSSnfiqdlwkdadrv 631
Cdd:cd14892 471 KQLLTIYHQTHLDkHPHYAKPRFECDE--FVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSSSK------------- 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 632 vgletitkmsessappkskkgmFRTvgqlykeSLGKLMTTLHNTQPNFVRCIIPNHEKRAGKMDSNLVLEQLRCNGVLEG 711
Cdd:cd14892 536 ----------------------FRT-------QLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEV 586
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 712 IRICRQGFPNRIVFQEFRQRYEILAAN-AIPKGFMDGKQACCLMVKHLD-----LDPNLYRIGQSKMFFR 775
Cdd:cd14892 587 VRIRREGFPIRRQFEEFYEKFWPLARNkAGVAASPDACDATTARKKCEEivaraLERENFQLGRTKVFLR 656
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
96-775 |
1.09e-162 |
|
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: 513.57 E-value: 1.09e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 96 ASVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLP-IYSEKIIEMYKGKKRHEVPPHIYSITDNAYRNMMQDREDQSILCT 174
Cdd:cd14873 1 GSIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 175 GESGAGKTENTKKVIQYLAVVASSHKGKKDATPQPQqagslaygeLEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKL 254
Cdd:cd14873 81 GESGAGKTESTKLILKFLSVISQQSLELSLKEKTSC---------VEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 255 NFDVTGYIVGANIDTYLLEKSRCIRQSMTERAFHIFYYMVAGAKDKLREELLLEDFSCYRFL-VAGHVEISGQEDDEMFI 333
Cdd:cd14873 152 NICQKGNIQGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTPENYHYLnQSGCVEDKTISDQESFR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 334 ETLEAMEIMGFTEEERMGMMKVVSTVLQLGNIKFekeRNSEQATMPDDTAAQKVCHLQGINITDFIRAiLTPRIKVGR-E 412
Cdd:cd14873 232 EVITAMEVMQFSKEEVREVSRLLAGILHLGNIEF---ITAGGAQVSFKTALGRSAELLGLDPTQLTDA-LTQRSMFLRgE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 413 VVQKAQTKQQADFAVEALAKAMYERLFRWILARVNKTLdkSKRQSSSFLGILDIAGFEIFEDNSFEQLCINYTNERLQQL 492
Cdd:cd14873 308 EILTPLNVQQAVDSRDSLAMALYARCFEWVIKKINSRI--KGKEDFKSIGILDIFGFENFEVNHFEQFNINYANEKLQEY 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 493 FNHTMFVLEQEEYKREGIQWSFIDFgLDLQPCIELIERpnnPPGILALLDEECWFPKATDVSFVEKLLNTHTGHVKFSKP 572
Cdd:cd14873 386 FNKHIFSLEQLEYSREGLVWEDIDW-IDNGECLDLIEK---KLGLLALINEESHFPQATDSTLLEKLHSQHANNHFYVKP 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 573 KQHKDklMFTVLHYAGKVDYNAANWLTKNMDPLNDNVTALLNNSSSNFIQDLWKDADRVVGLETITKMSESSAPpkskkg 652
Cdd:cd14873 462 RVAVN--NFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEHVSSRNNQDTLKCGSKHRRP------ 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 653 mfrTVGQLYKESLGKLMTTLHNTQPNFVRCIIPNHEKRAGKMDSNLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 732
Cdd:cd14873 534 ---TVSSQFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRY 610
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1604784239 733 EILAANAIPKGFMDGKqaCCLMVKHLDLDPNLYRIGQSKMFFR 775
Cdd:cd14873 611 KVLMRNLALPEDVRGK--CTSLLQLYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
96-773 |
4.48e-162 |
|
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: 512.03 E-value: 4.48e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 96 ASVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLPIYSEKIIEMY------KGKKRHEVPPHIYSITDNAYRNMMQDRE-- 167
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 168 --DQSILCTGESGAGKTENTKKVIQYLAVVASShkgkkdatpQPQQAGSLAYGELEKQLLQANPILEAFGNAKTIKNDNS 245
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLASVSSA---------TTHGQNATERENVRDRVLESNPILEAFGNARTNRNNNS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 246 SRFGKFIKLNFDVTGYIVGANIDTYLLEKSRCIRQSMTERAFHIFYYMVAGAKDKLREELLLEDFSCYRFLVAGHVEI-- 323
Cdd:cd14901 152 SRFGKFIRLGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYLNSSQCYDrr 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 324 SGQEDDEMFIETLEAMEIMGFTEEERMGMMKVVSTVLQLGNIKF-EKERNSEQATMPDDTAAQKVCHLQGINITDFIRAI 402
Cdd:cd14901 232 DGVDDSVQYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFvKKDGEGGTFSMSSLANVRAACDLLGLDMDVLEKTL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 403 LTPRIKVGREVVQKAQTKQQADFAVEALAKAMYERLFRWILARVNKTLD-KSKRQSSSFLGILDIAGFEIFEDNSFEQLC 481
Cdd:cd14901 312 CTREIRAGGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAySESTGASRFIGIVDIFGFEIFATNSLEQLC 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 482 INYTNERLQQLFNHTMFVLEQEEYKREGIQWSFIDFgldlqP----CIELIERpnNPPGILALLDEECWFPKATDVSFVE 557
Cdd:cd14901 392 INFANEKLQQLFGKFVFEMEQDEYVAEAIPWTFVEY-----PnndaCVAMFEA--RPTGLFSLLDEQCLLPRGNDEKLAN 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 558 KLLNTHTGHVKFSKPKQHKDKLMFTVLHYAGKVDYNAANWLTKNMDPLNDNVTALLNNSSSNFIqdlwkdadrvvgleti 637
Cdd:cd14901 465 KYYDLLAKHASFSVSKLQQGKRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFL---------------- 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 638 tkmseSSappkskkgmfrTVGQLYKESLGKLMTTLHNTQPNFVRCIIPNHEKRAGKMDSNLVLEQLRCNGVLEGIRICRQ 717
Cdd:cd14901 529 -----SS-----------TVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRS 592
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1604784239 718 GFPNRIVFQEFRQRYEILAANAIPKGFMDGKQACCLMVKH-----LDLDPNLYRIGQSKMF 773
Cdd:cd14901 593 GYPVRFPHDAFVHTYSCLAPDGASDTWKVNELAERLMSQLqhselNIEHLPPFQVGKTKVF 653
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
98-775 |
2.34e-153 |
|
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: 488.26 E-value: 2.34e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 98 VLQNLRERYFSSLIYTYSGLFCVVVNPYKMLPIYSEKIIEMYKGKKRHEVPPHIYSITDNAYRNMM----QDREDQSILC 173
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 174 TGESGAGKTENTKKVIQYLAVVASSHKgkkdatpqpqqagslaygELEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIK 253
Cdd:cd14889 83 SGESGAGKTESTKLLLRQIMELCRGNS------------------QLEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 254 LNFDvTGYIVGANIDTYLLEKSRCIRQSMTERAFHIFYYMVAGAKDKLREELLLEDFSCYRFLVAGHveisGQEDD---- 329
Cdd:cd14889 145 LRFR-NGHVKGAKINEYLLEKSRVVHQDGGEENFHIFYYMFAGISAEDRENYGLLDPGKYRYLNNGA----GCKREvqyw 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 330 -EMFIETLEAMEIMGFTEEERMGMMKVVSTVLQLGNIKFEkernseqatmPDDTAAQKVCHLQ-----------GINITD 397
Cdd:cd14889 220 kKKYDEVCNAMDMVGFTEQEEVDMFTILAGILSLGNITFE----------MDDDEALKVENDSngwlkaaagqfGVSEED 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 398 FIRAiLTPRIKVGR-EVVQKAQTKQQADFAVEALAKAMYERLFRWILARVNKTLdKSKRQSSSFL---GILDIAGFEIFE 473
Cdd:cd14889 290 LLKT-LTCTVTFTRgEQIQRHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLL-APKDDSSVELreiGILDIFGFENFA 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 474 DNSFEQLCINYTNERLQQLFNHTMFVLEQEEYKREGIQWSFIDFgLDLQPCIELIErpNNPPGILALLDEECWFPKATDV 553
Cdd:cd14889 368 VNRFEQACINLANEQLQYFFNHHIFLMEQKEYKKEGIDWKEITY-KDNKPILDLFL--NKPIGILSLLDEQSHFPQATDE 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 554 SFVEKLLNTHTGHVKFSKPKQHKDKlmFTVLHYAGKVDYNAANWLTKNMDPLNDNVTALLNNSSSNFIQDLWkdADRVVg 633
Cdd:cd14889 445 SFVDKLNIHFKGNSYYGKSRSKSPK--FTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLF--TATRS- 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 634 lETITKMSESSAPPKSKKGMFRT----VGQLYKESLGKLMTTLHNTQPNFVRCIIPNHEKRAGKMDSNLVLEQLRCNGVL 709
Cdd:cd14889 520 -RTGTLMPRAKLPQAGSDNFNSTrkqsVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLL 598
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1604784239 710 EGIRICRQGFPNRIVFQEFRQRYEILAANAIPKGfmdGKQACCLMVKHLDLDPnlYRIGQSKMFFR 775
Cdd:cd14889 599 ETIRIRREGFSWRPSFAEFAERYKILLCEPALPG---TKQSCLRILKATKLVG--WKCGKTRLFFK 659
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
96-738 |
1.25e-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: 472.98 E-value: 1.25e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 96 ASVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLP-IYSEKIIEMYKGKKRH--------EVPPHIYSITDNAYRNMMQDR 166
Cdd:cd14907 1 AELLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEQIIQngeyfdikKEPPHIYAIAALAFKQLFENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 167 EDQSILCTGESGAGKTENTKKVIQYLavVASSHKGKKDATPQPQQAGSLAYGE----LEKQLLQANPILEAFGNAKTIKN 242
Cdd:cd14907 81 KKQAIVISGESGAGKTENAKYAMKFL--TQLSQQEQNSEEVLTLTSSIRATSKstksIEQKILSCNPILEAFGNAKTVRN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 243 DNSSRFGKFIKLNFD-VTGYIVGANIDTYLLEKSRCIRQSMTERAFHIFYYMVAGAKDKLREELLLED----FSCYRFLV 317
Cdd:cd14907 159 DNSSRFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLKNqlsgDRYDYLKK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 318 AGHVEISGQEDDEMFIETLEAMEIMGFTEEERMGMMKVVSTVLQLGNIKFEKER--NSEQATMPDDTAAQKVCHLQGINI 395
Cdd:cd14907 239 SNCYEVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDSTldDNSPCCVKNKETLQIIAKLLGIDE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 396 TDFIRAILTPRIKVGREVVQKAQTKQQADFAVEALAKAMYERLFRWILARVNKTL-------DKSKRQSSSFLGILDIAG 468
Cdd:cd14907 319 EELKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpkdekdQQLFQNKYLSIGLLDIFG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 469 FEIFEDNSFEQLCINYTNERLQQLFNHTMFVLEQEEYKREGI-----QWSFIDFgldlQPCIELIErpNNPPGILALLDE 543
Cdd:cd14907 399 FEVFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLedylnQLSYTDN----QDVIDLLD--KPPIGIFNLLDD 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 544 ECWFPKATDVSFVEKLLNTHTGHVKFSKPKqHKDKLMFTVLHYAGKVDYNAANWLTKNMDPLNDNVTALLNNSSSNFIQD 623
Cdd:cd14907 473 SCKLATGTDEKLLNKIKKQHKNNSKLIFPN-KINKDTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISS 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 624 LWKDadrvvglETITKMSESSAPPKSKKGMfRTVGQLYKESLGKLMTTLHNTQPNFVRCIIPNHEKRAGKMDSNLVLEQL 703
Cdd:cd14907 552 IFSG-------EDGSQQQNQSKQKKSQKKD-KFLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQI 623
|
650 660 670
....*....|....*....|....*....|....*
gi 1604784239 704 RCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAAN 738
Cdd:cd14907 624 RYLGVLESIRVRKQGYPYRKSYEDFYKQYSLLKKN 658
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
97-741 |
9.62e-138 |
|
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: 443.98 E-value: 9.62e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 97 SVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLP-IYSEKIIEMY-----------KGKKRHEVPPHIYSITDNAYRNMMQ 164
Cdd:cd14900 2 TILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssstRNKGSDPMPPHIYQVAGEAYKAMML 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 165 ----DREDQSILCTGESGAGKTENTKKVIQYLAvvassHKGkkdATPQPQQAGSLAYGE-LEKQLLQANPILEAFGNAKT 239
Cdd:cd14900 82 glngVMSDQSILVSGESGSGKTESTKFLMEYLA-----QAG---DNNLAASVSMGKSTSgIAAKVLQTNILLESFGNART 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 240 IKNDNSSRFGKFIKLNFDVTGYIVGANIDTYLLEKSRCIRQSMTERAFHIFYYMVAGAKDKLREEllledfscyrflvag 319
Cdd:cd14900 154 LRNDNSSRFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASEAARKR--------------- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 320 hveisgqeddEMFIETLEAMEIMGFTEEERMGMMKVVSTVLQLGNIKFEKERNSE-QATMPDDTAAQKV------CHLQG 392
Cdd:cd14900 219 ----------DMYRRVMDAMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDrLGQLKSDLAPSSIwsrdaaATLLS 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 393 INITDFIRAILTPRIKVGREVVQKAQTKQQADFAVEALAKAMYERLFRWILARVN---KTLDKSK-RQSSSFLGILDIAG 468
Cdd:cd14900 289 VDATKLEKALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNaflKMDDSSKsHGGLHFIGILDIFG 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 469 FEIFEDNSFEQLCINYTNERLQQLFNHTMFVLEQEEYKREGIQWSFIDFGlDLQPCIELIERpnNPPGILALLDEECWFP 548
Cdd:cd14900 369 FEVFPKNSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFC-DNQDCVNLISQ--RPTGILSLIDEECVMP 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 549 KATDVSFVEKLLNTHTGHVKFSKPKQHKDKLMFTVLHYAGKVDYNAANWLTKNMDPLNDNVTallnnsssnfiqdlwkda 628
Cdd:cd14900 446 KGSDTTLASKLYRACGSHPRFSASRIQRARGLFTIVHYAGHVEYSTDGFLEKNKDVLHQEAV------------------ 507
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 629 drvvgletitkmsessappkskkGMFRTVGQlYKESLGKLMTTLHNTQPNFVRCIIPNHEKRAGKMDSNLVLEQLRCNGV 708
Cdd:cd14900 508 -----------------------DLFVYGLQ-FKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGV 563
|
650 660 670
....*....|....*....|....*....|...
gi 1604784239 709 LEGIRICRQGFPNRIVFQEFRQRYEILAANAIP 741
Cdd:cd14900 564 MEAVRVARAGFPIRLLHDEFVARYFSLARAKNR 596
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
96-761 |
7.58e-137 |
|
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: 443.58 E-value: 7.58e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 96 ASVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLPIYSEKIIEMYK--GKKRHE-------VPPHIYSITDNAYRNMMQD- 165
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSQgiespqaLGPHVFAIADRSYRQMMSEi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 166 REDQSILCTGESGAGKTENTKKVIQYLAVVASSHKGKkdatpqPQQAGSLAYGELEKQLLQANPILEAFGNAKTIKNDNS 245
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLTTLGNGEEGA------PNEGEELGKLSIMDRVLQSNPILEAFGNARTLRNDNS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 246 SRFGKFIKLNFDVTGYIVGANIDTYLLEKSRCIRQSMTERAFHIFYYMVAGAKDKLREELLLEDFSCYRFLVAGHVEISG 325
Cdd:cd14908 155 SRFGKFIELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEEEHEKYEFHDGITGGLQLPNEFHYTG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 326 Q---------EDDEMFIETLEAMEIMGFTEEERMGMMKVVSTVLQLGNIKFE---KERNSEQATMPDDTAAQKVCHLQGI 393
Cdd:cd14908 235 QggapdlrefTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFEskeEDGAAEIAEEGNEKCLARVAKLLGV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 394 NITDFIRAILTPRIKVGREVVQKAQTKQQADFAVEALAKAMYERLFRWILARVNKTLDKSKRQS-SSFLGILDIAGFEIF 472
Cdd:cd14908 315 DVDKLLRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSINWENDKDiRSSVGVLDIFGFECF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 473 EDNSFEQLCINYTNERLQQLFNHTMFVLEQEEYKREGIQWSFIDFGlDLQPCIELIERPnnPPGILALLDEECWFP-KAT 551
Cdd:cd14908 395 AHNSFEQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQAK--KKGILTMLDDECRLGiRGS 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 552 DVSFVEKLLN--------THTGHVKFSKPKQHKDKLMFTVLHYAGKVDYNA-ANWLTKNMDPLndnvtallnnsssnfiq 622
Cdd:cd14908 472 DANYASRLYEtylpeknqTHSENTRFEATSIQKTKLIFAVRHFAGQVQYTVeTTFCEKNKDEI----------------- 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 623 dlwkdadrvvgletitkmsessapPKSKKGMFRTvGQLYKESLGKLMTTLHNTQPNFVRCIIPNHEKRAGKMDSNLVLEQ 702
Cdd:cd14908 535 ------------------------PLTADSLFES-GQQFKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQ 589
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1604784239 703 LRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAAnAIPK----GFMDGKQACCLMVKHLDLD 761
Cdd:cd14908 590 LRYGGVLEAVRVARSGYPVRLPHKDFFKRYRMLLP-LIPEvvlsWSMERLDPQKLCVKKMCKD 651
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
96-732 |
1.62e-136 |
|
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: 443.56 E-value: 1.62e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 96 ASVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLP-IYSEKIIEMYK--------GKKRHEVPPHIYSITDNAYRNMMQ-D 165
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLKpE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 166 REDQSILCTGESGAGKTENTKKVIQYLAVVASShkgkkdaTPQPQQAGSLAYgELEKQLLQANPILEAFGNAKTIKNDNS 245
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLTSVGRD-------QSSTEQEGSDAV-EIGKRILQTNPILESFGNAQTIRNDNS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 246 SRFGKFIKLNFDVTGYIVGANIDTYLLEKSRCIRQSMTERAFHIFYYMVAGAKDKLREELLLEDFSCYRFLVA-----GH 320
Cdd:cd14902 153 SRFGKFIKIQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKGGKYELLNSygpsfAR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 321 VEISGQEDDEMFIETLEAMEIMGFTEEERMGMMKVVSTVLQLGNIKFEKERNSEQATMPDDTAA---QKVCHLQGINITD 397
Cdd:cd14902 233 KRAVADKYAQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAENGQEDATAVTAASRfhlAKCAELMGVDVDK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 398 FIRAILTPRIKVGREVVQKAQTKQQADFAVEALAKAMYERLFRWILARVNKTLD--------KSKRQSSSFLGILDIAGF 469
Cdd:cd14902 313 LETLLSSREIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINyfdsavsiSDEDEELATIGILDIFGF 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 470 EIFEDNSFEQLCINYTNERLQQLFNHTMFVLEQEEYKREGIQWSFIDFGlDLQPCIELIErpNNPPGILALLDEECWFPK 549
Cdd:cd14902 393 ESLNRNGFEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYP-SNAACLALFD--DKSNGLFSLLDQECLMPK 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 550 ATDVSFVEKLLNTHTGHVKfskpkqhkdklmFTVLHYAGKVDYNAANWLTKNMDPLNDNVTALLNNSSSNFIQDLWKDAD 629
Cdd:cd14902 470 GSNQALSTKFYRYHGGLGQ------------FVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVVVAIGADEN 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 630 RVvgletiTKMSESSAPPKSKKGMFRT--VGQLYKESLGKLMTTLHNTQPNFVRCIIPNHEKRAGKMDSNLVLEQLRCNG 707
Cdd:cd14902 538 RD------SPGADNGAAGRRRYSMLRApsVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVG 611
|
650 660
....*....|....*....|....*
gi 1604784239 708 VLEGIRICRQGFPNRIVFQEFRQRY 732
Cdd:cd14902 612 VLEAVRIARHGYSVRLAHASFIELF 636
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
96-775 |
1.16e-135 |
|
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: 438.71 E-value: 1.16e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 96 ASVLQNLRERyfSSLI----YTYSGLFCVVVNPYKMLPiysEKIIEMYKGKKRHEVPPHIYSITDNAYRNMMQDRE---D 168
Cdd:cd14891 1 AGILHNLEER--SKLDnqrpYTFMANVLIAVNPLRRLP---EPDKSDYINTPLDPCPPHPYAIAEMAYQQMCLGSGrmqN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 169 QSILCTGESGAGKTENTKKVIQYLAvvASSHKGKKDATPQPQQAGSLAYG---ELEKQLLQANPILEAFGNAKTIKNDNS 245
Cdd:cd14891 76 QSIVISGESGAGKTETSKIILRFLT--TRAVGGKKASGQDIEQSSKKRKLsvtSLDERLMDTNPILESFGNAKTLRNHNS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 246 SRFGKFIKLNFDVTGY-IVGANIDTYLLEKSRCIRQSMTERAFHIFYYMVAGAKDKLREELLLEDFSCYRFLVAGHVEIS 324
Cdd:cd14891 154 SRFGKFMKLQFTKDKFkLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSPEDFIYLNQSGCVSD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 325 GQEDDE-MFIETLEAMEIMGFTEEERMGMMKVVSTVLQLGNIKFEKERNSE----QATMPDDTAAQKVCHLQGINITDFI 399
Cdd:cd14891 234 DNIDDAaNFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEEDTSEgeaeIASESDKEALATAAELLGVDEEALE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 400 RAILTPRIKVGREVVQKAQTKQQADFAVEALAKAMYERLFRWILARVNKTLDKsKRQSSSFLGILDIAGFEIFE-DNSFE 478
Cdd:cd14891 314 KVITQREIVTRGETFTIKRNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGH-DPDPLPYIGVLDIFGFESFEtKNDFE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 479 QLCINYTNERLQQLFNHTMFVLEQEEYKREGIQ-----WSfidfglDLQPCIELI-ERPNnppGILALLDEECWFPKATD 552
Cdd:cd14891 393 QLLINYANEALQATFNQQVFIAEQELYKSEGIDvgvitWP------DNRECLDLIaSKPN---GILPLLDNEARNPNPSD 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 553 VSFVEKLLNTHTGHVKFSKPKQHKDKLMFTVLHYAGKVDYNAANWLTKNMDplndnvtallnnsssnfiqdlwkdadrvv 632
Cdd:cd14891 464 AKLNETLHKTHKRHPCFPRPHPKDMREMFIVKHYAGTVSYTIGSFIDKNND----------------------------- 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 633 gleTItkmsessapPKSKKGMFRTvGQLYKESLGKLMTTLHNTQPNFVRCIIPNHEKRAGKMDSNLVLEQLRCNGVLEGI 712
Cdd:cd14891 515 ---II---------PEDFEDLLAS-SAKFSDQMQELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTC 581
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1604784239 713 RICRQGFPNRIVFQEFRQRYEILAANAIPKGFmdGKQACCL---MVKHLDLDPNLYRIGQSKMFFR 775
Cdd:cd14891 582 EVLKVGLPTRVTYAELVDVYKPVLPPSVTRLF--AENDRTLtqaILWAFRVPSDAYRLGRTRVFFR 645
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
96-775 |
7.17e-133 |
|
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: 430.74 E-value: 7.17e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 96 ASVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLPIYSEKIIEMYKGKKRHEVPPHIYSITDNAYRNMMQDREDQSILCTG 175
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 176 ESGAGKTENTKKVIQYLAVVASSHKGKKdatpqpqqagslaygelEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKLN 255
Cdd:cd14896 81 HSGSGKTEAAKKIVQFLSSLYQDQTEDR-----------------LRQPEDVLPILESFGHAKTILNANASRFGQVLRLH 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 256 FDvTGYIVGANIDTYLLEKSRCIRQSMTERAFHIFYYMVAGAKDKLREELLLEDFSCYRFLVAGHV-EISGQEDDEMFIE 334
Cdd:cd14896 144 LQ-HGVIVGASVSHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQGPETYYYLNQGGAcRLQGKEDAQDFEG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 335 TLEAMEIMGFTEEERMGMMKVVSTVLQLGNIKFEK-ERNS-EQATMPDDTAAQKVCHLQGINiTDFIRAILTPRIKV--- 409
Cdd:cd14896 223 LLKALQGLGLCAEELTAIWAVLAAILQLGNICFSSsERESqEVAAVSSWAEIHTAARLLQVP-PERLEGAVTHRVTEtpy 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 410 GRevVQKAQTKQQADFAVEALAKAMYERLFRWILARVNKTLD-KSKRQSSSFLGILDIAGFEIFEDNSFEQLCINYTNER 488
Cdd:cd14896 302 GR--VSRPLPVEGAIDARDALAKTLYSRLFTWLLKRINAWLApPGEAESDATIGVVDAYGFEALRVNGLEQLCINLASER 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 489 LQQLFNHTMFVLEQEEYKREGIQWSFIDfGLDLQPCIELIErpNNPPGILALLDEECWFPKATDVSFVEKLLNTHTGHVK 568
Cdd:cd14896 380 LQLFSSQTLLAQEEEECQRELLPWVPIP-QPPRESCLDLLV--DQPHSLLSILDDQTWLSQATDHTFLQKCHYHHGDHPS 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 569 FSKPKQHKDklMFTVLHYAGKVDYNAANWLTKNMDPLNDNVTALLNNSSSNFIQDLWKDADRVVGLEtitkmsessaPPK 648
Cdd:cd14896 457 YAKPQLPLP--VFTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQEAEPQYGLG----------QGK 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 649 SkkgmfrTVGQLYKESLGKLMTTLHNTQPNFVRCIIPNHEKRAGKMDSNLVLEQLRCNGVLEGIRICRQGFPNRIVFQEF 728
Cdd:cd14896 525 P------TLASRFQQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAF 598
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1604784239 729 RQRYEILAANAIPkGFMDGKQACCLMVKHLDLDPNLYRIGQSKMFFR 775
Cdd:cd14896 599 LARFGALGSERQE-ALSDRERCGAILSQVLGAESPLYHLGATKVLLK 644
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
96-775 |
6.37e-132 |
|
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: 428.59 E-value: 6.37e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 96 ASVLQNLRERYFSSLIYTYSGLFCVVVNPYK-MLPIYSEKIIEMYKGKKRHEVPPHIYSITDNAYRNMMQDREDQSILCT 174
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKwIDNLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 175 GESGAGKTENTKKVIQYLAVVASshkGKKDATPQpqqagslaygelekQLLQANPILEAFGNAKTIKNDNSSRFGKFIKL 254
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVAG---GRKDKTIA--------------KVIDVNPLLESFGNAKTTRNDNSSRFGKFTQL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 255 NFDVTGYIVGANIDTYLLEKSRCIRQSMTERAFHIFYYMVAGAKDKLREELLLEDFSCYRFL--VAGHVEISGQEDDEMF 332
Cdd:cd14904 144 QFDGRGKLIGAKCETYLLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQYLgdSLAQMQIPGLDDAKLF 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 333 IETLEAMEIMGFTEEERMGMMKVVSTVLQLGNIKFEkERNSEQATMPDDTAAQKVCHLQGINITDFIRAILTPRIKVGRE 412
Cdd:cd14904 224 ASTQKSLSLIGLDNDAQRTLFKILSGVLHLGEVMFD-KSDENGSRISNGSQLSQVAKMLGLPTTRIEEALCNRSVVTRNE 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 413 VVQKAQTKQQADFAVEALAKAMYERLFRWILARVNKTLDKSKRQSSSFLGILDIAGFEIFEDNSFEQLCINYTNERLQQL 492
Cdd:cd14904 303 SVTVPLAPVEAEENRDALAKAIYSKLFDWMVVKINAAISTDDDRIKGQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQK 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 493 FNHTMFVLEQEEYKREGIQWSFIDFGlDLQPCIELIErpnNPPGILALLDEECWFPKATDVSFVEKLLNTHTG-----HV 567
Cdd:cd14904 383 FTTDVFKTVEEEYIREGLQWDHIEYQ-DNQGIVEVID---GKMGIIALMNDHLRQPRGTEEALVNKIRTNHQTkkdneSI 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 568 KFSKPKQHKdklmFTVLHYAGKVDYNAANWLTKNMDPLNDNVTALLNNSSSNFIQDLWKDADrvvgLETITKMSESSAPP 647
Cdd:cd14904 459 DFPKVKRTQ----FIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFGSSE----APSETKEGKSGKGT 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 648 KSKKgmfrTVGQLYKESLGKLMTTLHNTQPNFVRCIIPNHEKRAGKMDSNLVLEQLRCNGVLEGIRICRQGFPNRIVFQE 727
Cdd:cd14904 531 KAPK----SLGSQFKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKE 606
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 1604784239 728 FRQRYEILAANAIPKGfmDGKQACC-LMVKHLDLDPNLYRIGQSKMFFR 775
Cdd:cd14904 607 LATRYAIMFPPSMHSK--DVRRTCSvFMTAIGRKSPLEYQIGKSLIYFK 653
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
58-818 |
2.62e-128 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 424.06 E-value: 2.62e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 58 VELSNGQKMTVNKDDIQKMNPP-KFSKVEDMAALTFLNEASVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLPIYSEKII 136
Cdd:PTZ00014 71 IDPPTNSTFEVKPEHAFNANSQiDPMTYGDIGLLPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWI 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 137 EMYKGKKRHE-VPPHIYSITDNAYRNMMQDREDQSILCTGESGAGKTENTKKVIQYLAvvaSSHKGKKDATPQpqqagsl 215
Cdd:PTZ00014 151 RRYRDAKDSDkLPPHVFTTARRALENLHGVKKSQTIIVSGESGAGKTEATKQIMRYFA---SSKSGNMDLKIQ------- 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 216 aygeleKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKLNFDVTGYIVGANIDTYLLEKSRCIRQSMTERAFHIFYYMVA 295
Cdd:PTZ00014 221 ------NAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLK 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 296 GAKDKLREELLLEDFSCYRFLVAGHVEISGQEDDEMFIETLEAMEIMGFTEEERMGMMKVVSTVLQLGNIKFE-KERN-- 372
Cdd:PTZ00014 295 GANDEMKEKYKLKSLEEYKYINPKCLDVPGIDDVKDFEEVMESFDSMGLSESQIEDIFSILSGVLLLGNVEIEgKEEGgl 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 373 SEQATMPDDTAA--QKVCHLQGINITDFIRAILTPRIKVGREVVQKAQTKQQADFAVEALAKAMYERLFRWILARVNKTL 450
Cdd:PTZ00014 375 TDAAAISDESLEvfNEACELLFLDYESLKKELTVKVTYAGNQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATI 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 451 DKSKrQSSSFLGILDIAGFEIFEDNSFEQLCINYTNERLQQLFNHTMFVLEQEEYKREGIQWSFIDFgLDLQPCIELIER 530
Cdd:PTZ00014 455 EPPG-GFKVFIGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFVDIVFERESKLYKDEGISTEELEY-TSNESVIDLLCG 532
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 531 PNNppGILALLDEECWFPKATDVSFVEKLLNTHTGHVKFSKPKQHKDKlMFTVLHYAGKVDYNAANWLTKNMDPLNDNVT 610
Cdd:PTZ00014 533 KGK--SVLSILEDQCLAPGGTDEKFVSSCNTNLKNNPKYKPAKVDSNK-NFVIKHTIGDIQYCASGFLFKNKDVLRPELV 609
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 611 ALLNNSSSNFIQDLWKDADRVVGletitkmsessappKSKKGMFrtVGQLYKESLGKLMTTLHNTQPNFVRCIIPNHEKR 690
Cdd:PTZ00014 610 EVVKASPNPLVRDLFEGVEVEKG--------------KLAKGQL--IGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKK 673
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 691 AGKMDSNLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANAIPKGFMDGKQACCLMVKHLDLDPNLYRIGQS 770
Cdd:PTZ00014 674 PLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKYLDLAVSNDSSLDPKEKAEKLLERSGLPKDSYAIGKT 753
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|.
gi 1604784239 771 KMFF-RTGV--LAQLEEERDLKLTVVIIAFQAQARGFLARKAFSKRQQQLT 818
Cdd:PTZ00014 754 MVFLkKDAAkeLTQIQREKLAAWEPLVSVLEALILKIKKKRKVRKNIKSLV 804
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
102-775 |
2.78e-128 |
|
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: 420.13 E-value: 2.78e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 102 LRERYFSSLIYTYSGLFCVVVNPYKMLPiysekiiEMYKGKKRHE-------VPPHIYSITDNAYRNMMQ-------DRE 167
Cdd:cd14895 7 LAQRYGVDQVYCRSGAVLIAVNPFKHIP-------GLYDLHKYREempgwtaLPPHVFSIAEGAYRSLRRrlhepgaSKK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 168 DQSILCTGESGAGKTENTKKVIQYLAVVASSHKGKKDATPQPQQAGSlaygelekQLLQANPILEAFGNAKTIKNDNSSR 247
Cdd:cd14895 80 NQTILVSGESGAGKTETTKFIMNYLAESSKHTTATSSSKRRRAISGS--------ELLSANPILESFGNARTLRNDNSSR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 248 FGKFIKLNF-----DVTGYIVGANIDTYLLEKSRCIRQSMTERAFHIFYYMVAGAKDKLREELLLEDFSCYRFLVAG--- 319
Cdd:cd14895 152 FGKFVRMFFeghelDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQLELLSAQEFQYISggq 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 320 -HVEISGQEDDEMFIETLEAMEIMGFTEEERMGMMKVVSTVLQLGNIKFEKERNSE---------------QATMPDDTA 383
Cdd:cd14895 232 cYQRNDGVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEgeedngaasapcrlaSASPSSLTV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 384 AQK---VCHLQGINITDFIRAILTPRIKVGREVVQKAQTKQQADFAVEALAKAMYERLFRWILARVNKTLDKSK------ 454
Cdd:cd14895 312 QQHldiVSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASPQRQfalnpn 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 455 ----RQSSSFLGILDIAGFEIFEDNSFEQLCINYTNERLQQLFNHTMFVLEQEEYKREGIQWSFIDFGLDlQPCIELIER 530
Cdd:cd14895 392 kaanKDTTPCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDN-SVCLEMLEQ 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 531 pnNPPGILALLDEECWFPKATDVSFVEKLLNTHTGHVKFSKPKQHKDKLMFTVLHYAGKVDYNAANWLTKNMDPLNDNVT 610
Cdd:cd14895 471 --RPSGIFSLLDEECVVPKGSDAGFARKLYQRLQEHSNFSASRTDQADVAFQIHHYAGAVRYQAEGFCEKNKDQPNAELF 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 611 ALLNNSSSNFIQDLWKDADRVVGLEtitkMSESSAPPKSKKGMFRTV--GQLYKESLGKLMTTLHNTQPNFVRCIIPNHE 688
Cdd:cd14895 549 SVLGKTSDAHLRELFEFFKASESAE----LSLGQPKLRRRSSVLSSVgiGSQFKQQLASLLDVVQQTQTHYIRCIKPNDE 624
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 689 KRAGKMDSNLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANAIPKGFMDGKQACCLMVKHLDLdpnlyriG 768
Cdd:cd14895 625 SASDQFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLVAAKNASDATASALIETLKVDHAEL-------G 697
|
....*..
gi 1604784239 769 QSKMFFR 775
Cdd:cd14895 698 KTRVFLR 704
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
96-736 |
6.48e-123 |
|
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: 403.46 E-value: 6.48e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 96 ASVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLP-IYSEKIIEMYKGKKR-HEVPPHIYSITDNAYRNMMQDRE--DQSI 171
Cdd:cd14880 1 ETVLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQpQKLKPHIFTVGEQTYRNVKSLIEpvNQSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 172 LCTGESGAGKTENTKKVIQYLAVVASSHkgkkdATPQPQQAGSlaygELEKQLLQANPILEAFGNAKTIKNDNSSRFGKF 251
Cdd:cd14880 81 VVSGESGAGKTWTSRCLMKFYAVVAASP-----TSWESHKIAE----RIEQRILNSNPVMEAFGNACTLRNNNSSRFGKF 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 252 IKLNFDVTGYIVGANIDTYLLEKSRCIRQSMTERAFHIFYYMVAGAKDKLREELLLEDFSCYRFLvaGHVEISGQEDDem 331
Cdd:cd14880 152 IQLQLNRAQQMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAAFSWL--PNPERNLEEDC-- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 332 FIETLEAMEIMGFTEEERMGMMKVVSTVLQLGNIKFEKERNSEQATMPDDTAAQKV---CHLQGINITDFIRAILTPRIK 408
Cdd:cd14880 228 FEVTREAMLHLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPCQPMDDTKESVrtsALLLKLPEDHLLETLQIRTIR 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 409 VGRE--VVQKAQTKQQADFAVEALAKAMYERLFRWILARVNKTLDKSKRQSSSFLGILDIAGFEIFEDNSFEQLCINYTN 486
Cdd:cd14880 308 AGKQqqVFKKPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSICADTDSWTTFIGLLDVYGFESFPENSLEQLCINYAN 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 487 ERLQQLFNHTMFVLEQEEYKREGIQWSFIDFGlDLQPCIELIErpNNPPGILALLDEECWFPKATDV----SFVEKLLNT 562
Cdd:cd14880 388 EKLQQHFVAHYLRAQQEEYAVEGLEWSFINYQ-DNQTCLDLIE--GSPISICSLINEECRLNRPSSAaqlqTRIESALAG 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 563 HT--GHVKFSKpkqhkdKLMFTVLHYAGKVDYNAANWLTKNMDPLNDNVTALLNNSSSNFIQDLWKDADRVVGLETITKM 640
Cdd:cd14880 465 NPclGHNKLSR------EPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPANPEEKTQEEPSGQ 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 641 SESSAppkskkgmfRTVGQLYKESLGKLMTTLHNTQPNFVRCIIPNHEKRAGKMDSNLVLEQLRCNGVLEGIRICRQGFP 720
Cdd:cd14880 539 SRAPV---------LTVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFP 609
|
650
....*....|....*.
gi 1604784239 721 NRIVFQEFRQRYEILA 736
Cdd:cd14880 610 IRVSHQNFVERYKLLR 625
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
96-773 |
2.88e-122 |
|
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: 401.29 E-value: 2.88e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 96 ASVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLPIYSEKIIEMYKGKKRH-EVPPHIYSITDNAYRNMMQDREDQSILCT 174
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDAPDLtKLPPHVFYTARRALENLHGVNKSQTIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 175 GESGAGKTENTKKVIQYLAvvaSSHKGKKDATPQpqqagslaygeleKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKL 254
Cdd:cd14876 81 GESGAGKTEATKQIMRYFA---SAKSGNMDLRIQ-------------TAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 255 NFDVTGYIVGANIDTYLLEKSRCIRQSMTERAFHIFYYMVAGAKDKLREELLLEDFSCYRFLVAGHVEISGQEDDEMFIE 334
Cdd:cd14876 145 DVASEGGIRYGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLGLKEYKFLNPKCLDVPGIDDVADFEE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 335 TLEAMEIMGFTEEERMGMMKVVSTVLQLGNIKFEKErnsEQATMPDdtAA----------QKVCHLQGINITDFIRAILT 404
Cdd:cd14876 225 VLESLKSMGLTEEQIDTVFSIVSGVLLLGNVKITGK---TEQGVDD--AAaisneslevfKEACSLLFLDPEALKRELTV 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 405 PRIKVGREVVQKAQTKQQADFAVEALAKAMYERLFRWILARVNKTLDkSKRQSSSFLGILDIAGFEIFEDNSFEQLCINY 484
Cdd:cd14876 300 KVTKAGGQEIEGRWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIE-PPGGFKNFMGMLDIFGFEVFKNNSLEQLFINI 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 485 TNERLQQLFNHTMFVLEQEEYKREGIQWSFIDFgLDLQPCIELIERPNNppGILALLDEECWFPKATDVSFVEKLLNTHT 564
Cdd:cd14876 379 TNEMLQKNFIDIVFERESKLYKDEGIPTAELEY-TSNAEVIDVLCGKGK--SVLSILEDQCLAPGGSDEKFVSACVSKLK 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 565 GHVKFSKPKQHKDkLMFTVLHYAGKVDYNAANWLTKNMDPLNDNVTALLNNSSSNFIQDLWKDadrvvglETITKmsess 644
Cdd:cd14876 456 SNGKFKPAKVDSN-INFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEG-------VVVEK----- 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 645 apPKSKKGMFrtVGQLYKESLGKLMTTLHNTQPNFVRCIIPNHEKRAGKMDSNLVLEQLRCNGVLEGIRICRQGFPNRIV 724
Cdd:cd14876 523 --GKIAKGSL--IGSQFLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRP 598
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 1604784239 725 FQEFRQRYEILAANAIPKGFMDGKQACCLMVKHLDLDPNLYRIGQSKMF 773
Cdd:cd14876 599 FEEFLYQFKFLDLGIANDKSLDPKVAALKLLESSGLSEDEYAIGKTMVF 647
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
96-738 |
4.08e-119 |
|
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: 394.35 E-value: 4.08e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 96 ASVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLP-IYSEKIIEMYKGKKR-HEVPPHIYSITDNAYRNMMQDREDQSILC 173
Cdd:cd14906 1 AIILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 174 TGESGAGKTENTKKVIQYLAVVASSHKGKKDATPQPQQAgslaygeLEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIK 253
Cdd:cd14906 81 SGESGSGKTEASKTILQYLINTSSSNQQQNNNNNNNNNS-------IEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 254 LNFDVTGYIV-GANIDTYLLEKSRCI-RQSMTERAFHIFYYMVAGAKDKLREELLLE-DFSCYRFLVAGHVEIS------ 324
Cdd:cd14906 154 IEFRSSDGKIdGASIETYLLEKSRIShRPDNINLSYHIFYYLVYGASKDERSKWGLNnDPSKYRYLDARDDVISsfksqs 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 325 ---------GQEDDEMFIETLEAMEIMGFTEEERMGMMKVVSTVLQLGNIKFEKERNSEQATMPDDT---AAQKVCHLQG 392
Cdd:cd14906 234 snknsnhnnKTESIESFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSDFSKYAYQKDKvtaSLESVSKLLG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 393 INITDFIRAILTPRIKVG---------REVVQKAQTKqqadfavEALAKAMYERLFRWILARVNKTLDK----------S 453
Cdd:cd14906 314 YIESVFKQALLNRNLKAGgrgsvycrpMEVAQSEQTR-------DALSKSLYVRLFKYIVEKINRKFNQntqsndlaggS 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 454 KRQSSSFLGILDIAGFEIFEDNSFEQLCINYTNERLQQLFNHTMFVLEQEEYKREGIQWSFIDFgLDLQPCIELIERPNN 533
Cdd:cd14906 387 NKKNNLFIGVLDIFGFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELIEKKSD 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 534 ppGILALLDEECWFPKATDVSFVEKLLNTHtgHVKFSKPKQHKDKLMFTVLHYAGKVDYNAANWLTKNMDPLNDNVTALL 613
Cdd:cd14906 466 --GILSLLDDECIMPKGSEQSLLEKYNKQY--HNTNQYYQRTLAKGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLL 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 614 NNSSSNFIQDLWKdadrvvgletitkmSESSAPPKS--KKGMFRTVGQLYKESLGKLMTTLHNTQPNFVRCIIPNHEKRA 691
Cdd:cd14906 542 LASSNFLKKSLFQ--------------QQITSTTNTtkKQTQSNTVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDC 607
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1604784239 692 GKMDSNLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAAN 738
Cdd:cd14906 608 NNFNNVHVLSQLRNVGVLNTIKVRKMGYSYRRDFNQFFSRYKCIVDM 654
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
96-775 |
7.79e-119 |
|
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: 392.83 E-value: 7.79e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 96 ASVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLPIYSEKIIEMYKGKKRHEVPPHIYSITDNAYRNMMQDREDQSILCTG 175
Cdd:cd01386 1 SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 176 ESGAGKTENTKKVIQYLAVVASSHKGKkdatpqpqqagslaygeLEKQLLQA-NPILEAFGNAKTIKNDNSSRFGKFIKL 254
Cdd:cd01386 81 RSGSGKTTNCRHILEYLVTAAGSVGGV-----------------LSVEKLNAaLTVLEAFGNVRTALNGNATRFSQLFSL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 255 NFDVTGYIVGANIDTYLLEKSRCIRQSMTERAFHIFYYMVAGAKDKLREELLLEDF--SCYRFLVAGHVEISGQEDDEMF 332
Cdd:cd01386 144 DFDQAGQLASASIQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLaeSNSFGIVPLQKPEDKQKAAAAF 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 333 IETLEAMEIMGFTEEERMGMMKVVSTVLQLGNIKFEKERNSEQATMPDDTAAQKVCHLQGINITDFIRAI---------- 402
Cdd:cd01386 224 SKLQAAMKTLGISEEEQRAIWSILAAIYHLGAAGATKAASAGRKQFARPEWAQRAAYLLGCTLEELSSAIfkhhlsggpq 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 403 --LTPRIKVGREVVQKAQTKQQADFAVEALAKAMYERLFRWILARVNKTLdKSKRQSSSFLGILDIAGFeifeDN----- 475
Cdd:cd01386 304 qsTTSSGQESPARSSSGGPKLTGVEALEGFAAGLYSELFAAVVSLINRSL-SSSHHSTSSITIVDTPGF----QNpahsg 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 476 -----SFEQLCINYTNERLQQLFNHTMFVLEQEEYKREGIQWSFIDFGLDLQPCIELIERPN------------NPPGIL 538
Cdd:cd01386 379 sqrgaTFEDLCHNYAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQAPqqalvrsdlrdeDRRGLL 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 539 ALLDEECWFPKATDVSFVEKLLnTHTG---HVKFSKPKQHKDK-LMFTVLHYAGK--VDYNAANWLTK-NMDPLNDNVTA 611
Cdd:cd01386 459 WLLDEEALYPGSSDDTFLERLF-SHYGdkeGGKGHSLLRRSEGpLQFVLGHLLGTnpVEYDVSGWLKAaKENPSAQNATQ 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 612 LLNNSSSnfiqdlwkdadrvvgletitkmseSSAPPKsKKGMFRTVgqlyKESLGKLMTTLHNTQPNFVRCIIPNH--EK 689
Cdd:cd01386 538 LLQESQK------------------------ETAAVK-RKSPCLQI----KFQVDALIDTLRRTGLHFVHCLLPQHnaGK 588
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 690 RAGKMDSN----------LVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANAIPKGF-----MDGKQACCLM 754
Cdd:cd01386 589 DERSTSSPaagdelldvpLLRSQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPLTKKLGlnsevADERKAVEEL 668
|
730 740
....*....|....*....|.
gi 1604784239 755 VKHLDLDPNLYRIGQSKMFFR 775
Cdd:cd01386 669 LEELDLEKSSYRIGLSQVFFR 689
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
96-775 |
4.17e-114 |
|
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: 378.08 E-value: 4.17e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 96 ASVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLP-IYSEKIIEMYKGKKRH-----EVPPHIYSITDNAYRNMMQDREDQ 169
Cdd:cd14886 1 AVVIDILRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 170 SILCTGESGAGKTENTKKVIQYLAVVASSHKGKkdatpqpqqagslaygeLEKQLLQANPILEAFGNAKTIKNDNSSRFG 249
Cdd:cd14886 81 SCIVSGESGAGKTETAKQLMNFFAYGHSTSSTD-----------------VQSLILGSNPLLESFGNAKTLRNNNSSRFG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 250 KFIKLNFDVTGYIVGANIDTYLLEKSRCIRQSMTERAFHIFYYMVAGAKDKLREELLLEDFSCYRFLVAGHV-EISGQED 328
Cdd:cd14886 144 KFIKLLVGPDGGLKGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLESYNFLNASKCyDAPGIDD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 329 DEMFIETLEAMEIMgFTEEERMGMMKVVSTVLQLGNIKFEKERNS---EQATMPDDTAAQKVCHLQGINITDFIRAILTP 405
Cdd:cd14886 224 QKEFAPVRSQLEKL-FSKNEIDSFYKCISGILLAGNIEFSEEGDMgviNAAKISNDEDFGKMCELLGIESSKAAQAIITK 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 406 RIKVGREVVQKAQTKQQADFAVEALAKAMYERLFRWILARVNKTLdKSKRQSSSFLGILDIAGFEIFEDNSFEQLCINYT 485
Cdd:cd14886 303 VVVINNETIISPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEII-QFDADARPWIGILDIYGFEFFERNTYEQLLINYA 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 486 NERLQQLFNHTMFVLEQEEYKREGIQWSFIDFGlDLQPCIELIERPNNppGILALLDEECWFPKATDVSFVEKlLNTHTG 565
Cdd:cd14886 382 NERLQQYFINQVFKSEIQEYEIEGIDHSMITFT-DNSNVLAVFDKPNL--SIFSFLEEQCLIQTGSSEKFTSS-CKSKIK 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 566 HVKFSKPKqhKDKLMFTVLHYAGKVDYNAANWLTKNMDPLNDNVTALLNNSSSNFIQDLWKDADRVVGLetitkmsessa 645
Cdd:cd14886 458 NNSFIPGK--GSQCNFTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNKAFSDIPNEDGN----------- 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 646 ppksKKGMFrtVGQLYKESLGKLMTTLHNTQPNFVRCIIPNHEKRAGKMDSNLVLEQLRCNGVLEGIRICRQGFPNRIVF 725
Cdd:cd14886 525 ----MKGKF--LGSTFQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTF 598
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 1604784239 726 QEFRQRYEILA--ANAIPKGFMDGKQACCLMVKHLDLDPNLYRIGQSKMFFR 775
Cdd:cd14886 599 EEFFHRNKILIshNSSSQNAGEDLVEAVKSILENLGIPCSDYRIGKTKVFLR 650
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
96-775 |
3.57e-109 |
|
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: 364.13 E-value: 3.57e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 96 ASVLQNLRERyFSSLIYTYS--GLFCVVVNPYKMLPIYSEKIIEMY-KGKKRHEVPPHIYSITDNAYRNM-MQDREDQSI 171
Cdd:cd14875 1 ATLLHCIKER-FEKLHQQYSlmGEMVLSVNPFRLMPFNSEEERKKYlALPDPRLLPPHIWQVAHKAFNAIfVQGLGNQSV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 172 LCTGESGAGKTENTKKVIQYLAVVASSHKGKkdaTPQPQQAGSLAygeleKQLLQANPILEAFGNAKTIKNDNSSRFGKF 251
Cdd:cd14875 80 VISGESGSGKTENAKMLIAYLGQLSYMHSSN---TSQRSIADKID-----ENLKWSNPVMESFGNARTVRNDNSSRFGKY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 252 IKLNFD-VTGYIVGANIDTYLLEKSRCIRQSMTERAFHIFYYMVAGAKDKLREEL----LLEDFSCYR----FLVAGhVE 322
Cdd:cd14875 152 IKLYFDpTSGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELgglkTAQDYKCLNggntFVRRG-VD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 323 ISGQEDDEMFIETLEAMEIMGFTEEERMGMMKVVSTVLQLGNIKFEKERNsEQATMPDDTAAQKVCHLQGINITDFIRAI 402
Cdd:cd14875 231 GKTLDDAHEFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQN-DKAQIADETPFLTACRLLQLDPAKLRECF 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 403 LtprIKVGREVVQKAQTKQQADFAVEALAKAMYERLFRWILARVNKTLDKSKRQSS-SFLGILDIAGFEIFEDNSFEQLC 481
Cdd:cd14875 310 L---VKSKTSLVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNASITPQGDCSGcKYIGLLDIFGFENFTRNSFEQLC 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 482 INYTNERLQQLFNHTMFVLEQEEYKREGIQWSFIDFGlDLQPCIELIERPNNppGILALLDEECWFPKATDVSFVEKLLN 561
Cdd:cd14875 387 INYANESLQNHYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNMFDQKRT--GIFSMLDEECNFKGGTTERFTTNLWD 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 562 THTGHVK-FSKPKQHKDKlMFTVLHYAGKVDYNAANWLTKNMDPLNDNVTALLNNSSSNFIQDLWkdadrvvgletitkm 640
Cdd:cd14875 464 QWANKSPyFVLPKSTIPN-QFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTLL--------------- 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 641 sessappKSKKGMFR---TVGQLYKESLGKLMTTLHNTQPNFVRCIIPNHEKRAGKMDSNLVLEQLRCNGVLEGIRICRQ 717
Cdd:cd14875 528 -------STEKGLARrkqTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQ 600
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1604784239 718 GFPNRIVFQEF-RQRYEILAANAIpKGFMDGK--QACC-LMVKHLDL----DPNlYRIGQSKMFFR 775
Cdd:cd14875 601 GYPVRRPIEQFcRYFYLIMPRSTA-SLFKQEKysEAAKdFLAYYQRLygwaKPN-YAVGKTKVFLR 664
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
96-732 |
3.52e-105 |
|
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: 354.40 E-value: 3.52e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 96 ASVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLP-IYSEKIIEMYKgkKRHEVP------------PHIYSITDNAYRNM 162
Cdd:cd14899 1 ASILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYA--YDHNSQfgdrvtstdprePHLFAVARAAYIDI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 163 MQDREDQSILCTGESGAGKTENTKKVIQYLAVVASSHKGKKDATPQPQQAGSLAYGELEKQLLQANPILEAFGNAKTIKN 242
Cdd:cd14899 79 VQNGRSQSILISGESGAGKTEATKIIMTYFAVHCGTGNNNLTNSESISPPASPSRTTIEEQVLQSNPILEAFGNARTVRN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 243 DNSSRFGKFIKLNF-DVTGYIVGANIDTYLLEKSRCIRQSMTERAFHIFYYMVAG-----AKDKLREELLLEDFSCYRFL 316
Cdd:cd14899 159 DNSSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSAdnncvSKEQKQVLALSGGPQSFRLL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 317 VAG--HVEISGQEDDEMFIETLEAMEIMGFTEEERMGMMKVVSTVLQLGNIKFEK-----ERNS---EQATMPDDTAA-- 384
Cdd:cd14899 239 NQSlcSKRRDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEQiphkgDDTVfadEARVMSSTTGAfd 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 385 --QKVCHLQGINITDFIRAILTPRIKVGREVVQKAQTKQQADFAVEALAKAMYERLFRWILARVNKTL------------ 450
Cdd:cd14899 319 hfTKAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLqrqasapwgade 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 451 --DKSKRQSSSFLGILDIAGFEIFEDNSFEQLCINYTNERLQQLFNHTMFVLEQEEYKREGIQWSFIDFGlDLQPCIELI 528
Cdd:cd14899 399 sdVDDEEDATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFP-NNRACLELF 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 529 ErpNNPPGILALLDEECWFPKATDVSFVEKLlnthtgHVKFSKPKQH---------KDKLMFTVLHYAGKVDYNAANWLT 599
Cdd:cd14899 478 E--HRPIGIFSLTDQECVFPQGTDRALVAKY------YLEFEKKNSHphfrsapliQRTTQFVVAHYAGCVTYTIDGFLA 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 600 KNMDPLNDNVTALLNNSSSNFIQDLW---KDADRVVGLETITKMSESSAPPKSKKGMFrTVGQLYKESLGKLMTTLHNTQ 676
Cdd:cd14899 550 KNKDSFCESAAQLLAGSSNPLIQALAagsNDEDANGDSELDGFGGRTRRRAKSAIAAV-SVGTQFKIQLNELLSTVRATT 628
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 1604784239 677 PNFVRCIIPNHEKRAGKMDSNLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 732
Cdd:cd14899 629 PRYVRCIKPNDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRY 684
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
93-774 |
6.29e-101 |
|
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: 339.91 E-value: 6.29e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 93 LNEASVLQNLRERYFSSLIYTY---SGLfcVVVNPYKMLPIYSE----KIIEMYKG---KKRHEVPPHIYSITDNAYRNM 162
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRlgsSAL--VAVNPYKYLSSNSDaslgEYGSEYYDttsGSKEPLPPHAYDLAARAYLRM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 163 MQDREDQSILCTGESGAGKTENTKKVI-QYLAVVASSHKGKKdatpqpqqagslaygeLEKQLLQANPILEAFGNAKTIK 241
Cdd:cd14879 79 RRRSEDQAVVFLGETGSGKSESRRLLLrQLLRLSSHSKKGTK----------------LSSQISAAEFVLDSFGNAKTLT 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 242 NDNSSRFGKFIKLNFDVTGYIVGANIDTYLLEKSRCIRQSMTERAFHIFYYMVAGAKDKLREELLLEDFSCYRFLV--AG 319
Cdd:cd14879 143 NPNASRFGRYTELQFNERGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPSDYALLAsyGC 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 320 H--VEISGQEDDEMFIETLEAMEIMGFTEEERMGMMKVVSTVLQLGNIKF--EKERNSEQATM--PD--DTAAqkvcHLQ 391
Cdd:cd14879 223 HplPLGPGSDDAEGFQELKTALKTLGFKRKHVAQICQLLAAILHLGNLEFtyDHEGGEESAVVknTDvlDIVA----AFL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 392 GINITDfIRAILTPRIK-VGREVV----QKAQTKQQADfaveALAKAMYERLFRWILARVNKTLDKSKRQSSSFLGILDI 466
Cdd:cd14879 299 GVSPED-LETSLTYKTKlVRKELCtvflDPEGAAAQRD----ELARTLYSLLFAWVVETINQKLCAPEDDFATFISLLDF 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 467 AGFEIF---EDNSFEQLCINYTNERLQQLFNHTMFVLEQEEYKREGIQWSFIDFgLDLQPCIELIERPnnPPGILALLDE 543
Cdd:cd14879 374 PGFQNRsstGGNSLDQFCVNFANERLHNYVLRSFFERKAEELEAEGVSVPATSY-FDNSDCVRLLRGK--PGGLLGILDD 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 544 EC-WFPKATDVSFVEKLLNTHTGHVKFS---KPKQHKDKLMFTVLHYAGKVDYNAANWLTKNMDPLndnvtallnnsSSN 619
Cdd:cd14879 451 QTrRMPKKTDEQMLEALRKRFGNHSSFIavgNFATRSGSASFTVNHYAGEVTYSVEGFLERNGDVL-----------SPD 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 620 FIQdlwkdadrvvgletitkmsessappkskkgMFRTVGQLyKESLGKLMTTLHNTQPNFVRCIIPNHEKRAGKMDSNLV 699
Cdd:cd14879 520 FVN------------------------------LLRGATQL-NAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRV 568
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1604784239 700 LEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYeilaANAIPKGFMDGKQACClmVKHLDLDPNLYRIGQSKMFF 774
Cdd:cd14879 569 KAQIRSLGLPELAARLRVEYVVSLEHAEFCERY----KSTLRGSAAERIRQCA--RANGWWEGRDYVLGNTKVFL 637
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
96-775 |
4.48e-99 |
|
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: 337.01 E-value: 4.48e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 96 ASVLQNLRERYFS--------SLIYTYSGLFCVVVNPYKMLPIYSEKIIEMYKGKKRHEVPPHIYSITDNAYRNMMQDRE 167
Cdd:cd14887 1 PNLLENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 168 DQSILCTGESGAGKTENTKKVIQYLAVVASSHKGKKDATpqpqqagslaygeLEKQLLQANPILEAFGNAKTIKNDNSSR 247
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTYLAAVSDRRHGADSQG-------------LEARLLQSGPVLEAFGNAHTVLNANSSR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 248 FGKFIKLNFDVTGYIVGANIDTYLLEKSRCIRQSMTERAFHIFYYMVAGAKDKLREELL--LEDFSCY--RFLVAG--HV 321
Cdd:cd14887 148 FGKMLLLHFTGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAVAAATQKSSagEGDPESTdlRRITAAmkTV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 322 EISGQEDDEMFiETLEAMEIMG---FTE-EERMGMMKVVSTVLQLGNIKFEKERN--------------SEQATMPDDTA 383
Cdd:cd14887 228 GIGGGEQADIF-KLLAAILHLGnveFTTdQEPETSKKRKLTSVSVGCEETAADRShssevkclssglkvTEASRKHLKTV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 384 AQKVCHLQGINITDFIRAILTprIKVGREvVQKAQTKQQADFAVEALAKAMYERLFRWILARVNKTLDKSKRQSSS---- 459
Cdd:cd14887 307 ARLLGLPPGVEGEEMLRLALV--SRSVRE-TRSFFDLDGAAAARDAACKNLYSRAFDAVVARINAGLQRSAKPSESdsde 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 460 ---------FLGILDIAGFEIFED---NSFEQLCINYTNERLQQLFNHTMFVLEQEEYKREGIQWSFI--DFGLDLQPCI 525
Cdd:cd14887 384 dtpsttgtqTIGILDLFGFEDLRNhskNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGVFQNQDcsAFPFSFPLAS 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 526 ELIERPNN---------------------PPGILALLDE------ECWFPKATDVSFVEKLLNTHTGHVKFSK--PKQHK 576
Cdd:cd14887 464 TLTSSPSStspfsptpsfrsssafatspsLPSSLSSLSSslssspPVWEGRDNSDLFYEKLNKNIINSAKYKNitPALSR 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 577 DKLMFTVLHYAGKVDYNAANWLTKNMDPLNDNVTALLnNSSSNFIQDLWKDADRVVGLEtitkmsessappKSKKgmfRT 656
Cdd:cd14887 544 ENLEFTVSHFACDVTYDARDFCRANREATSDELERLF-LACSTYTRLVGSKKNSGVRAI------------SSRR---ST 607
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 657 VGQLYKESLGKLMTTLHNTQPNFVRCIIPNHEKRAGKMDSNLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILA 736
Cdd:cd14887 608 LSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVELWRRYETKL 687
|
730 740 750
....*....|....*....|....*....|....*....
gi 1604784239 737 ANAIpKGFMDGKQACCLMVKHLDLDPNLYRIGQSKMFFR 775
Cdd:cd14887 688 PMAL-REALTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
97-739 |
2.58e-96 |
|
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: 324.16 E-value: 2.58e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 97 SVLQNLRERYFSSLIYTYSGLFCVVVNPYKmlPIYSEKIIEMYKGKKRHeVPPHIYSITDNAYRNMMQdREDQSILCTGE 176
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYE--TIYGAGAMKAYLKNYSH-VEPHVYDVAEASVQDLLV-HGNQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 177 SGAGKTENTKKVIQYLAvvasshKGKKDATpqpqqagslaygELEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKLNF 256
Cdd:cd14898 78 SGSGKTENAKLVIKYLV------ERTASTT------------SIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKF 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 257 DvtGYIVGANIDTYLLEKSRCIRQSMTERAFHIFYyMVAGAKDkLReelLLEDFSCYRFLvAGHVE--ISGQEDDEMFIE 334
Cdd:cd14898 140 D--GKITGAKFETYLLEKSRVTHHEKGERNFHIFY-QFCASKR-LN---IKNDFIDTSST-AGNKEsiVQLSEKYKMTCS 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 335 TLEAMEIMGFTEEErmgmmKVVSTVLQLGNIKFekerNSEQAT-MPDDTAAQKVCHLQGINITDFIRAILTPRIKVGREV 413
Cdd:cd14898 212 AMKSLGIANFKSIE-----DCLLGILYLGSIQF----VNDGILkLQRNESFTEFCKLHNIQEEDFEESLVKFSIQVKGET 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 414 VQKAQTKQQADFAVEALAKAMYERLFRWILARVNKTLDKSKRQSSSflgILDIAGFEIFEDNSFEQLCINYTNERLQQLF 493
Cdd:cd14898 283 IEVFNTLKQARTIRNSMARLLYSNVFNYITASINNCLEGSGERSIS---VLDIFGFEIFESNGLDQLCINWTNEKIQNDF 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 494 NHTMFVLEQEEYKREGIQWSFIDFgLDLQPCIELIERPNnppGILALLDEECWFPKATDVSFVEKLLNTHTGHVKfskpK 573
Cdd:cd14898 360 IKKMFRAKQGMYKEEGIEWPDVEF-FDNNQCIRDFEKPC---GLMDLISEESFNAWGNVKNLLVKIKKYLNGFIN----T 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 574 QHKDKLMftVLHYAGKVDYNAANWLTKNMDplndnvtallnnsssnfiqdlwKDADRVVGLETItkmsessAPPKSKKGM 653
Cdd:cd14898 432 KARDKIK--VSHYAGDVEYDLRDFLDKNRE----------------------KGQLLIFKNLLI-------NDEGSKEDL 480
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 654 FRtvgqLYKESLGKLMTTLHNTQPNFVRCIIPNHEKRAGKMDSNLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 733
Cdd:cd14898 481 VK----YFKDSMNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYR 556
|
....*.
gi 1604784239 734 ILAANA 739
Cdd:cd14898 557 ILGITL 562
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
96-775 |
4.35e-94 |
|
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: 320.22 E-value: 4.35e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 96 ASVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLPIYSEKIIEMY---KGKKRHEVPPHIYSITDNAYRNMMQDREDQSIL 172
Cdd:cd14878 1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYlssSGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 173 CTGESGAGKTENTKKVIQYLAVVASSHKGKkdatpqpqqagslaygeLEKQLLQANPILEAFGNAKTIKNDNSSRFGKFI 252
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLTCRASSSRTT-----------------FDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYF 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 253 KLNF-DVTGYIVGANIDTYLLEKSRCIRQSMTERAFHIFYYMVAGAKDKLREELLLEDFSCYRFLVAGHVE----ISGQE 327
Cdd:cd14878 144 ELQFcERKKHLTGARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTMREdvstAERSL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 328 DDEMFIETLEAMEIMGFTEEERMGMMKVVSTVLQLGNIKFEKERNSEQATMPDDTAAQKVCHLQGINiTDFIRAILTPRI 407
Cdd:cd14878 224 NREKLAVLKQALNVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVS-TDELASALTTDI 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 408 KVGR-EVVQKAQTKQQADFAVEALAKAMYERLFRWILARVNKTLDKSKRQSSS---FLGILDIAGFEIFEDNSFEQLCIN 483
Cdd:cd14878 303 QYFKgDMIIRRHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLQSQDEQKSMqtlDIGILDIFGFEEFQKNEFEQLCVN 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 484 YTNERLQQLFNHTMFVLEQEEYKREGIQwsfidfgldlqpcIELIERPNN-----------PPGILALLDEECWFPKATD 552
Cdd:cd14878 383 MTNEKMHHYINEVLFLQEQTECVQEGVT-------------METAYSPGNqtgvldfffqkPSGFLSLLDEESQMIWSVE 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 553 VSFVEKL---LNTHTGHVKFSKPKQHKDKL-------MFTVLHYAGKVDYNAANWLTKNMDPLNDNVTALLNNSSSNFIQ 622
Cdd:cd14878 450 PNLPKKLqslLESSNTNAVYSPMKDGNGNValkdqgtAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVIN 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 623 DLWkdadrvvgletitkmsessappKSKkgmFRTVGQLYKESLGKLMTTLHNTQPNFVRCIIPNHEKRAGKMDSNLVLEQ 702
Cdd:cd14878 530 HLF----------------------QSK---LVTIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQ 584
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1604784239 703 LRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANAI-PKGFMDGKQACCLMVKHLDLDPnlYRIGQSKMFFR 775
Cdd:cd14878 585 LQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTLLgEKKKQSAEERCRLVLQQCKLQG--WQMGVRKVFLK 656
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
96-775 |
2.11e-87 |
|
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: 300.01 E-value: 2.11e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 96 ASVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLPIYsekiIEMYKGKKRHEVPPHIYSITDNAYRNMMQDREDQSILCTG 175
Cdd:cd14937 1 AEVLNMLALRYKKNYIYTIAEPMLISINPYQVIDVD----INEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 176 ESGAGKTENTKKVIQ-YLAVVasshkgKKDatpqpqqagslayGELEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKL 254
Cdd:cd14937 77 ESGSGKTEASKLVIKyYLSGV------KED-------------NEISNTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKI 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 255 NFDVTGYIVGANIDTYLLEKSRCIRQSMTERAFHIFYYMVAGAKDKLREELLLEDFSCYRFLVAGHVEISGQEDDEMFIE 334
Cdd:cd14937 138 ELDEYQNIVSSSIEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSENEYKYIVNKNVVIPEIDDAKDFGN 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 335 TLEAMEIMGFTEEERmGMMKVVSTVLQLGNIKF---EKERNSEQATMPDDT--AAQKVCHLQGINITDFIRAILTPRIKV 409
Cdd:cd14937 218 LMISFDKMNMHDMKD-DLFLTLSGLLLLGNVEYqeiEKGGKTNCSELDKNNleLVNEISNLLGINYENLKDCLVFTEKTI 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 410 GREVVQKAQTKQQADFAVEALAKAMYERLFRWILARVNKTLDKSKrQSSSFLGILDIAGFEIFEDNSFEQLCINYTNERL 489
Cdd:cd14937 297 ANQKIEIPLSVEESVSICKSISKDLYNKIFSYITKRINNFLNNNK-ELNNYIGILDIFGFEIFSKNSLEQLLINIANEEI 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 490 QQLFNHTMFVLEQEEYKREGIQWSFIDFGLDlQPCIELIeRPNNppGILALLDEECWFPKATDVSFVEKLLNTHTGHVKF 569
Cdd:cd14937 376 HSIYLYIVYEKETELYKAEDILIESVKYTTN-ESIIDLL-RGKT--SIISILEDSCLGPVKNDESIVSVYTNKFSKHEKY 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 570 SKPKQHKDKlMFTVLHYAGKVDYNAANWLTKNMDPLNDNVTALLNNSSSNFIQDLWKDADrvvgletitkMSESsappks 649
Cdd:cd14937 452 ASTKKDINK-NFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDVE----------VSES------ 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 650 kKGMFRTVGQLYKESLGKLMTTLHNTQPNFVRCIIPNHEKRAGKMDSNLVLEQLRCNGVLEGIRIcRQGFPNRIVFQEFR 729
Cdd:cd14937 515 -LGRKNLITFKYLKNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNI-SFFFQYKYTFDVFL 592
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 1604784239 730 QRYEILAANAIPKGFMDGKQACCLMVKHlDLDPNLYRIGQSKMFFR 775
Cdd:cd14937 593 SYFEYLDYSTSKDSSLTDKEKVSMILQN-TVDPDLYKVGKTMVFLK 637
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
96-727 |
3.09e-84 |
|
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: 292.20 E-value: 3.09e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 96 ASVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLP-IYSEKIIEMYKGKKRHE-------VPPHIYSITDNAYRNMMQDRE 167
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSaasaapfPKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 168 DQSILCTGESGAGKTENTKKVIQYLAVVasshkgkkdatpqpqQAGSLAYgELEKQLLQANPILEAFGNAKTIKNDNSSR 247
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYFHYI---------------QTDSQMT-ERIDKLIYINNILESMSNATTIKNNNSSR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 248 FGKFIKLNFD---------VTGYIVGANIDTYLLEKSRCIRQSMTERAFHIFYYMVAGAKDK-LREELLLEDFSCYRFL- 316
Cdd:cd14884 145 CGRINLLIFEeventqknmFNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGLSDEdLARRNLVRNCGVYGLLn 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 317 ---------VAGHVEISG----------QEDDEMFIETLEAMEIMGFTEEERMGMMKVVSTVLQLGNIKFekernseqat 377
Cdd:cd14884 225 pdeshqkrsVKGTLRLGSdsldpseeekAKDEKNFVALLHGLHYIKYDERQINEFFDIIAGILHLGNRAY---------- 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 378 mpddtaaQKVCHLQGINITDFIRAILTPRIKVGREVVQKAQTKQQADFAVEALAKAMYERLFRWILARVNKTL--DKSKR 455
Cdd:cd14884 295 -------KAAAECLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNVlkCKEKD 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 456 QS---------SSFLGILDIAGFEIFEDNSFEQLCINYTNERLQQLFNHTMFVLEQEEYKREGIQWSFIDFGlDLQPCIE 526
Cdd:cd14884 368 ESdnediysinEAIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDVAP-SYSDTLI 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 527 LIERpnnppgILALLDEECWFP----KATDVSFVEKLLNTHT----------GHV-----KFSKPKQHKDKLMFTVLHYA 587
Cdd:cd14884 447 FIAK------IFRRLDDITKLKnqgqKKTDDHFFRYLLNNERqqqlegkvsyGFVlnhdaDGTAKKQNIKKNIFFIRHYA 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 588 GKVDYNAANWLTKNMDPLNDNVTALLNNSSSNFIqdlwkdadrvvgletitkmseSSAPPKSKKGMFRTVGQLYKESLGK 667
Cdd:cd14884 521 GLVTYRINNWIDKNSDKIETSIETLISCSSNRFL---------------------REANNGGNKGNFLSVSKKYIKELDN 579
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 668 LMTTLHNTQPNFVRCIIPNHEKRAGKMDSNLVLEQLRCNGVLEGIRICRQGFPNRIVFQE 727
Cdd:cd14884 580 LFTQLQSTDMYYIRCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIPKKE 639
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
97-752 |
2.55e-76 |
|
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: 267.36 E-value: 2.55e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 97 SVLQNLRERYFSSLIYTYSGLFCVVVNPYkmlpiysekiieMYKGKKRHEVP-------PHIYSITDNAYRNMMQDREDQ 169
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPY------------RDVGNPLTLTStrssplaPQLLKVVQEAVRQQSETGYPQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 170 SILCTGESGAGKTENTKKVIQYLAVVAsshkgkkdatpqpqqaGSLAYGELEKQLLQANPILEAFGNAKTIKNDNSSRFG 249
Cdd:cd14881 70 AIILSGTSGSGKTYASMLLLRQLFDVA----------------GGGPETDAFKHLAAAFTVLRSLGSAKTATNSESSRIG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 250 KFIKLNFdVTGYIVGANIDTYLLEKSRCIRQSMTERAFHIFYYMVAGAKDKLREELLLEDFSCY--RFLVAGHVEISGQE 327
Cdd:cd14881 134 HFIEVQV-TDGALYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDGYSPAnlRYLSHGDTRQNEAE 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 328 DDEMFIETLEAMEIMG--FTEeermgMMKVVSTVLQLGNIKFeKERNSEQATMPDDTAAQKVCHLQGINITDFIRAiLTP 405
Cdd:cd14881 213 DAARFQAWKACLGILGipFLD-----VVRVLAAVLLLGNVQF-IDGGGLEVDVKGETELKSVAALLGVSGAALFRG-LTT 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 406 RIK-VGREVVQKAQTKQQADFAVEALAKAMYERLFRWILARVNKTL----DKSKRQSSSFLGILDIAGFEIFEDNSFEQL 480
Cdd:cd14881 286 RTHnARGQLVKSVCDANMSNMTRDALAKALYCRTVATIVRRANSLKrlgsTLGTHATDGFIGILDMFGFEDPKPSQLEHL 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 481 CINYTNERLQQLFNHTMFVLEQEEYKREGIQWSF-IDFgLDLQPCIELIErpNNPPGILALLDEECwFPKATDVSFVEKL 559
Cdd:cd14881 366 CINLCAETMQHFYNTHIFKSSIESCRDEGIQCEVeVDY-VDNVPCIDLIS--SLRTGLLSMLDVEC-SPRGTAESYVAKI 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 560 LNTHTGHVKFSKPKQHKDKlMFTVLHYAGKVDYNAANWLTKNMDPLNDNVTALLNNSSSNFiqdlwkdadrvvgletitk 639
Cdd:cd14881 442 KVQHRQNPRLFEAKPQDDR-MFGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYKQNCNF------------------- 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 640 msessappkskkgMFRTVGQLYKESLGKLMTTLHNTQPNFVRCIIPNHEKRAGKMDSNLVLEQLRCNGVLEGIRICRQGF 719
Cdd:cd14881 502 -------------GFATHTQDFHTRLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAGGY 568
|
650 660 670
....*....|....*....|....*....|...
gi 1604784239 720 PNRIVFQEFRQRYEILAANAIPKGFMDGKQACC 752
Cdd:cd14881 569 PHRMRFKAFNARYRLLAPFRLLRRVEEKALEDC 601
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
96-735 |
1.31e-74 |
|
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: 262.50 E-value: 1.31e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 96 ASVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLPIYSEKIIEMYkgkkrhevppHIYSITDNAYRNMMQDRED-QSILCT 174
Cdd:cd14874 1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 175 GESGAGKTENTKKVIQYLavvasshkgkkdaTPQPQQAGSlaygelEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKL 254
Cdd:cd14874 71 GESGSGKSYNAFQVFKYL-------------TSQPKSKVT------TKHSSAIESVFKSFGCAKTLKNDEATRFGCSIDL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 255 NFDvTGYIVGANID-TYLLEKSRCIRQSMTERAFHIFYYMVAGAKDKLREELLLEDFSCYRFLVAGHVEISGQEDDEMFI 333
Cdd:cd14874 132 LYK-RNVLTGLNLKyTVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGLQKFFYINQGNSTENIQSDVNHFK 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 334 ETLEAMEIMGFTEEERMGMMKVVSTVLQLGNIKFEKERNS----EQATMPDDTAAQKVCHLQGINItDFIRAILTPRIKV 409
Cdd:cd14874 211 HLEDALHVLGFSDDHCISIYKIISTILHIGNIYFRTKRNPnveqDVVEIGNMSEVKWVAFLLEVDF-DQLVNFLLPKSED 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 410 GREVvqkaqTKQQADFAVEALAKAMYERLFRWILARVNKTLDKSKRQSSsfLGILDIAGFEIFEDNSFEQLCINYTNERL 489
Cdd:cd14874 290 GTTI-----DLNAALDNRDSFAMLIYEELFKWVLNRIGLHLKCPLHTGV--ISILDHYGFEKYNNNGVEEFLINSVNERI 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 490 QQLFNHTMFVLEQEEYKREGIQwsfIDF----GLDLQPCIELIERpnNPPGILALLDEECWFPKATDVSFVEKLLNTHTG 565
Cdd:cd14874 363 ENLFVKHSFHDQLVDYAKDGIS---VDYkvpnSIENGKTVELLFK--KPYGLLPLLTDECKFPKGSHESYLEHCNLNHTD 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 566 HVKFSKPKQhKDKLMFTVLHYAGKVDYNAANWLTKNMDPLNDNVTALLNNSSSNFIQDLWKdadrvvgletitkmSESSa 645
Cdd:cd14874 438 RSSYGKARN-KERLEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFE--------------SYSS- 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 646 ppkSKKGMFRTVGQLYKESLGKLMTTLHNTQPNFVRCIIPNHEKRAGKMDSNLVLEQLRCNGVLEGIRICRQGFPNRIVF 725
Cdd:cd14874 502 ---NTSDMIVSQAQFILRGAQEIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISK 578
|
650
....*....|
gi 1604784239 726 QEFRQRYEIL 735
Cdd:cd14874 579 TTFARQYRCL 588
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
99-733 |
1.11e-70 |
|
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: 253.74 E-value: 1.11e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 99 LQNLRERYFSSLIYTYSGLFCVVVNPYKMLPIY----------SEKIIEMYKGKKRHEVPPHIYSITDNAYRNMMQDRED 168
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYtpdhmqaynkSREQTPLYEKDTVNDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 169 QSILCTGESGAGKTENTKKVIQYLAVVASShkgkkdATPQPQQAG-SLAYGELEKQLLQANPILEAFGNAKTIKNDNSSR 247
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQYLCEIGDE------TEPRPDSEGaSGVLHPIGQQILHAFTILEAFGNAATRQNRNSSR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 248 FGKFIKLNFDVTGYIVGANIDTYLLEKSRCIRQSMTERAFHIFYYMVAGAKD--KLREELLL----EDFSCYRFL--VAG 319
Cdd:cd14893 158 FAKMISVEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQHdpTLRDSLEMnkcvNEFVMLKQAdpLAT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 320 HVEISGQEddemFIETLEAMEIMGFTEEERMGMMKVVSTVLQLGNIKF--EKERNSEQATMPDDTaaqkVCHLQGINITD 397
Cdd:cd14893 238 NFALDARD----YRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFvpDPEGGKSVGGANSTT----VSDAQSCALKD 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 398 FIRAILTPRI-------------------KVGREVVQ--KAQTKQQADFAVEALAKAMYERLFRWILARVNKTL----DK 452
Cdd:cd14893 310 PAQILLAAKLlevepvvldnyfrtrqffsKDGNKTVSslKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILggifDR 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 453 SKRQS----SSFLGILDIAGFEIFED--NSFEQLCINYTNERLQQLF-------NHTMFVLEQEEYKREGIQWSFIDFGL 519
Cdd:cd14893 390 YEKSNivinSQGVHVLDMVGFENLTPsqNSFDQLCFNYWSEKVHHFYvqntlaiNFSFLEDESQQVENRLTVNSNVDITS 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 520 DLQPCIELIERPnnPPGILALLDEECWFPKATDVSFVEKLLNTHTGHVKFSKPKQHKD------------KLMFTVLHYA 587
Cdd:cd14893 470 EQEKCLQLFEDK--PFGIFDLLTENCKVRLPNDEDFVNKLFSGNEAVGGLSRPNMGADttneylapskdwRLLFIVQHHC 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 588 GKVDYNAANWLTKNMDPLNDNVTALLNNSSSNFIQdlwkdadrVVGLETIT-----KMSESSAPPKSKKGMFRTVGQLYK 662
Cdd:cd14893 548 GKVTYNGKGLSSKNMLSISSTCAAIMQSSKNAVLH--------AVGAAQMAaasseKAAKQTEERGSTSSKFRKSASSAR 619
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 663 ESLG--------------KLMTTLHNTQPNFVRCIIPNHEKRAGKMDSNLVLEQLRCNGVLEGIRICRQGFPNRIVFQEF 728
Cdd:cd14893 620 ESKNitdsaatdvynqadALLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHF 699
|
....*
gi 1604784239 729 RQRYE 733
Cdd:cd14893 700 FRRYK 704
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
97-728 |
2.20e-69 |
|
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: 248.08 E-value: 2.20e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 97 SVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLP-IYSEKIIEMYKgkKRHEVPPHIYSITDNAYRNMMQDREDQSILCTG 175
Cdd:cd14905 2 TLINIIQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNYN--QRRGLPPHLFALAAKAISDMQDFRRDQLIFIGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 176 ESGAGKTENTKKVIQYLAVVASSHKGKkdatpqpqqagslaygeLEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKLN 255
Cdd:cd14905 80 ESGSGKSENTKIIIQYLLTTDLSRSKY-----------------LRDYILESGIILESFGHASTDSNHNSSRWGKYFEMF 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 256 FDVTGYIVGANIDTYLLEKSRCIRQSMTERAFHIFYYMVAGAKDKLREELLLEDFSCYRFL-VAGHVEISGQEDDEMFIE 334
Cdd:cd14905 143 YSLYGEIQGAKLYSYFLDENRVTYQNKGERNFHIFYQFLKGITDEEKAAYQLGDINSYHYLnQGGSISVESIDDNRVFDR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 335 TLEAMEIMGFTEEERMGMMKVVSTVLQLGNIKFEKERNSEQatMPDDTAAQKVCHLQGINITDFIRAILTPRIKVGREVV 414
Cdd:cd14905 223 LKMSFVFFDFPSEKIDLIFKTLSFIIILGNVTFFQKNGKTE--VKDRTLIESLSHNITFDSTKLENILISDRSMPVNEAV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 415 QKAqtkqqadfavEALAKAMYERLFRWILARVNKTLDKSkrQSSSFLGILDIAGFEIFEDNSFEQLCINYTNERLQQLFN 494
Cdd:cd14905 301 ENR----------DSLARSLYSALFHWIIDFLNSKLKPT--QYSHTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYL 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 495 HTMFVLEQEEYKREGIQW-SFIDFGlDLQPCIELIERpnnppgILALLDEECWFPKATDVSFVEKLLNTHTGHVKFSKpK 573
Cdd:cd14905 369 QTVLKQEQREYQTERIPWmTPISFK-DNEESVEMMEK------IINLLDQESKNINSSDQIFLEKLQNFLSRHHLFGK-K 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 574 QHKdklmFTVLHYAGKVDYNAANWLTKNMDPLNDNVTALLNNSSSNFIqdlwKDADRVVGLE-TITKMSES-SAPPKSKK 651
Cdd:cd14905 441 PNK----FGIEHYFGQFYYDVRGFIIKNRDEILQRTNVLHKNSITKYL----FSRDGVFNINaTVAELNQMfDAKNTAKK 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 652 GMFRTVGQLY-----------------------------KESLGKLMTTLHNTQP---------NFVRCIIPNHEKRAGK 693
Cdd:cd14905 513 SPLSIVKVLLscgsnnpnnvnnpnnnsgggggggnsgggSGSGGSTYTTYSSTNKainnsncdfHFIRCIKPNSKKTHLT 592
|
650 660 670
....*....|....*....|....*....|....*....
gi 1604784239 694 MDSNLVLEQLRCNGVLEGIRICRQGFP----NRIVFQEF 728
Cdd:cd14905 593 FDVKSVNEQIKSLCLLETTRIQRFGYTihynNKIFFDRF 631
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
97-775 |
1.67e-66 |
|
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: 238.87 E-value: 1.67e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 97 SVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLPIYSEKIIEMYKGKKRHEVPPHIYSITDNAYRNMMQDREDQSILCTGE 176
Cdd:cd14882 2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 177 SGAGKTENTKKVIQYLAVVAsshKGKKDATpqpqqagslaygeleKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKLNF 256
Cdd:cd14882 82 SYSGKTTNARLLIKHLCYLG---DGNRGAT---------------GRVESSIKAILALVNAGTPLNADSTRCILQYQLTF 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 257 DVTGYIVGANIDTYLLEKSRCIRQSMTERAFHIFYYMVAG--AKDKLREELLLEDFScYRFL---------VAGHVEISG 325
Cdd:cd14882 144 GSTGKMSGAIFWMYQLEKLRVSTTDGNQSNFHIFYYFYDFieAQNRLKEYNLKAGRN-YRYLrippevppsKLKYRRDDP 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 326 QEDDEMFIETLEAMEIMGFTEEERMGMMKVVSTVLQLGNIKFeKERNSEqATMPDDTAAQKVCHLQGINITDFIRAILTP 405
Cdd:cd14882 223 EGNVERYKEFEEILKDLDFNEEQLETVRKVLAAILNLGEIRF-RQNGGY-AELENTEIASRVAELLRLDEKKFMWALTNY 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 406 RIKVGREVVQKAQTKQQADFAVEALAKAMYERLFRWILARVNKTLD--KSKRQSSSFLGILDIAGFEIFEDNSFEQLCIN 483
Cdd:cd14882 301 CLIKGGSAERRKHTTEEARDARDVLASTLYSRLVDWIINRINMKMSfpRAVFGDKYSISIHDMFGFECFHRNRLEQLMVN 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 484 YTNERLQQLFNHTMFV---LEQEEYKREGIQWSFIDFGLDLQpciELIERPNnppGILALLDEECwfPKATDVSFVekLL 560
Cdd:cd14882 381 TLNEQMQYHYNQRIFIsemLEMEEEDIPTINLRFYDNKTAVD---QLMTKPD---GLFYIIDDAS--RSCQDQNYI--MD 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 561 NTHTGHVKFSKPKQHKDklmFTVLHYAGKVDYNAANWLTKNMDPLNDNVTALLNNSSSNFIQDLWKDADrvvgletITKM 640
Cdd:cd14882 451 RIKEKHSQFVKKHSAHE---FSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTNSQ-------VRNM 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 641 sessappkskkgmfRTVGQLYKESLGKLMTTLHNTQPN----FVRCIIPNHEKRAGKMDSNLVLEQLRCNGVLEGIRICR 716
Cdd:cd14882 521 --------------RTLAATFRATSLELLKMLSIGANSggthFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQ 586
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 1604784239 717 QGFPNRIVFQEFRQRYEILAANAIPKGFMDgKQACCLMVKHLDLDPnlYRIGQSKMFFR 775
Cdd:cd14882 587 KGFSYRIPFQEFLRRYQFLAFDFDETVEMT-KDNCRLLLIRLKMEG--WAIGKTKVFLK 642
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
118-261 |
3.02e-58 |
|
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: 198.72 E-value: 3.02e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 118 FCVVVNPYKMLPIYSE-KIIEMYKGKKRHEVPPHIYSITDNAYRNMMQDREDQSILCTGESGAGKTENTKKVIQYLAVVA 196
Cdd:cd01363 1 VLVRVNPFKELPIYRDsKIIVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1604784239 197 SSHKGKKDAtpQPQQAGSLAYGELEKQLLQANPILEAFGNAKTIKNDNSSRFGKFIKLNFDVTGY 261
Cdd:cd01363 81 FNGINKGET--EGWVYLTEITVTLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEILLDIAGF 143
|
|
| MYSc_Myo24B |
cd14938 |
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
97-773 |
4.87e-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: 209.31 E-value: 4.87e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 97 SVLQNLRERYFSSLIYTYSGLFCVVVNPYKMLPIYSEKIIEMYK-GKKRHEVPPHIYSITDNAYRNMMQDREDQSILCTG 175
Cdd:cd14938 2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKcIDCIEDLSLNEYHVVHNALKNLNELKRNQSIIISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 176 ESGAGKTENTKKVIQYLAVVASSHKGKKDATPQPQQAGSLA------YGELEKQLLQANPILEAFGNAKTIKNDNSSRFG 249
Cdd:cd14938 82 ESGSGKSEIAKNIINFIAYQVKGSRRLPTNLNDQEEDNIHNeentdyQFNMSEMLKHVNVVMEAFGNAKTVKNNNSSRFS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 250 KFIKLNFDvTGYIVGANIDTYLLEKSRCIRQSMTERAFHIFYYMVAGAKDKLREELLLEDFSCYRFLVAGHVEISGQEDD 329
Cdd:cd14938 162 KFCTIHIE-NEEIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIENYSMLNNEKGFEKFSDYS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 330 EMFIETLEAMEIMGFTEEERMGMMKVVSTVLQLGNIKFEK---------ERNSEQATMPDDTAAQKV------------- 387
Cdd:cd14938 241 GKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNTEIVKafrkksllmGKNQCGQNINYETILSELensedigldenvk 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 388 -----CHLQGINITDFIRAILTPRIkVGREVVQKAQTKQQADFAVEALAKAMYERLFRWILARVNKTLDKSKR--QSSSF 460
Cdd:cd14938 321 nlllaCKLLSFDIETFVKYFTTNYI-FNDSILIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEKCTQLQNinINTNY 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 461 LGILDIAGFEIFEDNSFEQLCINYTNERLQQLFNHTMFVLEQEEYKREGIQWSFIDFGLDLQPCIELIERPNNppGILAL 540
Cdd:cd14938 400 INVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLYNLLVGPTE--GSLFS 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 541 LDEECWFPKATDVSfvekllNTHTGHV-KFSKPKQH-------KDKLMFTVLHYAGKVDYNAANWLTKNMDPLNDNVTAL 612
Cdd:cd14938 478 LLENVSTKTIFDKS------NLHSSIIrKFSRNSKYikkdditGNKKTFVITHSCGDIIYNAENFVEKNIDILTNRFIDM 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 613 LNNSSSNFIQDL-----WKDADRVVglETITKMSESSAPPKSKKGmFRTVGQ----LYKESLGKLMTTLHNTQPNFVRCI 683
Cdd:cd14938 552 VKQSENEYMRQFcmfynYDNSGNIV--EEKRRYSIQSALKLFKRR-YDTKNQmavsLLRNNLTELEKLQETTFCHFIVCM 628
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 684 IPNHEKRA-GKMDSNLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAAnaipkgfmDGKQACCLMVKHLDLDP 762
Cdd:cd14938 629 KPNESKRElCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIKNE--------DLKEKVEALIKSYQISN 700
|
730
....*....|.
gi 1604784239 763 NLYRIGQSKMF 773
Cdd:cd14938 701 YEWMIGNNMIF 711
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
861-1732 |
1.42e-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: 138.65 E-value: 1.42e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 861 KDEELKAAKEVAA--------KVETELK-DITQKHTQ-----LMEERAQLEmKLHAETELYAEAEEMRVRLEAKK----- 921
Cdd:TIGR02168 153 KPEERRAIFEEAAgiskykerRKETERKlERTRENLDrlediLNELERQLK-SLERQAEKAERYKELKAELRELElallv 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 922 ---QELEEVLHEMESRLEEEEDRSNALHNERKEMEQQLQLMEAHIAEEEDARQKLQMEKVSVEGKVKKLEEDILMMEDQN 998
Cdd:TIGR02168 232 lrlEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERL 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 999 NKLQKERKLLEERLADMSSNLAEEEEKSKNLSKLKTKHESMISELELRMKKEEKGRLDMEKAKRKVEAELGDLQEQHADL 1078
Cdd:TIGR02168 312 ANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQL 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1079 QAQLAELRAQLAAKEEELQATQARLEEECNQRGAAVKRVRELEVliSELQEDLEAERAARGKVEAARRDLGEELNALRTE 1158
Cdd:TIGR02168 392 ELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAEL--KELQAELEELEEELEELQEELERLEEALEELREE 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1159 LEdslgttAAQQELRAKR--EQEVSMLKKAMEDEGRSHEAQVQDLRQ--KHSQAVEELTEQLEQAKRVRAGLEKAKQALE 1234
Cdd:TIGR02168 470 LE------EAEQALDAAEreLAQLQARLDSLERLQENLEGFSEGVKAllKNQSGLSGILGVLSELISVDEGYEAAIEAAL 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1235 KESADLSADlRSLASAKQDVEHKKKKVEGQLNELnsrfneserqrtelgervsklttELDSVTGLLNEAEGKNIKLSKDv 1314
Cdd:TIGR02168 544 GGRLQAVVV-ENLNAAKKAIAFLKQNELGRVTFL-----------------------PLDSIKGTEIQGNDREILKNIE- 598
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1315 sslsSQLQDAQELLSEETRQKLNLSGRLRQTE--EDRNSLMEQLEEETEAKRAVERQVSSLNMQLSDSKKKLDEMSGTVE 1392
Cdd:TIGR02168 599 ----GFLGVAKDLVKFDPKLRKALSYLLGGVLvvDDLDNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSSILE 674
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1393 ALEEgKKRLQRELEAANSDYEEKASAYDKLEKSRGRMQQELEDVLMDLDSQRQLVSNLEKKqkkfdqmLAEERAVSCKFA 1472
Cdd:TIGR02168 675 RRRE-IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKD-------LARLEAEVEQLE 746
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1473 EERDRAEAEAREKETRVLALARALEENQGALEEAEKTMKGLRADMED-------LISSKDDVGKSVHDLEKAKRGLEAIV 1545
Cdd:TIGR02168 747 ERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQlkeelkaLREALDELRAELTLLNEEAANLRERL 826
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1546 DEMRTQMEELEDELQVAEDAKLRLDVNTQALRAQHERELHARDELgEEKRKQLLKQVRELEAELEEERKQRGQASGSKKK 1625
Cdd:TIGR02168 827 ESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEEL-ESELEALLNERASLEEALALLRSELEELSEELRE 905
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1626 LEGELKDMEDQLEATSRGRDEAVKQLRKIQGQVKDLQ--------RDLEDSRAAQKEVLASARESERRSKAMEADIVQLH 1697
Cdd:TIGR02168 906 LESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQerlseeysLTLEEAEALENKIEDDEEEARRRLKRLENKIKELG 985
|
890 900 910
....*....|....*....|....*....|....*..
gi 1604784239 1698 EM-LAAVERARKQAEvERDELSEELAS-NSSGKSLMS 1732
Cdd:TIGR02168 986 PVnLAAIEEYEELKE-RYDFLTAQKEDlTEAKETLEE 1021
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1000-1835 |
3.22e-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: 137.50 E-value: 3.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1000 KLQKERKLLEERLADMSSNLAEEE----EKSKNLSKLKTKHESMISELELRMKKEEKGR----LDMEKAKRKVEAelgdL 1071
Cdd:TIGR02168 169 KYKERRKETERKLERTRENLDRLEdilnELERQLKSLERQAEKAERYKELKAELRELELallvLRLEELREELEE----L 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1072 QEQHADLQAQLAELRAQLAAKEEELQATQARLEEECNQRGAAVKRVRELEVLISELQEDLEAERAARGKVEAARrdlgEE 1151
Cdd:TIGR02168 245 QEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQL----EE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1152 LNALRTELEDSLGTTAAQQELRAKREQEVSMLKKAMEDEGRSHEAQVQDLRQKhsqaVEELTEQLEQAKRVRAGLEKAKQ 1231
Cdd:TIGR02168 321 LEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESR----LEELEEQLETLRSKVAQLELQIA 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1232 ALEKESADLSADLRSLASAKQDV-----EHKKKKVEGQLNELNSRFNESERQRTELGERVSKLTTELDSVTGLLNEAEGK 1306
Cdd:TIGR02168 397 SLNNEIERLEARLERLEDRRERLqqeieELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQA 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1307 NIKLSKDVSSLSSQ---LQDAQELLSEETRQKLNLSGRLRQTEEDRNSLMEQLEEETEAKRAVERQV-SSLNMQLSDSKK 1382
Cdd:TIGR02168 477 LDAAERELAQLQARldsLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALgGRLQAVVVENLN 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1383 KLDEmsgTVEALEEGKKRLQRELEAansdyeeKASAYDKLEKSRGRMQQELEDVLMDLDSqrqLVSNLEKKQKKFDQMLA 1462
Cdd:TIGR02168 557 AAKK---AIAFLKQNELGRVTFLPL-------DSIKGTEIQGNDREILKNIEGFLGVAKD---LVKFDPKLRKALSYLLG 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1463 eeravSCKFAEERDRAEAEARE--KETRVLALARALEENQGAL----EEAEKTMKGLRADMEDLISSKDDVGKSVHDLEK 1536
Cdd:TIGR02168 624 -----GVLVVDDLDNALELAKKlrPGYRIVTLDGDLVRPGGVItggsAKTNSSILERRREIEELEEKIEELEEKIAELEK 698
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1537 AkrgleaiVDEMRTQMEELEDELQVAEDAKLRLDVNTQALRAQHEReLHARDELGEEKRKQLLKQVRELEAELEEERKQR 1616
Cdd:TIGR02168 699 A-------LAELRKELEELEEELEQLRKELEELSRQISALRKDLAR-LEAEVEQLEERIAQLSKELTELEAEIEELEERL 770
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1617 GQASGSKKKLEGELKDMEDQLEATSRGRDEAVKQLRKIQGQVKDLQRDLEDSRAAQKEVLASARESERRSKAMEADIVQL 1696
Cdd:TIGR02168 771 EEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEEL 850
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1697 HEMLAAVERARKQAEVERDELSEELASNssgkslmSDEKRRLDTKISQLEEELEEEQANVESLNDRLRKSQQLVEQLGAE 1776
Cdd:TIGR02168 851 SEDIESLAAEIEELEELIEELESELEAL-------LNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREK 923
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*....
gi 1604784239 1777 LAAERSTSQSREGSRQQLERQNRELKAKMQEMEGQGRSKLKASIAALEAKLREAEEQLE 1835
Cdd:TIGR02168 924 LAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIK 982
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
102-716 |
1.82e-31 |
|
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: 134.49 E-value: 1.82e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 102 LRERYFSSLIYTYSGLFCV-VVNPYKML------PIYSEKIIEMYKGKKRHE--VPPHIYSIT---------DNAY---- 159
Cdd:cd14894 7 LTSRFDDDRIYTYINHHTMaVMNPYRLLqtarftSIYDEQVVLTYADTANAEtvLAPHPFAIAkqslvrlffDNEHtmpl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 160 -------RNMMQDReDQSILCTGESGAGKTENTKKVIQYLAVVASS--HKGKKD------ATPQP--------------- 209
Cdd:cd14894 87 pstissnRSMTEGR-GQSLFLCGESGSGKTELAKDLLKYLVLVAQPalSKGSEEtckvsgSTRQPkiklftsstkstiqm 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 210 --QQAGSLA---------------------------------------------------YGELEKQL------------ 224
Cdd:cd14894 166 rtEEARTIAlleakgvekyeivlldlhperwdemtsvsrskrlpqvhvdglffgfyekleHLEDEEQLrmyfknphaakk 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 225 ----LQANPILEAFGNAKTIKNDNSSRFGKFIKLN--FDVTGY---IVGANIDTYLLEKSRCIRQ------SMTERAFHI 289
Cdd:cd14894 246 lsivLDSNIVLEAFGHATTSMNLNSSRFGKMTTLQvaFGLHPWefqICGCHISPFLLEKSRVTSErgresgDQNELNFHI 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 290 FYYMVAGAK-----DKLREELLLEDFSCYRFL--------VAGHV--EISGQEDDEMFIETLEAMEIMGFTEEERMGMMK 354
Cdd:cd14894 326 LYAMVAGVNafpfmRLLAKELHLDGIDCSALTylgrsdhkLAGFVskEDTWKKDVERWQQVIDGLDELNVSPDEQKTIFK 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 355 VVSTVLQLGNIKFEKERNSEQATMPDD---TAAQKVCHLQGI-NITDFIRAILTPRIKV--GREVVQKAQTKQQADFAVE 428
Cdd:cd14894 406 VLSAVLWLGNIELDYREVSGKLVMSSTgalNAPQKVVELLELgSVEKLERMLMTKSVSLqsTSETFEVTLEKGQVNHVRD 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 429 ALAKAMYERLFRWILARVNK-------TLDKSKRQ---------SSSFLGILDIAGFEIFEDNSFEQLCINYTNERLqql 492
Cdd:cd14894 486 TLARLLYQLAFNYVVFVMNEatkmsalSTDGNKHQmdsnasapeAVSLLKIVDVFGFEDLTHNSLDQLCINYLSEKL--- 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 493 fnhtmfvleqeeYKREGiqwSFIDFGLDLQPciELIERPN---------NPPGILALLDEECWFPKATDVS--------- 554
Cdd:cd14894 563 ------------YAREE---QVIAVAYSSRP--HLTARDSekdvlfiyeHPLGVFASLEELTILHQSENMNaqqeekrnk 625
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 555 -FVEKLLNTHTGHVK-----FSKPKQHKDKLM----FTVLHYAGKVDYNAANWLTKNMDPLNDNVTALLNNSSSNFIQDL 624
Cdd:cd14894 626 lFVRNIYDRNSSRLPepprvLSNAKRHTPVLLnvlpFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNSSHFCRM 705
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 625 WKDADRVvGLETITKMSESSAPPKSKKGMFRTVGQlYKESLGKLMTTLHNTQPNFVRCIIPNHEKRAGKMDSNLVLEQLR 704
Cdd:cd14894 706 LNESSQL-GWSPNTNRSMLGSAESRLSGTKSFVGQ-FRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCR 783
|
810
....*....|..
gi 1604784239 705 CNGVLEGIRICR 716
Cdd:cd14894 784 SQRLIRQMEICR 795
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
941-1555 |
2.76e-30 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 130.83 E-value: 2.76e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 941 RSNALHNERKEMEQQLQLMEAHIAEEEDARQKLQMEKVSVEGKVKKLEEDILMMEDQNNKLQKERKLLEERLADMSSNLA 1020
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1021 EEEEKSKNLSKLKTKHESMISELELRMKKEEKGRLDMEKAKRKVEAELGDLQEQHADLQAQLAELRAQLAAKEEELQATQ 1100
Cdd:COG1196 306 RLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1101 ARLEEECNQRGAAVKRVRELEVLISELQEDLEAERAARGKVEAARRDLGEELNALRTELEDSLGTTAAQQELRAKREQEV 1180
Cdd:COG1196 386 EELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELL 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1181 smlkKAMEDEGRSHEAQVQDLRQKHSQAVEELTEQLEQAKRVRAGLEKAKQALEKESAD-LSADLRSLASAKQDVEHKKK 1259
Cdd:COG1196 466 ----AELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRgLAGAVAVLIGVEAAYEAALE 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1260 KVEGQLNELNSRFNESERQRTELGERVSKLT--TELDSVTGLLNEAEGKNIKLSKDVSSLSSQLQDAQELLSEETRQKLN 1337
Cdd:COG1196 542 AALAAALQNIVVEDDEVAAAAIEYLKAAKAGraTFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDT 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1338 LSGRLRQTE--EDRNSLMEQLEEETEAKRAVERQVSSLNMQLSDSKKKLDEmsGTVEALEEGKKRLQRELEAANSDYEEK 1415
Cdd:COG1196 622 LLGRTLVAArlEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLA--ALLEAEAELEELAERLAEEELELEEAL 699
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1416 ASAYDKLEKSRGRMQQELEDVLMDLDSQRQLVSNLEKKQKKFDQMLAEERAVsckfAEERDRAEAEAREKETRVLALARA 1495
Cdd:COG1196 700 LAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEE----ALEELPEPPDLEELERELERLERE 775
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1604784239 1496 LEE----NQGALEEAEKtmkgLRADMEDLISSKDdvgksvhDLEKAKRGLEAIVDEMRTQMEEL 1555
Cdd:COG1196 776 IEAlgpvNLLAIEEYEE----LEERYDFLSEQRE-------DLEEARETLEEAIEEIDRETRER 828
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
985-1721 |
3.30e-29 |
|
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: 127.88 E-value: 3.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 985 KKLEEDILMMEDQNNKLQKERKLLEERLADMSSNLAEEEEKSKNLSKLKTKHESMISELELRMKKEE-------KGRLDM 1057
Cdd:TIGR02169 156 RKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREyegyellKEKEAL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1058 EKAKRKVEAELGDLQEQHADLQAQLAELRAQLAAKEEELQATQARLEEECNQRGAAVK-RVRELEVLISELQEDLEAERA 1136
Cdd:TIGR02169 236 ERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKeKIGELEAEIASLERSIAEKER 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1137 ARGKVEAARRDLGEELNALRTELEDSLGTTAAQQELRAKREQEVSMLKKAMED---EGRSHEAQVQDLRQKHSQAVEELt 1213
Cdd:TIGR02169 316 ELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDlraELEEVDKEFAETRDELKDYREKL- 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1214 eqlEQAKRVRAGLEKAKQALEKESADLSADLRSLASAKQDVEHKKKKVEGQLNELNSRFNESERQRTELGERVSKLTTEL 1293
Cdd:TIGR02169 395 ---EKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQEL 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1294 DSVTGLLNEAEGKNIKLSKDVSSLSSQLQ----------DAQELLSEETRQKLNLSGRLRQTEEDRNSLMEQ-------- 1355
Cdd:TIGR02169 472 YDLKEEYDRVEKELSKLQRELAEAEAQARaseervrggrAVEEVLKASIQGVHGTVAQLGSVGERYATAIEVaagnrlnn 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1356 --LEEETEAKRAVE----RQVSSLN------MQLSDSKKKLDEMSGT---------------------------VEALEE 1396
Cdd:TIGR02169 552 vvVEDDAVAKEAIEllkrRKAGRATflplnkMRDERRDLSILSEDGVigfavdlvefdpkyepafkyvfgdtlvVEDIEA 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1397 GKKRLQR-ELEAANSDYEEKASA----YDKLEKSRGRMQQELEDVLM---DLDSQRQLVSNLEKKQKKFDQMLAEERAvs 1468
Cdd:TIGR02169 632 ARRLMGKyRMVTLEGELFEKSGAmtggSRAPRGGILFSRSEPAELQRlreRLEGLKRELSSLQSELRRIENRLDELSQ-- 709
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1469 ckfaeERDRAEAEAREKETRVLALARALEENQGALEEAEKTMKGLRADMEDLISSKDDVGKSVHDLEKAKRGLEAIVDEM 1548
Cdd:TIGR02169 710 -----ELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDL 784
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1549 -----RTQMEELEDELQVAEDAKLRLDVNTQALRAQHEReLHARDELGEEKRKQLLKQVRELEAELEEERKQRGQASGSK 1623
Cdd:TIGR02169 785 earlsHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNR-LTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKK 863
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1624 -------KKLEGELKDMEDQLEATSRGRDEAVKQLRKIQGQVKDLQRDLEDSRAAQKEVLASARESERRSKAMEADIVQL 1696
Cdd:TIGR02169 864 eeleeelEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGED 943
|
810 820
....*....|....*....|....*
gi 1604784239 1697 HEMLAAVERARKQAEvERDELSEEL 1721
Cdd:TIGR02169 944 EEIPEEELSLEDVQA-ELQRVEEEI 967
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
833-1555 |
8.13e-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: 126.71 E-value: 8.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 833 LKNWQWWRLftkvkpLLQVTRQEEEMGQKDEELKAAKEVAAKVETELKDITQKHTQLMEERAQLEMKLH-AETELYAEAE 911
Cdd:TIGR02168 222 LRELELALL------VLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEeLQKELYALAN 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 912 EMRvRLEAKKQELEEVLHEMESRLEEEEDRSNALHNERKEMEQQLQLMEAHIAEeedarqkLQMEKVSVEGKVKKLEEDI 991
Cdd:TIGR02168 296 EIS-RLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEE-------LKEELESLEAELEELEAEL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 992 LMMEDQNNKLQKERKLLEERLADMSSNLAEEEEKSKNLSKLKTKHESMISEL-----ELRMKKEEKGRLDMEKAKRKVEA 1066
Cdd:TIGR02168 368 EELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLqqeieELLKKLEEAELKELQAELEELEE 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1067 ELGDLQEQHADLQAQLAELRAQLAAKEEELQATQARLEEEcNQRGAAVKRVRE------------------LEVLISELQ 1128
Cdd:TIGR02168 448 ELEELQEELERLEEALEELREELEEAEQALDAAERELAQL-QARLDSLERLQEnlegfsegvkallknqsgLSGILGVLS 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1129 EDLEAERAARGKVEAArrdLGEELNALRTE-----------LEDSLGTTAAQQELRAKREQEVSMLKKAMEDEGRSHEAQ 1197
Cdd:TIGR02168 527 ELISVDEGYEAAIEAA---LGGRLQAVVVEnlnaakkaiafLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGV 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1198 VQDLRQKHSQA-------------VEELTEQLEQAKRVRAG----------------------------LEKAKQ--ALE 1234
Cdd:TIGR02168 604 AKDLVKFDPKLrkalsyllggvlvVDDLDNALELAKKLRPGyrivtldgdlvrpggvitggsaktnssiLERRREieELE 683
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1235 KESADLSADLRSLASAKQDVEHKKKKVEGQLNELNSRFNESERQRTELGERVSKLTTELDSVTGLLNEAEGKNIKLSKDV 1314
Cdd:TIGR02168 684 EKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEI 763
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1315 SSLSSQLQDAQELLSEETRQKLNLSGRLRQTEEDRNSLMEQLEEETEAKRAVERQVSSLNMQLSDSKKKLDEMSGTVEAL 1394
Cdd:TIGR02168 764 EELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDL 843
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1395 EEGKKRLQRELEAANS-------DYEEKASAYDKLEKSRGRMQQELEDVLMDLDSQRQLVSNLEKKQKKFDQMLAEERAV 1467
Cdd:TIGR02168 844 EEQIEELSEDIESLAAeieeleeLIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREK 923
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1468 SCKFAEERDRAEAEAREKETRVLALARALEENQGALEEA-EKTMKGLRADMEDLISSKDDVG------------------ 1528
Cdd:TIGR02168 924 LAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKiEDDEEEARRRLKRLENKIKELGpvnlaaieeyeelkeryd 1003
|
810 820 830
....*....|....*....|....*....|
gi 1604784239 1529 ---KSVHDLEKAKRGLEAIVDEMRTQMEEL 1555
Cdd:TIGR02168 1004 fltAQKEDLTEAKETLEEAIEEIDREARER 1033
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1132-1917 |
2.42e-26 |
|
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: 118.62 E-value: 2.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1132 EAERaargKVEAARRDLgEELNALRTELEDSLGTTAAQ-------QELRA-KREQEVSMLKKAME------DEGRSHEAQ 1197
Cdd:TIGR02168 176 ETER----KLERTRENL-DRLEDILNELERQLKSLERQaekaeryKELKAeLRELELALLVLRLEelreelEELQEELKE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1198 VQDLRQKHSQAVEELTEQLEQAKRVRAGLEKAKQALEKESADLSADLRSLASAKQDVEHKKKKVEGQLNELNSRFNESER 1277
Cdd:TIGR02168 251 AEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELES 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1278 QRTELGERVSKLTTELDSVTGLLNEAEGKNIKLSKDVSSLSSQLQDAQELLSEETRQKLNLSGRLRQTEEDRNSLMEQLE 1357
Cdd:TIGR02168 331 KLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLE 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1358 EETEAKRAVERQVSSLNMQLSDSKKKldEMSGTVEALEEGKKRLQRELEAANSDYEEKASAYDKLEKSRGRMQQELEDVL 1437
Cdd:TIGR02168 411 RLEDRRERLQQEIEELLKKLEEAELK--ELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQ 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1438 MDLDSQRQLVSNLEKKQKKFDQMLAEERAVSCKFAEERDRAEAEAREKetrvLALARALEENQGALeeaekTMKGLRADM 1517
Cdd:TIGR02168 489 ARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYE----AAIEAALGGRLQAV-----VVENLNAAK 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1518 EDLISSKDDVGKSVHDLE---KAKRGLEAIVDEMRTQMEELEDELQVAEDAKLRLDVNTQALRAQhereLHARDELGE-- 1592
Cdd:TIGR02168 560 KAIAFLKQNELGRVTFLPldsIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGG----VLVVDDLDNal 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1593 EKRKQLLKQVRELEAELEEERKQRGQASGSK-------------KKLEGELKDMEDQLEATSRGRDEAVKQLRKIQGQVK 1659
Cdd:TIGR02168 636 ELAKKLRPGYRIVTLDGDLVRPGGVITGGSAktnssilerrreiEELEEKIEELEEKIAELEKALAELRKELEELEEELE 715
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1660 DLQRDLEDSRAAQKEVLASARESERRSKAMEADIVQLHEMLAAVERARKQAEVERDELSEELASNSSGKSLMSDEKRRLD 1739
Cdd:TIGR02168 716 QLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLK 795
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1740 TKISQLEEELEEEQANVESLNDRLRKSQQLVEQLGAELAAersTSQSREGSRQQLERQNRELKAKMQEMEGQGRS--KLK 1817
Cdd:TIGR02168 796 EELKALREALDELRAELTLLNEEAANLRERLESLERRIAA---TERRLEDLEEQIEELSEDIESLAAEIEELEELieELE 872
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1818 ASIAALEAKLREAEEQLEIESRERQANGKNLRQKEKKLKDLTIQMEDERKQAQQYKDQAEKGNVRVKQLKHQLEEA---- 1893
Cdd:TIGR02168 873 SELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEyslt 952
|
810 820
....*....|....*....|....*...
gi 1604784239 1894 ----EEEAQRMAAARRKLQRELDEATEA 1917
Cdd:TIGR02168 953 leeaEALENKIEDDEEEARRRLKRLENK 980
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
848-1445 |
1.27e-24 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 112.72 E-value: 1.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 848 LLQVTRQEEEMGQKDEELKAAKEVAAKVETELKDITQKHTQLMEERAQLEMKLHAETELYAEAEEMRVRLEAKKQELEEV 927
Cdd:COG1196 231 LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 928 LHEMESRLEEEEDRSNALHNERKEMEQQLQLMEAHIAEEEDARQKLQMEKVSVEGKVKKLEEDILMMEDQNNKLQKERKL 1007
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1008 LEERLADMSSNLAEEEEKSKNLSKLKTKHESMISELELRMKKEEKGRLDMEKAKRKVEAELGDLQEQHADLQAQLAELRA 1087
Cdd:COG1196 391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1088 QLAAKEEELQATQARLEEECNQRGAAVKRVRELE---------VLISELQEDLEAERAARGKVEAARRDLGEELNALRTE 1158
Cdd:COG1196 471 EAALLEAALAELLEELAEAAARLLLLLEAEADYEgflegvkaaLLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQN 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1159 LEDSLGTTAAQQELRAKREQEVSMLKKAMEDEGRSHEAQVQDLRQKHSQAVEELTEQLEQAKRVRAGLekakQALEKESA 1238
Cdd:COG1196 551 IVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVL----GDTLLGRT 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1239 DLSADLRSLASAKQDVEHKKKKVEGQLNELNSRFNESERQRTELGERVSKLTTELDSVTGLLNEAEGKNIKLSKDVSSLS 1318
Cdd:COG1196 627 LVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEE 706
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1319 SQLQDAQELLSEETRQKLNLSGRLRQTEEDRNSLMEQLEEETEAKRAVERQ----VSSLNMQLSDSKKKLDEMsGTV--E 1392
Cdd:COG1196 707 RELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPeppdLEELERELERLEREIEAL-GPVnlL 785
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 1604784239 1393 ALEegkkrlqrELEAANSDYEEKASAYDKLEKSRgrmqQELEDVLMDLDSQRQ 1445
Cdd:COG1196 786 AIE--------EYEELEERYDFLSEQREDLEEAR----ETLEEAIEEIDRETR 826
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1341-1877 |
2.36e-24 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 111.57 E-value: 2.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1341 RLRQTEED-------RNSLMEQLEE-ETEAKRAV----------ERQVSSLNMQLSDSKKKLDEMSGTVEALEEGKKRLQ 1402
Cdd:COG1196 180 KLEATEENlerlediLGELERQLEPlERQAEKAEryrelkeelkELEAELLLLKLRELEAELEELEAELEELEAELEELE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1403 RELEAANSDYEEKASAYDKLEKSRGRMQQELEDVLM-------DLDSQRQLVSNLEKKQKKFDQMLAEERAVSCKFAEER 1475
Cdd:COG1196 260 AELAELEAELEELRLELEELELELEEAQAEEYELLAelarleqDIARLEERRRELEERLEELEEELAELEEELEELEEEL 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1476 DRAEAEAREKETRVLALARALEENQGALEEAEKTMKGLRADMEDLISSKDDVGKSVHDLEKAKRGLEAIVDEMRTQMEEL 1555
Cdd:COG1196 340 EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERL 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1556 EDELQVAEDAKLRLDVNTQALRAQHERELHARDELGEEKRKQLLKQVRELEAELEEERK--QRGQASGSKKKLEGELKDM 1633
Cdd:COG1196 420 EEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAAlaELLEELAEAAARLLLLLEA 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1634 EDQLEATSRG--RDEAVKQLRKIQGQVKDLQRDLEDSRAAQKEVLASA-----RESERRSKAMEADIVQLHEMLAAVERA 1706
Cdd:COG1196 500 EADYEGFLEGvkAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAAlqnivVEDDEVAAAAIEYLKAAKAGRATFLPL 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1707 RKQAEVERDELSEELASNSSGKSLMSDEKRRLDTKISQLEEELEEEQANVESLNDRLRKSQQLVEQLGAELAAERSTSQS 1786
Cdd:COG1196 580 DKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAG 659
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1787 REGSRQQLERQNRELKAKMQEMEGQGRSKLKASIAALEAKLREAEEQLEIESRERQANGKNLRQKEKKLKDLTIQMEDER 1866
Cdd:COG1196 660 GSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLE 739
|
570
....*....|.
gi 1604784239 1867 KQAQQYKDQAE 1877
Cdd:COG1196 740 ELLEEEELLEE 750
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1171-1841 |
6.54e-24 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 110.41 E-value: 6.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1171 ELRAKREQEVSMLKKAMEDEGRsheaqVQDLRqkhsqavEELTEQLEQAKRVRaglEKAKQALEKESADLSADLRSLASA 1250
Cdd:COG1196 169 KYKERKEEAERKLEATEENLER-----LEDIL-------GELERQLEPLERQA---EKAERYRELKEELKELEAELLLLK 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1251 KQDVEHKKKKVEGQLNELNSRFNESERQRTELGERVSKLTTELDSVTGLLNEAEGKNIKLSKDVSSLSSQLQDAQELLSE 1330
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1331 ETRQKLNLSGRLRQTEEDRNSLMEQLEEETEAKRAVERQVSSLNMQLSDSKKKLDEMSGTVEALEEGKKRLQRELEAANS 1410
Cdd:COG1196 314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1411 DYEEKASAYDKLEKSRGRMQQELEdvlmdldsqrqlvsnlekkqkkfdqmlaeeravscKFAEERDRAEAEAREKETRVL 1490
Cdd:COG1196 394 AAAELAAQLEELEEAEEALLERLE-----------------------------------RLEEELEELEEALAELEEEEE 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1491 ALARALEENQGALEEAEKTMKGLRADMEDLISSKDDVGKSVHDLE---------------------------------KA 1537
Cdd:COG1196 439 EEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLeelaeaaarllllleaeadyegflegvkaalllAG 518
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1538 KRGLEAIVDEMRTQMEELEDELQVAEDAKLRLDVNTQALRAQHERELHARDELGEEKRKQLLKQVRELEAELEEERKQRG 1617
Cdd:COG1196 519 LRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIG 598
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1618 QASGSKKKLEGELKDMEDQLEATSRGRDEAVKQLRKIQGQVKDLQRDLEDSRAAQKEVLASARESERRSKAMEADIVQLH 1697
Cdd:COG1196 599 AAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAE 678
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1698 EMLAAVERARKQAEVERDELSEELASNSSGKSLMSDEKRRLDTKISQLEEELEEEQANVESLNDRLRKSQQLVEQLGAEL 1777
Cdd:COG1196 679 AELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPE 758
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1604784239 1778 AAERSTSQSR----EGSRQQLERQN-------RELKAKMQEMEGQgRSKLKASIaaleAKLREAEEQLEIESRER 1841
Cdd:COG1196 759 PPDLEELERElerlEREIEALGPVNllaieeyEELEERYDFLSEQ-REDLEEAR----ETLEEAIEEIDRETRER 828
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1196-1934 |
7.08e-23 |
|
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: 107.06 E-value: 7.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1196 AQVQDLRQKHSQAVEELTEQLEQAKRVRA------GLEKAKQALEKESADlsADLRSLASAKQDVEHKKKKVEGQLNELN 1269
Cdd:TIGR02168 189 DRLEDILNELERQLKSLERQAEKAERYKElkaelrELELALLVLRLEELR--EELEELQEELKEAEEELEELTAELQELE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1270 SRFNESERQRTELGERVSKLTTELDSVTGLLNEAEGKNIKLSKDVSSLSSQLQDAQELLSEETRQKLNLSGRLRQTEEDR 1349
Cdd:TIGR02168 267 EKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1350 NSLMEQLEEETEAKRAVERQVSSLNMQLSDSKKKLDEMSGTVEALEEGKKRLQRELEAANSDYEEkasaydkLEKSRGRM 1429
Cdd:TIGR02168 347 EELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLER-------LEDRRERL 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1430 QQELEDVLMDLDsqrqlvsnlEKKQKKFDQMLAEERAVSCKFAEERDRAEAEAREKETRVlalaRALEENQGALEEAEKT 1509
Cdd:TIGR02168 420 QQEIEELLKKLE---------EAELKELQAELEELEEELEELQEELERLEEALEELREEL----EEAEQALDAAERELAQ 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1510 MKGLRADMEDLISSKDDVGKSVHDLEKAKRGLEAIVDEMRTQMEeLEDELQVAEDAKLRLDVN------------TQALR 1577
Cdd:TIGR02168 487 LQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELIS-VDEGYEAAIEAALGGRLQavvvenlnaakkAIAFL 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1578 AQHERELHARDELGEEKRKQLLKQVRELEAELEEERKQRGQASGSKKKLEGELKDMEDQLEATSRGrDEAVKQLRKIQGQ 1657
Cdd:TIGR02168 566 KQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDL-DNALELAKKLRPG 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1658 VKDLQRDLE----------DSRAAQKEVLASARESER---RSKAMEADIVQLHEMLAAVERARKQAEVERDELSEELASN 1724
Cdd:TIGR02168 645 YRIVTLDGDlvrpggvitgGSAKTNSSILERRREIEEleeKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEEL 724
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1725 SSGKSLMSDEKRRLDTKISQLEEELEEEQANVESLNDRLRKSQQLVEQLGAELAAERSTSQSREGSRQQLERQNRELKAK 1804
Cdd:TIGR02168 725 SRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREA 804
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1805 MQEMEGQGRSkLKASIAaleaKLREAEEQLEIESRERQANGKNLRQKEKKLK-----------DLTIQMEDERKQAQQYK 1873
Cdd:TIGR02168 805 LDELRAELTL-LNEEAA----NLRERLESLERRIAATERRLEDLEEQIEELSedieslaaeieELEELIEELESELEALL 879
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1604784239 1874 DQAEKGNVRVKQLKHQLEEAEEEAQRMAAARRKLQRELDEATEANDTLSRDMASLRSKLRH 1934
Cdd:TIGR02168 880 NERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDN 940
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1117-1886 |
1.14e-22 |
|
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: 106.31 E-value: 1.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1117 VRELEVLISELQEDLEAERAARGKVEAARRDLGEELNALRTELEDSLGTTAAQQELRAKREQEVSMLKKAMEDEGRSHEA 1196
Cdd:TIGR02169 165 VAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1197 QVQDLRQKhsqaVEELTEQLEQ-AKRVRAGLEKAKQALEKESADLSADLRSLASAKQDVEHKKKKVEGQLNELNSRFNES 1275
Cdd:TIGR02169 245 QLASLEEE----LEKLTEEISElEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDA 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1276 ERQRTELGERVSKLTTELDSVTGLLNEAEGKNIKLSKDVSSLSSQLQDAQELLSE------ETRQKL-NLSGRLRQTEED 1348
Cdd:TIGR02169 321 EERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEvdkefaETRDELkDYREKLEKLKRE 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1349 RNSLMEQLEEETEAKRAVERQVSSLNMQLSDSKKKLDEMSGTVEAL-------EEGKKRLQRELEAANSDYEEKASAYDK 1421
Cdd:TIGR02169 401 INELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKaleikkqEWKLEQLAADLSKYEQELYDLKEEYDR 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1422 LEKSRGRMQQELedvlmdldsqrqlvSNLEKKQKKFDQMLAEERAVSCKFAEERDRAEAEAREketrvlaLARALEENQG 1501
Cdd:TIGR02169 481 VEKELSKLQREL--------------AEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQ-------LGSVGERYAT 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1502 ALEEAektmkgLRADMEDLISSKDDVGKSVHDLEKAKRGLEAIVDEMRTQMEELEDELQVAEDAKLRLDVNTQALRAQHE 1581
Cdd:TIGR02169 540 AIEVA------AGNRLNNVVVEDDAVAKEAIELLKRRKAGRATFLPLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKYE 613
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1582 RELH--------------ARDELGEEKRKQLLKQVRELEAELEEERKQRGQASGSKKKLEGELKDMEDQLEATSRGRDEA 1647
Cdd:TIGR02169 614 PAFKyvfgdtlvvedieaARRLMGKYRMVTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSL 693
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1648 VKQLRKIQGQVKDLQRDLEDsraAQKEVlasaRESERRSKAMEADIVQLHEMLAAVERARKQAEVERDELSEELASNSSG 1727
Cdd:TIGR02169 694 QSELRRIENRLDELSQELSD---ASRKI----GEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEAR 766
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1728 KSLMSDEKRRLDTKI-----SQLEEELEEEQANVESLNDRLRKSQQLVEQLGAELAAERSTSQSREGSRQQLERQNRELK 1802
Cdd:TIGR02169 767 IEELEEDLHKLEEALndleaRLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLK 846
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1803 AKMQEME-----GQGR-SKLKASIAALEAKLREAEEQLEIESRERQANGKNLRQKEKKLKDLTIQMEDERKQAQQYKDQA 1876
Cdd:TIGR02169 847 EQIKSIEkeienLNGKkEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKL 926
|
810
....*....|
gi 1604784239 1877 EKGNVRVKQL 1886
Cdd:TIGR02169 927 EALEEELSEI 936
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
867-1569 |
2.13e-22 |
|
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: 105.54 E-value: 2.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 867 AAKEVAAKVETELKDITQKHTQLMEERAQLEmklhaetELYAEAEEMRVRLEAKKQELEEVlheMESRLEEEEDRSNALH 946
Cdd:TIGR02169 224 EGYELLKEKEALERQKEAIERQLASLEEELE-------KLTEEISELEKRLEEIEQLLEEL---NKKIKDLGEEEQLRVK 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 947 NERKEMEQQLQLMEAHIAEEED-------ARQKLQMEKVSVEGKVKKLEEDILMMEDQNNKLQKERKLLEERLADMSSNL 1019
Cdd:TIGR02169 294 EKIGELEAEIASLERSIAEKEReledaeeRLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAEL 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1020 AEEEEKSK----NLSKLKTKHESMISEL-----ELRMKKEEKGRLDMEKAKrkVEAELGDLQEQHADLQAQLAELRAQLA 1090
Cdd:TIGR02169 374 EEVDKEFAetrdELKDYREKLEKLKREInelkrELDRLQEELQRLSEELAD--LNAAIAGIEAKINELEEEKEDKALEIK 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1091 AKEEELQATQARLEEECNQRGAAVKRVRELEVLISELQEDLEAERAARGKVEAARRDLGEELNALRTELEDSLGTTAaqq 1170
Cdd:TIGR02169 452 KQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVA--- 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1171 ELRAKREQEVSMLKKAMEdeGRSHEAQVQDlrqkhsQAVEEltEQLEQAKRVRAG------LEKAKQA-------LEKES 1237
Cdd:TIGR02169 529 QLGSVGERYATAIEVAAG--NRLNNVVVED------DAVAK--EAIELLKRRKAGratflpLNKMRDErrdlsilSEDGV 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1238 ADLSADL---------------------RSLASAK-QDVEHKKKKVEGQLNELNSRFNESERQRTELGERVSKLTTELDS 1295
Cdd:TIGR02169 599 IGFAVDLvefdpkyepafkyvfgdtlvvEDIEAARrLMGKYRMVTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQR 678
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1296 VTGLLNEAEGKNIKLSKDVSSLSSQLQDAQELLSEETRQKLNLSGRLRQTEEDRNSLMEQLEEeteakraVERQVSSLNM 1375
Cdd:TIGR02169 679 LRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEE-------LEEDLSSLEQ 751
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1376 QLSDSKKKLDEMSGTVEALEEGKKRLQRELEA-----ANSDYEEKASAYDKLEKSRGRMQQELEDVLMDLDSQRQLVSNL 1450
Cdd:TIGR02169 752 EIENVKSELKELEARIEELEEDLHKLEEALNDlearlSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYL 831
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1451 EKK-QKKFDQMLAEEravsckfaEERDRAEAEAREKETRVLALARALEENQGALEEAEKTMKGLRADMEDLISSKDDVGK 1529
Cdd:TIGR02169 832 EKEiQELQEQRIDLK--------EQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELER 903
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 1604784239 1530 SVHDLEKAKRGLEAIVDEMRTQMEELEDELQVAEDAKLRL 1569
Cdd:TIGR02169 904 KIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGED 943
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1178-1912 |
1.75e-21 |
|
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: 102.50 E-value: 1.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1178 QEVSMLKKAMedegrsheaqvQDLRQKHSQAVEELTEQLEQAKRVRAGLEKAKQALEKESADLSADLRSLASAKQDVEHK 1257
Cdd:pfam15921 120 QEMQMERDAM-----------ADIRRRESQSQEDLRNQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQE 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1258 KKKV-----EGQLNELNSRFNESERQRTELGERVSKLTTELDSVTGLLneaEGKNIKLSKDVSSLSSQLQDAQELLSEET 1332
Cdd:pfam15921 189 IRSIlvdfeEASGKKIYEHDSMSTMHFRSLGSAISKILRELDTEISYL---KGRIFPVEDQLEALKSESQNKIELLLQQH 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1333 RQKLN------------LSGRLRQTEEDRNSLMEQLEEETEAKRAVE----RQVSSLNMQLSDSKKKLDEMSGTVE-ALE 1395
Cdd:pfam15921 266 QDRIEqliseheveitgLTEKASSARSQANSIQSQLEIIQEQARNQNsmymRQLSDLESTVSQLRSELREAKRMYEdKIE 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1396 EgkkrLQRELEAANSDYEEKASAYDKLEKSRGRMQQELEDVLMDLDSQRQLVSnLEKKQKKfdqmLAEERAVSCKFAEER 1475
Cdd:pfam15921 346 E----LEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELS-LEKEQNK----RLWDRDTGNSITIDH 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1476 DRAEAEAREKET-RVLALARALE-ENQGALEEAEKTMKGLRADMEDlisskddVGKSVHDLEKAKRGLEAIVDEMRTQME 1553
Cdd:pfam15921 417 LRRELDDRNMEVqRLEALLKAMKsECQGQMERQMAAIQGKNESLEK-------VSSLTAQLESTKEMLRKVVEELTAKKM 489
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1554 ELEDELQVAEDAKLRLDVNTQALRAQHER--ELHARDELGEEKRKQLLKQVRELEAELEEERKQRGQASGSKKKLEGELK 1631
Cdd:pfam15921 490 TLESSERTVSDLTASLQEKERAIEATNAEitKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQ 569
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1632 DMEDQLEATSR-GRDEAVKQLRKIQ--GQVKDLQRDLEDSRAAQKEVLASARESERRSKAMEADIVQLHEMLAAVERARK 1708
Cdd:pfam15921 570 QIENMTQLVGQhGRTAGAMQVEKAQleKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVK 649
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1709 QAEVERDELSEELASNSSGKSLMSDEKRRLDTKISQleeELEEEQANVESLNDRLRKSQqlveqlgAELAAERSTSQSRE 1788
Cdd:pfam15921 650 DIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRN---KSEEMETTTNKLKMQLKSAQ-------SELEQTRNTLKSME 719
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1789 GSRQQLERQNRELKAKMQEMEGQgRSKLKASIAALEAKLREAEEQLEIESRERQANGKNLRQKEKKLKDLTIQMEDERKQ 1868
Cdd:pfam15921 720 GSDGHAMKVAMGMQKQITAKRGQ-IDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQ 798
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 1604784239 1869 AQQYKDQAEKGNVRVKQLKHQLEEAEE--EAQRMAAARRKLQRELD 1912
Cdd:pfam15921 799 ERRLKEKVANMEVALDKASLQFAECQDiiQRQEQESVRLKLQHTLD 844
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
855-1598 |
2.10e-21 |
|
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: 102.45 E-value: 2.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 855 EEEMGQKDEELKA-AKEVAAKVETELKDITQKHTQLMEERAQLEMKLHAETELYAEAEEMRVRLEAKKQELEEVLHEMES 933
Cdd:TIGR02169 264 EKRLEEIEQLLEElNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELER 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 934 RLEEEEDRSNALHNERKEMEQQLQLMEAHIAEEEDARQKLQMEKVSVEGKVKKLEEDILMMEDQNNKLQKERKLLEERLA 1013
Cdd:TIGR02169 344 EIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELA 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1014 DMSSNLAEEEEKSKNLSKLKTKHESMISELELRMKKEEKGRLDMEKAKRKVEAELGDLQEQHADLQAQLAELRAQLAAKE 1093
Cdd:TIGR02169 424 DLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASE 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1094 EELQATQARLEEECNQRGAAVKRVRELevliselqedLEAERAARGKVEAArrdLGEELNALrtELEDSLGTTAAQQELR 1173
Cdd:TIGR02169 504 ERVRGGRAVEEVLKASIQGVHGTVAQL----------GSVGERYATAIEVA---AGNRLNNV--VVEDDAVAKEAIELLK 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1174 AKREQEVSML-----KKAMEDEGRSHEAQVQDL-------RQKHSQAVEE------LTEQLEQAKRVRAGLEKAkqALEK 1235
Cdd:TIGR02169 569 RRKAGRATFLplnkmRDERRDLSILSEDGVIGFavdlvefDPKYEPAFKYvfgdtlVVEDIEAARRLMGKYRMV--TLEG 646
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1236 ESADLSADLRSLASAKQDVEHKKKKVEGQLNELNSRFNESERQRTELGERVSKLTTELDSVTGLLNEAEGKNIKLSKDVS 1315
Cdd:TIGR02169 647 ELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIE 726
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1316 SLSSQLQDAQELLSEETRQKLNLSGRLRQTEEDRNSLMEQLEEETEAKRAVERQVSSLNMQLSDSkkKLDEMSGTVEALE 1395
Cdd:TIGR02169 727 QLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHS--RIPEIQAELSKLE 804
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1396 EGKKRLQRELEAANSDYEEKASAYDKLEKSRGRMQQELEDVLMDLDSQRQLVSNLEKKQKKFDQMLAEERAVSCKFAEER 1475
Cdd:TIGR02169 805 EEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRL 884
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1476 DRAEAEAREKETRVLALARALEENQGALEEAEKTMKGLRADMEDLISSKDDVGKSVHDLEKAKrGLEAIVDEMRTQMEEL 1555
Cdd:TIGR02169 885 GDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIP-EEELSLEDVQAELQRV 963
|
730 740 750 760
....*....|....*....|....*....|....*....|...
gi 1604784239 1556 EDELQVAEdaklrlDVNTQALRaQHERELHARDELgEEKRKQL 1598
Cdd:TIGR02169 964 EEEIRALE------PVNMLAIQ-EYEEVLKRLDEL-KEKRAKL 998
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1209-1932 |
3.92e-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: 98.22 E-value: 3.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1209 VEELTEQLEQAKRVRAGLEKAkQALEKESADLSADLrsLASAKQDVEHKKKKVEGQLNELNSRFNESERQRTELGERVSK 1288
Cdd:TIGR02169 193 IDEKRQQLERLRREREKAERY-QALLKEKREYEGYE--LLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1289 LTTELDSVTGLLNE-AEGKNIKLSKDVSSLSSQLQDAQELLSEETRQKLNLSGRLRQTEEDRNSLMEQLEEETEAKRAVE 1367
Cdd:TIGR02169 270 IEQLLEELNKKIKDlGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEER 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1368 RQVSSLNMQLSDSKKKLDEMSGTVEALEEGKKRLQRELEAANSDYEEKASAYDKLEKSRGRMQQELEDVLMDLDSQRQLV 1447
Cdd:TIGR02169 350 KRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAI 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1448 SNLEKKQKKFDqmlaeeravsckfaEERDRAEAEAREKETRvlalaraLEENQGALEEAEKTMKGLRADMEDLISSKDDV 1527
Cdd:TIGR02169 430 AGIEAKINELE--------------EEKEDKALEIKKQEWK-------LEQLAADLSKYEQELYDLKEEYDRVEKELSKL 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1528 GKSVHDLEKAKRGLEAIVDEMRTQMEELEDELQ-----VAEDAKLRLDVNTqALRAQHERELHA---RDELGEEKRKQLL 1599
Cdd:TIGR02169 489 QRELAEAEAQARASEERVRGGRAVEEVLKASIQgvhgtVAQLGSVGERYAT-AIEVAAGNRLNNvvvEDDAVAKEAIELL 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1600 KQVRELEAELEEERK-QRGQASGSKKKLEG------ELKDMEDQLEATSRG--RD----EAVKQLRKIQGQVK--DLQRD 1664
Cdd:TIGR02169 568 KRRKAGRATFLPLNKmRDERRDLSILSEDGvigfavDLVEFDPKYEPAFKYvfGDtlvvEDIEAARRLMGKYRmvTLEGE 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1665 LED--------SRAAQKEVLASARESERrSKAMEADIVQLHEMLAAVERARKQAEVERDELSEELASNSSGKSLMSDEKR 1736
Cdd:TIGR02169 648 LFEksgamtggSRAPRGGILFSRSEPAE-LQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIE 726
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1737 RLDTKISQLEEELEEEQANVESLNDRLRKSQQLVEQLGAELAAERSTSQSREGSRQQLER-----QNRELKAKMQEMEGQ 1811
Cdd:TIGR02169 727 QLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEArlshsRIPEIQAELSKLEEE 806
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1812 gRSKLKASIAALEAKLREAEEQLEIESRERQANGKNLRQKEKKLKDLTIQMEDERKQAQQYKDQAEKGNVRVKQLKHQLE 1891
Cdd:TIGR02169 807 -VSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLG 885
|
730 740 750 760
....*....|....*....|....*....|....*....|.
gi 1604784239 1892 EAEEEAQRMAAARRKLQRELDEATEANDTLSRDMASLRSKL 1932
Cdd:TIGR02169 886 DLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKL 926
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1076-1593 |
2.69e-19 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 95.11 E-value: 2.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1076 ADLQAQLAELRAQLAAKEE------------ELQATQARLEEECNQRGAAVKRVRELEVLISE----------LQEDLEA 1133
Cdd:PRK02224 183 SDQRGSLDQLKAQIEEKEEkdlherlnglesELAELDEEIERYEEQREQARETRDEADEVLEEheerreeletLEAEIED 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1134 ERAARGKVEAARRDLGEELNALR---TELEDSLGTTAAQQELRAKREQEVSMLKKAMEDEgrshEAQVQDLRQKHSQAVE 1210
Cdd:PRK02224 263 LRETIAETEREREELAEEVRDLRerlEELEEERDDLLAEAGLDDADAEAVEARREELEDR----DEELRDRLEECRVAAQ 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1211 ELTEQLEQAKRVRAGLEKAKQALEKESADLSADLRSLASAKQDVEHKKKKVEGQLNELNSRFNESERQRTELGERVSKLT 1290
Cdd:PRK02224 339 AHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELR 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1291 TELDSVTGLLNEaegknikLSKDVSSLSSQLQDAQELLSE----ETRQKLNLSGRLRQTEEDRnslmEQLEEETEAKRAV 1366
Cdd:PRK02224 419 EERDELREREAE-------LEATLRTARERVEEAEALLEAgkcpECGQPVEGSPHVETIEEDR----ERVEELEAELEDL 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1367 ERQVSSLNMQLsDSKKKLDEMSGTVEALEEGKKRLQRELEAANSDYEEKAsayDKLEKSRGRmQQELEDvlmdldsqrql 1446
Cdd:PRK02224 488 EEEVEEVEERL-ERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKR---ERAEELRER-AAELEA----------- 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1447 vsnlEKKQKKFDQMLAEERAVSCkfAEERDRAEAEAREKETRVLALARaLEENQGALEEAEKTMKGLRADMEDLISSKDD 1526
Cdd:PRK02224 552 ----EAEEKREAAAEAEEEAEEA--REEVAELNSKLAELKERIESLER-IRTLLAAIADAEDEIERLREKREALAELNDE 624
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1604784239 1527 VGKSVHDLEKAKRGLEAIVDEMRtqMEELEDELQVAEDAKLRLDVNTQALRAQH----------ERELHARDELGEE 1593
Cdd:PRK02224 625 RRERLAEKRERKRELEAEFDEAR--IEEAREDKERAEEYLEQVEEKLDELREERddlqaeigavENELEELEELRER 699
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
889-1549 |
4.93e-19 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 94.36 E-value: 4.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 889 LMEERAQLEMKLHAETELYAEAEEMRVRLEAKKQELEEVLHEMESRLEEEEDrsnaLHNERKEMEQQLQLMEAHIAEEEd 968
Cdd:PRK03918 167 LGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPE----LREELEKLEKEVKELEELKEEIE- 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 969 arqKLQMEKVSVEGKVKKLEEDILMMEDQNNKLQKERKLLEERLADMSSnLAEEEEKSKNLSKLKTKHesmiselelrmk 1048
Cdd:PRK03918 242 ---ELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKE-LKEKAEEYIKLSEFYEEY------------ 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1049 keekgrldmEKAKRKVEAELGDLQEQHADLQAQLAElraqLAAKEEELQATQARLEEECNQRGAAVKRVRELEvLISELQ 1128
Cdd:PRK03918 306 ---------LDELREIEKRLSRLEEEINGIEERIKE----LEEKEERLEELKKKLKELEKRLEELEERHELYE-EAKAKK 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1129 EDLEAERAARG--KVEAARRDLgEELNALRTELEDSLGTTAAQqelRAKREQEVSMLKKAMEdegrsheaQVQDLRQKHS 1206
Cdd:PRK03918 372 EELERLKKRLTglTPEKLEKEL-EELEKAKEEIEEEISKITAR---IGELKKEIKELKKAIE--------ELKKAKGKCP 439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1207 QAVEELTEqleqakrvraglEKAKQALEKESADLSadlrslasakqDVEHKKKKVEGQLNELNSRFNESERQRTElGERV 1286
Cdd:PRK03918 440 VCGRELTE------------EHRKELLEEYTAELK-----------RIEKELKEIEEKERKLRKELRELEKVLKK-ESEL 495
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1287 SKLTTELDSVTGLLNEAEGKNIKLSKdvsslssqlQDAQELlsEETRQKLN-LSGRLRQTEEDrnslMEQLEEETEAKRA 1365
Cdd:PRK03918 496 IKLKELAEQLKELEEKLKKYNLEELE---------KKAEEY--EKLKEKLIkLKGEIKSLKKE----LEKLEELKKKLAE 560
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1366 VERQVSSLNMQLSDSKKKLDEMSgtVEALEEGKKRLQrELEAANSDYEEKASAYDKLEksrgRMQQELEDVLMDLDSQRQ 1445
Cdd:PRK03918 561 LEKKLDELEEELAELLKELEELG--FESVEELEERLK-ELEPFYNEYLELKDAEKELE----REEKELKKLEEELDKAFE 633
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1446 lvsNLEKKQKKFDQMLAEERAVSCKFAEER-DRAEAEAREKETRVLALARALEENQGALEEAEKTMKGLRADMEDLISSK 1524
Cdd:PRK03918 634 ---ELAETEKRLEELRKELEELEKKYSEEEyEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAK 710
|
650 660
....*....|....*....|....*
gi 1604784239 1525 ddvgKSVHDLEKAKRGLEAIVDEMR 1549
Cdd:PRK03918 711 ----KELEKLEKALERVEELREKVK 731
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
863-1393 |
5.23e-19 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 93.95 E-value: 5.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 863 EELKAAKEVAAKVETELKDITQKHTQLMEERAQLEMKLHAETELYAEAEEMRVRLEAKKQELEEVLHEMESRLEEEEDRS 942
Cdd:PRK02224 223 ERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEA 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 943 NALHNERKEMEQQLQLMEAhiaEEEDARQKLQMEKVSV---EGKVKKLEEDILMMEDQNNKLQKERKLLEERLADMSSNL 1019
Cdd:PRK02224 303 GLDDADAEAVEARREELED---RDEELRDRLEECRVAAqahNEEAESLREDADDLEERAEELREEAAELESELEEAREAV 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1020 AEEEEKsknlsklktkhesmISELELRMKKEEKGRLDMEKAKRKVEAELGDLQEQHADLQAQLAELRAQLAAKEEELQAT 1099
Cdd:PRK02224 380 EDRREE--------------IEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEA 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1100 QARLEE----ECNQ---RGAAVKRVRELEVLISELQEDLEAERAARGKVEaARRDLGEELNALRTELEDSLGTTAAQQEL 1172
Cdd:PRK02224 446 EALLEAgkcpECGQpveGSPHVETIEEDRERVEELEAELEDLEEEVEEVE-ERLERAEDLVEAEDRIERLEERREDLEEL 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1173 RAKREQEVsmlkKAMEDEGRSHEAQVQDLRQKHSQAVEELTEQLEQAKRVR---AGLEKAKQALEKES---ADLSADLRS 1246
Cdd:PRK02224 525 IAERRETI----EEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAReevAELNSKLAELKERIeslERIRTLLAA 600
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1247 LASAKQDVEHKKKKVEgQLNELNsrfNESERQRTELGERVSKLTTELDsvtgllneaegkniklskdvsslSSQLQDAQE 1326
Cdd:PRK02224 601 IADAEDEIERLREKRE-ALAELN---DERRERLAEKRERKRELEAEFD-----------------------EARIEEARE 653
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1604784239 1327 LLSEETRQKLNLSGRLRQTEEDRNSL----------MEQLEEETEAKRAVERQVSSLNmQLSDSKKKLDEMSGTVEA 1393
Cdd:PRK02224 654 DKERAEEYLEQVEEKLDELREERDDLqaeigaveneLEELEELRERREALENRVEALE-ALYDEAEELESMYGDLRA 729
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1330-1933 |
2.18e-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: 92.43 E-value: 2.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1330 EETRQKLN--------LSGRLRQTEEDRNSLMEQlEEETEAKRAVERQVSSLnmQLSDSKKKLDEMSGTVEALEEGKKRL 1401
Cdd:TIGR02168 175 KETERKLErtrenldrLEDILNELERQLKSLERQ-AEKAERYKELKAELREL--ELALLVLRLEELREELEELQEELKEA 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1402 QRELEAANSDYEEKASAYDKLEKSRGRMQQELEDVLMDLDSQRQLVSNLEKKQKKFDQMLAEERAvsckfaeERDRAEAE 1481
Cdd:TIGR02168 252 EEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLER-------QLEELEAQ 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1482 AREKETRVLALARALEENQGALEEAEKTMKGLRADMEDLISSKDDVGKSVHDLEKAKRGLEAIVDEMRTQMEELEDELQV 1561
Cdd:TIGR02168 325 LEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIER 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1562 AEDAKLRLDVNTQALRAqherelhardELGEEKRKQLLKQVRELEAELEEERKQRGQASGSKKKLEGELKDMEDQLEATS 1641
Cdd:TIGR02168 405 LEARLERLEDRRERLQQ----------EIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAE 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1642 RGRDEAVKQLRKIQGQVKDLQRDLEDSRAAQKEVLASARESERRSKAME--ADIVQLHE----MLAAVERARKQAEVERD 1715
Cdd:TIGR02168 475 QALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGvlSELISVDEgyeaAIEAALGGRLQAVVVEN 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1716 ELS-----EELASNSSGKSLMSDEKRRLDTKISQLEEELEEEQANVESLNDRLRKS---------------------QQL 1769
Cdd:TIGR02168 555 LNAakkaiAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFdpklrkalsyllggvlvvddlDNA 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1770 VEQLGAELAAER--------------STSQSREGSRQQLERQN--RELKAKMQEMEGQGRSkLKASIAALEAKLREAEEQ 1833
Cdd:TIGR02168 635 LELAKKLRPGYRivtldgdlvrpggvITGGSAKTNSSILERRReiEELEEKIEELEEKIAE-LEKALAELRKELEELEEE 713
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1834 LEIESRERQANGKNLRQKEKKLKDLTIQMEDERKQAQQYKDQAEKGNVRVKQLKHQLEEAEEEAQRMAAARRKLQRELDE 1913
Cdd:TIGR02168 714 LEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQ 793
|
650 660
....*....|....*....|
gi 1604784239 1914 ATEANDTLSRDMASLRSKLR 1933
Cdd:TIGR02168 794 LKEELKALREALDELRAELT 813
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1010-1495 |
9.29e-18 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 90.36 E-value: 9.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1010 ERLADMSSNLAEEEEKSKNLSKLKTKHESMIS-ELELRMKKEEKGRLDMEKAKRKV---EAELGDLQEQHADLQAQLAEL 1085
Cdd:COG4913 235 DDLERAHEALEDAREQIELLEPIRELAERYAAaRERLAELEYLRAALRLWFAQRRLellEAELEELRAELARLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1086 RAQLAAKEEELQATQARLeeecnqRGAAVKRVRELEVLISELQEDLEAERAARGKVEAARRDLGEELNALRTELEdslgt 1165
Cdd:COG4913 315 EARLDALREELDELEAQI------RGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFA----- 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1166 tAAQQELRAKREQEVSmLKKAMEDEGRSHEAQVQDLRQKHSQAVEELTEQLEQAKRVRAGLEKAKQALEKESADLSADL- 1244
Cdd:COG4913 384 -ALRAEAAALLEALEE-ELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLDEAELp 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1245 ----------------------------------RSLASAKQDVEHKKKKVEGQLNELNSRFNESERQRTELGERVSKLT 1290
Cdd:COG4913 462 fvgelievrpeeerwrgaiervlggfaltllvppEHYAAALRWVNRLHLRGRLVYERVRTGLPDPERPRLDPDSLAGKLD 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1291 TEL--------------------DSVTGLLNE-----AEGKnIKLSKD-----------------------VSSLSSQLQ 1322
Cdd:COG4913 542 FKPhpfrawleaelgrrfdyvcvDSPEELRRHpraitRAGQ-VKGNGTrhekddrrrirsryvlgfdnrakLAALEAELA 620
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1323 DAQELLSEETRQKLNLSGRLRQTEEDRNSLmEQLEEETEAK---RAVERQVSSLNMQLSDskkkLDEMSGTVEALEEGKK 1399
Cdd:COG4913 621 ELEEELAEAEERLEALEAELDALQERREAL-QRLAEYSWDEidvASAEREIAELEAELER----LDASSDDLAALEEQLE 695
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1400 RLQRELEAANSDYEEKASAYDKLEKSRGRMQQELEDVLMDLDSQRQLVSNLEKKQkkFDQMLAE------ERAVSCKFAE 1473
Cdd:COG4913 696 ELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL--LEERFAAalgdavERELRENLEE 773
|
570 580
....*....|....*....|..
gi 1604784239 1474 ERDRAEAEAREKETRVLALARA 1495
Cdd:COG4913 774 RIDALRARLNRAEEELERAMRA 795
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1357-1935 |
1.10e-17 |
|
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: 89.85 E-value: 1.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1357 EEETEAKravERQVSSLNMQLSDSKKKLDEMSGTVEALEEGKKRLQRELEAANSDYEEKasaydklEKSRGRM---QQEL 1433
Cdd:pfam01576 4 EEEMQAK---EEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEA-------EEMRARLaarKQEL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1434 EDVLMDLDSQ--------RQLVSNLEKKQ---KKFDQMLAEERAVSCKFAEERDRAEAEAREKETRVLALA--------- 1493
Cdd:pfam01576 74 EEILHELESRleeeeersQQLQNEKKKMQqhiQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEdqnsklske 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1494 -RALEE-------NQGALEEAEKTMKGLRADMEDLISSKDD----VGKSVHDLEKAKRGLEAIVDEMRTQMEELEDELQV 1561
Cdd:pfam01576 154 rKLLEEriseftsNLAEEEEKAKSLSKLKNKHEAMISDLEErlkkEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1562 AEDAKLRLDVNTQALRAQHERELHARDELgEEKRKQLLKQVRELEAELEEERKQRGQASGSKKKLEGELKDMEDQLEATs 1641
Cdd:pfam01576 234 LRAQLAKKEEELQAALARLEEETAQKNNA-LKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDT- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1642 RGRDEAVKQLR-KIQGQVKDLQRDLEDSRAAQKEVLASAREseRRSKAMEADIVQLHEML---AAVERARKQAEVERDEL 1717
Cdd:pfam01576 312 LDTTAAQQELRsKREQEVTELKKALEEETRSHEAQLQEMRQ--KHTQALEELTEQLEQAKrnkANLEKAKQALESENAEL 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1718 SEELASNSSGKSLMSDEKRRLDTKISQLEEELEEEQANVESLNDRLRKSQQLVEQLGAELAAERSTSQSREGSRQQLERQ 1797
Cdd:pfam01576 390 QAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQ 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1798 NRELKAKMQEmEGQGRSKLKASIAALEAKLREAEEQLEIESRERQANGKNLRQKEKKLKDLTIQMEDERKQAQQYKDQAE 1877
Cdd:pfam01576 470 LQDTQELLQE-ETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKK 548
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 1604784239 1878 KGNVRVKQLKHQLEEAEEEAQRMAAARRKLQRELDEATEANDTLSRDMASLRSKLRHY 1935
Cdd:pfam01576 549 RLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKF 606
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
852-1572 |
1.32e-16 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 86.73 E-value: 1.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 852 TRQEEEMGQKDEELKAAKEVAAKVETELKDITQKHTQLMEERAQLEMKLHAETELYAEAEEMRVRLEAKKQE----LEEV 927
Cdd:PTZ00121 1108 TGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEaarkAEEV 1187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 928 LHEMESRLEEEEDRSNalhnERKEMEQQLQLMEAHIAEEEDarqklQMEKVSVEGKVKKLEEDILMMEDQNNKlQKERKL 1007
Cdd:PTZ00121 1188 RKAEELRKAEDARKAE----AARKAEEERKAEEARKAEDAK-----KAEAVKKAEEAKKDAEEAKKAEEERNN-EEIRKF 1257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1008 LEERLADMSSNLAEEEEKSKNLSKLKTKHESMISELELRmKKEEKGRLD--MEKAKRKVEAELGDLQEQHADLQAQLAEL 1085
Cdd:PTZ00121 1258 EEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAK-KAEEKKKADeaKKKAEEAKKADEAKKKAEEAKKKADAAKK 1336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1086 RAQLAAKEEElqATQARLEEECNQRGAAVKRVRELEVLISELQEDLEAERAARGKVEAAR--RDLGEELNALRTELEDSL 1163
Cdd:PTZ00121 1337 KAEEAKKAAE--AAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADeaKKKAEEDKKKADELKKAA 1414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1164 GTTAAQQELRAKREQevsmLKKAMEDEGRSHEAQVQDLRQKHSQAVEELTEQLEQAKRVRAGLEKAKQALEKESADLSAd 1243
Cdd:PTZ00121 1415 AAKKKADEAKKKAEE----KKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAK- 1489
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1244 lRSLASAKQDVEHKKKKVEGQLNELNSRFNESERQRTELGERVSKLTTEldsvtgLLNEAEGKNiklskdvssLSSQLQD 1323
Cdd:PTZ00121 1490 -KKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKAD------EAKKAEEKK---------KADELKK 1553
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1324 AQELLSEETRQKLNlsgRLRQTEEDRNSLMEQLEEETEAKRAVERQVSSLNMQLSDSK----KKLDEMSGTVEAL--EEG 1397
Cdd:PTZ00121 1554 AEELKKAEEKKKAE---EAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKaeeaKKAEEAKIKAEELkkAEE 1630
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1398 KKRLQRELEAANSDYEEKASAYDKLEKSRG-RMQQELEDVLMDLDSQRQLVSNLEKKQKKFDQMLAEERavSCKFAEERD 1476
Cdd:PTZ00121 1631 EKKKVEQLKKKEAEEKKKAEELKKAEEENKiKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAE--EAKKAEELK 1708
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1477 RAEAEAREKETRVlalARALEENQGALEEAEKTMKGLRADMEDLISSKDDVGKSVHDLEKAKRGLEAIVDEMRTQMEELE 1556
Cdd:PTZ00121 1709 KKEAEEKKKAEEL---KKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEEL 1785
|
730
....*....|....*.
gi 1604784239 1557 DElqvaEDAKLRLDVN 1572
Cdd:PTZ00121 1786 DE----EDEKRRMEVD 1797
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
850-1189 |
1.90e-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: 1.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 850 QVTRQEEEMGQKDEELKAAKEVAAKVETELKDITQKHTQLMEERAQLEMKLHAETELYAEAEEMRVRLEAKKQELEEVLH 929
Cdd:TIGR02169 696 ELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLH 775
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 930 EMESRLEEEEDRSN-----ALHNERKEMEQQLQLMEAHIAEEEDARQKLQMEKVSVEGKVKKLEEDILMMEDQNNKLQKE 1004
Cdd:TIGR02169 776 KLEEALNDLEARLShsripEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKE 855
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1005 RKLLEERLADMSSNLAEeeeksknlsklktkHESMISELELRMKKEEKGRLDMEKAKRKVEAELGDLQEQHADLQAQLAE 1084
Cdd:TIGR02169 856 IENLNGKKEELEEELEE--------------LEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSE 921
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1085 LRAQLAAKEEELQATQARLEEecnqrgaavkrvrelEVLISELQEDLEAERAARGKVEAARRDLGEELNALRTELEDSLG 1164
Cdd:TIGR02169 922 LKAKLEALEEELSEIEDPKGE---------------DEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLK 986
|
330 340
....*....|....*....|....*
gi 1604784239 1165 TTAAQQELRAKREQEVSMLKKAMED 1189
Cdd:TIGR02169 987 RLDELKEKRAKLEEERKAILERIEE 1011
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1541-1878 |
3.71e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 84.99 E-value: 3.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1541 LEAIVDEMRTQMEELEDElqvAEdaklrldvntQALRAQherelhardELGEEKRkqllkqvreleaeleeeRKQRGQAS 1620
Cdd:COG1196 191 LEDILGELERQLEPLERQ---AE----------KAERYR---------ELKEELK-----------------ELEAELLL 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1621 GSKKKLEGELKDMEDQLEATSRGRDEAVKQLRKIQGQVKDLQRDLEDSRAAQKEVLASARESERRSKAMEADIVQLHEML 1700
Cdd:COG1196 232 LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERR 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1701 AAVERARKQAEVERDELSEELASNSSGKSLMSDEKRRLDTKISQLEEELEEEQANVESLNDRLRKSQQLVEQLGAELAAE 1780
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1781 RSTSQSREGSRQQLERQNRELKAKMQEMEGQGRSKLKASIAALEAKLREAEEQLEIESRERQANGKNLRQKEKKLKDLTI 1860
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471
|
330
....*....|....*...
gi 1604784239 1861 QMEDERKQAQQYKDQAEK 1878
Cdd:COG1196 472 AALLEAALAELLEELAEA 489
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
862-1430 |
4.70e-16 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 84.35 E-value: 4.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 862 DEELKAAKEVAAKVETELKDITQKHTQLMEERAQLEmklhaetELYAEAEEMRVRLEAKKQELEEVlhemesrleeeedr 941
Cdd:PRK03918 192 EELIKEKEKELEEVLREINEISSELPELREELEKLE-------KEVKELEELKEEIEELEKELESL-------------- 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 942 snalhnerkemEQQLQLMEAHIAEEEDARQKLQMEKVSVEGKVKKLEEdILMMEDQNNKLQKERKLLEERLADMSSNLAE 1021
Cdd:PRK03918 251 -----------EGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKE-LKEKAEEYIKLSEFYEEYLDELREIEKRLSR 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1022 EEEKSKNLSKLKTKHESMISELELRMKKEEKGRLDMEKAKRKVEaelgdLQEQHADLQAQLAELRAQLAAK-----EEEL 1096
Cdd:PRK03918 319 LEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHE-----LYEEAKAKKEELERLKKRLTGLtpeklEKEL 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1097 QATQARLEEECNQRGAAVKRVRELEVLISELQEDLEAERAARGKVEAARRDLGEE-----LNALRTELEDSLGTTAAQQE 1171
Cdd:PRK03918 394 EELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEhrkelLEEYTAELKRIEKELKEIEE 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1172 LRAKREQEVSMLKKAMEDEGR--SHEAQVQDLRQKHSQAVEELTEQLEQAKRVRAGLEKAKQALEKESADLSADLRSLA- 1248
Cdd:PRK03918 474 KERKLRKELRELEKVLKKESEliKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEe 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1249 --SAKQDVEHKKKKVEGQLNELNsrfneserqrTELGERVSKLTTELDSVTGLLNEAEGKNIKLSKDVSSLSSQLQDAQE 1326
Cdd:PRK03918 554 lkKKLAELEKKLDELEEELAELL----------KELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKK 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1327 LLSEETRQKLNLSGRLRQTEEDRNSLMEQLEEETEAK-RAVERQVSSLNMQLSDSKKKLDEMSGTVEALEEGKKRLQREL 1405
Cdd:PRK03918 624 LEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEyEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEEL 703
|
570 580
....*....|....*....|....*
gi 1604784239 1406 EAAnsdyEEKASAYDKLEKSRGRMQ 1430
Cdd:PRK03918 704 EER----EKAKKELEKLEKALERVE 724
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1249-1829 |
1.36e-15 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 83.17 E-value: 1.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1249 SAKQDVEHKKKKVEGQLNELNSRFNESERqrTELGERVSKLTTELDSVTGLLNEAEGKNIKLSkdvsslsSQLQDAQELL 1328
Cdd:PRK02224 173 DARLGVERVLSDQRGSLDQLKAQIEEKEE--KDLHERLNGLESELAELDEEIERYEEQREQAR-------ETRDEADEVL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1329 SEEtrqklnlsgrlRQTEEDRNSLMEQLEEETEAKRAVERQVSSLNMQLSDSKKKLDEmsgtveaLEEGKKRLQRELEAA 1408
Cdd:PRK02224 244 EEH-----------EERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEE-------LEEERDDLLAEAGLD 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1409 NSDYEEKASAYDKLEKSRGRMQQELEDVLMDLDSQRQLVSNLEKKQKKFDQMLAEERAVSCKFAEERDRAEAEAREKETR 1488
Cdd:PRK02224 306 DADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREE 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1489 VLALARALEENQGALEEAEKTMKGLRADMEDLISSKDDVGKSVHDLE-----------KAKRGLEA-------------- 1543
Cdd:PRK02224 386 IEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEatlrtarerveEAEALLEAgkcpecgqpvegsp 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1544 ---IVDEMRTQMEELEDELQVAEDAklRLDVNTQALRAQHERELHARDELGEEKRKQLLKQVRELEAELEEERKQRGQAS 1620
Cdd:PRK02224 466 hveTIEEDRERVEELEAELEDLEEE--VEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELR 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1621 GSKKKLEGElkdMEDQLEATSRGRDEAVKQLRKiqgqVKDLQRDLEDSrAAQKEVLASARESERRSKAMEADIVQLHEM- 1699
Cdd:PRK02224 544 ERAAELEAE---AEEKREAAAEAEEEAEEAREE----VAELNSKLAEL-KERIESLERIRTLLAAIADAEDEIERLREKr 615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1700 --LAAVERARKQAEVERDELSEELASNSSGKSL--MSDEKRRLDTKISQLEEELEEEQANVESLNDRLRKSQQLVEQLgA 1775
Cdd:PRK02224 616 eaLAELNDERRERLAEKRERKRELEAEFDEARIeeAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEEL-E 694
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 1604784239 1776 ELAAERSTSQSREGSRQQLERQNRELkakmQEMEGQGRSKLKA-SIAALEAKLRE 1829
Cdd:PRK02224 695 ELRERREALENRVEALEALYDEAEEL----ESMYGDLRAELRQrNVETLERMLNE 745
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1174-1889 |
1.81e-15 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 83.27 E-value: 1.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1174 AKREQEVSMLKKAMEDEGRSHEaqvqdlRQKHSQAVEELTEQLEQAKRVRAGLEKAKQALEKESADLSADLRSLASAKQD 1253
Cdd:PTZ00121 1075 SYKDFDFDAKEDNRADEATEEA------FGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKA 1148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1254 VEHKKKKVEGQLNELNsRFNESERQRTELGERVSKLTTELDSVTGLLNEAEGKNIKLSKDvsslSSQLQDAQELLSEETR 1333
Cdd:PTZ00121 1149 EDAKRVEIARKAEDAR-KAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARK----AEEERKAEEARKAEDA 1223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1334 QKLNlsgRLRQTEEDRnslmeqlEEETEAKRAVERQVSSLNMQLSDSKKKLDEMSGTVEALEEgkKRLQRELEAAnsdyE 1413
Cdd:PTZ00121 1224 KKAE---AVKKAEEAK-------KDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEE--ARKADELKKA----E 1287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1414 EKASAYDKLEKSRGRMQQELEDVLMDLDSQRQLVSNLEKKQKKFDQmlAEERAVSCKFAEERDRAEAEAREKEtrvlala 1493
Cdd:PTZ00121 1288 EKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADA--AKKKAEEAKKAAEAAKAEAEAAADE------- 1358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1494 raleenqgaLEEAEKTMKGLRADMEDLISSKDDVGKSVHDLEKAkrgleaivDEMRTQMEELE---DELQVAEDAKLRLD 1570
Cdd:PTZ00121 1359 ---------AEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKA--------DEAKKKAEEDKkkaDELKKAAAAKKKAD 1421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1571 VNTQalRAQHERELHARDELGEEKRK--QLLKQVRELEAELEEERKQRGQASGSKKKLEGELKDMEDQLEATSRGRDEAV 1648
Cdd:PTZ00121 1422 EAKK--KAEEKKKADEAKKKAEEAKKadEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKA 1499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1649 KQLRKIQGQVKDLQRDLEDSRAAQKEVLASARESERRSKAMEADIVQLHEMLAAVERARKQAEVERDELSEELASNSSGK 1728
Cdd:PTZ00121 1500 DEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMA 1579
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1729 SLMSDEKRRLDTKISQLEEELEEEQANVESlnDRLRKSQQlvEQLGAELAaeRSTSQSREGSRQQLERQNRELKAKMQEM 1808
Cdd:PTZ00121 1580 LRKAEEAKKAEEARIEEVMKLYEEEKKMKA--EEAKKAEE--AKIKAEEL--KKAEEEKKKVEQLKKKEAEEKKKAEELK 1653
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1809 EGQGRSKLKASIAA--LEAKLREAEEQLEIESRERQANGKNLRQKE--KKLKDLTIQMEDERKQAQQYKDQAEKGNVRVK 1884
Cdd:PTZ00121 1654 KAEEENKIKAAEEAkkAEEDKKKAEEAKKAEEDEKKAAEALKKEAEeaKKAEELKKKEAEEKKKAEELKKAEEENKIKAE 1733
|
....*
gi 1604784239 1885 QLKHQ 1889
Cdd:PTZ00121 1734 EAKKE 1738
|
|
| Myosin_N |
pfam02736 |
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ... |
29-73 |
1.98e-15 |
|
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: 71.69 E-value: 1.98e-15
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1604784239 29 TAKKMVWIPSEKEGFEAASIKEEKGDEVLVELSNGQKMTVNKDDI 73
Cdd:pfam02736 1 DAKKLVWVPDPKEGFVKGEIKEEEGDKVTVETEDGKTVTVKKDDV 45
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
890-1596 |
2.86e-15 |
|
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: 82.09 E-value: 2.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 890 MEERAQLEMKLHAETELYAEAE--EMRVRLEAKKQELEEVLHEMESRLEEEEDRSNALHNERKEMEQQLQLMEAHIAEEE 967
Cdd:pfam15921 90 LQRRLNESNELHEKQKFYLRQSviDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCLKEDMLEDSN 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 968 DARQKLQMEKVSVEGKVKKLEEDILMMEDQN-NKLQKERKLLEERLADMSSNLAEE-EEKSKNLSKLKTKHESMISELE- 1044
Cdd:pfam15921 170 TQIEQLRKMMLSHEGVLQEIRSILVDFEEASgKKIYEHDSMSTMHFRSLGSAISKIlRELDTEISYLKGRIFPVEDQLEa 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1045 LRMKKEEKGRLDMEKAKRKVEAELGDLQEQHADLQAQLAELRAQLAAKEEELQATQarlEEECNQRGAAVKRVRELEVLI 1124
Cdd:pfam15921 250 LKSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQ---EQARNQNSMYMRQLSDLESTV 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1125 SELQEDL-EAERAARGKVEAARRDL---GEELNALRTEL----EDSLGTTAAQQELRA---KREQEVSMLKKAME----- 1188
Cdd:pfam15921 327 SQLRSELrEAKRMYEDKIEELEKQLvlaNSELTEARTERdqfsQESGNLDDQLQKLLAdlhKREKELSLEKEQNKrlwdr 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1189 DEGRS----HEAQVQDLRQKHSQAVEELTEQLE-----QAKRVRAGLEKAKQALEKESAdLSADLRSlasakqdVEHKKK 1259
Cdd:pfam15921 407 DTGNSitidHLRRELDDRNMEVQRLEALLKAMKsecqgQMERQMAAIQGKNESLEKVSS-LTAQLES-------TKEMLR 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1260 KVEGQLNELNSRFNESERQrtelgerVSKLTTELDSVTGLLneaEGKNIKLSKDVSSLSSQLQDAQELLSEETR----QK 1335
Cdd:pfam15921 479 KVVEELTAKKMTLESSERT-------VSDLTASLQEKERAI---EATNAEITKLRSRVDLKLQELQHLKNEGDHlrnvQT 548
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1336 LNLSGRLRQTEEDR--NSLMEQLEEETE-------AKRAVERQVSSLNMQLSDSKKKLDEMsgtvEALEEGKKRLQRELE 1406
Cdd:pfam15921 549 ECEALKLQMAEKDKviEILRQQIENMTQlvgqhgrTAGAMQVEKAQLEKEINDRRLELQEF----KILKDKKDAKIRELE 624
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1407 AANSDYE-EKAsaydKLEKSRGRMQQELEDVLMDLDsqrQLVSNLEKKQKKFDQMLAEERAVSCKFaeeRDRAEaearEK 1485
Cdd:pfam15921 625 ARVSDLElEKV----KLVNAGSERLRAVKDIKQERD---QLLNEVKTSRNELNSLSEDYEVLKRNF---RNKSE----EM 690
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1486 ETRVLALARALEENQGALEEAEKTMKGLRadmedlisskddvGKSVHDLeKAKRGLEAIVDEMRTQMEELEDELQVAEDA 1565
Cdd:pfam15921 691 ETTTNKLKMQLKSAQSELEQTRNTLKSME-------------GSDGHAM-KVAMGMQKQITAKRGQIDALQSKIQFLEEA 756
|
730 740 750
....*....|....*....|....*....|.
gi 1604784239 1566 KLRLDVNTQALRAQHERELHARDELGEEKRK 1596
Cdd:pfam15921 757 MTNANKEKHFLKEEKNKLSQELSTVATEKNK 787
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
904-1240 |
9.83e-15 |
|
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: 80.50 E-value: 9.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 904 TELYAEAEEMRVRLEAKKQEL----------EEVLHEMESRLEEEEDRSNALHNERKEMEQQLQLMEAHIAEEEDARQKL 973
Cdd:TIGR02169 670 RSEPAELQRLRERLEGLKRELsslqselrriENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSL 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 974 QMEKVSVEGKVKKLEEDILMMEDQNNKLQKERKLLEERLADmsSNLAEEEEKSKNLSKLKTKHESMISELELRMKKEEKG 1053
Cdd:TIGR02169 750 EQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLE 827
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1054 RLDMEKAKRKVEAELGDLQEQHADLQAQLAELRAQLAAKEEELQATQARLEEECNQRGAAVKRVRELEVLISELQEDLea 1133
Cdd:TIGR02169 828 KEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKI-- 905
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1134 eraargkveaarrdlgEELNALRTELEDSLGTTAAQQELRAKREQEVSMLKKAMEDEGRSH--EAQVQDLRQKHSQAVEE 1211
Cdd:TIGR02169 906 ----------------EELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEElsLEDVQAELQRVEEEIRA 969
|
330 340 350
....*....|....*....|....*....|....*.
gi 1604784239 1212 L-------TEQLEQAKRVRAGLEKAKQALEKESADL 1240
Cdd:TIGR02169 970 LepvnmlaIQEYEEVLKRLDELKEKRAKLEEERKAI 1005
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1018-1674 |
1.07e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 80.11 E-value: 1.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1018 NLAEEEEKSKNLSKLKTKHESMISELELRMKKEEkgrlDMEKAKRKVEAELGDLQEQHADLQAQLAELRAQLAAKEEElq 1097
Cdd:PRK03918 156 GLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTE----NIEELIKEKEKELEEVLREINEISSELPELREELEKLEKE-- 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1098 atqarleeecnqrgaaVKRVRELEVLISELQEDLEAERAARGKVEAARRDLGEELNALRTELEDSLGTTAAQQELR--AK 1175
Cdd:PRK03918 230 ----------------VKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKekAE 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1176 REQEVSMLKKAMEDEGRSHEAQVQDLRQKhSQAVEELTEQLEQAKRVRAGLEKAKQALEKESADLSADLRSLASAKQDVE 1255
Cdd:PRK03918 294 EYIKLSEFYEEYLDELREIEKRLSRLEEE-INGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKE 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1256 ----HKKKKVEGQLNELNSRFNESERQRTELGERVSKLTTELDSVTGLLNEAEGKNIKLSKdvssLSSQLQDAQELLSEE 1331
Cdd:PRK03918 373 elerLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKK----AKGKCPVCGRELTEE 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1332 TRQKLnlsgrLRQTEEDRNSLMEQLEEETEAKRAVERQVSSLNMQLSDSKK--KLDEMSGTVEALEEGKKRLQREleaan 1409
Cdd:PRK03918 449 HRKEL-----LEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESEliKLKELAEQLKELEEKLKKYNLE----- 518
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1410 sDYEEKASAYDKLEKSRGRMQQELEDVLMDLDSQRQLVSNLEKKQKKFDQMlaeeravsckfaeERDRAEAEAREKEtrv 1489
Cdd:PRK03918 519 -ELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDEL-------------EEELAELLKELEE--- 581
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1490 lalaraleENQGALEEAEKTMKGLRADMEDLISSKDdvgkSVHDLEKAKRGLEAIVDEMRTQMEELEDELQVAEDAKLRL 1569
Cdd:PRK03918 582 --------LGFESVEELEERLKELEPFYNEYLELKD----AEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKEL 649
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1570 DvntqalraqherelHARDELGEEKRKQLLKQVRELEAELEEERKQRGQASGSKKKLEGELKDMEDQLEATSRGRDEaVK 1649
Cdd:PRK03918 650 E--------------ELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKE-LE 714
|
650 660
....*....|....*....|....*
gi 1604784239 1650 QLRKIQGQVKDLQRDLEDSRAAQKE 1674
Cdd:PRK03918 715 KLEKALERVEELREKVKKYKALLKE 739
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1020-1765 |
1.10e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 80.57 E-value: 1.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1020 AEEEEKSKNLSKLKTKHESMISELELRMKKEEKGRlDMEKAKRKVEAELGDLQEQHADLQAQLAELRAQLAAKEEELQAT 1099
Cdd:PTZ00121 1094 EEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDAR-KAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKA 1172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1100 QARLEEECNQRGAAVKRVRELEvliselqedlEAERAARgkVEAARRDLGEELNALRTELEDSLGTTAAQQELRAKREQE 1179
Cdd:PTZ00121 1173 EDAKKAEAARKAEEVRKAEELR----------KAEDARK--AEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAE 1240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1180 VSmlKKAMEDEGRSHEAQVQDLRQKHSQAVEELTEQLEqaKRVRAGLEKAKQALEKESADLSADLRSLASAKQDVEHKKK 1259
Cdd:PTZ00121 1241 EA--KKAEEERNNEEIRKFEEARMAHFARRQAAIKAEE--ARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKK 1316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1260 KvegqlNELNSRFNESERQRTELGERVSKLTTEldsvtgllNEAEGKNIKLSKDVSSLSSQLQDAQELLSEETRQKLNLS 1339
Cdd:PTZ00121 1317 A-----DEAKKKAEEAKKKADAAKKKAEEAKKA--------AEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAA 1383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1340 GRlrQTEEDRNSLMEQLEEETEAKRAVERQvsslnmQLSDSKKKLDEMSGTVEAL---EEGKKRLQ--RELEAANSDYEE 1414
Cdd:PTZ00121 1384 KK--KAEEKKKADEAKKKAEEDKKKADELK------KAAAAKKKADEAKKKAEEKkkaDEAKKKAEeaKKADEAKKKAEE 1455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1415 KASAYDKLEKSR-GRMQQELEDVLMDLDSQRQLVSNLEKKQKKFDQML----AEERAVSCKFAEERDRAEAEAREKETRV 1489
Cdd:PTZ00121 1456 AKKAEEAKKKAEeAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKkaaeAKKKADEAKKAEEAKKADEAKKAEEAKK 1535
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1490 LALARALEENQGA--LEEAEKTMKGL-RADMEDLISSKDDVGKSVHDLEKAKRGLEAIVDEMRTQMEELE----DELQVA 1562
Cdd:PTZ00121 1536 ADEAKKAEEKKKAdeLKKAEELKKAEeKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKkmkaEEAKKA 1615
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1563 EDAKLRLDvntQALRAQHERELHARDELGEEKRKQLLKQVRELEAELEEERKQRGQASGSKKKLEGELKDMEDQleatSR 1642
Cdd:PTZ00121 1616 EEAKIKAE---ELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEED----EK 1688
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1643 GRDEAVKQLRKIQGQVKDLQRDLEDSRaaqkevlasaRESERRSKAMEADIVQLHEMLAAVERARKQAEVERDELSEELA 1722
Cdd:PTZ00121 1689 KAAEALKKEAEEAKKAEELKKKEAEEK----------KKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKK 1758
|
730 740 750 760
....*....|....*....|....*....|....*....|...
gi 1604784239 1723 SNSSGKSLMSDEKRRLDTKISQLEEELEEEQANVESLNDRLRK 1765
Cdd:PTZ00121 1759 IAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIK 1801
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
947-1570 |
1.18e-14 |
|
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: 79.68 E-value: 1.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 947 NERKEMEQQLQLMEAHIAEEEDARQKLQMEKVSVEGKVKKLEEDILMMEDQNNKLQKERKLLEERLADMSSNLAEEEEKS 1026
Cdd:TIGR04523 33 TEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1027 KNLSKLKTKHESMISELELRMKKEEKGRLDMEKAKRKVEAELGDLQEQHADLQAQLAELRAQLAAKEEELQATQARLEEE 1106
Cdd:TIGR04523 113 KNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKI 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1107 CNQRgaavkrvRELEVLISELQEDLEAERAARGKVeaarrdlgEELNALRTELEDSLgtTAAQQELRAKR------EQEV 1180
Cdd:TIGR04523 193 KNKL-------LKLELLLSNLKKKIQKNKSLESQI--------SELKKQNNQLKDNI--EKKQQEINEKTteisntQTQL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1181 SMLKKAMEDEGRSHEAQVQDLrQKHSQAVEELTEQLEQAKRVRAGLEKAKQalEKESADLSADLRSLASAKQDVEHKKKK 1260
Cdd:TIGR04523 256 NQLKDEQNKIKKQLSEKQKEL-EQNNKKIKELEKQLNQLKSEISDLNNQKE--QDWNKELKSELKNQEKKLEEIQNQISQ 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1261 VEGQLNELNSRFNESERQRTELGERVSKLTTELDSVTGLLNEAEGKNIKLSKDVSSLSSQLQDAQELLSEETRQKLNLSG 1340
Cdd:TIGR04523 333 NNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDE 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1341 RLRQTEEDRNSLMEQLEEETEAKRAVERQVSSLNMQLSDSKKKLDEMSGTVEALEEGKKRLQRELEAANSDYEEKasayd 1420
Cdd:TIGR04523 413 QIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQK----- 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1421 kleksrgrmQQELEDVLMDLDSQRQLVSNLEKKQKKFDQMLAEERAVSCKFAEERDRAEAEAREKETRVLALARALEENQ 1500
Cdd:TIGR04523 488 ---------QKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKEN 558
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1604784239 1501 --GALEEAEKTMKGLRADMEDLISSKDDVGKSVHDLEKAKRGLEAIVDEMRTQMEELEDELQVAEDAKLRLD 1570
Cdd:TIGR04523 559 leKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLS 630
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
866-1358 |
1.32e-14 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 79.96 E-value: 1.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 866 KAAKEVAAKVETELKDITQKHTQLMEERAQLEMkLHAETELYAEAEEMRVRLEAKKQELEEVLHEMESRLEEEEDrsNAL 945
Cdd:COG4913 221 PDTFEAADALVEHFDDLERAHEALEDAREQIEL-LEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLE--AEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 946 HNERKEMEQQLQLMEAHIAEEEDARQKLQMEKVSVEG----KVKKLEEDILMMEDQNNKLQKERKLLEERLADMSSNLAE 1021
Cdd:COG4913 298 EELRAELARLEAELERLEARLDALREELDELEAQIRGnggdRLEQLEREIERLERELEERERRRARLEALLAALGLPLPA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1022 EEEkskNLSKLKTKHESMISELElrmkkEEKGRLdmEKAKRKVEAELGDLQEQHADLQAQLAELRAQLAAKEEELQATQA 1101
Cdd:COG4913 378 SAE---EFAALRAEAAALLEALE-----EELEAL--EEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRD 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1102 RLEEECNQRGAAVKRVRELeVLISELQEDLE--AERAARG---------KVEAA------RRDLGEELN--ALRTELEDS 1162
Cdd:COG4913 448 ALAEALGLDEAELPFVGEL-IEVRPEEERWRgaIERVLGGfaltllvppEHYAAalrwvnRLHLRGRLVyeRVRTGLPDP 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1163 LGTTAAQQELRAK--------------------------REQEVSMLKKAMEDEG------RSHE--------------- 1195
Cdd:COG4913 527 ERPRLDPDSLAGKldfkphpfrawleaelgrrfdyvcvdSPEELRRHPRAITRAGqvkgngTRHEkddrrrirsryvlgf 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1196 ---AQVQDLRQKHSQAVEEL---TEQLEQAKRVRAGLEKAKQAL----------------EKESADLSADLRSLASAKQD 1253
Cdd:COG4913 607 dnrAKLAALEAELAELEEELaeaEERLEALEAELDALQERREALqrlaeyswdeidvasaEREIAELEAELERLDASSDD 686
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1254 VEhkkkKVEGQLNELNSRFNESERQRTELGERVSKLTTELDSVTGLLNEAEGKNIKLSKDVSSLSSQLQDAQ--ELLSEE 1331
Cdd:COG4913 687 LA----ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERfaAALGDA 762
|
570 580
....*....|....*....|....*....
gi 1604784239 1332 TRQKL--NLSGRLRQTEEDRNSLMEQLEE 1358
Cdd:COG4913 763 VERELreNLEERIDALRARLNRAEEELER 791
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1132-1889 |
3.32e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 79.03 E-value: 3.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1132 EAERAARGKVEAARRDLGEELNALRTELEDSLGTTAAQQELRAKREQEVSML---KKAMEDEGRSHEAQVQDLRQKHSQA 1208
Cdd:PTZ00121 1091 EATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAeeaRKAEDAKRVEIARKAEDARKAEEAR 1170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1209 VEELTEQLEQAKR---VRAGLE--KAKQALEKESADLSADLRSLASAKQDVEHKKKKVEGQLNELNSRFNESERQRTELG 1283
Cdd:PTZ00121 1171 KAEDAKKAEAARKaeeVRKAEElrKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERN 1250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1284 ERVSKLTTELDSVTGLLNEAEGKniklskdvsslSSQLQDAQELLSEETRQKlnlSGRLRQTEEDRNSlmEQLEEETEAK 1363
Cdd:PTZ00121 1251 NEEIRKFEEARMAHFARRQAAIK-----------AEEARKADELKKAEEKKK---ADEAKKAEEKKKA--DEAKKKAEEA 1314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1364 RAVE---RQVSSLNMQLSDSKKKLDEMSGTVEALEEGKKRLQRELEAAnsdyEEKASAYDKLEKSRGRMQQELEDVLMDL 1440
Cdd:PTZ00121 1315 KKADeakKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAA----EEKAEAAEKKKEEAKKKADAAKKKAEEK 1390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1441 DSQRQLVSNLEKKQKKFDQMlaEERAVSCKFAEERDRAEAEAREKETrvlaLARALEENQGALEEAEKTMKGLRAdmEDL 1520
Cdd:PTZ00121 1391 KKADEAKKKAEEDKKKADEL--KKAAAAKKKADEAKKKAEEKKKADE----AKKKAEEAKKADEAKKKAEEAKKA--EEA 1462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1521 ISSKDDVGKSVHDLEKAKRGLEAivDEMRTQMEELE---DELQVAEDAKLRLDvntQALRAQHERELHARDELGEEKRKQ 1597
Cdd:PTZ00121 1463 KKKAEEAKKADEAKKKAEEAKKA--DEAKKKAEEAKkkaDEAKKAAEAKKKAD---EAKKAEEAKKADEAKKAEEAKKAD 1537
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1598 LLKQVRELEAELEEERKQRGQASGSKKKLEGELKDMEDQLEATSRGrdEAVKQLRKiqgqvkdlqrdledsraAQKEVLA 1677
Cdd:PTZ00121 1538 EAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKA--EEAKKAEE-----------------ARIEEVM 1598
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1678 SARESERRSKAmeadivqlhEMLAAVERARKQAEVERDElSEELASNSSGKSLMSDEKRRLDtkisqleeeleeeqanve 1757
Cdd:PTZ00121 1599 KLYEEEKKMKA---------EEAKKAEEAKIKAEELKKA-EEEKKKVEQLKKKEAEEKKKAE------------------ 1650
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1758 slndRLRKSQQLVEQLGAELA--AERSTSQSREGSRQQLERQNRELKAKMQEMEGQGRSKLKASiaalEAKLREAEEQLE 1835
Cdd:PTZ00121 1651 ----ELKKAEEENKIKAAEEAkkAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKK----EAEEKKKAEELK 1722
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....
gi 1604784239 1836 IESRERQANGKNLRQKEKklkdltiqmEDERKQAQQYKDQAEKGnvRVKQLKHQ 1889
Cdd:PTZ00121 1723 KAEEENKIKAEEAKKEAE---------EDKKKAEEAKKDEEEKK--KIAHLKKE 1765
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1343-1932 |
3.70e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 78.16 E-value: 3.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1343 RQTEEDRNSLMEQLEEETEAKRAVErqvssLNMQLSDSKKKLDEMSGTVEALEEGKKRLQRELEAANS---DYEEKasay 1419
Cdd:PRK02224 179 ERVLSDQRGSLDQLKAQIEEKEEKD-----LHERLNGLESELAELDEEIERYEEQREQARETRDEADEvleEHEER---- 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1420 dkleksrgrmQQELEDVLMDLDSQRQLVSNLEKKQKKFDQMLAEERAVSCKFAEERDRAEAEA--------------REK 1485
Cdd:PRK02224 250 ----------REELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAglddadaeavearrEEL 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1486 ETRVLALARALEENQGALEEAEKTMKGLRADMEDLISSKDDVGKSVHDLEKAKRGLEAIVDEMRTQMEELEDELQVAEda 1565
Cdd:PRK02224 320 EDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELR-- 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1566 klrldvntqalraqhERELHARDELGE-EKRKQLLkqvreleaeleeeRKQRGQASGSKKKLEGELKDMEDQLEATSRGR 1644
Cdd:PRK02224 398 ---------------ERFGDAPVDLGNaEDFLEEL-------------REERDELREREAELEATLRTARERVEEAEALL 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1645 DEavkqlrkiqGQVKDLQRDLEDSRAAqkEVLASARESerrskameadivqlhemLAAVERARKQAEVERDELSEELASn 1724
Cdd:PRK02224 450 EA---------GKCPECGQPVEGSPHV--ETIEEDRER-----------------VEELEAELEDLEEEVEEVEERLER- 500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1725 ssGKSLMSDEKRrldtkisqleeeleeeqanVESLNDRLRKSQQLVEQLGAELAAERSTSQSREGSRQQLERQNRELKAK 1804
Cdd:PRK02224 501 --AEDLVEAEDR-------------------IERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREA 559
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1805 MQEMEGQGRSKLKAsIAALEAKLREAEEQLE----IESR--ERQANGKNLRQKEKKLKDLTiQMEDERKqaqqykDQAEK 1878
Cdd:PRK02224 560 AAEAEEEAEEAREE-VAELNSKLAELKERIEslerIRTLlaAIADAEDEIERLREKREALA-ELNDERR------ERLAE 631
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 1604784239 1879 GNVRVKQLKHQLEEAEEEAQRMAAAR-----RKLQRELDEATEANDTLSRDMASLRSKL 1932
Cdd:PRK02224 632 KRERKRELEAEFDEARIEEAREDKERaeeylEQVEEKLDELREERDDLQAEIGAVENEL 690
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
832-1399 |
3.99e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 78.64 E-value: 3.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 832 KLKNWQWWRLFTKVKPLLQVTRQ---EEEMGQKDEELKAAKEVaaKVETELKDITQKHtQLMEERAQLEMKLHAEtELYA 908
Cdd:PTZ00121 1247 EERNNEEIRKFEEARMAHFARRQaaiKAEEARKADELKKAEEK--KKADEAKKAEEKK-KADEAKKKAEEAKKAD-EAKK 1322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 909 EAEEMRVRLEAKKQELEEVLHEMESRLEEEEDRSNALHNERKEMEQQLQLMEAHIAEEEDARQKLQMEKVSVEGKvKKLE 988
Cdd:PTZ00121 1323 KAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAK-KKAE 1401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 989 EDILMMEDQNNKLQKERKlleerlADMSSNLAEEEEKSKNLSK----------LKTKHESMISELELRMKKEEKGRLDME 1058
Cdd:PTZ00121 1402 EDKKKADELKKAAAAKKK------ADEAKKKAEEKKKADEAKKkaeeakkadeAKKKAEEAKKAEEAKKKAEEAKKADEA 1475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1059 KAKRKVEAELGDLQEQHADLQAQLAELRAQLAAK---------EEELQATQARLEEEcnQRGAAVKRVRELEVLISELQE 1129
Cdd:PTZ00121 1476 KKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKkkadeakkaEEAKKADEAKKAEE--AKKADEAKKAEEKKKADELKK 1553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1130 DLEAERA-ARGKVEAARRDLGEELNALRTELEDSLGTTAAQQELRAKREQEVSM----LKKAMEDEGRSHEA-QVQDLRQ 1203
Cdd:PTZ00121 1554 AEELKKAeEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMkaeeAKKAEEAKIKAEELkKAEEEKK 1633
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1204 KHSQAVEELTEQLEQAKRVRAGLEKAKQALEKESADLSADLRSLASAKQDVEHKKKKVEGQLNElnsrfnESERQRTElg 1283
Cdd:PTZ00121 1634 KVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKE------AEEAKKAE-- 1705
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1284 ERVSKLTTELDSVTGLLNEAEGKNIKLSKDVSSLSSQLQDAQELLSEETRQKlnlsgRLRQTEEDRNSLMEQLEEETEAK 1363
Cdd:PTZ00121 1706 ELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKK-----KIAHLKKEEEKKAEEIRKEKEAV 1780
|
570 580 590
....*....|....*....|....*....|....*.
gi 1604784239 1364 RAVERQVSSLNMQLSDSKKKLDEMSGTVEALEEGKK 1399
Cdd:PTZ00121 1781 IEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKE 1816
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1054-1722 |
8.15e-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: 8.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1054 RLDMEKAKRKVEAeLGDLQEQHADLQAQLAELRAQlaakeeelqatqarleEECNQRGAAVKRVRELEvlisELQEDLEA 1133
Cdd:COG4913 241 HEALEDAREQIEL-LEPIRELAERYAAARERLAEL----------------EYLRAALRLWFAQRRLE----LLEAELEE 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1134 ERAARGKVEAARRDLGEELNALRTELEdslgttAAQQELRAKREQEVSMLKKAMEDEGRSHEaQVQDLRQKHSQAVEELT 1213
Cdd:COG4913 300 LRAELARLEAELERLEARLDALREELD------ELEAQIRGNGGDRLEQLEREIERLERELE-ERERRRARLEALLAALG 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1214 EQL----EQAKRVRAGLEKAKQALEKESADLSADLRSLASAKQDVEHKKKKVEGQLNELNSRFN----ESERQRTELGER 1285
Cdd:COG4913 373 LPLpasaEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSnipaRLLALRDALAEA 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1286 VSKLTTELDSVTGLLneaegkniklskDVSSLSSQLQDAQE---------LLSEETRQK--------LNLSGRLR----- 1343
Cdd:COG4913 453 LGLDEAELPFVGELI------------EVRPEEERWRGAIErvlggfaltLLVPPEHYAaalrwvnrLHLRGRLVyervr 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1344 -------QTEEDRNSLMEQLE-EETEAKRAVERQVSSlnmqlSDSKKKLDemsgTVEALEEGKKRLQRE-LEAANSDYEE 1414
Cdd:COG4913 521 tglpdpeRPRLDPDSLAGKLDfKPHPFRAWLEAELGR-----RFDYVCVD----SPEELRRHPRAITRAgQVKGNGTRHE 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1415 K-------------ASAYDKLEKSRGRMqQELEDVLMDLDSQRQlvsNLEKKQKKFDQMLAEERAVSCKFAEERDRAEAE 1481
Cdd:COG4913 592 KddrrrirsryvlgFDNRAKLAALEAEL-AELEEELAEAEERLE---ALEAELDALQERREALQRLAEYSWDEIDVASAE 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1482 AR--EKETRVlalaRALEENQGALEEAEKTMKGLRADMEDLISSKDDVGKSVHDLEKAkrgleaivdemRTQMEELEDEL 1559
Cdd:COG4913 668 REiaELEAEL----ERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKE-----------LEQAEEELDEL 732
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1560 QVAEDAKLRLDVNTQALRAQHERELHARDELGEEKRKQLLKQVRELEAELEEERKQ-RGQASGSKKKLEGELKDMEDQLE 1638
Cdd:COG4913 733 QDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEElERAMRAFNREWPAETADLDADLE 812
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1639 AtsrgRDEAVKQLRKiqgqvkdlqrdLEDSRAAQKEvlasARESERRSKAMEADIVQLHemlAAVERARKQAEVERDELS 1718
Cdd:COG4913 813 S----LPEYLALLDR-----------LEEDGLPEYE----ERFKELLNENSIEFVADLL---SKLRRAIREIKERIDPLN 870
|
....
gi 1604784239 1719 EELA 1722
Cdd:COG4913 871 DSLK 874
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
856-1860 |
1.29e-13 |
|
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: 76.62 E-value: 1.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 856 EEMGQKDEELKAAKEVAAKVETeLKDITQKHTQLMEERaqlEMKLHAETELYAEAEEMRVRLEAKKQELEevlhEMESRL 935
Cdd:TIGR00606 169 KALKQKFDEIFSATRYIKALET-LRQVRQTQGQKVQEH---QMELKYLKQYKEKACEIRDQITSKEAQLE----SSREIV 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 936 EEEEDRSNALHNERKEMEQQLQlmeahiaeeedarqklqmekvsvegKVKKLEEDILMMEDQNNKLQKERKLLEERLADM 1015
Cdd:TIGR00606 241 KSYENELDPLKNRLKEIEHNLS-------------------------KIMKLDNEIKALKSRKKQMEKDNSELELKMEKV 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1016 SSNLAEEeeksknLSKLKTKHESMISELELRMKKEEKGRLDMEKAKRKVEAELGDLQEQHADLQAQLAELRAQLAAKEEE 1095
Cdd:TIGR00606 296 FQGTDEQ------LNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSL 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1096 LQATQARLEEECNQRGAAVKR-VRELEVLISELQEDlEAERAAR--GKVEAARRDLGEELNALRTELEDSLGTTAAQQEL 1172
Cdd:TIGR00606 370 IQSLATRLELDGFERGPFSERqIKNFHTLVIERQED-EAKTAAQlcADLQSKERLKQEQADEIRDEKKGLGRTIELKKEI 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1173 RAKREQEVSMLKKamedEGRSHEAQVQDLRQKHSQAVEELTE-QLEQAKRVRAGLEKAKQALEKESADLSADLRSLASAK 1251
Cdd:TIGR00606 449 LEKKQEELKFVIK----ELQQLEGSSDRILELDQELRKAERElSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEM 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1252 QDVEHKKkkvegqlnELNSRFNESERQRTELGERVSKLTTE-LDSVTGLLNEAEGKNI------KLSKDVSSLSSQLQDA 1324
Cdd:TIGR00606 525 EQLNHHT--------TTRTQMEMLTKDKMDKDEQIRKIKSRhSDELTSLLGYFPNKKQledwlhSKSKEINQTRDRLAKL 596
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1325 QELLSEETRQKLNLSGRLRQTEEDRNSLMEQLEEETEAKrAVERQVSSLNMQLSDSKKKLDEMSGTVEALEEGKKRLQRE 1404
Cdd:TIGR00606 597 NKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQ-DEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDE 675
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1405 LEAANSDYEEKASAYDKLEKSRGRMQQELedvLMDLDSQRQLVSNLEKKQKKFDQMLAEERAVsckfAEERDRAEAEARE 1484
Cdd:TIGR00606 676 NQSCCPVCQRVFQTEAELQEFISDLQSKL---RLAPDKLKSTESELKKKEKRRDEMLGLAPGR----QSIIDLKEKEIPE 748
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1485 KETRVLALARALEENQGALEEAEKTMKGLRADMEDLISSKDDVGksvhdlekakrgleaIVDEMRTQMEELED--ELQVA 1562
Cdd:TIGR00606 749 LRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVT---------------IMERFQMELKDVERkiAQQAA 813
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1563 EDAKLRLDVNTQALRAQHERELHARDELGEEkrKQLLKQVRELEAELEEERKQRGQASGSKKKLEGE----LKDMEDQLE 1638
Cdd:TIGR00606 814 KLQGSDLDRTVQQVNQEKQEKQHELDTVVSK--IELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTnlqrRQQFEEQLV 891
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1639 ATSRGRDEAVKQLRKIQGQVKDLQRDLEDSRAAQKEVLASARESERRSK----AMEADIVQLHEMLAAV--------ERA 1706
Cdd:TIGR00606 892 ELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQdkvnDIKEKVKNIHGYMKDIenkiqdgkDDY 971
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1707 RKQAEVERDELSEELASNSSGKSLMSDEKRRLDTKISQLEEELEEEQANV--ESLNDRLRKSQQLVEQLGAELAAERSTS 1784
Cdd:TIGR00606 972 LKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLtlRKRENELKEVEEELKQHLKEMGQMQVLQ 1051
|
970 980 990 1000 1010 1020 1030
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1604784239 1785 QSREgsRQQLERQNRELKAKMQEMEGQGRSKLKASIAAlEAKLREAEEQlEIESRERQANgKNLRQKEKKLKDLTI 1860
Cdd:TIGR00606 1052 MKQE--HQKLEENIDLIKRNHVLALGRQKGYEKEIKHF-KKELREPQFR-DAEEKYREMM-IVMRTTELVNKDLDI 1122
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1239-1811 |
2.29e-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: 2.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1239 DLSADLRSLASAKQDVEHKKKKVE--GQLNELNSRFNESERQRTELGERVSKLTTEldsvtgllnEAEGKNIKLSKDVSS 1316
Cdd:COG4913 229 ALVEHFDDLERAHEALEDAREQIEllEPIRELAERYAAARERLAELEYLRAALRLW---------FAQRRLELLEAELEE 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1317 LSSQLQDAQELLSEETRQKLNLSGRLRQTEEDRNSL----MEQLEEETEAKRAVERQVSSLNMQLSDSKKKLD-EMSGTV 1391
Cdd:COG4913 300 LRAELARLEAELERLEARLDALREELDELEAQIRGNggdrLEQLEREIERLERELEERERRRARLEALLAALGlPLPASA 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1392 EALEEGKKRLQRELEAANSDYEEKASAYDKLEKSRGRMQQELEDVLMDLDSQRQLVSNLEKKQKKFDQMLAEE---RAVS 1468
Cdd:COG4913 380 EEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEAlglDEAE 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1469 CKFAeerdrAEA-EAREKEtrvlalaralEENQGAleeAEKTMKGLRADMedLISSKddvgksvhDLEKAKRGLEAIVDE 1547
Cdd:COG4913 460 LPFV-----GELiEVRPEE----------ERWRGA---IERVLGGFALTL--LVPPE--------HYAAALRWVNRLHLR 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1548 MRTQMEELEDELQVAEDAKL-------RLDVNTQALRAQHERELHAR---------DELGEEKR----KQLLKQVRELEA 1607
Cdd:COG4913 512 GRLVYERVRTGLPDPERPRLdpdslagKLDFKPHPFRAWLEAELGRRfdyvcvdspEELRRHPRaitrAGQVKGNGTRHE 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1608 ELEEERKQR----GQASGSKkklegeLKDMEDQLEATSRGRDEAVKQLRKIQGQVKDLQRdledsRAAQKEVLASARESE 1683
Cdd:COG4913 592 KDDRRRIRSryvlGFDNRAK------LAALEAELAELEEELAEAEERLEALEAELDALQE-----RREALQRLAEYSWDE 660
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1684 RRSKAMEADIVQLHEMLAAVERAR---KQAEVERDELSEELASNSSGKSLMSDEKRRLDTKISQLEEELEEEQANVESLN 1760
Cdd:COG4913 661 IDVASAEREIAELEAELERLDASSddlAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAE 740
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 1604784239 1761 DRLRKSQ-QLVEQLGAELAAERSTSQSREGSRQQLERQNRELKAKMQEMEGQ 1811
Cdd:COG4913 741 DLARLELrALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERA 792
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
853-1600 |
2.44e-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: 75.78 E-value: 2.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 853 RQEEEMGQKDEELKAAKEVAAKVETELKDITQKHTQLMEERAQLEMKLHAETELYAEAEEMRVRLEAKKQELEEVLHEME 932
Cdd:pfam02463 262 KEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 933 SRLEEEEDRSNALHNERKEMEQQLQLMEAHIAE-------------EEDARQKLQMEKVSVEGKVKKLEEDILMME--DQ 997
Cdd:pfam02463 342 KELKELEIKREAEEEEEEELEKLQEKLEQLEEEllakkkleserlsSAAKLKEEELELKSEEEKEAQLLLELARQLedLL 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 998 NNKLQKERKLLEERLADMSSNLAEEEEKSKNLSKLKTKHESMISELELRMKKEEKGRLDMEKAKRKvEAELGDLQEQHAD 1077
Cdd:pfam02463 422 KEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLE-LLLSRQKLEERSQ 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1078 LQAQLAELRAQLAAKEEELQATQARLEEECNQRGAAVKRVRELEVLISELQEDLEAERAARGKVEAARRDLGEELNALRT 1157
Cdd:pfam02463 501 KESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKL 580
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1158 ELEDSLgttaAQQELRAKREQEVSMLKKAMEDEGRSHEAQVQDLRQKHSQAVEELTEQLEQAKRVRAGLEKAKQALEKES 1237
Cdd:pfam02463 581 RLLIPK----LKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEE 656
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1238 ADLSADLRSLASAKQDVEHKKKKVEGQLNELNSRFNESERQRTELGERVSKLTTELDSVTGLLNEAEGKNIKLSKDVSSL 1317
Cdd:pfam02463 657 GLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINE 736
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1318 SSQLQDAQELLSEETRQKLNLSGRLRQTEEDRNSLMEQLEEETEAKRAVERQVSSLNMQLSDSKKKLDEMSGTVEALEEG 1397
Cdd:pfam02463 737 ELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAEL 816
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1398 KKRLQRELEAANSDYEEKASAYDKLEKSRGRMQQEL-EDVLMDLDSQRQLVSNLEKKQKKFDQMLAEERAVScKFAEERD 1476
Cdd:pfam02463 817 LEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAeEELERLEEEITKEELLQELLLKEEELEEQKLKDEL-ESKEEKE 895
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1477 RAEAEAREKETRVLALARALE-----------ENQGALEEAEKTMKGLRADMEDLISSKDDVGKSVHDLEKAKRGLEAIV 1545
Cdd:pfam02463 896 KEEKKELEEESQKLNLLEEKEneieerikeeaEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKV 975
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*
gi 1604784239 1546 DEMRTQMEELEDELQVAEDAKLrldvntQALRAQHERELHARDELGEEKRKQLLK 1600
Cdd:pfam02463 976 NLMAIEEFEEKEERYNKDELEK------ERLEEEKKKLIRAIIEETCQRLKEFLE 1024
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
854-1722 |
2.60e-13 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 75.76 E-value: 2.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 854 QEEEMGQKDEELKAAKEVAAKVETELKDiTQKHTQLMEERAQLEMKLHAETELYAEAEEMRVRLEAKKQELEEVLHEMES 933
Cdd:PRK04863 319 LNEAESDLEQDYQAASDHLNLVQTALRQ-QEKIERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKS 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 934 RLEEEEDRSNALHNERKEMEQQLQLMEahiaeeeDARQKLQMEKVSVEGKVKKLEEdilmMEDQNNKLQKERKLLEERLa 1013
Cdd:PRK04863 398 QLADYQQALDVQQTRAIQYQQAVQALE-------RAKQLCGLPDLTADNAEDWLEE----FQAKEQEATEELLSLEQKL- 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1014 DMSSNLAEEEEKSKNLSKLKTkhesmiselelrmkkeekGRLDMEKAKRKVEAELGDLQEQHAdLQAQLAELRAQLAAKE 1093
Cdd:PRK04863 466 SVAQAAHSQFEQAYQLVRKIA------------------GEVSRSEAWDVARELLRRLREQRH-LAEQLQQLRMRLSELE 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1094 EEL--QATQARLEEECNQRgaavkrvrelevLISELQEDLEAERaargkveaarrdLGEELNALRTELEDSLGTTAAQQ- 1170
Cdd:PRK04863 527 QRLrqQQRAERLLAEFCKR------------LGKNLDDEDELEQ------------LQEELEARLESLSESVSEARERRm 582
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1171 ELRAKREQevsmlkkamedegrsHEAQVQDLRQKHSQ------AVEELTEQLEQAKRVRAGLEKAKQA-LEKEsadlsad 1243
Cdd:PRK04863 583 ALRQQLEQ---------------LQARIQRLAARAPAwlaaqdALARLREQSGEEFEDSQDVTEYMQQlLERE------- 640
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1244 lRSLASAKQDVEHKKKKVEGQLNELNSRFNESERQRTELGERVSK-LTTEL-DSVTglLNEA--------EGKNIKLSKD 1313
Cdd:PRK04863 641 -RELTVERDELAARKQALDEEIERLSQPGGSEDPRLNALAERFGGvLLSEIyDDVS--LEDApyfsalygPARHAIVVPD 717
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1314 VSSLSSQLQDAQELLSEetrqklnlsgrLRQTEEDRNSLMEQLEEETEAKRAVERQVSSLNM------------------ 1375
Cdd:PRK04863 718 LSDAAEQLAGLEDCPED-----------LYLIEGDPDSFDDSVFSVEELEKAVVVKIADRQWrysrfpevplfgraarek 786
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1376 QLSDSKKKLDEMSGTVEALEEGKKRLQRELEAANSDYEEKAS-AYD-----KLEKSRGRmQQELEDVLMDLDSQRQLVSN 1449
Cdd:PRK04863 787 RIEQLRAEREELAERYATLSFDVQKLQRLHQAFSRFIGSHLAvAFEadpeaELRQLNRR-RVELERALADHESQEQQQRS 865
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1450 LEKKQKKFDQMLAEERAVSCKFAEER--DRAEaEAREKETRVLALARALEENQGALEEAEKTMKGLRADMEDLISSKDDV 1527
Cdd:PRK04863 866 QLEQAKEGLSALNRLLPRLNLLADETlaDRVE-EIREQLDEAEEAKRFVQQHGNALAQLEPIVSVLQSDPEQFEQLKQDY 944
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1528 GKSVHDLEKAKRGLEAI--VDEMRTQMEELEDELQVAEDAKLrldvnTQALRAQHERELHARDELGEEKRkQLLKQVREL 1605
Cdd:PRK04863 945 QQAQQTQRDAKQQAFALteVVQRRAHFSYEDAAEMLAKNSDL-----NEKLRQRLEQAEQERTRAREQLR-QAQAQLAQY 1018
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1606 EAELEEERKQRGQASGSKKKLEGELKDM-----EDQLEATSRGRDEAVKQLRKIQGQVKDLQRDLEDSRAAQKEVLASAR 1680
Cdd:PRK04863 1019 NQVLASLKSSYDAKRQMLQELKQELQDLgvpadSGAEERARARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLR 1098
|
890 900 910 920
....*....|....*....|....*....|....*....|..
gi 1604784239 1681 ESERRSKAMEADIVQLHEMLAAVERARKQAEVERDELSEELA 1722
Cdd:PRK04863 1099 KLERDYHEMREQVVNAKAGWCAVLRLVKDNGVERRLHRRELA 1140
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1072-1321 |
2.91e-13 |
|
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: 73.64 E-value: 2.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1072 QEQHADLQAQLAELRAQLAAKEEELQATQARLEEECNQRGAAVKRVRELEVLISELQEDLEAERAARGKVEAARRDLGEE 1151
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1152 LNALRTELEDSLGttAAQqelRAKREQEVSMLKKAmedegrSHEAQVQDLRQKHSQAVEELTEQLEQAKRVRAGLEKAKQ 1231
Cdd:COG4942 99 LEAQKEELAELLR--ALY---RLGRQPPLALLLSP------EDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1232 ALEKESADLSADLRSLASAKQDVEHKKKKVEGQLNELNSRFNESERQRTELGERVSKLTTELDSVTGllNEAEGKNIKLS 1311
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEA--EAAAAAERTPA 245
|
250
....*....|
gi 1604784239 1312 KDVSSLSSQL 1321
Cdd:COG4942 246 AGFAALKGKL 255
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1023-1243 |
3.64e-13 |
|
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: 73.26 E-value: 3.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1023 EEKSKNLSKLKTKhesmISELELRMKKEEKGRLDMEKAKRKVEAELGDLQEQHADLQAQLAELRAQLAAKEEELQATQAR 1102
Cdd:COG4942 23 AEAEAELEQLQQE----IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1103 LEEecnQRGAAVKRVR---------ELEVLISelQED-LEAERAAR--GKVEAARRDLGEELNALRTELEDSLGTTAAQQ 1170
Cdd:COG4942 99 LEA---QKEELAELLRalyrlgrqpPLALLLS--PEDfLDAVRRLQylKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1604784239 1171 ELRAKREQEVSMLKKAMEDEGRSHEAQVQDLRQKHSQAVEELTEQLEQAKRVRAGLEKAKQALEKESADLSAD 1243
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1081-1873 |
4.00e-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: 75.37 E-value: 4.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1081 QLAELRAQLAAKEEELQATQARLEEecnqrgaavkRVRELEVLiSELQEDLEAEraargkVEAARRDLGEELNALR---- 1156
Cdd:COG3096 286 RALELRRELFGARRQLAEEQYRLVE----------MARELEEL-SARESDLEQD------YQAASDHLNLVQTALRqqek 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1157 -----TELEDSLGTTAAQQELRAKREQEVSML---KKAMEDEGRSHEAQVQDLRqkhsQAVEELTEQLEQAKRVRAGLEK 1228
Cdd:COG3096 349 ieryqEDLEELTERLEEQEEVVEEAAEQLAEAearLEAAEEEVDSLKSQLADYQ----QALDVQQTRAIQYQQAVQALEK 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1229 AKQALEKesADLSADlrSLASAKQDVEHKKKKVEGQLNELNSRFNESE---RQRTELGERVSKLTTELDSvtgllNEAEG 1305
Cdd:COG3096 425 ARALCGL--PDLTPE--NAEDYLAAFRAKEQQATEEVLELEQKLSVADaarRQFEKAYELVCKIAGEVER-----SQAWQ 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1306 KNIKLSKDVSSLSSQLQDAQELlseetRQKLnlsGRLRQTEEDRNSLMEQLEEetEAKRAvERQVSS---LNMQLSDSKK 1382
Cdd:COG3096 496 TARELLRRYRSQQALAQRLQQL-----RAQL---AELEQRLRQQQNAERLLEE--FCQRI-GQQLDAaeeLEELLAELEA 564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1383 KLDEMSGTVEALEEGKKRLQRELEAANSDYEEKAS-------AYDKLEKSRGRMQQELEDvLMDLDSQRQlvsnlekkqk 1455
Cdd:COG3096 565 QLEELEEQAAEAVEQRSELRQQLEQLRARIKELAArapawlaAQDALERLREQSGEALAD-SQEVTAAMQ---------- 633
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1456 kfdQMLAEERAVSC---KFAEERDRAEAEARE-------KETRVLALARALeenqGALeeaektmkgLRADMEDLISSKD 1525
Cdd:COG3096 634 ---QLLEREREATVerdELAARKQALESQIERlsqpggaEDPRLLALAERL----GGV---------LLSEIYDDVTLED 697
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1526 D------VGKSVH-----DLEKAKRGLEAI----------------VDEMRTQMEELEDE-LQVAEDAKLR------LDV 1571
Cdd:COG3096 698 ApyfsalYGPARHaivvpDLSAVKEQLAGLedcpedlyliegdpdsFDDSVFDAEELEDAvVVKLSDRQWRysrfpeVPL 777
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1572 NTQALRAQHERELHA-RDELGEEKRKQ---LLKQVRELE-------------------AELEEERKQRGQASGSKKKLEG 1628
Cdd:COG3096 778 FGRAAREKRLEELRAeRDELAEQYAKAsfdVQKLQRLHQafsqfvgghlavafapdpeAELAALRQRRSELERELAQHRA 857
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1629 ELKDMEDQLEATSrgrdEAVKQLRKIQGQVKDL-QRDLEDSRAAQKEVLASARESERRSKAMEADIVQLHEMLA------ 1701
Cdd:COG3096 858 QEQQLRQQLDQLK----EQLQLLNKLLPQANLLaDETLADRLEELREELDAAQEAQAFIQQHGKALAQLEPLVAvlqsdp 933
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1702 ----AVERARKQAEVERDELS------EELASNS-----SGKSLMSDEKRRLDTKISQLEEELEEEQanvESLNDRLRKS 1766
Cdd:COG3096 934 eqfeQLQADYLQAKEQQRRLKqqifalSEVVQRRphfsyEDAVGLLGENSDLNEKLRARLEQAEEAR---REAREQLRQA 1010
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1767 QQLVEQLGAELAAERStsqSREGSRQQLerqnRELKAKMQEMEGQG-----------RSKLKASIAALEAKLREAEEQLE 1835
Cdd:COG3096 1011 QAQYSQYNQVLASLKS---SRDAKQQTL----QELEQELEELGVQAdaeaeerarirRDELHEELSQNRSRRSQLEKQLT 1083
|
890 900 910
....*....|....*....|....*....|....*...
gi 1604784239 1836 IESRERQANGKNLRQKEKKLKdltiqmeDERKQAQQYK 1873
Cdd:COG3096 1084 RCEAEMDSLQKRLRKAERDYK-------QEREQVVQAK 1114
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
846-1676 |
4.85e-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: 75.01 E-value: 4.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 846 KPLLQVTRQEEEMGQKDEELKAAKEVAAKVETElkdiTQKHTQLMEERAQLEMKLHAETELYAEAEEMRvRLEAKKQELE 925
Cdd:pfam02463 176 KKLIEETENLAELIIDLEELKLQELKLKEQAKK----ALEYYQLKEKLELEEEYLLYLDYLKLNEERID-LLQELLRDEQ 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 926 EVLHEMESRLEEEEDRSNALHNERKEMEQQLQLMEAH-------IAEEEDARQKLQMEKVSVEGKVKKLEEDILMMEDQN 998
Cdd:pfam02463 251 EEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEElkllakeEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKEL 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 999 NK-------LQKERKLLE----ERLADMSSNLAEEEEKSKNLSKLKTKHESMISELELRMKKEEKGRLDMEKAKRKVEAE 1067
Cdd:pfam02463 331 KKekeeieeLEKELKELEikreAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLL 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1068 LGDLQEQHADLQAQLAELRAQLAAKEEELQATQARLEEECNQrgaavKRVRELEVLISELQEDLEAERAARGKVEAARRD 1147
Cdd:pfam02463 411 LELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEE-----LEKQELKLLKDELELKKSEDLLKETQLVKLQEQ 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1148 LGEELNALRTELEDSLGTTAAQQE--LRAKREQEVSMLKKAMEDEGRSHEAQVQDLRQKHSQAVEELTEQLEQAKRVRAG 1225
Cdd:pfam02463 486 LELLLSRQKLEERSQKESKARSGLkvLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQK 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1226 LEKAKQALEKESADLSadLRSLASAKQDVEHKKKKVEGQLNELNSRFNESERQRTELGERVSKLTTELDSVTGLLNEAEG 1305
Cdd:pfam02463 566 LVRALTELPLGARKLR--LLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKA 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1306 KNIKLSKDVSSLSSQLQdaqellseetRQKLNLSGRLRQTEEDRNSLMEQLEEETEAKRAVERQvsSLNMQLSDSKKKLD 1385
Cdd:pfam02463 644 KESGLRKGVSLEEGLAE----------KSEVKASLSELTKELLEIQELQEKAESELAKEEILRR--QLEIKKKEQREKEE 711
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1386 EMSGTVEALEEGKKRLQRELEAANSDYEEKASAYDKLEKSRGRMQQELEDVLMDLDSQRQLVSNLEKKQKKFDQMLAEER 1465
Cdd:pfam02463 712 LKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEE 791
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1466 AVSCKFAEERDRAEAEAREKETRVLALARALEENQG-------ALEEAEKTMKGLRADMEDLISSKDDVGKSVHDLEKAK 1538
Cdd:pfam02463 792 KEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEekikeeeLEELALELKEEQKLEKLAEEELERLEEEITKEELLQE 871
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1539 RGLEAIVDEMRTQMEELEDELQVAEDAKLRLDVNTQALRAQHERELHArDELGEEKRKQLLKQVRELEAELEEERKQRGQ 1618
Cdd:pfam02463 872 LLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEI-EERIKEEAEILLKYEEEPEELLLEEADEKEK 950
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*...
gi 1604784239 1619 ASGSKKKLEGELKDMEDQLEATSRGRDEAVKQLRKIQGQVKDLQRDLEDSRAAQKEVL 1676
Cdd:pfam02463 951 EENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLI 1008
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1070-1802 |
6.15e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 74.57 E-value: 6.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1070 DLQEQHADLQAQLAEL-RAQLAAKEEELQATQ-ARLEEECNQRGAAVKRVRELEVLISELqeDLEAERAARGKVEAARRD 1147
Cdd:COG4913 222 DTFEAADALVEHFDDLeRAHEALEDAREQIELlEPIRELAERYAAARERLAELEYLRAAL--RLWFAQRRLELLEAELEE 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1148 LGEELNALRTELEdslgttAAQQELRAKREQEVSMLKKAMEDEGRsheaQVQDLRQKhsqaVEELTEQLEQAKRVRAGLE 1227
Cdd:COG4913 300 LRAELARLEAELE------RLEARLDALREELDELEAQIRGNGGD----RLEQLERE----IERLERELEERERRRARLE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1228 KAKQALEkesADLSADLRSLASAKQDVEHKKKKVEGQLNELNSRFNESERQRTELGERVSKLTTELDSvtgllneaegkn 1307
Cdd:COG4913 366 ALLAALG---LPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS------------ 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1308 ikLSKDVSSLSSQLQDAQELLSEEtrqklnlsgrLRQTEEDRN---SLMEQLEEETEAKRAVERQVSSLNMQLSDSKKKL 1384
Cdd:COG4913 431 --LERRKSNIPARLLALRDALAEA----------LGLDEAELPfvgELIEVRPEEERWRGAIERVLGGFALTLLVPPEHY 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1385 DEMSGTVEALEEGKK----RLQRELEAANSDYEEKASAYDKLEKSRGRMQQELEDVLMDlDSQRQLVSNLEkkqkkfdQM 1460
Cdd:COG4913 499 AAALRWVNRLHLRGRlvyeRVRTGLPDPERPRLDPDSLAGKLDFKPHPFRAWLEAELGR-RFDYVCVDSPE-------EL 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1461 LAEERAV--SCKFAEERDRAEAEAREKETRVLALARaleENQGALEEAEKTMKGLRADMEDLISSKDDVGKSVHDLEKAK 1538
Cdd:COG4913 571 RRHPRAItrAGQVKGNGTRHEKDDRRRIRSRYVLGF---DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERR 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1539 RGLEAI--VDEMRTQMEELEDELQVAEDAKLRLDVNTQALRaqherelhardelgeekrkQLLKQVRELEAELEEERKQR 1616
Cdd:COG4913 648 EALQRLaeYSWDEIDVASAEREIAELEAELERLDASSDDLA-------------------ALEEQLEELEAELEELEEEL 708
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1617 GQASGSKKKLEGELKDMEDQLEATSRGRDEAVKQLRKIQGQVKDLQRDLEDSRAAQKEVLASARESERRSKAMEADIVQl 1696
Cdd:COG4913 709 DELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEE- 787
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1697 hEMLAAVERARKQAEVERDELSEELASNssgkslmsDEKRRLDTKISQLEEELEEEQANvESLNdrlRKSQQLVEQLGAE 1776
Cdd:COG4913 788 -ELERAMRAFNREWPAETADLDADLESL--------PEYLALLDRLEEDGLPEYEERFK-ELLN---ENSIEFVADLLSK 854
|
730 740
....*....|....*....|....*.
gi 1604784239 1777 LAAERstsqsREGsRQQLERQNRELK 1802
Cdd:COG4913 855 LRRAI-----REI-KERIDPLNDSLK 874
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
940-1720 |
9.29e-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: 73.85 E-value: 9.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 940 DRSNALHNERKEMEQQLQLmEAHIAEEEDARQKLQME-----KVSVEGKVKKLEEDILMMEDQNNKLQKERKLLEERLAD 1014
Cdd:pfam02463 170 KKKEALKKLIEETENLAEL-IIDLEELKLQELKLKEQakkalEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRD 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1015 MSSNLAEEEEKSKNLSKLKTKHESMISELELRMKKEEKGRLDMEKAKRKVEAELGDLQEQHADLQAQLAELRAQLAAKEE 1094
Cdd:pfam02463 249 EQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEK 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1095 ELQATQARLEEECNQRGAAVKRVRELEVLISELQEDLEAERAARGKVEAARRDLGEELNA------------LRTELEDS 1162
Cdd:pfam02463 329 ELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSaaklkeeelelkSEEEKEAQ 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1163 LGTTAAQQELRAKREQEVSMLKKAMEDEGRSHEAQVQDLRQKHSQAVEELTE-----QLEQAKRVRAGLEKAKQALEKES 1237
Cdd:pfam02463 409 LLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLlkdelELKKSEDLLKETQLVKLQEQLEL 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1238 ADLSADLRSLASAKQDVEHKKKKVEGQLNELNSRFNESERQRTELGERVSKLTTELDSVTGLLNEAEGKNIKLSKDVSSL 1317
Cdd:pfam02463 489 LLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVR 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1318 SSQLQDAQELLSEETRQKLNLSGRLRQTEEDRNSLMEQLEEETEAKRAVERQVSSLNMQLSDSKKKLDEMSGTVEALEEG 1397
Cdd:pfam02463 569 ALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGL 648
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1398 KKrlQRELEAANSDYEEKASAYDKLEKSRGRMQQELEDVLMDLD-----SQRQLVSNLEKKQKKFDQMLAEERAVS--CK 1470
Cdd:pfam02463 649 RK--GVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAkeeilRRQLEIKKKEQREKEELKKLKLEAEELlaDR 726
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1471 FAEERDRAEAEAREKETRVLALARALEENQGALEEAEKTMKGLRADMEDLISSKDDVGKSVHDLEKAKRGLEAIVDEmrt 1550
Cdd:pfam02463 727 VQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEEL--- 803
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1551 QMEELEDELQVAEDAKLRLDVNTQALRAQHERELHARDELGEEKRKQLLKQVRELEAELEEERKQRGQASGSKKKL-EGE 1629
Cdd:pfam02463 804 RALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELeEQK 883
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1630 LKDMEDQLEATSRGRDEAVKQLRKIQGQVKDLQRDLEDSRAAQKEVLASARESERRSKAMEADIVQLHEMLAAVERARKQ 1709
Cdd:pfam02463 884 LKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNK 963
|
810
....*....|.
gi 1604784239 1710 AEVERDELSEE 1720
Cdd:pfam02463 964 RLLLAKEELGK 974
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1017-1370 |
9.35e-13 |
|
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: 73.95 E-value: 9.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1017 SNLAEEEEKSKNLSKLKTKHESMISELELRMKKEEKGRLDMEKAKRKV---EAELGDLQEQHADLQAQLAELRAQLAAKE 1093
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIgeiEKEIEQLEQEEEKLKERLEELEEDLSSLE 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1094 EELQATQARLEEecnqrgaavkrvreLEVLISELQEDLEAERAARGKVEAarRDLGEELNALRTELEDsLGTTAAQQELR 1173
Cdd:TIGR02169 751 QEIENVKSELKE--------------LEARIEELEEDLHKLEEALNDLEA--RLSHSRIPEIQAELSK-LEEEVSRIEAR 813
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1174 A----KREQEVSMLKKAMEDEGRSHEAQVQDLRQKHS---QAVEELTEQLEQAKRVRAGLEKAKQALEKESADLSADLRS 1246
Cdd:TIGR02169 814 LreieQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKsieKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDE 893
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1247 LASAKQDVEHKKKKVEGQLNELNSRFNESERQRTELGERVSKLTTELDSV------TGLLNEAEGKNIKLSKDVSSLSSQ 1320
Cdd:TIGR02169 894 LEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDeeipeeELSLEDVQAELQRVEEEIRALEPV 973
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1321 LQDAQELLSEETRQKLNLSGRLRQTEEDRNSLMEQLEEETEAKRAVERQV 1370
Cdd:TIGR02169 974 NMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREVFMEA 1023
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
851-1432 |
1.07e-12 |
|
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: 73.61 E-value: 1.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 851 VTRQEEEMGQKDEELKAAKEVAAKVETELKDITQK----HTQLMEERAQLEMKLhaeTELYAEAEEMRVRLEAKKQELEE 926
Cdd:pfam15921 273 ISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQarnqNSMYMRQLSDLESTV---SQLRSELREAKRMYEDKIEELEK 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 927 VLHEMESRLEEEEDRSNALHNERKEMEQQLQ--LMEAHIAEEEDARQKLQMEKVSVEGKVKKLEEDILMME--DQNNKLQ 1002
Cdd:pfam15921 350 QLVLANSELTEARTERDQFSQESGNLDDQLQklLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRREldDRNMEVQ 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1003 KERKLLE----ERLADMSSNLAEEEEKSKNLSKLKTKHESMISELELRMKKEEK---GRLDMEKAKRKVEAELGDLQEQH 1075
Cdd:pfam15921 430 RLEALLKamksECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEEltaKKMTLESSERTVSDLTASLQEKE 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1076 ADLQAQLAE---LRAQLAAKEEELQATQAR------LEEECN----QRGAAVKRVRELEVLISELQEDLEAERAARGKVE 1142
Cdd:pfam15921 510 RAIEATNAEitkLRSRVDLKLQELQHLKNEgdhlrnVQTECEalklQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQ 589
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1143 AARRDLGEELNALRTELedslgttaaqqelrakreQEVSMLKKAMEDEGRSHEAQVQDLrqkhsqaveelteQLEQAKRV 1222
Cdd:pfam15921 590 VEKAQLEKEINDRRLEL------------------QEFKILKDKKDAKIRELEARVSDL-------------ELEKVKLV 638
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1223 RAGLEKakqalekesadlsadLRSLASAKQDVEHKKKKVEGQLNELNSRFNESERQRTELGERVSKLTTELDSVTGLLNE 1302
Cdd:pfam15921 639 NAGSER---------------LRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKS 703
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1303 AEGKNIKLSKDVSSLSSQLQDAQELLSEETRQKLNLSGRLRQTEEDRNSLMEQLEEETEAKRAVERQVSSLNMQLSDSKK 1382
Cdd:pfam15921 704 AQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVAT 783
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1383 KLDEMSGTVEALEEGKKRLQRELEAANSDYEEKASAYDKLEKSRGRMQQE 1432
Cdd:pfam15921 784 EKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQE 833
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
854-1699 |
1.13e-12 |
|
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: 73.54 E-value: 1.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 854 QEEEMGQKDEELKAAKEVAAKVETELKDITQKHTQLMEE--RAQLEMKLHAETELYAEAEEMRVRLEAKKQELEEvlhem 931
Cdd:TIGR00606 310 HQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEqgRLQLQADRHQEHIRARDSLIQSLATRLELDGFER----- 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 932 ESRLEEEEDRSNALHNERKEMEQQL--QLMEAHIAEEEDARQKLQMEKVSVEGKVKKLEEDILMMEDQNNKLQKERKLLE 1009
Cdd:TIGR00606 385 GPFSERQIKNFHTLVIERQEDEAKTaaQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQ 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1010 ERLADMSSNLAEEEEKSKNLSKL-KTKHESMISELELRMKKEEKGRLDMEKAKRKVEAELGDLqEQHADLQAQLAELRAQ 1088
Cdd:TIGR00606 465 QLEGSSDRILELDQELRKAERELsKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQL-NHHTTTRTQMEMLTKD 543
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1089 LAAKEEELQATQARLEEECNQRGAAVKRVRELEVLISELQEDLEAERAARGKVEAARRDLGEELNALRTEL--------- 1159
Cdd:TIGR00606 544 KMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELeskeeqlss 623
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1160 -EDSLGTTAAQQELRAKREQEVSMLKKAmedegRSHEAQVQDLRQKHSQAVEELTEQLEQAKRVRAGLEKAKQALEKESA 1238
Cdd:TIGR00606 624 yEDKLFDVCGSQDEESDLERLKEEIEKS-----SKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFIS 698
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1239 DLSADLRSLASakqdvehkkkkvegQLNELNSRFNESERQRTELGERVSKLTTELDSVTGLLNEAEGKNIKLSKDVSSLS 1318
Cdd:TIGR00606 699 DLQSKLRLAPD--------------KLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLK 764
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1319 SQLQDAQELLseETRQKLNLSGRLRQTEEdrnSLMEQLEEETEakrAVERQVSSLNMQLSDSKKKLdemsgTVEALEEGK 1398
Cdd:TIGR00606 765 NDIEEQETLL--GTIMPEEESAKVCLTDV---TIMERFQMELK---DVERKIAQQAAKLQGSDLDR-----TVQQVNQEK 831
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1399 KRLQRELEAANSDYEEKasayDKLEKSRGRMQQELEDVLMDLDSQR-QLVSNLEKKQKkfdqmLAEERAVSCKFAEERDR 1477
Cdd:TIGR00606 832 QEKQHELDTVVSKIELN----RKLIQDQQEQIQHLKSKTNELKSEKlQIGTNLQRRQQ-----FEEQLVELSTEVQSLIR 902
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1478 AEAEAREKetrVLALARALEENQGALEE-----------AEKTMKGLRADMEDLISSKDDVGKSVHD-LEKAKRGLEAIV 1545
Cdd:TIGR00606 903 EIKDAKEQ---DSPLETFLEKDQQEKEElissketsnkkAQDKVNDIKEKVKNIHGYMKDIENKIQDgKDDYLKQKETEL 979
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1546 DEMRTQMEELEdelQVAEDAKLRLDVNTQALRAQHERELHARDELGEEKRKQLLKQVRELEAELEeerKQRGQASGSKKK 1625
Cdd:TIGR00606 980 NTVNAQLEECE---KHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRENELKEVEEELKQHL---KEMGQMQVLQMK 1053
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1626 leGELKDMEDQLEATSRGRDEAVKQLRKIQGQVKDLQRDLEDSRAAQKE--------VLASARES----ERRSKAMEADI 1693
Cdd:TIGR00606 1054 --QEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQFRDAEekyremmiVMRTTELVnkdlDIYYKTLDQAI 1131
|
....*.
gi 1604784239 1694 VQLHEM 1699
Cdd:TIGR00606 1132 MKFHSM 1137
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
947-1375 |
1.31e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 72.88 E-value: 1.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 947 NERKEMEQQLQLME---AHIAEEEDARQKLQMEKVSVEGKVKKLEEDILMMED--QNNKLQKERKLLEERLADMSSNLAE 1021
Cdd:COG4717 71 KELKELEEELKEAEekeEEYAELQEELEELEEELEELEAELEELREELEKLEKllQLLPLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1022 EEEKSKNLSKLKTKHESMISELElrmKKEEKGRLDMEKAKRKVEAELGDLQEQHADLQAQLAELRAQLAAKEEELQATQA 1101
Cdd:COG4717 151 LEERLEELRELEEELEELEAELA---ELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1102 RLEEECNQ--RGAAVKRVRELEVLISELQEDLEAErAARGKVEAARRDLGEELNALRTELEDSLGTTAAQQELRAKREQE 1179
Cdd:COG4717 228 ELEQLENEleAAALEERLKEARLLLLIAAALLALL-GLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEE 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1180 VSMLKKAMEDEGRSHEAQVQDLRQKHSQAVEELTEQLEQAKRVRAGLEKAKQALEKESADLSADLRSLASAKQDVEHkkk 1259
Cdd:COG4717 307 LQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVED--- 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1260 kvEGQLNELNSRFNESERQRTELGERVSKLTTELDSVTGLLNEAEGKNIKlsKDVSSLSSQLQDAQELLSEETRQKLNLS 1339
Cdd:COG4717 384 --EEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELE--EELEELEEELEELEEELEELREELAELE 459
|
410 420 430
....*....|....*....|....*....|....*...
gi 1604784239 1340 GRLRQTEEDRN--SLMEQLEEETEAKRAVERQVSSLNM 1375
Cdd:COG4717 460 AELEQLEEDGElaELLQELEELKAELRELAEEWAALKL 497
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1402-1829 |
1.34e-12 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 73.45 E-value: 1.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1402 QRELEAANSDYEEKASAYDKLEKSRGRMQQELEDvlmdLDSQRQLVSNLEKKQKKFDQM----------LAEERAVSCKF 1471
Cdd:PRK04863 299 RRQLAAEQYRLVEMARELAELNEAESDLEQDYQA----ASDHLNLVQTALRQQEKIERYqadleeleerLEEQNEVVEEA 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1472 AEERDRAEAEAREKETRVLALARALEENQGALEEAEKtmkglRADMEDlisskddvgKSVHDLEKAKR----------GL 1541
Cdd:PRK04863 375 DEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQT-----RAIQYQ---------QAVQALERAKQlcglpdltadNA 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1542 EAIVDEMRTQMEELEDELQvaeDAKLRLDVnTQALRAQHERELhardelgeekrkQLLKQVRELEAeleeerkqRGQASG 1621
Cdd:PRK04863 441 EDWLEEFQAKEQEATEELL---SLEQKLSV-AQAAHSQFEQAY------------QLVRKIAGEVS--------RSEAWD 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1622 SKKKLEGELKDMEDQLEatsrgrdeavkQLRKIQGQVKDLQRDLEDSRAAQKevlaSARESERRSKAMEADIVQLhemla 1701
Cdd:PRK04863 497 VARELLRRLREQRHLAE-----------QLQQLRMRLSELEQRLRQQQRAER----LLAEFCKRLGKNLDDEDEL----- 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1702 avERARKQAEVERDELSEELASNSSGKSLMSDEKRRLDTKISQLEEELEEEQANVESLNdrlrksqQLVEQLGAELAaer 1781
Cdd:PRK04863 557 --EQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALA-------RLREQSGEEFE--- 624
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1604784239 1782 sTSQSREGSRQQLERQNRELKakmqemegQGRSKLKASIAALEAKLRE 1829
Cdd:PRK04863 625 -DSQDVTEYMQQLLERERELT--------VERDELAARKQALDEEIER 663
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
944-1169 |
1.39e-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: 71.72 E-value: 1.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 944 ALHNERKEMEQQLQLMEAHIAEEEDARQKLQMEKVSVEGKVKKLEEDILMMEDQNNKLQKERKLLEERLADMSSNLAE-- 1021
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAElr 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1022 --EEEKSKNLSKLKTKHESMISELELRMKKEEKGRLDMEKAKRKVEAELGDLQEQHADLQAQLAELRAQLAAKEEELQAT 1099
Cdd:COG4942 97 aeLEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1100 QARLEEECNQRGAAVKRVRELEVLISELQEDLEAERAARGKVEAARRDLGEELNALRTELEDSLGTTAAQ 1169
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
859-1634 |
1.56e-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: 73.08 E-value: 1.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 859 GQKDEELKAAKEVAAKVETELKDITQKHTQLMEERAQ---LEMKLHAETELYA----EAEEMRVRLEAKKQELEEVLHEM 931
Cdd:TIGR00618 152 GEFAQFLKAKSKEKKELLMNLFPLDQYTQLALMEFAKkksLHGKAELLTLRSQlltlCTPCMPDTYHERKQVLEKELKHL 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 932 ESRLEEEEDRSNALHNERKEMEQqlqlmeahiaeeedaRQKLQMEKVSVEGKVKKLEEDILMMEDQNNKLQKERKLleER 1011
Cdd:TIGR00618 232 REALQQTQQSHAYLTQKREAQEE---------------QLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKA--AP 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1012 LAdmssnlaeeeEKSKNLSKLKTKHESMISELELRMKKEEKGRLDMEKAKrKVEAELGDLQEQHADLQAQLAELR--AQL 1089
Cdd:TIGR00618 295 LA----------AHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHV-KQQSSIEEQRRLLQTLHSQEIHIRdaHEV 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1090 AAKEEELQATQARLEEECNQRGAAVKRVRELEVLISELQEDLEAERAARGKVEAARRDLGEELNALRTELEDSLGTTAAQ 1169
Cdd:TIGR00618 364 ATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELC 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1170 QELRAKREQEVSMLKKAMEDEGRSHEAQVQDLRQKhsqavEELTEQLEQAKRVRaglEKAKQALEKESADLSADLRSLAS 1249
Cdd:TIGR00618 444 AAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTK-----EQIHLQETRKKAVV---LARLLELQEEPCPLCGSCIHPNP 515
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1250 AKQDV---------------EHKK-----KKVEGQLNELNSRFNESERQRTELGERVSKLTTELDSVTGLLNeaegknik 1309
Cdd:TIGR00618 516 ARQDIdnpgpltrrmqrgeqTYAQletseEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIP-------- 587
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1310 lskDVSSLSSQLQDAQELLSEETRQKLNLSGR-LRQTEEDRNSLMEQLEEETEAKRAVERQVSSLNMQLSDSKKKLDEMS 1388
Cdd:TIGR00618 588 ---NLQNITVRLQDLTEKLSEAEDMLACEQHAlLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHA 664
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1389 GTVEALEEGK-KRLQRELEAANSDYEEKASAYDKLEKSRGRMqQELEDVLMDLDSQRQLVSNLEKKQKkfdqmlAEERAV 1467
Cdd:TIGR00618 665 LSIRVLPKELlASRQLALQKMQSEKEQLTYWKEMLAQCQTLL-RELETHIEEYDREFNEIENASSSLG------SDLAAR 737
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1468 SCKFAEERDRAEAEAREKetrvlALARALEENQGALEEAEKTMKGlrADMEDLISskddvgksvhDLEKAKRGLEAIVDE 1547
Cdd:TIGR00618 738 EDALNQSLKELMHQARTV-----LKARTEAHFNNNEEVTAALQTG--AELSHLAA----------EIQFFNRLREEDTHL 800
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1548 MRTQMEELEDELQVAEDAKLRldvnTQALRAQHERELHARdelgEEKRKQLLKQVRELEAELEEERKQRGQASGSKKKLE 1627
Cdd:TIGR00618 801 LKTLEAEIGQEIPSDEDILNL----QCETLVQEEEQFLSR----LEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKII 872
|
....*..
gi 1604784239 1628 GELKDME 1634
Cdd:TIGR00618 873 QLSDKLN 879
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1644-1933 |
1.67e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 73.05 E-value: 1.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1644 RDEAVKQLRKIQG---QVKDLQRDLEdsraAQKEVLASARESERRSKAMEADIVQLHEMLAAVERARKQAEVERDELSEE 1720
Cdd:COG1196 174 KEEAERKLEATEEnleRLEDILGELE----RQLEPLERQAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELE 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1721 LASNssgkslmsdEKRRLDTKISQLEEELEEEQANVESLNDRLRKSQQLVEQLGAELAAERSTSQSREGSRQQLERQNRE 1800
Cdd:COG1196 250 ELEA---------ELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1801 LKAKMQEMEGQgRSKLKASIAALEAKLREAEEQLEIESRERQANGKNLRQKEKKLKDLTIQMEDERKQAQQYKDQAEKGN 1880
Cdd:COG1196 321 LEEELAELEEE-LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELA 399
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1604784239 1881 VRVKQLKHQLEEAEEEAQRMAAARRKLQRELDEATEANDTLSRDMASLRSKLR 1933
Cdd:COG1196 400 AQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
837-1402 |
1.96e-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: 72.69 E-value: 1.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 837 QWWRLFTKVKPLLQVTRQEEEMGQkdeELKAAKEVAAKVETELKDITQKHTQLMEERAQLEMKLHAETELYAEAEEMRVR 916
Cdd:TIGR00618 291 KAAPLAAHIKAVTQIEQQAQRIHT---ELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSI 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 917 LEAKKQELEEV--LHEMESRLEEEEDRSNALHNERKEMEQQLQLMEAHIAEEEDARQKLQMEKVSVEGKVKKLEEDILMM 994
Cdd:TIGR00618 368 REISCQQHTLTqhIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAI 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 995 EDQN----------NKLQKERKLLEERLADMSSNLAEEEEKSKNLSKLKTKHESMISELELRMKKEEKGRLDMEKAK--- 1061
Cdd:TIGR00618 448 TCTAqceklekihlQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGplt 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1062 ---RKVEAELGDLQEQHADLQAQLAELRAQLA---AKEEELQATQARLEEECNQRGAAVKRVRELEVLI-SELQEDLEAE 1134
Cdd:TIGR00618 528 rrmQRGEQTYAQLETSEEDVYHQLTSERKQRAslkEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLqDLTEKLSEAE 607
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1135 RAARGKVEAARRDLGEELNALRTELEDSLGTTAAQQELRAKREQEVSMLKKAMEDEGRSHEAQVQDLRQKHSQAVEELTE 1214
Cdd:TIGR00618 608 DMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQS 687
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1215 QLEQAKRVRAGLEKAKQALEKESADLSADLRSLASAKQDVEHKKKKVEGQLNELNSRFNESERQRTElgerVSKLTTELD 1294
Cdd:TIGR00618 688 EKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQART----VLKARTEAH 763
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1295 SVTgllNEAEGKNIKLSKDVSSLSSQLQDAQELLSEETRQKLNLSGRLRQtEEDRNSLMEQLEEETEAKRaverqVSSLN 1374
Cdd:TIGR00618 764 FNN---NEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQ-EIPSDEDILNLQCETLVQE-----EEQFL 834
|
570 580
....*....|....*....|....*...
gi 1604784239 1375 MQLSDSKKKLDEMSGTVEALEEGKKRLQ 1402
Cdd:TIGR00618 835 SRLEEKSATLGEITHQLLKYEECSKQLA 862
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1529-1890 |
2.10e-12 |
|
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: 72.79 E-value: 2.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1529 KSVHDLEKAKRGLE---AIVDEMRTQMEELEDElqvaedaklrldvntqalRAQHERELHARDELGEEKRKQLLKQVREL 1605
Cdd:TIGR02169 174 KALEELEEVEENIErldLIIDEKRQQLERLRRE------------------REKAERYQALLKEKREYEGYELLKEKEAL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1606 EAELEEERKQRGQASGSKKKLEGELKDMEDQLEATSRGRDEAVKQLRKI-QGQVKDLQRDLEDSRAAQKEVLASARESER 1684
Cdd:TIGR02169 236 ERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKER 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1685 RSKAMEADivqlhemlaaveraRKQAEVERDELSEELASnssgkslmsdekrrLDTKISQLEEELEEEQANVESLNDRLR 1764
Cdd:TIGR02169 316 ELEDAEER--------------LAKLEAEIDKLLAEIEE--------------LEREIEEERKRRDKLTEEYAELKEELE 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1765 KSQQLVEQLGAELAAERSTSQSREGSRQQLERQNRELKAKMQEMEGQGRsKLKASIAALEAKLREAEEQLEIESRERQAN 1844
Cdd:TIGR02169 368 DLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQ-RLSEELADLNAAIAGIEAKINELEEEKEDK 446
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1604784239 1845 GKNLRQKEKKLKDLTIQMEDERKQAQQYKDQAEKGNVRVKQLKHQL 1890
Cdd:TIGR02169 447 ALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQREL 492
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
851-1403 |
3.55e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 72.02 E-value: 3.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 851 VTRQEEEMGQKDEELKAAKEVAAKVETELKDITQKHTQLMEERAQLEMKLHAETELYAEAEEMRvRLEAKKQELEEVLHE 930
Cdd:PRK03918 226 LEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELK-EKAEEYIKLSEFYEE 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 931 MESRLEEEEDRSNALHNERKEMEQQLQ---LMEAHIAEEEDARQKLQMEKVSVEGKVKKLEEdILMMEDQNNKLQKERKL 1007
Cdd:PRK03918 305 YLDELREIEKRLSRLEEEINGIEERIKeleEKEERLEELKKKLKELEKRLEELEERHELYEE-AKAKKEELERLKKRLTG 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1008 LE-ERLADMssnLAEEEEKSKNLSKLKTKHESMISELELRMKKEEKGRLDMEKAKRKVEAELGDLQEQHAdlQAQLAELR 1086
Cdd:PRK03918 384 LTpEKLEKE---LEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHR--KELLEEYT 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1087 AQLAAKEEELQATQARLEEecnqrgaAVKRVRELEVLISELQEDLeaeraargkveaARRDLGEELNALRTELEdslgtT 1166
Cdd:PRK03918 459 AELKRIEKELKEIEEKERK-------LRKELRELEKVLKKESELI------------KLKELAEQLKELEEKLK-----K 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1167 AAQQELRAKREQEVSMLKKAMEDEGRsheaqvqdlrqkhSQAVEELTEQLEQAKRVRAGLEKAKQALEKESADLSADLRS 1246
Cdd:PRK03918 515 YNLEELEKKAEEYEKLKEKLIKLKGE-------------IKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEE 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1247 LA-SAKQDVEHKKKKVEGQLNELNSRFNeSERQRTELGERVSKLTTELDsvtgllnEAEGKNIKLSKDVSSLSSQLQDAQ 1325
Cdd:PRK03918 582 LGfESVEELEERLKELEPFYNEYLELKD-AEKELEREEKELKKLEEELD-------KAFEELAETEKRLEELRKELEELE 653
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1604784239 1326 ELLSEETRQklNLSGRLRQTEEDRNSLMEQLEEETEAKRAVERQVSSLNMQLSDSKKKLDEmsgtVEALEEGKKRLQR 1403
Cdd:PRK03918 654 KKYSEEEYE--ELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKE----LEKLEKALERVEE 725
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1055-1773 |
3.61e-12 |
|
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: 71.91 E-value: 3.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1055 LDMEKAKRKVEAELGDLQEQHADLQAQLAELRAQLAAKEEELQATQ---ARLEEECNQRGAAVKRVRELEVLISELQEDL 1131
Cdd:COG3096 288 LELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASdhlNLVQTALRQQEKIERYQEDLEELTERLEEQE 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1132 EAERAARGKVEAARRDLG---EELNALRTELED------SLGTTAAQ--QELRAKRE-QEVSMLKKAMEDEGRSHEAQVQ 1199
Cdd:COG3096 368 EVVEEAAEQLAEAEARLEaaeEEVDSLKSQLADyqqaldVQQTRAIQyqQAVQALEKaRALCGLPDLTPENAEDYLAAFR 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1200 DLRQKHSQAVEELTEQLEQAKRVRAGLEKAKQALEKESADLSA------------DLRSLASAKQDVEHkkkkVEGQLNE 1267
Cdd:COG3096 448 AKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKIAGEVERsqawqtarellrRYRSQQALAQRLQQ----LRAQLAE 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1268 LNSRF---NESERQRTELGERVSKLTTELDSVTGLLNEAEGKNIKLS-------KDVSSLSSQLQDAQELLSE------- 1330
Cdd:COG3096 524 LEQRLrqqQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEeqaaeavEQRSELRQQLEQLRARIKElaarapa 603
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1331 --ETRQKLN-LSGRLRQTEEDRNSLME----QLEEETEA----------KRAVERQVSSLNMQLSDSKKKL----DEMSG 1389
Cdd:COG3096 604 wlAAQDALErLREQSGEALADSQEVTAamqqLLEREREAtverdelaarKQALESQIERLSQPGGAEDPRLlalaERLGG 683
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1390 T-----------------------------VEALEEGKKRLQrELEAANSDY---EEKASAYDklekSRGRMQQELEDVL 1437
Cdd:COG3096 684 VllseiyddvtledapyfsalygparhaivVPDLSAVKEQLA-GLEDCPEDLyliEGDPDSFD----DSVFDAEELEDAV 758
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1438 MDLDSQRQL-VSNLEK--------KQKKFDQMLAEERAVSCKFAEER------DRAEAEAREKETRVLALA------RAL 1496
Cdd:COG3096 759 VVKLSDRQWrYSRFPEvplfgraaREKRLEELRAERDELAEQYAKASfdvqklQRLHQAFSQFVGGHLAVAfapdpeAEL 838
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1497 EENQGALEEAEKTMKGLRADMEDLISSKDDVGKSVHDLEKAKRGLEAIVDEMRTQ-MEELEDELQVAEDAKLRLDVNTQA 1575
Cdd:COG3096 839 AALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQANLLADETLADrLEELREELDAAQEAQAFIQQHGKA 918
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1576 LR-------------AQHErELHARDELGEEKRKQLLKQV--------RELEAELEEERKQRGQASGSKKKLEGELKDME 1634
Cdd:COG3096 919 LAqleplvavlqsdpEQFE-QLQADYLQAKEQQRRLKQQIfalsevvqRRPHFSYEDAVGLLGENSDLNEKLRARLEQAE 997
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1635 DQleatsrgRDEAVKQLRKIQGQVKD---LQRDLEDSRAAQKEVLasaRESERRSKAMEadiVQLHEmlAAVERARkqae 1711
Cdd:COG3096 998 EA-------RREAREQLRQAQAQYSQynqVLASLKSSRDAKQQTL---QELEQELEELG---VQADA--EAEERAR---- 1058
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1604784239 1712 VERDELSEELASNssgkslmsdekrrlDTKISQLEEELEEEQANVESLNDRLRKSQQLVEQL 1773
Cdd:COG3096 1059 IRRDELHEELSQN--------------RSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQE 1106
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1003-1457 |
4.52e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 71.34 E-value: 4.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1003 KERKLLEERLADMSSNLAEEEEKSKNLSKLKTKHESMISEL-----ELRMKKEEKGRLDMEKAKRKVEAELGDLQEQHAD 1077
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELeelreELEKLEKLLQLLPLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1078 LQAQLA---ELRAQLAAKEEELQATQARLEEECNQRGAAVKRvrelevLISELQEDLEAERAARGKVEAARRDLGEELNA 1154
Cdd:COG4717 151 LEERLEelrELEEELEELEAELAELQEELEELLEQLSLATEE------ELQDLAEELEELQQRLAELEEELEEAQEELEE 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1155 LRTELEDSLGTTAAQQELRAKREQEVSMLKkamedegrshEAQVQDLRQKHSQAVEELTEQLEQAKRVRAGLEKAKQALE 1234
Cdd:COG4717 225 LEEELEQLENELEAAALEERLKEARLLLLI----------AAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1235 KESADLSADLRSLASAKQDVEHKKKKVEGQLNELNSRFNESERQRTELGERVSKLTTELDSVTGLLNEAEGKNIKLSKDv 1314
Cdd:COG4717 295 REKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIA- 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1315 sslsSQLQDAQELLSEETRQKLNLSGRLRQTEEDRNSLMEQLEEETEAKRAVERQVS--SLNMQLSDSKKKLDEMSGTVE 1392
Cdd:COG4717 374 ----ALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDeeELEEELEELEEELEELEEELE 449
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1604784239 1393 ALEEGKKRLQRELEAAnsdyeEKASAYDKLEKSRGRMQQELEDVLMDLDSQRQLVSNLEKKQKKF 1457
Cdd:COG4717 450 ELREELAELEAELEQL-----EEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEY 509
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
898-1684 |
5.81e-12 |
|
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: 71.41 E-value: 5.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 898 MKLHAETELYAEAEEMRVRLEAKKQELEEVLHEMESRLEEEEDRSNALhneRKEMEQQLQLMEAHIAEEEDArqkLQMEK 977
Cdd:pfam12128 237 MKIRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQET---SAELNQLLRTLDDQWKEKRDE---LNGEL 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 978 VSVEGKVKKLEEDILMMEDQNNKLQKER----KLLEERLADMSSNLAEEEEKSKNLS----KLKTKHESMISELELRMKK 1049
Cdd:pfam12128 311 SAADAAVAKDRSELEALEDQHGAFLDADietaAADQEQLPSWQSELENLEERLKALTgkhqDVTAKYNRRRSKIKEQNNR 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1050 EEKGrLDMEKAKRKVEAELGdLQEQHADLQAQLAELRAQLAAKEEELQATQARLEEecnqrgaavkRVRELEVLISELQ- 1128
Cdd:pfam12128 391 DIAG-IKDKLAKIREARDRQ-LAVAEDDLQALESELREQLEAGKLEFNEEEYRLKS----------RLGELKLRLNQATa 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1129 --EDLEAERAARGKVEAARrdlgEELNALRTELEDslgttaAQQELRAKReqevsmlkkamedeGRSHEAQVQdLRQKHs 1206
Cdd:pfam12128 459 tpELLLQLENFDERIERAR----EEQEAANAEVER------LQSELRQAR--------------KRRDQASEA-LRQAS- 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1207 QAVEELTEQLEQAKRVraGLEKAKQALE---KESADLSADLRSLASAKQ------DVEHKKKKVEGQLNELNSRFNESER 1277
Cdd:pfam12128 513 RRLEERQSALDELELQ--LFPQAGTLLHflrKEAPDWEQSIGKVISPELlhrtdlDPEVWDGSVGGELNLYGVKLDLKRI 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1278 QRTELGERVSKLTTELDSVTGLLNEAEGKNIKLSKDVSSLSSQLQDAQELLSEETRQKLNLSGRLRQTEEDRNSLMEQLE 1357
Cdd:pfam12128 591 DVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKN 670
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1358 EE-TEAKRAVERQVSSLNMQlsdskkkldemsgtvealeegKKRLQRELEAANSDYEEKASaydkleKSRGRMQQELEDV 1436
Cdd:pfam12128 671 KAlAERKDSANERLNSLEAQ---------------------LKQLDKKHQAWLEEQKEQKR------EARTEKQAYWQVV 723
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1437 LMDLDSQRQLVSnlEKKQKKFDQMLAEERAVSckfaEERDRAEAEAREKETRVLALARALEENQGALEEAEKTmkglrad 1516
Cdd:pfam12128 724 EGALDAQLALLK--AAIAARRSGAKAELKALE----TWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVR------- 790
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1517 mEDLISSKDDVGKSVHDLEKAKRGLEaiVDEMRTQMEELEDEL-QVAEDAKLRldvntqalRAQHERELHARDELgEEKR 1595
Cdd:pfam12128 791 -RQEVLRYFDWYQETWLQRRPRLATQ--LSNIERAISELQQQLaRLIADTKLR--------RAKLEMERKASEKQ-QVRL 858
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1596 KQLLKQVRELEAELEEERKQRGQASgskkkLEGELKDMEDQLEATSRGRDEAVKQLRKIQGQVKDLQRDLedSRAAQKEV 1675
Cdd:pfam12128 859 SENLRGLRCEMSKLATLKEDANSEQ-----AQGSIGERLAQLEDLKLKRDYLSESVKKYVEHFKNVIADH--SGSGLAET 931
|
....*....
gi 1604784239 1676 LASARESER 1684
Cdd:pfam12128 932 WESLREEDH 940
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
853-1336 |
9.72e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 70.94 E-value: 9.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 853 RQEEEMGQKDEELKAAKEVAAKVETELK-DITQKHTQLMEERAQlEMKLHAETELYAE----AEEMRVRLEAKKQE---- 923
Cdd:PTZ00121 1457 KKAEEAKKKAEEAKKADEAKKKAEEAKKaDEAKKKAEEAKKKAD-EAKKAAEAKKKADeakkAEEAKKADEAKKAEeakk 1535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 924 LEEVLHEMESRLEEEEDRSNALHN--ERKEMEQQLQLMEAHIAEEEDARQKLQMEKVSVEGKVKKLEEDILMMEDQNNKL 1001
Cdd:PTZ00121 1536 ADEAKKAEEKKKADELKKAEELKKaeEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKA 1615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1002 QKERKLLEErladmssnLAEEEEKSKNLSKLKTKHESMISELELRMKKEEKGRLDMEKAKRKVEAELGDLQEQHADLQAQ 1081
Cdd:PTZ00121 1616 EEAKIKAEE--------LKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDE 1687
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1082 LAELRAQLAAKEEELQATQARLEEECNQRGAAVKRVRELEVLISELQEDLEAERAARgKVEAARRDLGEELNALRTELED 1161
Cdd:PTZ00121 1688 KKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKK-KAEEAKKDEEEKKKIAHLKKEE 1766
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1162 SLGTTAAQQELRAKREQEVsmlKKAMEDEGRSHEAQVQDLRQKHsqavEELTEQLEQAKRVRAGLEKAKQALEKESADLS 1241
Cdd:PTZ00121 1767 EKKAEEIRKEKEAVIEEEL---DEEDEKRRMEVDKKIKDIFDNF----ANIIEGGKEGNLVINDSKEMEDSAIKEVADSK 1839
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1242 ADLRSLASAKQDVEHKKKKVEGQLNELNSRFNESERQRTELGERVSKlTTELDSVTGLLNEAEGKNIKLSKDVSSLSSQL 1321
Cdd:PTZ00121 1840 NMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEE-ADEIEKIDKDDIEREIPNNNMAGKNNDIIDDK 1918
|
490
....*....|....*...
gi 1604784239 1322 QDAQELL---SEETRQKL 1336
Cdd:PTZ00121 1919 LDKDEYIkrdAEETREEI 1936
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1639-1879 |
3.30e-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: 67.48 E-value: 3.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1639 ATSRGRDEAVKQLRKIQGQVKDLQRDLEDSRAAQKEVLASARESERRSKAMEADIVQLHEMLAAVERARKQAEVERDELS 1718
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1719 EELASNssgKSLMSDEKRRLDTKISQLEEELEEEQANVESLNDRLRKSQQLVEQLGAELAAERSTSQSREGSRQQLERQN 1798
Cdd:COG4942 97 AELEAQ---KEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1799 RELKAKMQEMEGQgRSKLKASIAALEAKLREAEEQLEIESRERQANGKNLRQKEKKLKDLTIQMEDERKQAQQYKDQAEK 1878
Cdd:COG4942 174 AELEALLAELEEE-RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
.
gi 1604784239 1879 G 1879
Cdd:COG4942 253 G 253
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
775-1408 |
3.57e-11 |
|
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: 68.66 E-value: 3.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 775 RTGVLAQLEEERDLKLTVVIIAFQAQARGFLARKAFSKRQQQLTAMKVIQRNCACYLKLKNWQwwrLFTKVKPLLQVTRQ 854
Cdd:pfam01576 498 RNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQ---LEEKAAAYDKLEKT 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 855 EEEMGQKDEELKAAKEVAAKVETELKDITQKHTQLMEERAQLEMKLHAETE-LYAEAEEMRVRLEAKKQELEEVLHEMES 933
Cdd:pfam01576 575 KNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDrAEAEAREKETRALSLARALEEALEAKEE 654
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 934 RLEEEE-----------------DRSNALHNERKEMEQQLQLMEAHIAEEEDARQ-----KLQMEkVSVEGKVKKLEEDI 991
Cdd:pfam01576 655 LERTNKqlraemedlvsskddvgKNVHELERSKRALEQQVEEMKTQLEELEDELQatedaKLRLE-VNMQALKAQFERDL 733
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 992 LMMEDQNnklQKERKLLEERLADMSSNLAEEEEKSKNLSKLKTKHESMISELELRMKKEEKGRLDMEKAKRKVEAELGDL 1071
Cdd:pfam01576 734 QARDEQG---EEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDL 810
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1072 QEQHADLQAQLAELRAQlaAKEEElqatqarleeecnqrgaavKRVRELEVLISELQEDLEAERAARGKVEAARRDLGEE 1151
Cdd:pfam01576 811 QRELEEARASRDEILAQ--SKESE-------------------KKLKNLEAELLQLQEDLAASERARRQAQQERDELADE 869
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1152 LNalrteleDSLGTTAAQQELRAKREQEVSMLKKAMEDEGRSHEAqVQDLRQKHSQAVEELTEQLEQAKRVRAGLEKAKQ 1231
Cdd:pfam01576 870 IA-------SGASGKSALQDEKRRLEARIAQLEEELEEEQSNTEL-LNDRLRKSTLQVEQLTTELAAERSTSQKSESARQ 941
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1232 ALEKESADLSADLRSLASAKQDvehkkkkvegqlnelnsrfneserqrtelgervskltteldsvtgllneaegkniKLS 1311
Cdd:pfam01576 942 QLERQNKELKAKLQEMEGTVKS-------------------------------------------------------KFK 966
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1312 KDVSSLSSQLQDAQELLSEETRQKLNLSGRLRQTEEDRNSLMEQLEEETEAKRAVERQVSSLNMQLSDSKKKLDEMSGTV 1391
Cdd:pfam01576 967 SSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEA 1046
|
650
....*....|....*..
gi 1604784239 1392 EALEEGKKRLQRELEAA 1408
Cdd:pfam01576 1047 SRANAARRKLQRELDDA 1063
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
916-1455 |
5.58e-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: 67.74 E-value: 5.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 916 RLEAKKQELEEVLHEMESRLEEEEDRSNALHN-------ERKEMEQQLQLMEAHIAEEEDARQKLQMEKVSVE------- 981
Cdd:TIGR04523 128 KLEKQKKENKKNIDKFLTEIKKKEKELEKLNNkyndlkkQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLElllsnlk 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 982 ---GKVKKLEEDILMMEDQNNKLQKERKLLEERLADMSSNLAEEEEKSKNLSKLKTKHESMISELELRMKKEEKGRLDME 1058
Cdd:TIGR04523 208 kkiQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELE 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1059 KAKRKVEAELGDLQEQHAdlQAQLAELRAQLAAKEEELQATQARLEE------ECNQRGAAVKR-VRELEVLISELQEDL 1131
Cdd:TIGR04523 288 KQLNQLKSEISDLNNQKE--QDWNKELKSELKNQEKKLEEIQNQISQnnkiisQLNEQISQLKKeLTNSESENSEKQREL 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1132 EAERAARGKVEAARRDLGEELNALRTELEDSLGTTAAQQELRAKREQEVsmlkKAMEDEGRSHEAQVQDLRQ---KHSQA 1208
Cdd:TIGR04523 366 EEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQI----KKLQQEKELLEKEIERLKEtiiKNNSE 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1209 VEELTEQLEQAKRVRAGLEKAKQALEKESADLSADLRSLASAKQDVEHKKKKVEGQLNELNSRFNESERQRTELGERVSK 1288
Cdd:TIGR04523 442 IKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISS 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1289 LTTELDSVTGLLNEAEGKNIKLSKDVSSLSSQLQdaQELLSEETRQKlnlsgrlrqteedrNSLMEQLEEETEAKRAVER 1368
Cdd:TIGR04523 522 LKEKIEKLESEKKEKESKISDLEDELNKDDFELK--KENLEKEIDEK--------------NKEIEELKQTQKSLKKKQE 585
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1369 QVSSLNMQLSDSKKKLDEmsgTVEALEEGKKRLQRELEAANSDYEEKASAYDKLEKSRGRMQQELEDVLMDLDSQRQLVS 1448
Cdd:TIGR04523 586 EKQELIDQKEKEKKDLIK---EIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWP 662
|
....*..
gi 1604784239 1449 NLEKKQK 1455
Cdd:TIGR04523 663 EIIKKIK 669
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1284-1858 |
1.08e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 67.01 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1284 ERVSKLTTELDSVTGLLNEAEGKNIKLSKDVSSLSSQLQDAQELLSEETRQKLnlsgRLRQTEEDRNSLMEQLEEETEAK 1363
Cdd:PRK03918 179 ERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVK----ELEELKEEIEELEKELESLEGSK 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1364 RAVERQVSSLNMQLSDSKKKLDEMSGTVEALEEgkkrlqreleaansdYEEKASAYDKLEKSRGRMQQELEDVLMDLDSQ 1443
Cdd:PRK03918 255 RKLEEKIRELEERIEELKKEIEELEEKVKELKE---------------LKEKAEEYIKLSEFYEEYLDELREIEKRLSRL 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1444 RQLVSNLEKKQKKFDQMLAEERAVSCKFAEERDRAEAeaREKETRVLALARALEENQGAL--EEAEKTMKGLRADMEDLI 1521
Cdd:PRK03918 320 EEEINGIEERIKELEEKEERLEELKKKLKELEKRLEE--LEERHELYEEAKAKKEELERLkkRLTGLTPEKLEKELEELE 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1522 SSKDDVGKSVHDLEKAKRGLEAIVDEMRTQMEELEDelqvaedAKLRLDVNTQALRAQHERELHAR------------DE 1589
Cdd:PRK03918 398 KAKEEIEEEISKITARIGELKKEIKELKKAIEELKK-------AKGKCPVCGRELTEEHRKELLEEytaelkriekelKE 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1590 LGEEKRKQL--LKQVRELEAELEEERKQRGQASgSKKKLEGELKDME-DQLEATSRGRDEAVKQLRKIQGQVKDLQRDLE 1666
Cdd:PRK03918 471 IEEKERKLRkeLRELEKVLKKESELIKLKELAE-QLKELEEKLKKYNlEELEKKAEEYEKLKEKLIKLKGEIKSLKKELE 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1667 dsraaqkevlaSARESERRSKAMEADIVQLHEMLAAVERARKQAEVER-DELSEELASNSS------GKSLMSDEKRRLD 1739
Cdd:PRK03918 550 -----------KLEELKKKLAELEKKLDELEEELAELLKELEELGFESvEELEERLKELEPfyneylELKDAEKELEREE 618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1740 TKISQLEEELEEEQANVESLNDRLRKSQQLVEQLGAELAAERstsqsREGSRQQLERQNRELKAKMQEMEG--QGRSKLK 1817
Cdd:PRK03918 619 KELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEE-----YEELREEYLELSRELAGLRAELEEleKRREEIK 693
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 1604784239 1818 ASIAALEAKLREAEE-QLEIESRER-QANGKNLRQKEKKLKDL 1858
Cdd:PRK03918 694 KTLEKLKEELEEREKaKKELEKLEKaLERVEELREKVKKYKAL 736
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1336-1733 |
1.81e-10 |
|
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: 66.24 E-value: 1.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1336 LNLSGRLRQTEEDRNSLMEQLEEETEAKR----AVERQVSSLNMQLSDSKKKLDEMSGTVEALEEGKKrLQRELEAAnsD 1411
Cdd:TIGR02169 148 ISMSPVERRKIIDEIAGVAEFDRKKEKALeeleEVEENIERLDLIIDEKRQQLERLRREREKAERYQA-LLKEKREY--E 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1412 YEEKASAYDKLEKSRGRMQQELEDVLMDLDSQRQLVSNLEKKQKKFDQMLAE-ERAVSCKFAEERDRAEAEAREKETRVL 1490
Cdd:TIGR02169 225 GYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEElNKKIKDLGEEEQLRVKEKIGELEAEIA 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1491 ALARALEENQGALEEAEKTMKGLRADMEDLISSKDDVGKSVHDLEKAKRGLEAIVDEMRTQMEELEDELQvaedaklRLD 1570
Cdd:TIGR02169 305 SLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELE-------EVD 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1571 VNTQALRAQHERELHARDELGEEKRKQLLKQVRELEAELeeerkqrgQASGSKKKLEGELKDMEDQLEATSRGRDEAVKQ 1650
Cdd:TIGR02169 378 KEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQ--------RLSEELADLNAAIAGIEAKINELEEEKEDKALE 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1651 LRKIQGQVKDLQRDLEDSraaqkevlasaresERRSKAMEADIVQLHEMLAAVERARKQAEVERDELSEELASNSSGKSL 1730
Cdd:TIGR02169 450 IKKQEWKLEQLAADLSKY--------------EQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEV 515
|
...
gi 1604784239 1731 MSD 1733
Cdd:TIGR02169 516 LKA 518
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
955-1106 |
2.32e-10 |
|
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: 62.63 E-value: 2.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 955 QLQLMEAHIAEEEDARQKLQMEKVSVEGKVKKLEEDILMMEDQNNKLQKERKLLEERLADMSSNLAEEEEKSKNLSKLK- 1033
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKe 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1604784239 1034 -TKHESMISELELRMKKEEKGRLDMEKAKRKVEAELGDLQEQHADLQAQLAELRAQLAAKEEELQATQARLEEE 1106
Cdd:COG1579 91 yEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE 164
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1084-1878 |
2.78e-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: 65.84 E-value: 2.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1084 ELRAQLAAKEEELQATQARLEEECNQRGAAVKRVRELEVLISELQEdLEAERAARGKVEAARRDLGEELNALRTELedSL 1163
Cdd:TIGR00606 221 EIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMK-LDNEIKALKSRKKQMEKDNSELELKMEKV--FQ 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1164 GTTAAQQELRAKREQEVSMLKKAMEDEGRSHEA---QVQDLRQKHSQAVEELTEQLEQAKRVRA-----GLEKAKQALEK 1235
Cdd:TIGR00606 298 GTDEQLNDLYHNHQRTVREKERELVDCQRELEKlnkERRLLNQEKTELLVEQGRLQLQADRHQEhirarDSLIQSLATRL 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1236 ESADLSADLRSLASAKQDVEHKKKKVEGQLNELNSRFNESERQRTELGERVSKLTtelDSVTGLLNEAEGKNIKLSKDVS 1315
Cdd:TIGR00606 378 ELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIR---DEKKGLGRTIELKKEILEKKQE 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1316 SLSSQLQDAQELLSEETRQkLNLSGRLRQTEEDRNSLMEQLEEETEAKRaverqVSSLNMQLSDSKKKLDEMSGTVEALE 1395
Cdd:TIGR00606 455 ELKFVIKELQQLEGSSDRI-LELDQELRKAERELSKAEKNSLTETLKKE-----VKSLQNEKADLDRKLRKLDQEMEQLN 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1396 EGKKRLQRELEAAnsdyEEKASAYDKLEKSRGRMQQELEDVLMDLDSQRQLVSNLEKKQKKFDQMLAEERAVSCKFAEER 1475
Cdd:TIGR00606 529 HHTTTRTQMEMLT----KDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLE 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1476 DRAEAEAREKETrvlalaraLEENQGALEEAEKTMKGLRADMEDLISSKDDVGKSVHDLEKakrgLEAIVDEMRTQMEEL 1555
Cdd:TIGR00606 605 QNKNHINNELES--------KEEQLSSYEDKLFDVCGSQDEESDLERLKEEIEKSSKQRAM----LAGATAVYSQFITQL 672
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1556 EDELQVAEDAKLRlDVNTQALRAQHERELHARDELGEEKRKQLLKQVreleaeleeerkqrgqasgskKKLEGELKDMED 1635
Cdd:TIGR00606 673 TDENQSCCPVCQR-VFQTEAELQEFISDLQSKLRLAPDKLKSTESEL---------------------KKKEKRRDEMLG 730
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1636 QLEATSRGRDEAVKQLRKIQGQVKDLQRDLEDSR---AAQKEVLASARESERRSKAMEADIV---QLHEMLAAVERARKQ 1709
Cdd:TIGR00606 731 LAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKndiEEQETLLGTIMPEEESAKVCLTDVTimeRFQMELKDVERKIAQ 810
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1710 AEVERDELSEELASNSSGKSlMSDEKRRLDTKISQLEEELEEEQanveslnDRLRKSQQLVEQLGaELAAERSTSQSREG 1789
Cdd:TIGR00606 811 QAAKLQGSDLDRTVQQVNQE-KQEKQHELDTVVSKIELNRKLIQ-------DQQEQIQHLKSKTN-ELKSEKLQIGTNLQ 881
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1790 SRQQLERQNRELKAKMQEME---GQGRSKLKASIAALEAKLREAEEQLEIESRERQANGKNLRQKEKKLKDLTIQMEDER 1866
Cdd:TIGR00606 882 RRQQFEEQLVELSTEVQSLIreiKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIE 961
|
810
....*....|..
gi 1604784239 1867 KQAQQYKDQAEK 1878
Cdd:TIGR00606 962 NKIQDGKDDYLK 973
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1101-1856 |
3.34e-10 |
|
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: 65.63 E-value: 3.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1101 ARLEEECNQRGAAVKRVRELEVLISELQ--EDLEAERAARGKVEAARrdlgEELNALRTELEDSLGTTAAQQELRAKREQ 1178
Cdd:pfam12128 204 AILEDDGVVPPKSRLNRQQVEHWIRDIQaiAGIMKIRPEFTKLQQEF----NTLESAELRLSHLHFGYKSDETLIASRQE 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1179 EVSMLKKAMEDEGRSHEAQVQDLRQKHSQAVEELTEQLEQAKRVRAGLEKAKQALEKESAD-LSADLRSLASAKQDVEHK 1257
Cdd:pfam12128 280 ERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIEtAAADQEQLPSWQSELENL 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1258 KKKVEGQLNELNSRFNESERQRTELGERVSKLTTELDSVTGLLNEAEGKniklskdvssLSSQLQDAQELLSEETRQKLN 1337
Cdd:pfam12128 360 EERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIREARDR----------QLAVAEDDLQALESELREQLE 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1338 lsGRLRQTEEDRNSLMEQLEEETEAKRAVERQvSSLNMQLSDSKKKLDEMSGTVEALEEGKKRLQRELEAANSDYEEKAS 1417
Cdd:pfam12128 430 --AGKLEFNEEEYRLKSRLGELKLRLNQATAT-PELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASE 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1418 AYDKLEKSRGRMQQELEDVLMDLDSQR-QLVSNLEKkqkkfdqmlaeeravsckfaEERDRAEAEAREKETRVLALARAL 1496
Cdd:pfam12128 507 ALRQASRRLEERQSALDELELQLFPQAgTLLHFLRK--------------------EAPDWEQSIGKVISPELLHRTDLD 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1497 EENQGALEEAEKTMKGLRADMEDLisskddvgksvhdlekakrgleaivdemrtqmeELEDELQVAEDAKLRLDVNTQAL 1576
Cdd:pfam12128 567 PEVWDGSVGGELNLYGVKLDLKRI---------------------------------DVPEWAASEEELRERLDKAEEAL 613
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1577 RAQHERELHARDELGeekrkQLLKQVRELEAELEEERKQRGQASGSKKKLEGELKDMEDQL-EATSRGRDEAVKQLRKIQ 1655
Cdd:pfam12128 614 QSAREKQAAAEEQLV-----QANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKnKALAERKDSANERLNSLE 688
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1656 GQVKDLQRDLEDSRAAQKEVLASAR-ESERRSKAMEADI-VQLHEMLAAVERARKQAEVERDELSEELASNSSGKSL--- 1730
Cdd:pfam12128 689 AQLKQLDKKHQAWLEEQKEQKREARtEKQAYWQVVEGALdAQLALLKAAIAARRSGAKAELKALETWYKRDLASLGVdpd 768
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1731 ----MSDEKRRLDTKISQLEEELEEEQANVESLNDR-LRKSQQLVEQLgaelaaeRSTSQSREGSRQQLERQNRELKAKM 1805
Cdd:pfam12128 769 viakLKREIRTLERKIERIAVRRQEVLRYFDWYQETwLQRRPRLATQL-------SNIERAISELQQQLARLIADTKLRR 841
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1604784239 1806 QEMEGQGRSKLKASIAALE------------AKLREAE--EQLEIESRERQANGKNLRQKEKKLK 1856
Cdd:pfam12128 842 AKLEMERKASEKQQVRLSEnlrglrcemsklATLKEDAnsEQAQGSIGERLAQLEDLKLKRDYLS 906
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
844-1249 |
4.08e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 64.79 E-value: 4.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 844 KVKPLLQVTRQEEEMGQKDEELKAAKEvAAKVETELKDITQKHTQLMEERAQLEMKLHAETELYAEAEEMRVRLEAKKQE 923
Cdd:COG4717 86 KEEEYAELQEELEELEEELEELEAELE-ELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEE 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 924 LE----EVLHEMESRLEEEEDRSNALHNERKEMEQQLQLMEAHIAEEEDARQKLQMEKVSVEGKVKKLEEDiLMMEDQNN 999
Cdd:COG4717 165 LEeleaELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENE-LEAAALEE 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1000 KLQKERKLL------------EERLADMSSNLAE-----------------EEEKSKNLSKLKTKHESMISELELRMKKE 1050
Cdd:COG4717 244 RLKEARLLLliaaallallglGGSLLSLILTIAGvlflvlgllallflllaREKASLGKEAEELQALPALEELEEEELEE 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1051 EKGRLDMEKAKRKVEA-ELGDLQEQHADLQAQLAELRAQLAAKEEE------LQATQARLEEECNQRGAAVKRVRELEVL 1123
Cdd:COG4717 324 LLAALGLPPDLSPEELlELLDRIEELQELLREAEELEEELQLEELEqeiaalLAEAGVEDEEELRAALEQAEEYQELKEE 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1124 ISELQEDLEAERAARGKVEAA--RRDLGEELNALRTELEDSLGTTAAQQELRAKREQEVSMLKKamedegrshEAQVQDL 1201
Cdd:COG4717 404 LEELEEQLEELLGELEELLEAldEEELEEELEELEEELEELEEELEELREELAELEAELEQLEE---------DGELAEL 474
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1604784239 1202 RQKHSQAVEELTEQLEQAKRVRAGLEKAKQALEKESADLSADLRSLAS 1249
Cdd:COG4717 475 LQELEELKAELRELAEEWAALKLALELLEEAREEYREERLPPVLERAS 522
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
812-1445 |
6.04e-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: 64.68 E-value: 6.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 812 KRQQQLTAMKVIQRNCACY---LKLKNWQWWRLFTKVKPLLQVTRQEEE-MGQKDEELKAAKEVAAKVETELKDITQKHT 887
Cdd:TIGR00606 399 VIERQEDEAKTAAQLCADLqskERLKQEQADEIRDEKKGLGRTIELKKEiLEKKQEELKFVIKELQQLEGSSDRILELDQ 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 888 QLMEERAQLEMklhAETELYAEAEEMRVR-LEAKKQELEEVLhemesrleEEEDRSNALHNERKEMEQQlqlMEAHIAEE 966
Cdd:TIGR00606 479 ELRKAERELSK---AEKNSLTETLKKEVKsLQNEKADLDRKL--------RKLDQEMEQLNHHTTTRTQ---MEMLTKDK 544
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 967 EDARQKLQMEKVSVEGKVKKLEEDI---LMMEDQNNKLQKERKLLEERLADMSSNLAEEEEKSKNLSKLKTKHESMISEL 1043
Cdd:TIGR00606 545 MDKDEQIRKIKSRHSDELTSLLGYFpnkKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSY 624
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1044 ElrmkkeekGRLDMEKAKRKVEAELGDLQEQHADLQAQLAELRAQLAAKEEELQATQARLEEECNQRGAAVKRVRELEVL 1123
Cdd:TIGR00606 625 E--------DKLFDVCGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEF 696
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1124 ISELQEDLeaeRAARGKVEaarrDLGEELNALRTELEDSLGTTAAQQELRAKREQEVSMLKKAMEDEGRSHEAQVQDLRQ 1203
Cdd:TIGR00606 697 ISDLQSKL---RLAPDKLK----STESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEE 769
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1204 KHSQ-------------------AVEELTEQLEQAKRvraglEKAKQALEKESADLSADLRSLASAKQDVEHKKKKVEGQ 1264
Cdd:TIGR00606 770 QETLlgtimpeeesakvcltdvtIMERFQMELKDVER-----KIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSK 844
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1265 LNELNSRFNESERQRTELGERVSKLTTELDSVTGLLNEA---EGKNIKLSKDVSSLSSQLQDAQEllseetrqklnlsgr 1341
Cdd:TIGR00606 845 IELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRqqfEEQLVELSTEVQSLIREIKDAKE--------------- 909
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1342 lrQTEEDRNSLMEQLEEETEAKRAVERQVSSLNMQLSDSKKKLDEMSGTVEALE----EGKKRLQRELEaanSDYEEKAS 1417
Cdd:TIGR00606 910 --QDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIEnkiqDGKDDYLKQKE---TELNTVNA 984
|
650 660
....*....|....*....|....*...
gi 1604784239 1418 AYDKLEKSRGRMQQELEDVLMDLDSQRQ 1445
Cdd:TIGR00606 985 QLEECEKHQEKINEDMRLMRQDIDTQKI 1012
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
853-1147 |
6.81e-10 |
|
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: 64.37 E-value: 6.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 853 RQEEEMGQKDEELKAAKEvaakvETELKDITQKHTQLMEERAQLEMKLHAETELYAEAEEM---------RVRLEAKKQE 923
Cdd:pfam17380 287 RQQQEKFEKMEQERLRQE-----KEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMamerereleRIRQEERKRE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 924 LEEVlhemeSRLEEEEDRSNALHNERKEMEQQLQLMEAHIAEEEDARQKLQMEKVSVEGKVKKLEEDILMMEDQNNKLQK 1003
Cdd:pfam17380 362 LERI-----RQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQRE 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1004 ERKLLEERLADMSSNLAEEEEKSKNLSKLKTKHESMISElELRMKKEEKGRLDMEKAKRKVEAelgdlQEQHADLQAQLA 1083
Cdd:pfam17380 437 VRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRK-KLELEKEKRDRKRAEEQRRKILE-----KELEERKQAMIE 510
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1604784239 1084 ELRAQlAAKEEELQATQARLEEECNQRGAAVKRVRELEV-LISELQEDLEAERAARGKVEAARRD 1147
Cdd:pfam17380 511 EERKR-KLLEKEMEERQKAIYEEERRREAEEERRKQQEMeERRRIQEQMRKATEERSRLEAMERE 574
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1122-1603 |
7.10e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 64.02 E-value: 7.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1122 VLISELQEDLEAERAARGKVEAARRDLGEELNALRTELEDSLGTTAAQQELRAKREQEVSMLKKAMEdegrshEAQVQDL 1201
Cdd:COG4717 46 MLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELE------ELREELE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1202 RQKHSQAVEELTEQLEQAKRVRAGLEKAKQALEKESADLSADLRSLASAKQDVEHKKKKVEGQLNELNsrfNESERQRTE 1281
Cdd:COG4717 120 KLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLS---LATEEELQD 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1282 LGERVSKLTTELDSVTGLLNEAEGKNIKLSKDVSSLSSQLQDAQELLS-EETRQKLNLSGRLRQTEEDRNSLMEQLEEET 1360
Cdd:COG4717 197 LAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERlKEARLLLLIAAALLALLGLGGSLLSLILTIA 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1361 EAKRAVERQVSSLNMQLSDSKKKLDEMSGTVEALEEGKKRLQRELEAANSDYE-EKASAYDKLEKSRGRMQ--QELEDVL 1437
Cdd:COG4717 277 GVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGlPPDLSPEELLELLDRIEelQELLREA 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1438 MDLDSQRQLVSNLEKKQKKFDQMLA---EERAVSCKFAEERDRAEAEAREKETRVLALARALEEN---------QGALEE 1505
Cdd:COG4717 357 EELEEELQLEELEQEIAALLAEAGVedeEELRAALEQAEEYQELKEELEELEEQLEELLGELEELlealdeeelEEELEE 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1506 AEKTMKGLRADMEDLISSKDDVGKSVHDLEKAKRgleaiVDEMRTQMEELEDELQVAEDAKLRLDVNTQALRaqherelH 1585
Cdd:COG4717 437 LEEELEELEEELEELREELAELEAELEQLEEDGE-----LAELLQELEELKAELRELAEEWAALKLALELLE-------E 504
|
490
....*....|....*...
gi 1604784239 1586 ARDELGEEKRKQLLKQVR 1603
Cdd:COG4717 505 AREEYREERLPPVLERAS 522
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
904-1674 |
7.92e-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: 63.97 E-value: 7.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 904 TELYAEAEEMRVRLEAKKQELEEvlhemesrleeeedRSNALHNERKEMEQQlqlmeahiaeeEDARQKLQM--EKVSVe 981
Cdd:pfam05483 81 SKLYKEAEKIKKWKVSIEAELKQ--------------KENKLQENRKIIEAQ-----------RKAIQELQFenEKVSL- 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 982 gkvkKLEEDILMMED---QNNKLQKERKLLEE---RLADMSSNLAEEEEKSKNL-SKLKTKHESMISELELRMKKEEKGR 1054
Cdd:pfam05483 135 ----KLEEEIQENKDlikENNATRHLCNLLKEtcaRSAEKTKKYEYEREETRQVyMDLNNNIEKMILAFEELRVQAENAR 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1055 LDMEkakrkveaelGDLQEQHADLQAQLAELRAQLAAKEEELQATQARLEEECNqrgaavkRVRELEVLISELQEDLEAE 1134
Cdd:pfam05483 211 LEMH----------FKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKEN-------KMKDLTFLLEESRDKANQL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1135 RAARGKVEAARRDLGEELNALRTELEDslgttaaqqeLRAKREQEVSMLKKAMEDegrsheaqVQDLRQKHSQAVEELTE 1214
Cdd:pfam05483 274 EEKTKLQDENLKELIEKKDHLTKELED----------IKMSLQRSMSTQKALEED--------LQIATKTICQLTEEKEA 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1215 QLEQAKRVRAGLEKAKQALEKESADLSADLRSlasakqdVEHKKKKVEGQLNELNSRFNESERQRTELGERVSKLTTELD 1294
Cdd:pfam05483 336 QMEELNKAKAAHSFVVTEFEATTCSLEELLRT-------EQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELE 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1295 SVTGLLNEAEgKNIKLSKDVSSLSSQLQDAQEllseetrqklNLSGRLRQTEEDRNSLMEQLEEETEAKRAVERQVSSLN 1374
Cdd:pfam05483 409 ELKKILAEDE-KLLDEKKQFEKIAEELKGKEQ----------ELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLK 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1375 MQLSDSKKKLDEMSGTVEALEEGKKRLQRELEAANSDYEEKASAYDKLEKSRGRMQQELEDVlmdLDSQRQLVSNLEKKQ 1454
Cdd:pfam05483 478 TELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENL---EEKEMNLRDELESVR 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1455 KKFDQMLAEERAVSCKFAEERDRAEAEAREKETRVLA-------LARALEENQGALEEAEKTMKGLR----ADMEDLISS 1523
Cdd:pfam05483 555 EEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKIlenkcnnLKKQIENKNKNIEELHQENKALKkkgsAENKQLNAY 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1524 KDDVGKSVHDLEKAKRGLEAIVDEMRTQMEEL----EDELQVAEDAKLRLDvntQALRAQHERELHARDELGE-----EK 1594
Cdd:pfam05483 635 EIKVNKLELELASAKQKFEEIIDNYQKEIEDKkiseEKLLEEVEKAKAIAD---EAVKLQKEIDKRCQHKIAEmvalmEK 711
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1595 RKQLLKQVRELEAELEEERKQRGQ-ASGSKKKLEGELKDMEDQLEATSrgrdeavKQLRKIQGQVKDLQRDLEDSRAAQK 1673
Cdd:pfam05483 712 HKHQYDKIIEERDSELGLYKNKEQeQSSAKAALEIELSNIKAELLSLK-------KQLEIEKEEKEKLKMEAKENTAILK 784
|
.
gi 1604784239 1674 E 1674
Cdd:pfam05483 785 D 785
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
957-1406 |
1.38e-09 |
|
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: 63.22 E-value: 1.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 957 QLMEAHIAEEEDARQKLQMEK------VSVEGKVKKLEEDILMMEDQNNKLQKERKLLEERLADMSSNLAEEEEKSKNLS 1030
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQMELehkrarIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1031 KlktkhesmiSELELRMKKEEKgrldmekakrkvEAELGDLQEQHADLQAQLAELRAQLAAKEEELQATQARLEE----- 1105
Cdd:pfam05557 83 K---------YLEALNKKLNEK------------ESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEElqerl 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1106 -------------------ECNQRGAAVKRVRELEVLI------SELQEDLEAERAARGKVEAARRDLGEELNALRTELE 1160
Cdd:pfam05557 142 dllkakaseaeqlrqnlekQQSSLAEAEQRIKELEFEIqsqeqdSEIVKNSKSELARIPELEKELERLREHNKHLNENIE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1161 DSLGTTAAQQELRAKREQEVSMLKKA--MEDEGRSHEAQVQD---LRQKHSQAV---EELTEQLEQakrvragLEKAKQA 1232
Cdd:pfam05557 222 NKLLLKEEVEDLKRKLEREEKYREEAatLELEKEKLEQELQSwvkLAQDTGLNLrspEDLSRRIEQ-------LQQREIV 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1233 LEKESADLSADLRSLASAKQDVEHKKKKVEGQLNELNSRFNESERQRTELGERVSKLTTELDSVTGLLnEAEGKNIKLSK 1312
Cdd:pfam05557 295 LKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAIL-ESYDKELTMSN 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1313 DVSSLSSQLQDAQELLSEETRQKLNLSGRLRQTEEDRNSLMEQ---LEEETEAKRAVERQ--VSSLNMQLSDSKKKLDEM 1387
Cdd:pfam05557 374 YSPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQaqtLERELQALRQQESLadPSYSKEEVDSLRRKLETL 453
|
490
....*....|....*....
gi 1604784239 1388 SGTVEALEEGKKRLQRELE 1406
Cdd:pfam05557 454 ELERQRLREQKNELEMELE 472
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1486-1734 |
1.91e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 63.01 E-value: 1.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1486 ETRVLALARALEENQGALEEAEKTMKGLRADMEDLisskddvgksvhdlekakRGLEAIVDEMRTQMEELEdeLQVAEDA 1565
Cdd:COG4913 220 EPDTFEAADALVEHFDDLERAHEALEDAREQIELL------------------EPIRELAERYAAARERLA--ELEYLRA 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1566 KLRLDVNTQALRAQHERELHARDELG--EEKRKQLLKQVRELEAELEEERKQRGQASGSKKK-LEGELKDMEDQLEATSR 1642
Cdd:COG4913 280 ALRLWFAQRRLELLEAELEELRAELArlEAELERLEARLDALREELDELEAQIRGNGGDRLEqLEREIERLERELEERER 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1643 GRDEAVKQLRKIQGQVKDLQRDLEDSRAAQKEVLASARESERRskameadivqLHEMLAAVERARKQAEVERDELSEELA 1722
Cdd:COG4913 360 RRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEA----------LEEALAEAEAALRDLRRELRELEAEIA 429
|
250
....*....|..
gi 1604784239 1723 SNSSGKSLMSDE 1734
Cdd:COG4913 430 SLERRKSNIPAR 441
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
948-1293 |
2.14e-09 |
|
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: 61.62 E-value: 2.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 948 ERKEMEQQLQLMEAHIAEEEDARQKLQMEKVSVEGKVK-------KLEEDILMMEDQNNKLQKERKLLEERLADMSSNLA 1020
Cdd:pfam19220 21 DLRSLKADFSQLIEPIEAILRELPQAKSRLLELEALLAqeraaygKLRRELAGLTRRLSAAEGELEELVARLAKLEAALR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1021 EEEEKSKNLSKLKTKHESMISELELRMKKEEKGRLDMEKAKRKVEAELGDLQEQHADLQAQLAELRAQLAAKEEELQATQ 1100
Cdd:pfam19220 101 EAEAAKEELRIELRDKTAQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQ 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1101 ARLEEECNQRGAAVKRVRELEVL-------ISELQEDLEAERAARGKVEAARRD----LGEELNALRTELEDSLGTTAAQ 1169
Cdd:pfam19220 181 ALSEEQAAELAELTRRLAELETQldatrarLRALEGQLAAEQAERERAEAQLEEaveaHRAERASLRMKLEALTARAAAT 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1170 QELRAkreqEVSMLKKAMEDEGRSHEAQVQDL---RQKHSQAVEELTEQLEQAKRVRAGLEKAKQALEKESADLSADLRS 1246
Cdd:pfam19220 261 EQLLA----EARNQLRDRDEAIRAAERRLKEAsieRDTLERRLAGLEADLERRTQQFQEMQRARAELEERAEMLTKALAA 336
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1604784239 1247 LASAKQDVEHKKKKVEGQLNELNSRFnesERQRTELGERVSKLTTEL 1293
Cdd:pfam19220 337 KDAALERAEERIASLSDRIAELTKRF---EVERAALEQANRRLKEEL 380
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1195-1436 |
2.64e-09 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 62.34 E-value: 2.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1195 EAQVQDLRQKHSQAVEELTEQLEQakrVRAGLEKAKQALE--KESADLSadlrslasakqDVEHKKKKVEGQLNELNSRF 1272
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPE---LRKELEEAEAALEefRQKNGLV-----------DLSEEAKLLLQQLSELESQL 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1273 NESERQRTELGERVSKLTTELDSVTGLLNEAEGkniklSKDVSSLSSQLQDAQELLSEETRQKLNLSGRLRQTEEDRNSL 1352
Cdd:COG3206 229 AEARAELAEAEARLAALRAQLGSGPDALPELLQ-----SPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAAL 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1353 MEQLEEETEAKRA-VERQVSSLNMQLSDSKKKLDEMSGTVEALEEGK---KRLQRELEAANSDYEekaSAYDKLEKSRGR 1428
Cdd:COG3206 304 RAQLQQEAQRILAsLEAELEALQAREASLQAQLAQLEARLAELPELEaelRRLEREVEVARELYE---SLLQRLEEARLA 380
|
....*...
gi 1604784239 1429 MQQELEDV 1436
Cdd:COG3206 381 EALTVGNV 388
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1592-1786 |
2.73e-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: 61.32 E-value: 2.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1592 EEKRKQLLKQVRELEAELEEERKQRGQASGSKKKLEGELKDMEDQLEATSRGRDEAVKQLRKIQGQVKDLQRDLEDSRAA 1671
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1672 QKEVLA------------------SARESERR-------SKAMEADIVQLHEMLAAVERARKQAEVERDELSEELASNSS 1726
Cdd:COG4942 106 LAELLRalyrlgrqpplalllspeDFLDAVRRlqylkylAPARREQAEELRADLAELAALRAELEAERAELEALLAELEE 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1727 GKSLMSDEKRRLDTKISQLEEELEEEQANVESLNDRLRKSQQLVEQLGAELAAERSTSQS 1786
Cdd:COG4942 186 ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
850-1274 |
3.22e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.09 E-value: 3.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 850 QVTRQEEEMGQKDEELKAAKEVAAKVETELKDITQKHTQLMEERAQLEmKLHAETELYAEAEEMRVRLEAKKQELEEVLH 929
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLE-KLLQLLPLYQELEALEAELAELPERLEELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 930 EMEsrleeeedrsnalhnERKEMEQQLQLMEAHIAE-EEDARQKLQMEKVSVEGKVKKLEEDILMMEDQNNKLQKERKLL 1008
Cdd:COG4717 154 RLE---------------ELRELEEELEELEAELAElQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEA 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1009 EERLADMSSNLAEEEEKSKNLSKLKTKHE--------SMISELELRMKKEEKGRLDMEKAKRKVEA----ELGDLQEQHA 1076
Cdd:COG4717 219 QEELEELEEELEQLENELEAAALEERLKEarlllliaAALLALLGLGGSLLSLILTIAGVLFLVLGllalLFLLLAREKA 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1077 DLQAQLAELRAQLAAKEEELQATQARLEEECNQRGAAVKRVRELEVLISELQEDLE--AERAARGKVEAARRDLGEELNA 1154
Cdd:COG4717 299 SLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLReaEELEEELQLEELEQEIAALLAE 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1155 LRTELEDSLGTTAAQQELRAKREQEVSMLKKAMEDEGRSHEAQVQDLRQkhsqavEELTEQLEQAKRVRAGLEKAKQALE 1234
Cdd:COG4717 379 AGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDE------EELEEELEELEEELEELEEELEELR 452
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1604784239 1235 KESADLSADLRSLASaKQDVEHKKKKVEGQLNELNSRFNE 1274
Cdd:COG4717 453 EELAELEAELEQLEE-DGELAELLQELEELKAELRELAEE 491
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1226-1714 |
3.24e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.09 E-value: 3.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1226 LEKAKQALEKESADL-SADLRSLASAKQDVEHKKKKVEgQLNELNSRFNESERQRTELGERVSKLTTELDSVTGLLNEAE 1304
Cdd:COG4717 51 LEKEADELFKPQGRKpELNLKELKELEEELKEAEEKEE-EYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1305 gkniklskdvssLSSQLQDAQELLSEETRQKLNLSGRLRQTEEDRNSLMEQLEEETEAKRAVERQVSSLNM----QLSDS 1380
Cdd:COG4717 130 ------------LYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLateeELQDL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1381 KKKLDEMSGTVEALEEGKKRLQRELEAANSDYE----EKASAYDKLEKSRGRMQQELEDVLMDLDSQRQLVSNLEKKQKK 1456
Cdd:COG4717 198 AEELEELQQRLAELEEELEEAQEELEELEEELEqlenELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAG 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1457 FDQMLAeerAVSCKFAEERDRAEAEAREKETRVLALARALEENQGALEEAektmkgLRADMEDLISSKDDVGKSVHDLEK 1536
Cdd:COG4717 278 VLFLVL---GLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEEL------LAALGLPPDLSPEELLELLDRIEE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1537 AKrgleaivdEMRTQMEELEDELQVaEDAKLRLDVNTQALRAQHERELHARDELGEEkRKQLLKQVRELEAELEEERKQR 1616
Cdd:COG4717 349 LQ--------ELLREAEELEEELQL-EELEQEIAALLAEAGVEDEEELRAALEQAEE-YQELKEELEELEEQLEELLGEL 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1617 GQ--ASGSKKKLEGELKDMEDQLEATSRGRDEAVKQLRKIQGQVKDLQRDLEDSRAAQKEvlaSARESERRSKAMEADIV 1694
Cdd:COG4717 419 EEllEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQEL---EELKAELRELAEEWAAL 495
|
490 500
....*....|....*....|
gi 1604784239 1695 QLheMLAAVERARKQAEVER 1714
Cdd:COG4717 496 KL--ALELLEEAREEYREER 513
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1058-1369 |
4.87e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.85 E-value: 4.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1058 EKAKRKVEAELGDLQEQHADLQAQLAELR------------AQLAAKEEELQATQARLEEECNQRGAAVKRVRELEVLIS 1125
Cdd:COG4913 623 EEELAEAEERLEALEAELDALQERREALQrlaeyswdeidvASAEREIAELEAELERLDASSDDLAALEEQLEELEAELE 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1126 ELQEDLEAERAARGKVEAARRDLGEELNALRTELED--SLGTTAAQQELRAKREQEvsMLKKAMEDEGRSHEAQVQDLRQ 1203
Cdd:COG4913 703 ELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAaeDLARLELRALLEERFAAA--LGDAVERELRENLEERIDALRA 780
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1204 KHSQAVEELTEQLEQAKRVRAGlekakqalekESADLSADLRSLAS--------AKQDVEHKKKKVEGQLNELNSRF--- 1272
Cdd:COG4913 781 RLNRAEEELERAMRAFNREWPA----------ETADLDADLESLPEylalldrlEEDGLPEYEERFKELLNENSIEFvad 850
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1273 --NESERQRTELGERVSKLTTELDSVtgllNEAEGKNIKL------SKDVSSLSSQLQDAQELLSEETRQKLNLSGRLRQ 1344
Cdd:COG4913 851 llSKLRRAIREIKERIDPLNDSLKRI----PFGPGRYLRLearprpDPEVREFRQELRAVTSGASLFDEELSEARFAALK 926
|
330 340
....*....|....*....|....*
gi 1604784239 1345 TeedrnsLMEQLEEETEAKRAVERQ 1369
Cdd:COG4913 927 R------LIERLRSEEEESDRRWRA 945
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1213-1890 |
5.50e-09 |
|
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: 61.52 E-value: 5.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1213 TEQLEQAKRVRAGLEKAKQALEKESADLSADLRSLASAKQDVEHKKKKVEGQLNELNSRFNESERQRTELGERvSKLTTE 1292
Cdd:TIGR00618 183 LMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQ-LKKQQL 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1293 LDSVTGLLNEAEGKNIKLSKDVSSLSSQLQDAQELLSEEtrqklnlsgRLRQTEEDRNSLMEQLEEeTEAKRAVERQVSS 1372
Cdd:TIGR00618 262 LKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIK---------AVTQIEQQAQRIHTELQS-KMRSRAKLLMKRA 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1373 LNMQLSDSKKKLDEMSGTVEALEEgkkRLQRELEAANSDYEEKASAYDKLEKSRgRMQQELEDVLMDLDSQRQLVSNLEK 1452
Cdd:TIGR00618 332 AHVKQQSSIEEQRRLLQTLHSQEI---HIRDAHEVATSIREISCQQHTLTQHIH-TLQQQKTTLTQKLQSLCKELDILQR 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1453 KQKKFDQMLAEERAVSCKFAEERDRAEAEAREKETRVLALARALEENQGALEEAEKTMKGLRADMEDLISSKddvgkSVH 1532
Cdd:TIGR00618 408 EQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKE-----QIH 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1533 DLEKAKRGLEAIV----DEMRTQMEELEDELQVAEDAKLRLDVNTQAL------RAQHERELHARDELGEEKRKQ---LL 1599
Cdd:TIGR00618 483 LQETRKKAVVLARllelQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMqrgeqtYAQLETSEEDVYHQLTSERKQrasLK 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1600 KQVRELEAELEEERKQRGQASGSKKKLEGELKDMEDQLEATSRGRD----EAVKQLRKIQGQVKDLQRDLEDSRAAQKEV 1675
Cdd:TIGR00618 563 EQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDmlacEQHALLRKLQPEQDLQDVRLHLQQCSQELA 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1676 LASArESERRSKAMEADIVQLHEMLAAVERARKQAEVERDELSEElasnsSGKSLMSDEKRRLDTKISqleeeLEEEQAN 1755
Cdd:TIGR00618 643 LKLT-ALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQ-----SEKEQLTYWKEMLAQCQT-----LLRELET 711
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1756 VESLNDRLRKSQQLVEQ-LGAELAAERSTSQSregSRQQLERQNRElKAKMQEMEGQGRSKLKASIAALEAKLREAEEQL 1834
Cdd:TIGR00618 712 HIEEYDREFNEIENASSsLGSDLAAREDALNQ---SLKELMHQART-VLKARTEAHFNNNEEVTAALQTGAELSHLAAEI 787
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1604784239 1835 EIESRERQANGKNLRQKEKKLKD--------LTIQMEDERKQAQQYKDQAEKGNVRVKQLKHQL 1890
Cdd:TIGR00618 788 QFFNRLREEDTHLLKTLEAEIGQeipsdediLNLQCETLVQEEEQFLSRLEEKSATLGEITHQL 851
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1058-1285 |
5.97e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 60.23 E-value: 5.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1058 EKAKRKVEAELGDLQEQHADLQAQLAELRAQLAAKEEELQATQARLEEecnqrgaAVKRVRELEVLISELQEDLEAERAA 1137
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEA-------LQAEIDKLQAEIAEAEAEIEERREE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1138 RGKVEAARRDLGEELNALRTELE-DSLGTTAAQqelrakreqeVSMLKKAMEDEGRSHEaQVQDLRQKHSQAVEELTEQL 1216
Cdd:COG3883 88 LGERARALYRSGGSVSYLDVLLGsESFSDFLDR----------LSALSKIADADADLLE-ELKADKAELEAKKAELEAKL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1604784239 1217 EQAKRVRAGLEKAKQALEKESADLSADLRSLASAKQDVEHKKKKVEGQLNELNSRFNESERQRTELGER 1285
Cdd:COG3883 157 AELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAA 225
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1325-1915 |
7.45e-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: 60.89 E-value: 7.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1325 QELLSEETRQKLNLSGRLRQTEEDRNSLMEQLEEETEAKravERQVSSLNMQLSDSKKKLDEMSGTVEALEEGKKRLQRE 1404
Cdd:pfam05483 200 EELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDK---EKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEK 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1405 LEAANSDYEEKASAYDKLEKsrgrmqqELEDVLMDLdsQRQLVSnlekkQKKFDQMLAEERAVSCKFAEERDRAEAEARE 1484
Cdd:pfam05483 277 TKLQDENLKELIEKKDHLTK-------ELEDIKMSL--QRSMST-----QKALEEDLQIATKTICQLTEEKEAQMEELNK 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1485 KETRVLALARALEENQGALEEAektmkgLRADMEDLISSKDDVGKSVHDLEKAKRGLEAIVDEMRTQMEELEDELQVAED 1564
Cdd:pfam05483 343 AKAAHSFVVTEFEATTCSLEEL------LRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAE 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1565 AKLRLDVNTQALRAQHERElhardelGEEKRKQLLKQVRELEAELEEErkQRGQASGSKKKLEGELKDMEDQLEATSRGR 1644
Cdd:pfam05483 417 DEKLLDEKKQFEKIAEELK-------GKEQELIFLLQAREKEIHDLEI--QLTAIKTSEEHYLKEVEDLKTELEKEKLKN 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1645 DEAVKQLRKIQGQVKDLQRDLEDS----RAAQKEVLASARESERRSKAMEADIVQLHEMLAAVERARKQAEVERDELSEE 1720
Cdd:pfam05483 488 IELTAHCDKLLLENKELTQEASDMtlelKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCK 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1721 LASNSSGKSLMSDEKRRLDTKISQLEEELEEEQANVESLNDRLRKSQQLVEQLGAELAAERSTSQSREGSRQQLERQNRE 1800
Cdd:pfam05483 568 LDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELAS 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1801 LKAKMQEMEGQGRSKLKASIAALEAKLREAEE-----------QLEIESR--ERQANGKNLRQKEKKLKDLTIQMEDERK 1867
Cdd:pfam05483 648 AKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKakaiadeavklQKEIDKRcqHKIAEMVALMEKHKHQYDKIIEERDSEL 727
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 1604784239 1868 QAQQYKDQAEKG-----NVRVKQLKHQLEEAEEEAQRMAAARRKLQRELDEAT 1915
Cdd:pfam05483 728 GLYKNKEQEQSSakaalEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENT 780
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1310-1539 |
8.01e-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: 59.78 E-value: 8.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1310 LSKDVSSLSSQLQDAQELLSEETRQKLNLSGRLRQTEEDRNSLMEQLEEETEAKRAVERQVSSLNMQLSDSKKKLDEmsg 1389
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1390 tveaLEEGKKRLQRELEAANSDYEEKASAYDKLEKSRGRM----QQELEDVLMDLDSQRQLVSNLEKKQKKFDQMLAEER 1465
Cdd:COG4942 88 ----LEKEIAELRAELEAQKEELAELLRALYRLGRQPPLAlllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1604784239 1466 AVSCKFAEERDRAEAEAREKETRVLALARALEENQGALEEAEKTMKGLRADMEDLISSKDDVGKSVHDLEKAKR 1539
Cdd:COG4942 164 ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
919-1137 |
9.72e-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: 59.78 E-value: 9.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 919 AKKQELEEVLHEMESRLEEEEDRSNALHNERKEMEQQLQLMEAHIAEEEDARQKLQMEKVSVEGKVKKLEEDIlmmEDQN 998
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI---AELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 999 NKLQKERKLLEERLADM--------------SSNLAEEEEKSKNLSKLKTKHESMISELELRMKKEEKGRLDMEKAKRKV 1064
Cdd:COG4942 97 AELEAQKEELAELLRALyrlgrqpplalllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1604784239 1065 EAELGDLQEQHADLQAQLAELRAQLAAKEEELQATQARLEEecnqrgaAVKRVRELEVLISELQEDLEAERAA 1137
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAE-------LQQEAEELEALIARLEAEAAAAAER 242
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
940-1145 |
1.19e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 59.46 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 940 DRSNALHNERKEMEQQLQLMEAHIAEEEDARQKLQMEKVSVEGKVKKLEEDIlmmEDQNNKLQKERKLLEERLADM---- 1015
Cdd:COG3883 23 KELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEI---AEAEAEIEERREELGERARALyrsg 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1016 -----------SSNLAEEEEKSKNLSKLKTKHESMISELelrmkKEEKGRLdmEKAKRKVEAELGDLQEQHADLQAQLAE 1084
Cdd:COG3883 100 gsvsyldvllgSESFSDFLDRLSALSKIADADADLLEEL-----KADKAEL--EAKKAELEAKLAELEALKAELEAAKAE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1604784239 1085 LRAQLAAKEEELQATQARLEEECNQRGAAVKRVRELEVLISELQEDLEAERAARGKVEAAR 1145
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
869-1353 |
1.49e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.78 E-value: 1.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 869 KEVAAKVETELKDITQKHTQLMEERAQLEMKLHAETELYAEAEEMRVRLEAKKQELEEVlhemesrleeeEDRSNALHNE 948
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEEL-----------EAELEELREE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 949 RKEMEQQLQLMEAHIaeeedARQKLQMEKVSVEGKVKKLEEDIlmmedqnnklqKERKLLEERLADMSSNLAEEEEKSKN 1028
Cdd:COG4717 118 LEKLEKLLQLLPLYQ-----ELEALEAELAELPERLEELEERL-----------EELRELEEELEELEAELAELQEELEE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1029 LsklkTKHESMISELELRMKKEEKGRLdmEKAKRKVEAELGDLQEQHADLQAQLAELRAQLAAKEEELQATQARleeecn 1108
Cdd:COG4717 182 L----LEQLSLATEEELQDLAEELEEL--QQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEAR------ 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1109 QRGAAVKRVRELEVLISELQEDLEAERAARGKVEAARRDLGEELNALRTELEDSLGTTAAQQELRAKREQEVSMLKKAME 1188
Cdd:COG4717 250 LLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALG 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1189 DEGRSHEAQVQDLRQKHSQAVEELTEQLEQAKRVR-AGLEKAKQAL-EKESADLSADLRSLASAKQdvehKKKKVEGQLN 1266
Cdd:COG4717 330 LPPDLSPEELLELLDRIEELQELLREAEELEEELQlEELEQEIAALlAEAGVEDEEELRAALEQAE----EYQELKEELE 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1267 ELNSRFNESERQRTELGERVSK--LTTELDSVTGLLNEAEGKNIKLSKDVSSLSSQLQDA--QELLSEETRQKLNLSGRL 1342
Cdd:COG4717 406 ELEEQLEELLGELEELLEALDEeeLEEELEELEEELEELEEELEELREELAELEAELEQLeeDGELAELLQELEELKAEL 485
|
490
....*....|.
gi 1604784239 1343 RQTEEDRNSLM 1353
Cdd:COG4717 486 RELAEEWAALK 496
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1244-1662 |
1.52e-08 |
|
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: 60.35 E-value: 1.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1244 LRSLASAKQDVEHKKKkvegQLNELNSRFNESERQRTELGERVSKLTTELDSVTGLLNeaegknikLSKDVSSLSSQLQD 1323
Cdd:COG3096 284 SERALELRRELFGARR----QLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLN--------LVQTALRQQEKIER 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1324 AQELLSEetrqklnLSGRLRQTEEDRNSLMEQLEEETEAKRAVERQVSSLNMQLSDSKKKLDEMSG-------TVEALEE 1396
Cdd:COG3096 352 YQEDLEE-------LTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTraiqyqqAVQALEK 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1397 GKKRLQR-ELEAANsdyeekasAYDKLEKSRGRMQQELEDVLmdldSQRQLVSNLEKKQKKFDQMLAeerAVsCKFAEER 1475
Cdd:COG3096 425 ARALCGLpDLTPEN--------AEDYLAAFRAKEQQATEEVL----ELEQKLSVADAARRQFEKAYE---LV-CKIAGEV 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1476 DRAEAEAREKEtrVLALARALEenqgALEEAEKTMKGLRADMEDLISSKDDVGKSVHDLEKAKRGLEAIVDEMRTQMEEL 1555
Cdd:COG3096 489 ERSQAWQTARE--LLRRYRSQQ----ALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAEL 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1556 EDELQVAEDAKlrldVNTQALRAQHERELhardELGEEKRKQLLKQV---RELEAELEEERKQRGQASGSKKKLEGELKD 1632
Cdd:COG3096 563 EAQLEELEEQA----AEAVEQRSELRQQL----EQLRARIKELAARApawLAAQDALERLREQSGEALADSQEVTAAMQQ 634
|
410 420 430
....*....|....*....|....*....|
gi 1604784239 1633 MEDQLEATSRGRDEAVKQLRKIQGQVKDLQ 1662
Cdd:COG3096 635 LLEREREATVERDELAARKQALESQIERLS 664
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1071-1851 |
1.75e-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: 59.84 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1071 LQEQHADLQAQLAELRAQLAAKEEELQAT---------------QARLEEECNQRGAAVKRVR-------ELEVLISELQ 1128
Cdd:pfam10174 1 LQAQLRDLQRENELLRRELDIKESKLGSSmnsiktfwspelkkeRALRKEEAARISVLKEQYRvtqeenqHLQLTIQALQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1129 EDLEAERAARGKVEAAR---RDLGEELNALRTELEDSLGTTAAQQELRAKreqEVSMLKKAMEDEGRSHEAQVQDLRQKh 1205
Cdd:pfam10174 81 DELRAQRDLNQLLQQDFttsPVDGEDKFSTPELTEENFRRLQSEHERQAK---ELFLLRKTLEEMELRIETQKQTLGAR- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1206 SQAVEELTEQLeQAKRVRAGLEKAKQALEKESADLSADLRSLASAKQDVEHKKKKVEGQLNELNSRFNESERQRTelger 1285
Cdd:pfam10174 157 DESIKKLLEML-QSKGLPKKSGEEDWERTRRIAEAEMQLGHLEVLLDQKEKENIHLREELHRRNQLQPDPAKTKA----- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1286 vskLTTELDSVTGLLNEAEGKNIKLSKDVSSLSSQLqdaqeLLSEETRQKlnlsgRLRQTEEDRN------SLMEQLEEE 1359
Cdd:pfam10174 231 ---LQTVIEMKDTKISSLERNIRDLEDEVQMLKTNG-----LLHTEDREE-----EIKQMEVYKShskfmkNKIDQLKQE 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1360 TEAKR----AVERQVSSLNMQLSDSKKKLDEMSGTVEALEEGKKRLQRELEAANSDYEEKASAYDKLEKSRGRMQQELED 1435
Cdd:pfam10174 298 LSKKEsellALQTKLETLTNQNSDCKQHIEVLKESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKST 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1436 VLMDLDSQRQLVSNLEKK----QKKFDQMLAEERAVSCKFAEERDRAEAEAREKETRVLALArALEEnqgALEEAEKTMK 1511
Cdd:pfam10174 378 LAGEIRDLKDMLDVKERKinvlQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALT-TLEE---ALSEKERIIE 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1512 GLRadmedlisskddvgksvhdlekakrglEAIVDEMRTQMEELEDELQVAEDAKLRLDVnTQALRAQHERELHARDELG 1591
Cdd:pfam10174 454 RLK---------------------------EQREREDRERLEELESLKKENKDLKEKVSA-LQPELTEKESSLIDLKEHA 505
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1592 EEKRKQLLKQVRELEAELEEERKQRGQASgskkKLEGELKDMEdQLEATSRGRDEAVKQLRKIQgqvKDLQRDLEDSRAA 1671
Cdd:pfam10174 506 SSLASSGLKKDSKLKSLEIAVEQKKEECS----KLENQLKKAH-NAEEAVRTNPEINDRIRLLE---QEVARYKEESGKA 577
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1672 QKEV---LASARESERRSKAMEADIVQLHEMlaAVERARKQAEVERDELSEELASNSSGKSLMSDEKRRLDtkisqlEEE 1748
Cdd:pfam10174 578 QAEVerlLGILREVENEKNDKDKKIAELESL--TLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRRED------NLA 649
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1749 LEEEQANVESLNDRLRKSQQLVEQLGAELAAERSTSQSREGSRQQLERQNRELKAKMQEMEGQGR----SKLKASIAALE 1824
Cdd:pfam10174 650 DNSQQLQLEELMGALEKTRQELDATKARLSSTQQSLAEKDGHLTNLRAERRKQLEEILEMKQEALlaaiSEKDANIALLE 729
|
810 820 830
....*....|....*....|....*....|
gi 1604784239 1825 ---AKLREAEEQLEIESRERQANGKNLRQK 1851
Cdd:pfam10174 730 lssSKKKKTQEEVMALKREKDRLVHQLKQQ 759
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1078-1304 |
2.43e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 59.26 E-value: 2.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1078 LQAQLAELRAQLAAKEEELQATQAR-----LEEecnQRGAAVKRVRELEVLISELQEDLeaeRAARGKVEAARRDLGEEL 1152
Cdd:COG3206 180 LEEQLPELRKELEEAEAALEEFRQKnglvdLSE---EAKLLLQQLSELESQLAEARAEL---AEAEARLAALRAQLGSGP 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1153 NALRTELEDSlgttaAQQELRAKREQEVSMLKKAMEDEGRSHEaQVQDLRQKhsqaVEELTEQLEQ-AKRVRAGLEKAKQ 1231
Cdd:COG3206 254 DALPELLQSP-----VIQQLRAQLAELEAELAELSARYTPNHP-DVIALRAQ----IAALRAQLQQeAQRILASLEAELE 323
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1604784239 1232 ALEKESADLSADLRslasakqdvehkkkkvegQLNELNSRFNESERQRTELGERVSKLTTELDSVTGLLNEAE 1304
Cdd:COG3206 324 ALQAREASLQAQLA------------------QLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEAR 378
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1698-1933 |
3.02e-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: 57.85 E-value: 3.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1698 EMLAAVERARKQAEVERDELSEELASNSSGKSLMSDEKRRLDTKISQLEEELEEEQANVESLNDRLRKSQQLVEQLGAEL 1777
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1778 AAERSTSQSREGSRQQLERQNReLKAKMQEMEGQGRSKLKASIAALEAKLREAEEQLEIESRERQANGKNLRQKEKKLKD 1857
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQPP-LALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1858 LTIQMEDERKQAQQYKDQAEKgnvRVKQLKHQLEEAEEEAQRMAAARRKLQRELD-----EATEANDTLSRDMASLRSKL 1932
Cdd:COG4942 179 LLAELEEERAALEALKAERQK---LLARLEKELAELAAELAELQQEAEELEALIArleaeAAAAAERTPAAGFAALKGKL 255
|
.
gi 1604784239 1933 R 1933
Cdd:COG4942 256 P 256
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1343-1871 |
3.49e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.77 E-value: 3.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1343 RQTEEDRNSLMEQLEEETEAKRAVE---RQVSSLNmQLSDSKKKLDEMSGTVEALEEGKKRLQreLEAANSDYEEKASAY 1419
Cdd:COG4913 221 PDTFEAADALVEHFDDLERAHEALEdarEQIELLE-PIRELAERYAAARERLAELEYLRAALR--LWFAQRRLELLEAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1420 DKLEKSRGRMQQELEDVLMDLDSQRQLVSNLEKKQKKFDQMLAEEravsckFAEERDRAEAEAREKETRVLALARALEEN 1499
Cdd:COG4913 298 EELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQ------LEREIERLERELEERERRRARLEALLAAL 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1500 QGALEEAEKTMKGLRADMEDLissKDDVGKSVHDLEKAKRGLEAIVDEMRTQMEELEDELQVAEDAKLRLDVNTQALRAQ 1579
Cdd:COG4913 372 GLPLPASAEEFAALRAEAAAL---LEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDA 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1580 HEREL-HARDEL-----------GEEK-------------------------------RKQLLKQVRELEAELEEERKQR 1616
Cdd:COG4913 449 LAEALgLDEAELpfvgelievrpEEERwrgaiervlggfaltllvppehyaaalrwvnRLHLRGRLVYERVRTGLPDPER 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1617 GQASGSK--KKLEGELKDMEDQLEATSRGRD-----EAVKQLRK------IQGQVKDLQRDLE-DSRAAQKEVLASARES 1682
Cdd:COG4913 529 PRLDPDSlaGKLDFKPHPFRAWLEAELGRRFdyvcvDSPEELRRhpraitRAGQVKGNGTRHEkDDRRRIRSRYVLGFDN 608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1683 ERRSKAMEADIVQLHEMLAAVERARKQAEVERDELSEELASNSSGKSLMSDEK--RRLDTKISQLEEELEEEQAN---VE 1757
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIdvASAEREIAELEAELERLDASsddLA 688
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1758 SLNDRLRKSQQLVEQLGAELAAERSTSQSREGSRQQLERQNRELKAKMQEMEGQGRSklkASIAALEAKLREAEEQlEIE 1837
Cdd:COG4913 689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL---ELRALLEERFAAALGD-AVE 764
|
570 580 590
....*....|....*....|....*....|....
gi 1604784239 1838 SRERQANGKNLRQKEKKLKDLTIQMEDERKQAQQ 1871
Cdd:COG4913 765 RELRENLEERIDALRARLNRAEEELERAMRAFNR 798
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1489-1711 |
3.90e-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: 57.85 E-value: 3.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1489 VLALARALEENQGALEEAEKTMKGLRADMEDLISSKDDVGKSVHDLEKAKRGLEAIVDEMRTQMEELEDELQVAEDAKLR 1568
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1569 LDVNTQALRAQHERELHARDELGEEKRKQLLKQVRELEAELEEERKQRGQASGSKKKLEgELKDMEDQLEATSRGRDEAV 1648
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAE-ELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1604784239 1649 KQLRKIQGQVKDLQRDLEDSRAAQKEVLASARES----ERRSKAMEADIVQLHEMLAAVERARKQAE 1711
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKElaelAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
840-1734 |
3.97e-08 |
|
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: 58.81 E-value: 3.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 840 RLFTKVKPLLQVTRQEEEMGQkdeELKAAKEVAAKVETELKDiTQKHTQLMEERAQLEMKLHAETELYAEAEEMRVRLEA 919
Cdd:COG3096 307 RLVEMARELEELSARESDLEQ---DYQAASDHLNLVQTALRQ-QEKIERYQEDLEELTERLEEQEEVVEEAAEQLAEAEA 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 920 KKQELEEvlhEMESRLEEEEDRSNALHnerkemEQQ---LQLMEAHIAEEEdARQKLQMEKVSVEGKVKKLEEdilmMED 996
Cdd:COG3096 383 RLEAAEE---EVDSLKSQLADYQQALD------VQQtraIQYQQAVQALEK-ARALCGLPDLTPENAEDYLAA----FRA 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 997 QNNKLQKERKLLEERLADMSSNLAEEEEKSKNLsklktkhESMISELElRMKKEEKGRLDMEKAkrkveAELGDLQEQHA 1076
Cdd:COG3096 449 KEQQATEEVLELEQKLSVADAARRQFEKAYELV-------CKIAGEVE-RSQAWQTARELLRRY-----RSQQALAQRLQ 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1077 DLQAQLAELRaQLAAKEEELQatqaRLEEECNQRgaaVKRVRELEVLISELQEDLEAERAArgkVEAARRDLGEELNALR 1156
Cdd:COG3096 516 QLRAQLAELE-QRLRQQQNAE----RLLEEFCQR---IGQQLDAAEELEELLAELEAQLEE---LEEQAAEAVEQRSELR 584
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1157 TELEDslgTTAAQQELRAKreqevsmlkkamedEGRSHEAQvqdlrqkhsQAVEELTEQLEQAKRVRAGLEKAKQ-ALEK 1235
Cdd:COG3096 585 QQLEQ---LRARIKELAAR--------------APAWLAAQ---------DALERLREQSGEALADSQEVTAAMQqLLER 638
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1236 EsadlsadlRSLASAKQDVEHKKKKVEGQLNELnSRFNESERQR-TELGERVS-KLTTEL-DSVTglLNEA--------E 1304
Cdd:COG3096 639 E--------REATVERDELAARKQALESQIERL-SQPGGAEDPRlLALAERLGgVLLSEIyDDVT--LEDApyfsalygP 707
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1305 GKNIKLSKDVSSLSSQLQDAQELLSEetrqklnlsgrLRQTEEDRNSLMEQLEEETEAKRAVERQVSslNMQLSDSK--- 1381
Cdd:COG3096 708 ARHAIVVPDLSAVKEQLAGLEDCPED-----------LYLIEGDPDSFDDSVFDAEELEDAVVVKLS--DRQWRYSRfpe 774
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1382 ----------KKLDEMSGTVEALEE-------GKKRLQReLEAANSDY----------EEKASAYDKLEKSRGRMQQELE 1434
Cdd:COG3096 775 vplfgraareKRLEELRAERDELAEqyakasfDVQKLQR-LHQAFSQFvgghlavafaPDPEAELAALRQRRSELERELA 853
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1435 DVLMDLDSQRQLVSNLEKKQKKFDQMLAEERAvsckFAEE--RDRAEaEAREKETRVLALARALEENQGALEEAEKTMKG 1512
Cdd:COG3096 854 QHRAQEQQLRQQLDQLKEQLQLLNKLLPQANL----LADEtlADRLE-ELREELDAAQEAQAFIQQHGKALAQLEPLVAV 928
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1513 LRADMEDLISSKDDVGKSVHDLEKAKRGLEAIVDEM--RTQMEELEDELQVAEDAKLrldvnTQALRAQHERELHARDEL 1590
Cdd:COG3096 929 LQSDPEQFEQLQADYLQAKEQQRRLKQQIFALSEVVqrRPHFSYEDAVGLLGENSDL-----NEKLRARLEQAEEARREA 1003
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1591 GEEKRkQLLKQVRELEAELEEERKQRGQASGSKKKLEGELKDMEDQL----EATSRG-RDEAVKQLRKIQGQVKDLQRDL 1665
Cdd:COG3096 1004 REQLR-QAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELGVQAdaeaEERARIrRDELHEELSQNRSRRSQLEKQL 1082
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1666 EDSRAAQKEVLASARESERRSKAMEADIVQLHEMLAAVERARKQAEVERDELSEELASNSSGK-SLMSDE 1734
Cdd:COG3096 1083 TRCEAEMDSLQKRLRKAERDYKQEREQVVQAKAGWCAVLRLARDNDVERRLHRRELAYLSADElRSMSDK 1152
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1460-1810 |
4.45e-08 |
|
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: 58.53 E-value: 4.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1460 MLAEERAVSCKFAEERDRAE---AEAREKETRVLALARALEENQGALE-EAEKTMK--GLRADMEDLisSKDDVGKSVHD 1533
Cdd:TIGR02168 159 AIFEEAAGISKYKERRKETErklERTRENLDRLEDILNELERQLKSLErQAEKAERykELKAELREL--ELALLVLRLEE 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1534 LEKAKRGLEAIVDEMRTQMEELEDELQVAEdAKLrldvntqalrAQHERELHARDELGEEKRKQLLKQVRELEAELEeeR 1613
Cdd:TIGR02168 237 LREELEELQEELKEAEEELEELTAELQELE-EKL----------EELRLEVSELEEEIEELQKELYALANEISRLEQ--Q 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1614 KQRGQASgsKKKLEGELKDMEDQLEATSRGRDEAVKQLRKIQGQVKDLQRDLEDSRAAQKEVLASARESERRSKAMEADI 1693
Cdd:TIGR02168 304 KQILRER--LANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1694 VQLHEMLAAVERARKQAEVERDELSEELAS------------NSSGKSLMSDEKRRLDTKIS---QLEEELEEE----QA 1754
Cdd:TIGR02168 382 ETLRSKVAQLELQIASLNNEIERLEARLERledrrerlqqeiEELLKKLEEAELKELQAELEeleEELEELQEElerlEE 461
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1604784239 1755 NVESLNDRLRKSQQLVEQLGAELAAERSTSQSREGSRQQLERQNRELKAKMQEMEG 1810
Cdd:TIGR02168 462 ALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSG 517
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1299-1920 |
5.10e-08 |
|
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: 58.52 E-value: 5.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1299 LLNEAEGKNIKLSKDVSSLSSQLQDAQELLSEETRQKLNLSGRLRQTEEDRNSLMEqLEEETEAKRAVERQVSSLNMQLS 1378
Cdd:TIGR00606 211 YLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMK-LDNEIKALKSRKKQMEKDNSELE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1379 DSKKK-----------LDEMSG-TVEALEEGKKRLQRELEAANSDYEEKASAYDKLEKSRGRMQ---------------- 1430
Cdd:TIGR00606 290 LKMEKvfqgtdeqlndLYHNHQrTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQlqadrhqehirardsl 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1431 -------QELEDVLMDLDSQRQLVSNLEKKQKKFDQMLAEERAVSCKFAEERDRAEAEAREKETRVLALARALEENQGAL 1503
Cdd:TIGR00606 370 iqslatrLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEIL 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1504 EEAEKTMKGLRADMEDLISSKDDVGKSVHDLEKAKRGLEAIvdEMRTQMEELEDELQVAEDAKLRLDVNTQALRAQHERE 1583
Cdd:TIGR00606 450 EKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKA--EKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQL 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1584 LHARdelgeEKRKQLLKQVRELEAELEEERKQRGQASGSKKKLEGEL---KDMEDQLEATSRGRDEAVKQLRKIQGQVKD 1660
Cdd:TIGR00606 528 NHHT-----TTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFpnkKQLEDWLHSKSKEINQTRDRLAKLNKELAS 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1661 LQ------RDLEDSRAAQKEVLASARESERRSKAMEADIVQLHEMLAAVERARK-------------------------- 1708
Cdd:TIGR00606 603 LEqnknhiNNELESKEEQLSSYEDKLFDVCGSQDEESDLERLKEEIEKSSKQRAmlagatavysqfitqltdenqsccpv 682
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1709 -----QAEVERDELSEELASNS--------SGKSLMSDEKRRLDTKISQLEEELEEEQANVESLNDRLRKSQQLV----- 1770
Cdd:TIGR00606 683 cqrvfQTEAELQEFISDLQSKLrlapdklkSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNrdiqr 762
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1771 ---------EQLGAELAAERSTS--QSREGSRQQLERQNRELKAKMQEMEGQGRS-KLKASIAALEAKLREAEEQL---- 1834
Cdd:TIGR00606 763 lkndieeqeTLLGTIMPEEESAKvcLTDVTIMERFQMELKDVERKIAQQAAKLQGsDLDRTVQQVNQEKQEKQHELdtvv 842
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1835 -EIE-----SRERQANGKNLRQKEKKLKDLTIQMEDERKQAQQYKDQAEKGNVRVKQLKHQLEEAEEEAQRMAAARRKLQ 1908
Cdd:TIGR00606 843 sKIElnrklIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQ 922
|
730
....*....|..
gi 1604784239 1909 RELDEATEANDT 1920
Cdd:TIGR00606 923 QEKEELISSKET 934
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
890-1261 |
5.70e-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: 57.60 E-value: 5.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 890 MEERAQLEMKLHAETE------LYAEAEEMRVRLEAKKQELEEVLHEMESRLEEEEDRSNALHNERKEMEQQLQLMEAHI 963
Cdd:pfam07888 3 LDELVTLEEESHGEEGgtdmllVVPRAELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 964 AEeedarqkLQMEKVSVEGKVKKLEEDILMMEDQNNKLQKERKLLEERLADMSSNLAEEEEKSKNLSKLKTKHESMISEL 1043
Cdd:pfam07888 83 AE-------LKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1044 ELRMKKEEKGRLDMEKAKRKVEAELGDLQEQHADLQAQLAELRAQLAAKEEELQATQARLEEECNQRGAAVKRVRELEVL 1123
Cdd:pfam07888 156 KERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEAL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1124 ISELQEDLEAERAARGKVEAARRDLGE----------ELNALRTELEDSLGTTA----AQQELRAKREQEVSMLKKAMED 1189
Cdd:pfam07888 236 LEELRSLQERLNASERKVEGLGEELSSmaaqrdrtqaELHQARLQAAQLTLQLAdaslALREGRARWAQERETLQQSAEA 315
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1604784239 1190 EGRSHEAQVQDLRQKHSQAVEELTEQleQAKRVRAGLEK-----AKQALEKESADLSADLRSLASAKQDVEHKKKKV 1261
Cdd:pfam07888 316 DKDRIEKLSAELQRLEERLQEERMER--EKLEVELGREKdcnrvQLSESRRELQELKASLRVAQKEKEQLQAEKQEL 390
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1318-1890 |
5.71e-08 |
|
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: 58.21 E-value: 5.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1318 SSQLQDAQELLSEET----RQK-------LNLSGRLRQTEEDRNSLMEQLEEETEAKRAVERQVSSLNMQLSDSKK-KLD 1385
Cdd:pfam15921 84 SHQVKDLQRRLNESNelheKQKfylrqsvIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKClKED 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1386 EMSGTVEALEEGKKRL------QRELEAANSDYEEKASA------------YDKLEKSRGRMQQEL-------------- 1433
Cdd:pfam15921 164 MLEDSNTQIEQLRKMMlshegvLQEIRSILVDFEEASGKkiyehdsmstmhFRSLGSAISKILRELdteisylkgrifpv 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1434 EDVLMDL--DSQRQLVSNLEKKQKKFDQMLAEERAVSCKFAEERDRAEAEAREKETRvLALARALEENQGA-----LEEA 1506
Cdd:pfam15921 244 EDQLEALksESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQ-LEIIQEQARNQNSmymrqLSDL 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1507 EKTMKGLRADMEDLISSKDDvgkSVHDLEKAKRGLEAIVDEMRTQMEELEDElqvaedaKLRLDVNTQALRAqherELHA 1586
Cdd:pfam15921 323 ESTVSQLRSELREAKRMYED---KIEELEKQLVLANSELTEARTERDQFSQE-------SGNLDDQLQKLLA----DLHK 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1587 RDE---LGEEKRKQLLKQVRELEAELEEERKQRGQASGSKKKLEGELKDMEDQLE-------ATSRGRDEAVKQ------ 1650
Cdd:pfam15921 389 REKelsLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQgqmerqmAAIQGKNESLEKvsslta 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1651 --------LRKIQGQVKDLQRDLEDSRAAQKEVLASARESERRSKAMEADIVQLhemlaaveraRKQAEVERDELsEELA 1722
Cdd:pfam15921 469 qlestkemLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKL----------RSRVDLKLQEL-QHLK 537
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1723 SNssgkslmSDEKRRLDTKISQLEEELEEEQANVESLNDRLRKSQQLVEQLGaelaaerSTSQSREGSRQQLERQNRELK 1802
Cdd:pfam15921 538 NE-------GDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHG-------RTAGAMQVEKAQLEKEINDRR 603
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1803 AKMQEMEGQgRSKLKASIAALEAKLREAE-EQLEI--ESRERQANGKNLRQKEKKL--------KDLTIQMEDERKQAQQ 1871
Cdd:pfam15921 604 LELQEFKIL-KDKKDAKIRELEARVSDLElEKVKLvnAGSERLRAVKDIKQERDQLlnevktsrNELNSLSEDYEVLKRN 682
|
650
....*....|....*....
gi 1604784239 1872 YKDQAEKGNVRVKQLKHQL 1890
Cdd:pfam15921 683 FRNKSEEMETTTNKLKMQL 701
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1762-1934 |
6.33e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.02 E-value: 6.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1762 RLRKSQQLVEQLGAELAAERSTSQSREGSRQQLERQNRELKAKMQEMEGQgRSKLKASIAALEAKLREAEEQLEIESRER 1841
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELE-LEEAQAEEYELLAELARLEQDIARLEERR 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1842 QANGKNLRQKEKKLKDLTIQMEDERKQAQQYKDQAEKGNVRVKQLKHQLEEAEEEAQRMAAARRKLQRELDEATEANDTL 1921
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
|
170
....*....|...
gi 1604784239 1922 SRDMASLRSKLRH 1934
Cdd:COG1196 392 LRAAAELAAQLEE 404
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
994-1220 |
6.65e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 57.72 E-value: 6.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 994 MEDQNNKLQKERKLLEERLADMSSNLAEEEEKsknLSKLKTKHESMISELELRMkkeekgrldmekakrkVEAELGDLQE 1073
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAA---LEEFRQKNGLVDLSEEAKL----------------LLQQLSELES 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1074 QHADLQAQLAELRAQLAAKEEELQATQARLEEECNQRG--AAVKRVRELEVLISELQEDLEAE----RAARGKVEAARRD 1147
Cdd:COG3206 227 QLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPViqQLRAQLAELEAELAELSARYTPNhpdvIALRAQIAALRAQ 306
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1604784239 1148 LGEELNALRTELEDSLGTTAAQ-QELRAKREQEVSMLKKAMEDegrshEAQVQDLRQKHSQAV---EELTEQLEQAK 1220
Cdd:COG3206 307 LQQEAQRILASLEAELEALQAReASLQAQLAQLEARLAELPEL-----EAELRRLEREVEVARelyESLLQRLEEAR 378
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1239-1854 |
6.69e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 57.99 E-value: 6.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1239 DLSADLRSLASAKQDVEHKKKKVEGQLNELNSRFNESERQRTELGERVSKLTTELdsvtgllNEAEGKNIKLSKDVSSLS 1318
Cdd:PRK01156 173 DVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEY-------NNAMDDYNNLKSALNELS 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1319 SQLQDAQELLSEETRQKLNLSGRLRQTEEDRNS---LMEQLEEETEAKRAVERQVSSLNMQLSDSKKKLDEMSGTVEALE 1395
Cdd:PRK01156 246 SLEDMKNRYESEIKTAESDLSMELEKNNYYKELeerHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYH 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1396 EGKKRLQrELEAANSDYEEKASAYDKLEKSRgrmqQELEDVLMDLDSqrqLVSNLEKKQKKFDQMLAEERAVSCKFAEER 1475
Cdd:PRK01156 326 AIIKKLS-VLQKDYNDYIKKKSRYDDLNNQI----LELEGYEMDYNS---YLKSIESLKKKIEEYSKNIERMSAFISEIL 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1476 DRAEAEAREketrvlaLARALEENQGALEEAEKTMKGLRADMEDLISSKDDVGKSVHDLEK-----------AKRGLEAI 1544
Cdd:PRK01156 398 KIQEIDPDA-------IKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGqsvcpvcgttlGEEKSNHI 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1545 VDEMRTQMEELEDELQVAEDAKLRLDVNTQALRAQHE-------RELHARDELGEEKRKQLlKQVRELEAELEEERKQRG 1617
Cdd:PRK01156 471 INHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEyleseeiNKSINEYNKIESARADL-EDIKIKINELKDKHDKYE 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1618 QASGSKKKLEGELKDMEDQ-------------LEATSRGRDEAVKQLRKIQGQVKDLQRDLEDSRAAQKEVLasaRESER 1684
Cdd:PRK01156 550 EIKNRYKSLKLEDLDSKRTswlnalavislidIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSI---REIEN 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1685 RSKAMEADIVQLHEMLAAVERARKQAEverdelseELASNSSGKSLMSDEKRRLDTKISQleeeleeeqanvesLNDRLR 1764
Cdd:PRK01156 627 EANNLNNKYNEIQENKILIEKLRGKID--------NYKKQIAEIDSIIPDLKEITSRIND--------------IEDNLK 684
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1765 KSQQLVEQLGAELAAERSTSQSREGSRQQLERQNRELKAKMQEMEgqgrsKLKASIAALEaKLREAEEQLEIESRERQAN 1844
Cdd:PRK01156 685 KSRKALDDAKANRARLESTIEILRTRINELSDRINDINETLESMK-----KIKKAIGDLK-RLREAFDKSGVPAMIRKSA 758
|
650
....*....|
gi 1604784239 1845 GKNLRQKEKK 1854
Cdd:PRK01156 759 SQAMTSLTRK 768
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1240-1503 |
6.83e-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: 57.08 E-value: 6.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1240 LSADLRSLASAKQDVEHKKKKVEGQLNELNSRFNESERQRTELGERVSKLTTELDSVTGLLNEAEGKNIKLSKDVSSLSS 1319
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1320 QLQDAQELLSEetrQKLNLSGRLRQTEE-DRNSLMEQLEEETEAKRAVERqvsslnmqLSDSKKKLDEMSGTVEALEEGK 1398
Cdd:COG4942 91 EIAELRAELEA---QKEELAELLRALYRlGRQPPLALLLSPEDFLDAVRR--------LQYLKYLAPARREQAEELRADL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1399 KRLQRELEAANSDYEEKASAYDKLEKSRGRMQQELEDvlmdldsQRQLVSNLEKKQKKFDQMLAEERAVSCKFAEERDRA 1478
Cdd:COG4942 160 AELAALRAELEAERAELEALLAELEEERAALEALKAE-------RQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
250 260
....*....|....*....|....*
gi 1604784239 1479 EAEAREKETRvlALARALEENQGAL 1503
Cdd:COG4942 233 EAEAAAAAER--TPAAGFAALKGKL 255
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1040-1178 |
7.06e-08 |
|
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: 55.32 E-value: 7.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1040 ISELELRMKKEEKGRLDMEKAKRKVEAELGDLQEQHADLQAQLAELRAQLAAKEEELQATQARLEEECNQR--------- 1110
Cdd:COG1579 19 LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKeyealqkei 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1604784239 1111 GAAVKRVRELEVLISELQEDLEAERAARGKVEAARRDLGEELNALRTELEDSLGTTAAQ-QELRAKREQ 1178
Cdd:COG1579 99 ESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAElEELEAEREE 167
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1345-1803 |
7.66e-08 |
|
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: 58.04 E-value: 7.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1345 TEEDRNSLMEQLEEETEAKRAVERQVSSLNMQLSDSKKKLDEMSGTVEALEEgkkrlqrELEAANSDYEEKASAYDKLEK 1424
Cdd:COG3096 276 HANERRELSERALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQ-------DYQAASDHLNLVQTALRQQEK 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1425 SrGRMQQELEDVLMDLDSQrqlvsnlekkqkkfdQMLAEERavsckfAEERDRAEAEAREKETRVLALARALEENQGALE 1504
Cdd:COG3096 349 I-ERYQEDLEELTERLEEQ---------------EEVVEEA------AEQLAEAEARLEAAEEEVDSLKSQLADYQQALD 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1505 EAEKtmkglRAdmedlISSKddvgKSVHDLEKAKR-------GLEAIVDEMRTQMEELEDELQVAEDAKLRLDVnTQALR 1577
Cdd:COG3096 407 VQQT-----RA-----IQYQ----QAVQALEKARAlcglpdlTPENAEDYLAAFRAKEQQATEEVLELEQKLSV-ADAAR 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1578 AQHERELhardelgeekrkQLLKQVRELEAeleeerkqRGQASGSKKKLEGELKDMEDQLEatsrgrdeavkQLRKIQGQ 1657
Cdd:COG3096 472 RQFEKAY------------ELVCKIAGEVE--------RSQAWQTARELLRRYRSQQALAQ-----------RLQQLRAQ 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1658 VKDLQRDLEdsraAQKEVLASARESERRSKAMEADIVQLHEMLAaverarkQAEVERDELSEELASNSSGKSLMSDEKRR 1737
Cdd:COG3096 521 LAELEQRLR----QQQNAERLLEEFCQRIGQQLDAAEELEELLA-------ELEAQLEELEEQAAEAVEQRSELRQQLEQ 589
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1604784239 1738 LDTKISQLEEEL---EEEQANVESLND----RLRKSQQLVEQLGAELAAERSTSQSRE---GSRQQLERQNRELKA 1803
Cdd:COG3096 590 LRARIKELAARApawLAAQDALERLREqsgeALADSQEVTAAMQQLLEREREATVERDelaARKQALESQIERLSQ 665
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1163-1429 |
8.00e-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: 56.70 E-value: 8.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1163 LGTTAAQQELRAKREQEVSMLKKAMedegrsheaqvqdlrqkhsqavEELTEQLEQAKRVRAGLEKAKQALEKESADLSA 1242
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEI----------------------AELEKELAALKKEEKALLKQLAALERRIAALAR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1243 DLRSLASAKQDVEHKKKKVEGQLNELNSRFnesERQRTELGERVSKL--TTELDSVTGLLNEAEGKniKLSKDVSSLSSQ 1320
Cdd:COG4942 70 RIRALEQELAALEAELAELEKEIAELRAEL---EAQKEELAELLRALyrLGRQPPLALLLSPEDFL--DAVRRLQYLKYL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1321 LQDAQELLSEETRQKLNLSGRLRQTEEDRNSLMEQLEEETEAKRAVERQVSSLNMQLSDSKKKLDEMSGTVEALEEGKKR 1400
Cdd:COG4942 145 APARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
250 260 270
....*....|....*....|....*....|.
gi 1604784239 1401 LQRELEAANSDYEEKASAY--DKLEKSRGRM 1429
Cdd:COG4942 225 LEALIARLEAEAAAAAERTpaAGFAALKGKL 255
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
922-1236 |
9.59e-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: 57.06 E-value: 9.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 922 QELEEVLHEMESRLEEEEDRSNALHNER--KEMEQQLQLMEAH--IAEEEDARQKLQMEKVSVEGkvkklEEDILMMEDQ 997
Cdd:pfam17380 273 QLLHIVQHQKAVSERQQQEKFEKMEQERlrQEKEEKAREVERRrkLEEAEKARQAEMDRQAAIYA-----EQERMAMERE 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 998 NnklQKERKLLEERLADM----SSNLAEEEEKSKNLSKLKTKhesmiselelRMKKEEKGRLDMEKAKRKVEAElgdlQE 1073
Cdd:pfam17380 348 R---ELERIRQEERKRELerirQEEIAMEISRMRELERLQME----------RQQKNERVRQELEAARKVKILE----EE 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1074 QHADLQAQLAELRAQLAAKEEELQATQARLEEEcnqRGAAVKRVRELEV----LISELQEDLEAERAARGKVEAARRD-- 1147
Cdd:pfam17380 411 RQRKIQQQKVEMEQIRAEQEEARQREVRRLEEE---RAREMERVRLEEQerqqQVERLRQQEEERKRKKLELEKEKRDrk 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1148 LGEELN--ALRTELEDSLGTTAAQQELRAKREQEVSMLKKAMEDEGRSHEAQVQDLRQKHSQAVEELTEQLEQAKRVRAG 1225
Cdd:pfam17380 488 RAEEQRrkILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSR 567
|
330
....*....|.
gi 1604784239 1226 LEkakqALEKE 1236
Cdd:pfam17380 568 LE----AMERE 574
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1071-1276 |
1.10e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 56.95 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1071 LQEQHADLQAQLAELRAQLAAKEEELQATQARLE---EECN------QRGAAVKRVRELEVLISELQEDLeaeRAARGKV 1141
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAALEefrQKNGlvdlseEAKLLLQQLSELESQLAEARAEL---AEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1142 EAARRDLGEELNALRTELEDSlgttaAQQELRAKREQEVSMLKKAMEDEGRSH------EAQVQDLRQK----HSQAVEE 1211
Cdd:COG3206 243 AALRAQLGSGPDALPELLQSP-----VIQQLRAQLAELEAELAELSARYTPNHpdvialRAQIAALRAQlqqeAQRILAS 317
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1604784239 1212 LTEQLEQAKRVRAGLEKAKQALEKESADLSADLRSLASAKQDVEHKKKkvegQLNELNSRFNESE 1276
Cdd:COG3206 318 LEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARE----LYESLLQRLEEAR 378
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
940-1566 |
1.29e-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: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 940 DRSNALHNERKEMEQQLQLMEAHIAEEEDARQKLQmekvSVEGKVkkleedilmmeDQNNKLQKERKLLEE--------- 1010
Cdd:COG3096 448 AKEQQATEEVLELEQKLSVADAARRQFEKAYELVC----KIAGEV-----------ERSQAWQTARELLRRyrsqqalaq 512
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1011 RLADMSSNLAEEEEKSKNLSKLktkhESMISELELRMKKEEKGRLDMEKAKRKVEAELGDLQEQHADLQAQLAELRA--- 1087
Cdd:COG3096 513 RLQQLRAQLAELEQRLRQQQNA----ERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQqle 588
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1088 QLAAKEEELQAT-------QARLEEECNQRGAAVK--------------RVRELEVLISELQE-----DLEAER-AARGK 1140
Cdd:COG3096 589 QLRARIKELAARapawlaaQDALERLREQSGEALAdsqevtaamqqlleREREATVERDELAArkqalESQIERlSQPGG 668
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1141 VEAAR-----------------------------------------RDLG---EELNAL--------------------- 1155
Cdd:COG3096 669 AEDPRllalaerlggvllseiyddvtledapyfsalygparhaivvPDLSavkEQLAGLedcpedlyliegdpdsfddsv 748
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1156 --RTELEDSLGTTAAQQELRAKREQEVSMLKKAmedegrSHEAQVQDLRQKHsqavEELTEQLEQAKRVRAGLEKAKQAL 1233
Cdd:COG3096 749 fdAEELEDAVVVKLSDRQWRYSRFPEVPLFGRA------AREKRLEELRAER----DELAEQYAKASFDVQKLQRLHQAF 818
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1234 EkesaDLSADLRSLASAkQDVEHKKKKVEGQLNELNSRFNESERQRTELGERVSKLTTELDSVTGLLNEAEgknikLSKD 1313
Cdd:COG3096 819 S----QFVGGHLAVAFA-PDPEAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQAN-----LLAD 888
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1314 vSSLSSQLQDAQELLS--EETRQKLNLSGR-----------LRQTEEDRNSLMEQLEEETEAKRAVERQVSSLN--MQ-- 1376
Cdd:COG3096 889 -ETLADRLEELREELDaaQEAQAFIQQHGKalaqleplvavLQSDPEQFEQLQADYLQAKEQQRRLKQQIFALSevVQrr 967
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1377 ----LSDSKKKLDEMSGTVEALEEgkkrlqrELEAANsdyEEKASAYDKLEKSRGRMQQELEdVLMDLDSQRQL-VSNLE 1451
Cdd:COG3096 968 phfsYEDAVGLLGENSDLNEKLRA-------RLEQAE---EARREAREQLRQAQAQYSQYNQ-VLASLKSSRDAkQQTLQ 1036
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1452 KKQKKFDQM------LAEERAvsckfAEERDRAEAEAREKETRVLAL-------ARALEENQGALEEAEKTMKGLRADME 1518
Cdd:COG3096 1037 ELEQELEELgvqadaEAEERA-----RIRRDELHEELSQNRSRRSQLekqltrcEAEMDSLQKRLRKAERDYKQEREQVV 1111
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1604784239 1519 DLISSKDDVGKSV--HDLEK--AKRGL---EAivDEMR--------------TQMEELEDELQVAEDAK 1566
Cdd:COG3096 1112 QAKAGWCAVLRLArdNDVERrlHRRELaylSA--DELRsmsdkalgalrlavADNEHLRDALRLSEDPR 1178
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
864-1387 |
2.04e-07 |
|
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: 56.18 E-value: 2.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 864 ELKAAKEVAAKVETELKDITQKHTQLMEERAQLEMKLHAETELYAEAEEmrvrLEAKKQELEEVLhemesrlEEEEDRSN 943
Cdd:TIGR04523 174 ELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISE----LKKQNNQLKDNI-------EKKQQEIN 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 944 ALHNERKEMEQQLQLMEAHIAEEEDARQKLQMEKVSVEGKVKKLEEDILMMEDQNNKLQKERKllEERLADMSSNLAEEE 1023
Cdd:TIGR04523 243 EKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKE--QDWNKELKSELKNQE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1024 EKSKNLSKLKTKHESMISELELRMKKEEKGRLDMEKAKRKVEAELGDLQEQHADLQAQLAELRAQLAAKEEELQATQARL 1103
Cdd:TIGR04523 321 KKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKI 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1104 EEECNQRGAAVKRVRELEVLISELQEDLEAERAARGKVEAARRDLGEELNALRTELEdSLGTTAAQQelrakrEQEVSML 1183
Cdd:TIGR04523 401 QNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIK-NLDNTRESL------ETQLKVL 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1184 KKAMEDEGRSHEAQVQDLRQKHSQaVEELTEQleqakrvraglekaKQALEKESADLSADLRSLASAKQDVEHKKKKVEG 1263
Cdd:TIGR04523 474 SRSINKIKQNLEQKQKELKSKEKE-LKKLNEE--------------KKELEEKVKDLTKKISSLKEKIEKLESEKKEKES 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1264 QLNELNSRFNE--SERQRTELGERVSKLTTELDSVTGLLNEAEGKNIKLSKDVSSLSSQLQDAQELLSEETRQKLNLSGR 1341
Cdd:TIGR04523 539 KISDLEDELNKddFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKE 618
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1604784239 1342 LRQTEEDRNSLMEQLEEETEAKRAVERQVSSLNMQLSDSKKKLDEM 1387
Cdd:TIGR04523 619 LEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEI 664
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
806-1306 |
2.31e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.08 E-value: 2.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 806 ARKAFSKRQQQLTAMKVIQRNCACYLKLKNWQwwRLFTKVKPLLQVTRQEEEMGQKDEELKAAKEVAAKVETELKDITQK 885
Cdd:COG4913 240 AHEALEDAREQIELLEPIRELAERYAAARERL--AELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEAR 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 886 HTQLMEERAQLEMKLHA-----ETELYAEAEEMRVRLEAKKQELEEVLHEMESRLEEEEDRSNALHNERKEMEQQLQLME 960
Cdd:COG4913 318 LDALREELDELEAQIRGnggdrLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALE 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 961 AHIAEEEDARQKLQMEKVSVEGKVKKLEEDILMMEDQNN----KLQKERKLLEERLADMSSNL---------AEEEEKSK 1027
Cdd:COG4913 398 EELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSnipaRLLALRDALAEALGLDEAELpfvgelievRPEEERWR 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1028 N-----LSKLKT------KHESMISELELRMKKeeKGRLDMEKAKRKVEAELGdLQEQHADLQAQL--------AELRAQ 1088
Cdd:COG4913 478 GaiervLGGFALtllvppEHYAAALRWVNRLHL--RGRLVYERVRTGLPDPER-PRLDPDSLAGKLdfkphpfrAWLEAE 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1089 LAAK--------EEELQATQARLEEEC---NQRGAAVK----RVRELEVLISELQEDLEAERAARGKVEAARRDLGEELN 1153
Cdd:COG4913 555 LGRRfdyvcvdsPEELRRHPRAITRAGqvkGNGTRHEKddrrRIRSRYVLGFDNRAKLAALEAELAELEEELAEAEERLE 634
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1154 ALRTELEDSLGTTAAQQELRAKREQEVSMlkKAMEDEGRSHEAQVQDLRqKHSQAVEELTEQLEQAKRVRAGLEKAKQAL 1233
Cdd:COG4913 635 ALEAELDALQERREALQRLAEYSWDEIDV--ASAEREIAELEAELERLD-ASSDDLAALEEQLEELEAELEELEEELDEL 711
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1234 EKESADLSADlrsLASAKQDVEHKKKKVE--GQLNELNSRFNESERQRTELGERVSK-----LTTELDSVTGLLNEAEGK 1306
Cdd:COG4913 712 KGEIGRLEKE---LEQAEEELDELQDRLEaaEDLARLELRALLEERFAAALGDAVERelrenLEERIDALRARLNRAEEE 788
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1341-1543 |
2.41e-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: 55.16 E-value: 2.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1341 RLRQTEEDRNSLMEQLEEETEAKRAVERQVSSLNMQLSDSKKKLDEMSGTVEALEEGKKRLQRELEAANSDYEEKASAYD 1420
Cdd:COG4942 28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1421 KLEKSRGRM-QQELEDVLMDLDSQRQLVSNLE--KKQKKFDQMLAEE-RAVSCKFAEERDRAEAEAREKETRVLALARAL 1496
Cdd:COG4942 108 ELLRALYRLgRQPPLALLLSPEDFLDAVRRLQylKYLAPARREQAEElRADLAELAALRAELEAERAELEALLAELEEER 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1604784239 1497 EENQGALEEAEKTMKGLRADMEDLISSKDDVGKSVHDLEKAKRGLEA 1543
Cdd:COG4942 188 AALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEA 234
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
849-1150 |
2.46e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.84 E-value: 2.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 849 LQVTRQEEEMGQKDEELKAAKEVAAKVETELKditqKHTQLMEERAQLEMKLHAETELYAEAEEmrvRLEAKKQELEEV- 927
Cdd:PRK03918 459 AELKRIEKELKEIEEKERKLRKELRELEKVLK----KESELIKLKELAEQLKELEEKLKKYNLE---ELEKKAEEYEKLk 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 928 -----LHEMESRLEEEEDRSNALHNERKEMEQQLQLMEAHIAEEEDARQKLQMEKV-SVEGKVKKLEEdilmMEDQNNKL 1001
Cdd:PRK03918 532 eklikLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVeELEERLKELEP----FYNEYLEL 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1002 QKERKLLEERLADMSSNLAEEEEKSKNLSKLKTKHEsmiselELRMKKEEKGRLDMEKAKRKVEAELGDLQEQHADLQAQ 1081
Cdd:PRK03918 608 KDAEKELEREEKELKKLEEELDKAFEELAETEKRLE------ELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAE 681
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1604784239 1082 LAELRAQLaakeEELQATQARLEEECNQRGAAVKRVRELEVLISELQEdlEAERAARGKVEAARRDLGE 1150
Cdd:PRK03918 682 LEELEKRR----EEIKKTLEKLKEELEEREKAKKELEKLEKALERVEE--LREKVKKYKALLKERALSK 744
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1228-1436 |
2.52e-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: 55.16 E-value: 2.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1228 KAKQALEKESADLSADLRSLASAKQDVEHKKKKVEGQLNELNSRFNESERQRTELGERVSKLTTELDSVTGLLNEAEGKN 1307
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1308 IKLSKDVSSLSSQLQDAQE-------LLSEETRQKLNLSGRLRQTEEDRNSLMEQLEEETEakrAVERQVSSLNMQLSDS 1380
Cdd:COG4942 100 EAQKEELAELLRALYRLGRqpplallLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA---ELAALRAELEAERAEL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1604784239 1381 KKKLDEMSGTVEALEEGKKRLQRELEAANSDYEEKASAYDKLEKSRGRMQQELEDV 1436
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1150-1444 |
2.53e-07 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 55.96 E-value: 2.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1150 EELNALRTELEDSLGTTAAQQELRAKREQEVSMLKKAMEDEGRSHEAQvQDLRQKHSQAVEELTEQLEQAKRVRAGLEKA 1229
Cdd:PRK10246 191 EQHKSARTELEKLQAQASGVALLTPEQVQSLTASLQVLTDEEKQLLTA-QQQQQQSLNWLTRLDELQQEASRRQQALQQA 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1230 KQALEKESADLSA--------DLRSLASAKQDVEHKKKKVEGQLNELNSRFNESERQRTEL----GERVSKLTTELDSVT 1297
Cdd:PRK10246 270 LAAEEKAQPQLAAlslaqparQLRPHWERIQEQSAALAHTRQQIEEVNTRLQSTMALRARIrhhaAKQSAELQAQQQSLN 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1298 GLLNEAEGKNI---------KLSKDVSSLSSQLQDAQELLSEETRQKLNL-SGRLRQTEEDRNSLMEQLEEEteakRAVE 1367
Cdd:PRK10246 350 TWLAEHDRFRQwnnelagwrAQFSQQTSDREQLRQWQQQLTHAEQKLNALpAITLTLTADEVAAALAQHAEQ----RPLR 425
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1604784239 1368 RQVSSLNMQLSDSKKKLDEMSGTVEALEEGKKRLQRELEAANSDYEEKASAYDKLeksrgRMQQELEDVLMDLDSQR 1444
Cdd:PRK10246 426 QRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQLADV-----KTICEQEARIKDLEAQR 497
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
838-1230 |
2.84e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.84 E-value: 2.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 838 WWRLFTKVKPLLQVTRQ------EEEMGQKDEELKAAKEVAAKVETELKDITQKHTQLMEERAQL--------------- 896
Cdd:PRK03918 360 RHELYEEAKAKKEELERlkkrltGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELkkaieelkkakgkcp 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 897 ----EMKLHAETELYAEAEEMRVRLEAKKQELEEVLHEMESRLEEEEdrsNALHNER-----KEMEQQLQLMEAHIAE-- 965
Cdd:PRK03918 440 vcgrELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELE---KVLKKESeliklKELAEQLKELEEKLKKyn 516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 966 ----EEDAR--QKLQMEKVSVEGKVKKLEEDIlmmeDQNNKLQKERKLLEERLADMssnlaeEEEKSKNLSKLKTKHESM 1039
Cdd:PRK03918 517 leelEKKAEeyEKLKEKLIKLKGEIKSLKKEL----EKLEELKKKLAELEKKLDEL------EEELAELLKELEELGFES 586
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1040 ISELELRMKKEEKGRLDMEKAKrKVEAELGDLQEQHADLQAQLAELRAQLAAKEEELQATQARLEEEcnQRGAAVKRVRE 1119
Cdd:PRK03918 587 VEELEERLKELEPFYNEYLELK-DAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEEL--EKKYSEEEYEE 663
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1120 LEVLISELQEDLEAERAARgkveaarrdlgEELNALRTELEDSLGTTAAQQELRAKREQEVSMLKKAMEDegrsheaqVQ 1199
Cdd:PRK03918 664 LREEYLELSRELAGLRAEL-----------EELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALER--------VE 724
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1200 DLRQK-------------------HSQAVEELTEQLEQAKRVRAGLEKAK 1230
Cdd:PRK03918 725 ELREKvkkykallkeralskvgeiASEIFEELTEGKYSGVRVKAEENKVK 774
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1040-1216 |
3.27e-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: 53.39 E-value: 3.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1040 ISELELRMKKEEKGRLDMEKAKRKVEAELGDLQEQHADLQAQLAELRAQLAAKEEELQATQARLEEEcNQRGAAVKRVRE 1119
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY-EEQLGNVRNNKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1120 LEVLISELqedlEAERAARGKVEAARRDLGEELNALRTELEdslgttaAQQELRAKREQEVSMLKKAMEDEGRSHEAQVQ 1199
Cdd:COG1579 91 YEALQKEI----ESLKRRISDLEDEILELMERIEELEEELA-------ELEAELAELEAELEEKKAELDEELAELEAELE 159
|
170
....*....|....*..
gi 1604784239 1200 DLRQKHSQAVEELTEQL 1216
Cdd:COG1579 160 ELEAEREELAAKIPPEL 176
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1239-1801 |
5.78e-07 |
|
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: 54.64 E-value: 5.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1239 DLSADLRSLASAKQDVEHKKKKVEGQLNELNSRFNESERQRTELGERVSKLTTELDSVTGLLNEAEGKNIKLSKDVSSLS 1318
Cdd:TIGR04523 100 KLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLE 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1319 SQLQDAQELLSEETRQKLNLSGRL---RQTEEDRNSLMEQLEEETEAKRAVERQVSSLNMQLSDSKKKLDEMSGTVEALE 1395
Cdd:TIGR04523 180 KEKLNIQKNIDKIKNKLLKLELLLsnlKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLK 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1396 EGKKRLQRELEAANSDYEEKASAYDKLEKSrgrmQQELEDVLMDLDSQRQ------LVSNLEKKQKKFDQM---LAEERA 1466
Cdd:TIGR04523 260 DEQNKIKKQLSEKQKELEQNNKKIKELEKQ----LNQLKSEISDLNNQKEqdwnkeLKSELKNQEKKLEEIqnqISQNNK 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1467 VSCKFAEERDRAEAEAREKETRVLALARALEENQGALEeaektmkglradmeDLISSKDDVGKSVHDLEKAKRGLEAIVD 1546
Cdd:TIGR04523 336 IISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIE--------------KLKKENQSYKQEIKNLESQINDLESKIQ 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1547 EMRTQMEELEDELQVAEDAKLRLDVNTQALRAQHERELHARDELgEEKRKQLLKQVRELEAELEEERKQrgqasgsKKKL 1626
Cdd:TIGR04523 402 NQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDL-TNQDSVKELIIKNLDNTRESLETQ-------LKVL 473
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1627 EGELKDMEDQLEATSRGRDEAVKQLRKIQGQVKDLQRDLEDSRAAQKEVLASARESERRSKAMEADIVQLhemlaavera 1706
Cdd:TIGR04523 474 SRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDL---------- 543
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1707 rkqaEVERDELSEELAsnssgKSLMSDEKRRLDTKISQLEEELEEEQANVESLNDRLRKSQQLVEQLGAELAAERSTSQS 1786
Cdd:TIGR04523 544 ----EDELNKDDFELK-----KENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISS 614
|
570
....*....|....*
gi 1604784239 1787 REGSRQQLERQNREL 1801
Cdd:TIGR04523 615 LEKELEKAKKENEKL 629
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
850-1080 |
6.95e-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: 54.36 E-value: 6.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 850 QVTRQEEEMGQKDEELKAAKEVAAKVETELKDITQKHTQLMEERAQLEmklhAETElYAEAEEMRVRLEAKKQELEEVlh 929
Cdd:pfam17380 379 ELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIR----AEQE-EARQREVRRLEEERAREMERV-- 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 930 emesrleeeedrsnalhnERKEMEQQLQLMEAHIAEEEDARQKLQMEKVSVEGK-VKKLEEDILMMEDQNNKL-----QK 1003
Cdd:pfam17380 452 ------------------RLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKrAEEQRRKILEKELEERKQamieeER 513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1004 ERKLLEERLADMSSNLAEEEEKSKNLSKLKTKHE----SMISElELRMKKEEKGRLDMEKAKRKVEAELGDLQEQHADLQ 1079
Cdd:pfam17380 514 KRKLLEKEMEERQKAIYEEERRREAEEERRKQQEmeerRRIQE-QMRKATEERSRLEAMEREREMMRQIVESEKARAEYE 592
|
.
gi 1604784239 1080 A 1080
Cdd:pfam17380 593 A 593
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1447-1845 |
6.97e-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: 54.57 E-value: 6.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1447 VSNLEKKQKKFDQMLAEERAVSC---KFAEERDRAEAEAREKETRVlALARALE-ENQGALEEAEKTMKGLRADmEDLIS 1522
Cdd:COG3096 274 MRHANERRELSERALELRRELFGarrQLAEEQYRLVEMARELEELS-ARESDLEqDYQAASDHLNLVQTALRQQ-EKIER 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1523 SKDDVGKSVHDLEKAkrglEAIVDEMRTQMEELEDELQVAED----AKLRLDVNTQALRAQHERELHARDELGEEKRKQL 1598
Cdd:COG3096 352 YQEDLEELTERLEEQ----EEVVEEAAEQLAEAEARLEAAEEevdsLKSQLADYQQALDVQQTRAIQYQQAVQALEKARA 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1599 LKQVRELEAELEEERKQRGQASgsKKKLEGELKDMEDQL---EATSRGRDEAVKQLRKIQGQVkdlqrdlEDSRAAQ--K 1673
Cdd:COG3096 428 LCGLPDLTPENAEDYLAAFRAK--EQQATEEVLELEQKLsvaDAARRQFEKAYELVCKIAGEV-------ERSQAWQtaR 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1674 EVLASARESERRSKAMEADIVQLHEmlaAVERARKQAEVER--DELSEELASNSSGKSLMSDEKRRLDTKISQLEEELEE 1751
Cdd:COG3096 499 ELLRRYRSQQALAQRLQQLRAQLAE---LEQRLRQQQNAERllEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAE 575
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1752 EQANVESLNDRLRKSQQLVEQLGAE----LAAERSTSQSREGSRQQLErQNRELKAKMQEMEGQGRsklkaSIAALEAKL 1827
Cdd:COG3096 576 AVEQRSELRQQLEQLRARIKELAARapawLAAQDALERLREQSGEALA-DSQEVTAAMQQLLERER-----EATVERDEL 649
|
410
....*....|....*...
gi 1604784239 1828 REAEEQLEIESRERQANG 1845
Cdd:COG3096 650 AARKQALESQIERLSQPG 667
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
878-1493 |
7.04e-07 |
|
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: 54.44 E-value: 7.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 878 ELKDITQKHTQLMEERAQLEMKLhaeteLYAEAEEMRVRLEAKKQELEevlhemesrleeEEDRSNalhNERKEMEQQLQ 957
Cdd:pfam10174 112 ELTEENFRRLQSEHERQAKELFL-----LRKTLEEMELRIETQKQTLG------------ARDESI---KKLLEMLQSKG 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 958 LMEAHIAEEEDARQKLqmekVSVEGKVKKLEediLMMEDQNNKLQKERKLLEERladmsSNLAEEEEKSKNLSKLKTKHE 1037
Cdd:pfam10174 172 LPKKSGEEDWERTRRI----AEAEMQLGHLE---VLLDQKEKENIHLREELHRR-----NQLQPDPAKTKALQTVIEMKD 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1038 SMISELElRMKKEEKGRLDMEKA-------KRKVEAELGDLQEQHAD-LQAQLAELRAQLAAKEEELQATQARLEEECNQ 1109
Cdd:pfam10174 240 TKISSLE-RNIRDLEDEVQMLKTngllhteDREEEIKQMEVYKSHSKfMKNKIDQLKQELSKKESELLALQTKLETLTNQ 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1110 RG--------------AAVKRVRELEVLISELQEDLEAERAARGKVEAARRDLGEELNALRTELEDslgttaAQQELRAK 1175
Cdd:pfam10174 319 NSdckqhievlkesltAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRD------LKDMLDVK 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1176 rEQEVSMLKKAME---DEGRSHEAQVQDLRQK----------HSQAVEELTEQLEQAKRVRAGLEKAKQALEKESADLSA 1242
Cdd:pfam10174 393 -ERKINVLQKKIEnlqEQLRDKDKQLAGLKERvkslqtdssnTDTALTTLEEALSEKERIIERLKEQREREDRERLEELE 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1243 DLRSlasakqdvehKKKKVEGQLNELNSRFNESERQRTELGERVSKLTTELDSVTGLLNEAEGKNIKLSKDVSSLSSQLQ 1322
Cdd:pfam10174 472 SLKK----------ENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLK 541
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1323 DAQElLSEETRQKLNLSGRLRQTEEDRNSlmeQLEEETEAKRAVERQVSSL---NMQLSDSKKKLDEMSGTveALEEGKK 1399
Cdd:pfam10174 542 KAHN-AEEAVRTNPEINDRIRLLEQEVAR---YKEESGKAQAEVERLLGILrevENEKNDKDKKIAELESL--TLRQMKE 615
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1400 RLQRELEAANSDYEEKASAYDKLEKSRGR--------MQQELEDVLMDLDSQRQLVSNLEKKQKKFDQMLAEERAVSCKF 1471
Cdd:pfam10174 616 QNKKVANIKHGQQEMKKKGAQLLEEARRRednladnsQQLQLEELMGALEKTRQELDATKARLSSTQQSLAEKDGHLTNL 695
|
650 660
....*....|....*....|..
gi 1604784239 1472 AEERDRAEAEAREKETRVLALA 1493
Cdd:pfam10174 696 RAERRKQLEEILEMKQEALLAA 717
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1276-1462 |
7.25e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 54.25 E-value: 7.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1276 ERQRTELGERVSKLTTELDSVTGLLNEAEGK--NIKLSKDVSSLSSQLQDAQELLSEETRQKLNLSGRLRQTEEDRNSLM 1353
Cdd:COG3206 167 ELRREEARKALEFLEEQLPELRKELEEAEAAleEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALR 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1354 EQLEEETEAKRAVER--QVSSLNMQLSDSKKKLDEMSGTV---------------EALEEGKKRLQRELEAANSDYEEKA 1416
Cdd:COG3206 247 AQLGSGPDALPELLQspVIQQLRAQLAELEAELAELSARYtpnhpdvialraqiaALRAQLQQEAQRILASLEAELEALQ 326
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1604784239 1417 SAYDKLEKSRGRMQQELEDVLMDLDSQRQLVSNLEKKQKKFDQMLA 1462
Cdd:COG3206 327 AREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQ 372
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1155-1578 |
7.79e-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: 54.13 E-value: 7.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1155 LRTELEDSLGTTAAQQELRAKREQEVSMLKKAMEDEGRSHEAQVQDLRQKhsqaVEELTEQLEQAKRVRAGLEKAKQALE 1234
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESR----VAELKEELRQSREKHEELEEKYKELS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1235 KESADLSADLRSLASAKQDVEHKKKKVEGQLNELNSRFNESERQRTELGERVSKLTTELDSVTGLLNEAEGKNIKLSKDV 1314
Cdd:pfam07888 108 ASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEEL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1315 SSLSSQLQDAQELLSEETRQKLNLSGRLRQTEEDRNSlMEQLEEETEAKRAverQVSSLNMQLSDSKKKLDEMSGTVEAL 1394
Cdd:pfam07888 188 RSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTT-AHRKEAENEALLE---ELRSLQERLNASERKVEGLGEELSSM 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1395 EEGKKRLQRELEAANSDYEEK----ASAYDKLEKSRGRMQQELEDVLMDLDSQRQLVSNLEKKQKKFDQMLAEERAvsck 1470
Cdd:pfam07888 264 AAQRDRTQAELHQARLQAAQLtlqlADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERM---- 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1471 faeERDRAEAEareketrvlaLARALEENQGALEEAEKTMKGLRAdmedlisskddvgkSVHDLEKAKRGLEAIVDEMRT 1550
Cdd:pfam07888 340 ---EREKLEVE----------LGREKDCNRVQLSESRRELQELKA--------------SLRVAQKEKEQLQAEKQELLE 392
|
410 420
....*....|....*....|....*...
gi 1604784239 1551 QMEELEDELQVAEDAKLRLDVNTQALRA 1578
Cdd:pfam07888 393 YIRQLEQRLETVADAKWSEAALTSTERP 420
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1127-1366 |
7.83e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 54.25 E-value: 7.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1127 LQEDLEAERAArgkVEAARRDLGEELNALRTELEdslgttAAQQELRAKREQEVSMlkkAMEDEGRSHEAQVQDLRQKHS 1206
Cdd:COG3206 162 LEQNLELRREE---ARKALEFLEEQLPELRKELE------EAEAALEEFRQKNGLV---DLSEEAKLLLQQLSELESQLA 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1207 QAveelTEQLEQAKRVRAGLEKAKQALEKESADLSADlrslaSAKQDVEHKKKKVEGQLNELNSRFNESERQRTELGERV 1286
Cdd:COG3206 230 EA----RAELAEAEARLAALRAQLGSGPDALPELLQS-----PVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQI 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1287 SKLTTELDSvtgllnEAEGKNIKLSKDVSSLSSQLQDAQELLSEETRQKLNLSGRLRQteedrnslMEQLEEETEAKRAV 1366
Cdd:COG3206 301 AALRAQLQQ------EAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAE--------LRRLEREVEVAREL 366
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1478-1702 |
9.60e-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: 53.23 E-value: 9.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1478 AEAEAREKETRVLALARALEENQGALEEAEKTMKGLRADMEDLISSKDDVGKSVHDLEKAKRGLEAIVDEMRTQMEELED 1557
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1558 ELQVAEDAKLRLDVNTQALRAQHERE--LHARDELGEEKRKQLLKQV-RELEAELEEERKQRGQASGSKKKLEGELKDME 1634
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRQPPLAllLSPEDFLDAVRRLQYLKYLaPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1604784239 1635 DQLEATSRGRDEAVKQLRKIQGQVKDLQRDLEDSRAAQKEVLASARESERRSKAMEADIVQLHEMLAA 1702
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
855-1415 |
1.17e-06 |
|
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: 53.57 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 855 EEEMGQKDEELKAAKEVAAKVETELKDITQKHTQLMEERAQLEMKLHAETELYAEAEEMRVRLeakKQELEEVLHEMESR 934
Cdd:pfam05483 232 KKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHL---TKELEDIKMSLQRS 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 935 LEEEEDRSNALHNERKEMEQQLQLMEAHIAEEEDARQKLQMEKVSVEGKVKKLEEDILMMEDQNNKLQKERKLLEERLAD 1014
Cdd:pfam05483 309 MSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQK 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1015 MSSNLAEeeeksknLSKLKTKHESMISELELRMKKEEKgRLDMEKAKRKVEAElgdlqeqhadLQAQLAELRAQLAAKEE 1094
Cdd:pfam05483 389 KSSELEE-------MTKFKNNKEVELEELKKILAEDEK-LLDEKKQFEKIAEE----------LKGKEQELIFLLQAREK 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1095 ELQATQARLEEECNQRGAAVKRVRELEVliselqeDLEAERAARGKVEAARRDLGEELNALRTELED-SLGTTAAQQELR 1173
Cdd:pfam05483 451 EIHDLEIQLTAIKTSEEHYLKEVEDLKT-------ELEKEKLKNIELTAHCDKLLLENKELTQEASDmTLELKKHQEDII 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1174 AKREQEVSMLKK--AMEDEGRSHEAQVQDLRQKHSQAVEELTEQLEQAKRVRAGLEKAKQALEKESADLSADLRSLasaK 1251
Cdd:pfam05483 524 NCKKQEERMLKQieNLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNL---K 600
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1252 QDVEHKKKKVEGQLNE---LNSRFNESERQRTELGERVSKLTTELDSVT---GLLNEAEGKNIKLSK-DVSSLSSQLQDA 1324
Cdd:pfam05483 601 KQIENKNKNIEELHQEnkaLKKKGSAENKQLNAYEIKVNKLELELASAKqkfEEIIDNYQKEIEDKKiSEEKLLEEVEKA 680
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1325 QELLSEETRQKLNLSGRLRQTEEDRNSLME-------QLEEETEAK----RAVERQVSS----LNMQLSDSKKKLDEMSG 1389
Cdd:pfam05483 681 KAIADEAVKLQKEIDKRCQHKIAEMVALMEkhkhqydKIIEERDSElglyKNKEQEQSSakaaLEIELSNIKAELLSLKK 760
|
570 580
....*....|....*....|....*.
gi 1604784239 1390 TVEALEEGKKRLQRELEAANSDYEEK 1415
Cdd:pfam05483 761 QLEIEKEEKEKLKMEAKENTAILKDK 786
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1431-1935 |
1.53e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.38 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1431 QELEDVLMDLDSQRQLVSNLEKKQKkfdqMLAEERAVSCKFAEERDRAEA-EAREKETRVLALARALEENQGALEEAEKT 1509
Cdd:COG4913 228 DALVEHFDDLERAHEALEDAREQIE----LLEPIRELAERYAAARERLAElEYLRAALRLWFAQRRLELLEAELEELRAE 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1510 MKGLRADMEDLISSKDDVGKSVHDLEKAKRGLE-AIVDEMRTQMEELEDELQVAEDAKLRLDvntQALRAQHERELHARD 1588
Cdd:COG4913 304 LARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLE---ALLAALGLPLPASAE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1589 ELgEEKRKQLLKQVRELEAELEEERKQRGQASGSKKKLEGELKDMEDQLEATSRGR---DEAVKQLRK-IQGQVKDLQRD 1664
Cdd:COG4913 381 EF-AALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKsniPARLLALRDaLAEALGLDEAE 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1665 L-----------EDSR---AAQKeVLASAR-----ESERRSKAMEAdIVQLH-------EMLAAVERARKQAEVERDELS 1718
Cdd:COG4913 460 LpfvgelievrpEEERwrgAIER-VLGGFAltllvPPEHYAAALRW-VNRLHlrgrlvyERVRTGLPDPERPRLDPDSLA 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1719 EELASNSSG-----KSLMS-----------DEKRRLDTKIS---QLEEELEEEQANVESLNDR--------LRKSQQLVE 1771
Cdd:COG4913 538 GKLDFKPHPfrawlEAELGrrfdyvcvdspEELRRHPRAITragQVKGNGTRHEKDDRRRIRSryvlgfdnRAKLAALEA 617
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1772 QLgAELAAERSTSQSREGSRQQLERQNRELKAKMQEMEGQGRSK-----LKASIAALEAK----------LREAEEQLEI 1836
Cdd:COG4913 618 EL-AELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEidvasAEREIAELEAElerldassddLAALEEQLEE 696
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1837 ESRERQANGKNLRQKEKKLKDLTIQMEDERKQAQQYKDQAEKGNVRVKQLKHQLEEAEEEAQRMAAARRKLQRELDEATE 1916
Cdd:COG4913 697 LEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERID 776
|
570 580
....*....|....*....|
gi 1604784239 1917 ANDT-LSRDMASLRSKLRHY 1935
Cdd:COG4913 777 ALRArLNRAEEELERAMRAF 796
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
850-1160 |
1.84e-06 |
|
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: 53.10 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 850 QVTRQEEEMGQKDEELKAAKEVAAKVETELKDITQKHTQLMEERAQLEMKLHAETELYAEAEEMRVRLEAKKQELEEVLH 929
Cdd:TIGR04523 350 ELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIE 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 930 EMESRLEEEEDRSNALHNERKEMEQQLQLMEAHIAEEEDARQKLQMEKVSVEGKVKKLEEDILMMEDQNNKLQKERKLLE 1009
Cdd:TIGR04523 430 RLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELE 509
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1010 ERLADMSSNLAEEEEKSKNLSKLKTKHESMISELElrmkkEEKGRLDMEKAKRKVEAELGDLQEQhadlQAQLAELRAQL 1089
Cdd:TIGR04523 510 EKVKDLTKKISSLKEKIEKLESEKKEKESKISDLE-----DELNKDDFELKKENLEKEIDEKNKE----IEELKQTQKSL 580
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1604784239 1090 AAKEEELQATQARLEEEcnqRGAAVKRVRELEVLISELQEDLEAERAARGKVEAARRDLGEELNALRTELE 1160
Cdd:TIGR04523 581 KKKQEEKQELIDQKEKE---KKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVK 648
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1446-1916 |
2.33e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.46 E-value: 2.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1446 LVSNLEKKQKKFDQMLAEERAVSCKFAEERDRAEAEAREKETRVLALARALEENQGALEEAEKTMKGLRADMEDLisskd 1525
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL----- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1526 DVGKSVHDLEKAKRGLEAIVDEMRTQMEELEDELQVAEDAKLRLDvntqALRAQHERELHARDELGEEKRKQLLKQVREL 1605
Cdd:COG4717 122 EKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELE----ELEAELAELQEELEELLEQLSLATEEELQDL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1606 EAELEEERKQRGQASGSKKKLEGELKDMEDQLEATSRG--RDEAVKQLRKIQGQVKdlqrdLEDSRAAQKEVLASARESE 1683
Cdd:COG4717 198 AEELEELQQRLAELEEELEEAQEELEELEEELEQLENEleAAALEERLKEARLLLL-----IAAALLALLGLGGSLLSLI 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1684 RRSKAMEADIVQLHEMLAAV-ERARKQAEVERDELSEELASNSSGKSLMSDEKRRLDTKISQLEEELEEEQANVESLNDR 1762
Cdd:COG4717 273 LTIAGVLFLVLGLLALLFLLlAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQEL 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1763 LRKSQQLVEQLGAELAAERSTS-------QSREGSRQQLE--RQNRELKAKMQEMEGQGRSKLKASIAALEA----KLRE 1829
Cdd:COG4717 353 LREAEELEEELQLEELEQEIAAllaeagvEDEEELRAALEqaEEYQELKEELEELEEQLEELLGELEELLEAldeeELEE 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1830 AEEQLEIESRERQANGKNLRQKEKKLKDLTIQMEDERKQAQQYKDQAEkgnvrvkqLKHQLEEAEEEAQRMAAARRKLQR 1909
Cdd:COG4717 433 ELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEE--------LKAELRELAEEWAALKLALELLEE 504
|
....*..
gi 1604784239 1910 ELDEATE 1916
Cdd:COG4717 505 AREEYRE 511
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
879-1462 |
3.02e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 52.60 E-value: 3.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 879 LKDITQKHTQLMEERAQLEMKLHAETELYAEAEEMRVRLEAKKQELEEVLHEMESRLEEEEDRSNALHNERKEMEQQLQL 958
Cdd:PRK01156 171 LKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDM 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 959 MEAHIAEEEDARQKLQMEKVSVEgKVKKLEEDilMMEDQNNKLQKERKLLEERLADMsSNLAEEEEKSKNLSKLKTKHES 1038
Cdd:PRK01156 251 KNRYESEIKTAESDLSMELEKNN-YYKELEER--HMKIINDPVYKNRNYINDYFKYK-NDIENKKQILSNIDAEINKYHA 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1039 MISELELrMKKEEKGRLDMEKAKRKVEAELGDLQEQHADLQAQLAELRaQLAAKEEELQATQARLEEECNQR-------- 1110
Cdd:PRK01156 327 IIKKLSV-LQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIE-SLKKKIEEYSKNIERMSAFISEIlkiqeidp 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1111 GAAVKRVRELEVLISELQEDLEAERAARGKVEAARRDLGEELNALRTELEDSL-GTTAAQQELRAKREqEVSMLKKAMED 1189
Cdd:PRK01156 405 DAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVCPVcGTTLGEEKSNHIIN-HYNEKKSRLEE 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1190 EGRSHEAQVQDLRQKHSQaVEELTEQLEQAKRVRagLEKAKQALEKESADLSADLRSLASAKqdveHKKKKVEGQLNELN 1269
Cdd:PRK01156 484 KIREIEIEVKDIDEKIVD-LKKRKEYLESEEINK--SINEYNKIESARADLEDIKIKINELK----DKHDKYEEIKNRYK 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1270 SRFNESERQRtelgervsklTTELDSVTGLLNEAEGKNIKLSKDvsSLSSQLQDA----QELLSEETRQKLNLSGRLRQT 1345
Cdd:PRK01156 557 SLKLEDLDSK----------RTSWLNALAVISLIDIETNRSRSN--EIKKQLNDLesrlQEIEIGFPDDKSYIDKSIREI 624
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1346 EEDRNSLMEQLEEETEAKRAVERqvssLNMQLSDSKKKLDEMSGtveaLEEGKKRLQRELEAANSDYEEKASAYDKLEKS 1425
Cdd:PRK01156 625 ENEANNLNNKYNEIQENKILIEK----LRGKIDNYKKQIAEIDS----IIPDLKEITSRINDIEDNLKKSRKALDDAKAN 696
|
570 580 590
....*....|....*....|....*....|....*..
gi 1604784239 1426 RGRMQQELEDVLMDLDSQRQLVSNLEKKQKKFDQMLA 1462
Cdd:PRK01156 697 RARLESTIEILRTRINELSDRINDINETLESMKKIKK 733
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1076-1720 |
3.48e-06 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 52.52 E-value: 3.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1076 ADLQAQLAELRAQLAAKEEELQATQARLEEEcnqRGAAVKRV---RELEVLISELQEDL----EAERAARGKVEAARRDL 1148
Cdd:NF041483 533 AERLRAEAEEQAEEVRAAAERAARELREETE---RAIAARQAeaaEELTRLHTEAEERLtaaeEALADARAEAERIRREA 609
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1149 GEELNALRTELEDSLGTTAAQQELRAKR-EQEVSMLKKAMEDEGrshEAQVQDLRQKHSQAVEEL-TEQLEQAKRVRAGL 1226
Cdd:NF041483 610 AEETERLRTEAAERIRTLQAQAEQEAERlRTEAAADASAARAEG---ENVAVRLRSEAAAEAERLkSEAQESADRVRAEA 686
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1227 EKAKQALEKESADLSADLR------------SLASAKQDVEHKKKKVEGQLNEL----NSRFNESERQRTELGERVSKLT 1290
Cdd:NF041483 687 AAAAERVGTEAAEALAAAQeeaarrrreaeeTLGSARAEADQERERAREQSEELlasaRKRVEEAQAEAQRLVEEADRRA 766
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1291 TEL------------DSVTGLLNEAEgkniklsKDVSSLSSQLQDAQELLSEETRQKlnlSGRLR--------QTEEDRN 1350
Cdd:NF041483 767 TELvsaaeqtaqqvrDSVAGLQEQAE-------EEIAGLRSAAEHAAERTRTEAQEE---ADRVRsdayaereRASEDAN 836
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1351 SLMEQLEEETEAKRAV-ERQVSS-------LNMQLSDSKKKL-DEMSGTVEALEEGKKRLQREL-EAANSDYEEKASAYD 1420
Cdd:NF041483 837 RLRREAQEETEAAKALaERTVSEaiaeaerLRSDASEYAQRVrTEASDTLASAEQDAARTRADArEDANRIRSDAAAQAD 916
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1421 KLEKSRGRMQQELEDVLMDLDSQRQLVSNLEKKQKKFDQMLAEERAVSCKFAE-ERDRAEA-----EAREKETRVLALAR 1494
Cdd:NF041483 917 RLIGEATSEAERLTAEARAEAERLRDEARAEAERVRADAAAQAEQLIAEATGEaERLRAEAaetvgSAQQHAERIRTEAE 996
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1495 ALEENqgALEEAEKTMKGLRADMEDLI-SSKDDVGKSVHD-LEKAKRGLEAIVDEMRTQMEELEDE-LQVAEDAKLRLDV 1571
Cdd:NF041483 997 RVKAE--AAAEAERLRTEAREEADRTLdEARKDANKRRSEaAEQADTLITEAAAEADQLTAKAQEEaLRTTTEAEAQADT 1074
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1572 NTQALRAQHER-------ELHARDELGEEKRKQLLKQVRELEAELeeerkqRGQASGSKKKLEGELKDMEDqleatsRGR 1644
Cdd:NF041483 1075 MVGAARKEAERivaeatvEGNSLVEKARTDADELLVGARRDATAI------RERAEELRDRITGEIEELHE------RAR 1142
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1645 DEAVKQLRKIQGQVKDLQRDLEDSRAAqkevlASARESERRSKA-MEADIVQlhemLAAVERAR---KQAEVERDELSEE 1720
Cdd:NF041483 1143 RESAEQMKSAGERCDALVKAAEEQLAE-----AEAKAKELVSDAnSEASKVR----IAAVKKAEgllKEAEQKKAELVRE 1213
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1244-1601 |
3.72e-06 |
|
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: 51.82 E-value: 3.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1244 LRSLASAKQDVEHKKKKVEGQLNELNSRFNESERQRTELGERVSKLTTELDSVTGLLNEAEGKNiklsKDVSSLSSQLQD 1323
Cdd:pfam07888 40 LQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKY----KELSASSEELSE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1324 AQELLSEETRQKLnlsGRLRQTEEDRNSLMEQ-LEEETEAKRAVERQVSSLNmQLSDSKKKLDEMSGTVEALEEGKKRLQ 1402
Cdd:pfam07888 116 EKDALLAQRAAHE---ARIRELEEDIKTLTQRvLERETELERMKERAKKAGA-QRKEEEAERKQLQAKLQQTEEELRSLS 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1403 RELEAANSDYEEKASAYDKLEKSRGRMQQ----------ELEDVLMDLDSQRQLVSNLEKKQKKFDQMLAEeravsckFA 1472
Cdd:pfam07888 192 KEFQELRNSLAQRDTQVLQLQDTITTLTQklttahrkeaENEALLEELRSLQERLNASERKVEGLGEELSS-------MA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1473 EERDRAEAEAREKETRVLALARALEENQGALEEAEKTMKGLRadmEDLISSKDDVGKSVHDLEKAKRGLEAIVDEMRTQM 1552
Cdd:pfam07888 265 AQRDRTQAELHQARLQAAQLTLQLADASLALREGRARWAQER---ETLQQSAEADKDRIEKLSAELQRLEERLQEERMER 341
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1553 EELEDELQVAEDAKLrldvnTQALRAQHE-RELHARDELGEEKRKQLLKQ 1601
Cdd:pfam07888 342 EKLEVELGREKDCNR-----VQLSESRRElQELKASLRVAQKEKEQLQAE 386
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
843-1405 |
4.25e-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: 51.75 E-value: 4.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 843 TKVKPLLQVTRQEEEMGQKDEELKAAKEVAAKVETELKDITQKHTQLMEERAQLEMKLHAETELYAEAEEMRVRLEAKKQ 922
Cdd:pfam10174 259 LKTNGLLHTEDREEEIKQMEVYKSHSKFMKNKIDQLKQELSKKESELLALQTKLETLTNQNSDCKQHIEVLKESLTAKEQ 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 923 eleevlhemesrleeeedRSNALHNERKEMEQQLQLMEAHIAEEEDARQKLQMEKVSVEGKVKKLEEDILMMEDQNNKLQ 1002
Cdd:pfam10174 339 ------------------RAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQ 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1003 KERKLLEERLADMSSNLAEEEEKSKNLSKLKTKHESMISELE---------LRMKKEEKGRLDMEKAKrkveaELGDLQE 1073
Cdd:pfam10174 401 KKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEealsekeriIERLKEQREREDRERLE-----ELESLKK 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1074 QHADLQAQLAELRAQLAAKEEELQATQarlEEECNQRGAAVKRVRELEVLISELQEDLeaeraargkveaarrdlgEELN 1153
Cdd:pfam10174 476 ENKDLKEKVSALQPELTEKESSLIDLK---EHASSLASSGLKKDSKLKSLEIAVEQKK------------------EECS 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1154 ALRTELEdslgtTAAQQELRAKREQEVSMLKKAMEDEGRSHeaqvQDLRQKHSQAVEELTEQLEQAKRVRAGLEKAKQAL 1233
Cdd:pfam10174 535 KLENQLK-----KAHNAEEAVRTNPEINDRIRLLEQEVARY----KEESGKAQAEVERLLGILREVENEKNDKDKKIAEL 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1234 EKESADLSADLRSLASAKQDVEHKKKKVEGQLNELNSRF------NESERQRTELGERVSKLTTELDSVtgllneaegkn 1307
Cdd:pfam10174 606 ESLTLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRRednladNSQQLQLEELMGALEKTRQELDAT----------- 674
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1308 iklskdvsslSSQLQDAQELLSEETRQKLNLSGrlrqteEDRNSLMEQLEEETEAKRAV--ERQVSSLNMQLSDSKKKld 1385
Cdd:pfam10174 675 ----------KARLSSTQQSLAEKDGHLTNLRA------ERRKQLEEILEMKQEALLAAisEKDANIALLELSSSKKK-- 736
|
570 580
....*....|....*....|
gi 1604784239 1386 EMSGTVEALEEGKKRLQREL 1405
Cdd:pfam10174 737 KTQEEVMALKREKDRLVHQL 756
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1262-1509 |
4.57e-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: 4.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1262 EGQLNELNSRFNESERQRTELGERVSKLTTELDSVTGLLNEAEGKNIKLSKDVSSLSSQLQDAQELLsEETRQKLNLSGR 1341
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEI-EERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1342 LRQTEEDRNSLMEQLEEETEAKRAVERqVSSLNMQLSDSKKKLDEMsgtvealeegkKRLQRELEAANSDYEEKAsayDK 1421
Cdd:COG3883 94 ALYRSGGSVSYLDVLLGSESFSDFLDR-LSALSKIADADADLLEEL-----------KADKAELEAKKAELEAKL---AE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1422 LEKSRGRMQQELEDVLMDLDSQRQLVSNLEKKQKKFDQMLAEERAVSCKfAEERDRAEAEAREKETRVLALARALEENQG 1501
Cdd:COG3883 159 LEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAA-AEAAAAAAAAAAAAAAAAAAAAAAAAAAAA 237
|
....*...
gi 1604784239 1502 ALEEAEKT 1509
Cdd:COG3883 238 AAAAAAAS 245
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1066-1218 |
4.76e-06 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 50.73 E-value: 4.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1066 AELGDL----QEQHADLQAQLAELRAQLAAKEEELQATQARLEEECNQRGAAVKRvrelevlISELQEDLEAERA----A 1137
Cdd:PRK09039 63 AELADLlsleRQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGR-------AGELAQELDSEKQvsarA 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1138 RGKVEaarrDLGEELNALRTELedslgtTAAQQELRAKreqevsmlkkamEDEGRSHEAQVQDLRQKHSQAVEELTEQLE 1217
Cdd:PRK09039 136 LAQVE----LLNQQIAALRRQL------AALEAALDAS------------EKRDRESQAKIADLGRRLNVALAQRVQELN 193
|
.
gi 1604784239 1218 Q 1218
Cdd:PRK09039 194 R 194
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1062-1272 |
5.23e-06 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 51.23 E-value: 5.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1062 RKVEAELGDLQEQHADLQAQLAELRAQL----AAK-----EEELQATQARLEeecnqrgAAVKRVRELEVLISELQEDle 1132
Cdd:COG0497 168 RALKKELEELRADEAERARELDLLRFQLeeleAAAlqpgeEEELEEERRRLS-------NAEKLREALQEALEALSGG-- 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1133 aERAARGKVEAARRDLG------EELNALRTELEDSLGTTA-AQQELRAKREQevsmlkkaME-DEGRSHE-----AQVQ 1199
Cdd:COG0497 239 -EGGALDLLGQALRALErlaeydPSLAELAERLESALIELEeAASELRRYLDS--------LEfDPERLEEveerlALLR 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1200 DLRQKHSQAVEELTEQLEQAKRVRAGLEKAKQ---ALEKESADLSADLRSLASA-----KQDVEHKKKKVEGQLNEL--- 1268
Cdd:COG0497 310 RLARKYGVTVEELLAYAEELRAELAELENSDErleELEAELAEAEAELLEAAEKlsaarKKAAKKLEKAVTAELADLgmp 389
|
....
gi 1604784239 1269 NSRF 1272
Cdd:COG0497 390 NARF 393
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
953-1170 |
5.73e-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: 5.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 953 EQQLQLMEAHIAEEEDARQKLQMEKVSVEGKVKKLEEDILMMEDQNNKLQKERKLLEERLADMSSNLAEEEEKSKNLSKL 1032
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1033 KTKHESMISELELRMKKEEKGR-LDMEKAKRKVEAELGDLQEQHADLQAQLAELRAQLAAKEEELQATQARLEEecnQRG 1111
Cdd:COG3883 95 LYRSGGSVSYLDVLLGSESFSDfLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEA---AKA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1604784239 1112 AAVKRVRELEVLISELQEDLEAERAARGKVEAARRDLGEELNALRTELEDSLGTTAAQQ 1170
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
940-1181 |
5.92e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.56 E-value: 5.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 940 DRSNALHNERKEMEQQLQLMEAHIAEEEDARQKLQMEK--VSVEGKVKKLEEDILMMEDQNNKLQKERKLLEERLADMSS 1017
Cdd:COG3206 168 LRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNglVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRA 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1018 NLAEEEEKSKNLSKlktkhESMISELelrmkkeekgRLDMEKAKRKVEAELGDLQEQHADLQAQLAELRAQLAAKEEELQ 1097
Cdd:COG3206 248 QLGSGPDALPELLQ-----SPVIQQL----------RAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQ 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1098 ATQARLEeecNQRGAAVKRVRELEvlisELQEDLEAERAARGKVEAARRDLGEELNALRTELEDSLgttAAQQELRAKRE 1177
Cdd:COG3206 313 RILASLE---AELEALQAREASLQ----AQLAQLEARLAELPELEAELRRLEREVEVARELYESLL---QRLEEARLAEA 382
|
....
gi 1604784239 1178 QEVS 1181
Cdd:COG3206 383 LTVG 386
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1037-1252 |
6.19e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.60 E-value: 6.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1037 ESMISELELRMKKEEKGRLDMEKAKRKVEAELGDLQEQHADLQAQLAELRAQLAAKEEELQATQARLEEecnQRGAAVKR 1116
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEE---RREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1117 VRE----------LEVLI-SELQEDLEAERAARGKVEAARRDL-------GEELNALRTELEDSLGTTAAQQELRAKREQ 1178
Cdd:COG3883 92 ARAlyrsggsvsyLDVLLgSESFSDFLDRLSALSKIADADADLleelkadKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1604784239 1179 EVSMLKKAMEDEGRSHEAQVQDLRQKHSQAVEELTEQLEQAKRVRAGLEKAKQALEKESADLSADLRSLASAKQ 1252
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAS 245
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
850-1381 |
8.44e-06 |
|
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: 50.88 E-value: 8.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 850 QVTRQEEEMGQKDEELKAAKEVAAKVETELKDITQKHTQLMEERAQLEMKLHAETELYAEAEEMRvrlEAKKQELEEVLH 929
Cdd:pfam05483 269 KANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEK---EAQMEELNKAKA 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 930 EMESRLEEEEDRSNALHNERKEMEQQLQlmeahiaEEEDARQKLQMEkvsVEGKVKKLEEDILMMEDQNNKLQKERKLLE 1009
Cdd:pfam05483 346 AHSFVVTEFEATTCSLEELLRTEQQRLE-------KNEDQLKIITME---LQKKSSELEEMTKFKNNKEVELEELKKILA 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1010 ERLADMSSN-----LAEE-EEKSKNLSKLKTKHESMISELELRMKKEEKGRLDMEKAKRKVEAELGDLQEQHADLQAQLA 1083
Cdd:pfam05483 416 EDEKLLDEKkqfekIAEElKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCD 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1084 ELraqLAAKEEELQATQARLEEECNQRGAAVKRVRELEVLISELQEDLEAERAARGKVEAARRDLGEELNALRTELEDSL 1163
Cdd:pfam05483 496 KL---LLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSE 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1164 GTTAAQQELRAKREQEVsmlkKAMEDEGRSHEAQVQDlrqkHSQAVEELTEQLEQAKRVRAGLEKAKQALEKESADLSAD 1243
Cdd:pfam05483 573 ENARSIEYEVLKKEKQM----KILENKCNNLKKQIEN----KNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELE 644
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1244 lrsLASAKQDVEH----KKKKVEGQLNELNSRFNESERQRTELGERVsKLTTELD-----SVTGLLNEAEGKNIKLSKDV 1314
Cdd:pfam05483 645 ---LASAKQKFEEiidnYQKEIEDKKISEEKLLEEVEKAKAIADEAV-KLQKEIDkrcqhKIAEMVALMEKHKHQYDKII 720
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1604784239 1315 SSLSSQLQDAQELLSEETRQKLNLSGRLRQTEEDRNSLMEQLEEETEAKRAVERQVSSLNMQLSDSK 1381
Cdd:pfam05483 721 EERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKDKK 787
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
864-1147 |
1.01e-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: 50.07 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 864 ELKAAKEVAAKVETELKDITQKHTQLMEERAQLEMKLHAETELYAEAEEMRVRLEAKKQELEEVLHEMESRLEEEEDRSN 943
Cdd:pfam19220 112 ELRDKTAQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAAELA 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 944 ALHNERKEMEQQL-------QLMEAHIAEEEDARQKLQMEkvsvegkvkkleedilmMEDQNNKLQKERKLLEERLADMS 1016
Cdd:pfam19220 192 ELTRRLAELETQLdatrarlRALEGQLAAEQAERERAEAQ-----------------LEEAVEAHRAERASLRMKLEALT 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1017 SNLAEEEEKSKNLSKLKTKHESMISELELRMKKEEKGRLDMEKAKRKVEAELGDLQEQHADLQAQLAELRAQ-------L 1089
Cdd:pfam19220 255 ARAAATEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQFQEMQRARAELEERaemltkaL 334
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1604784239 1090 AAKEEELQATQARLEEECNQRGAAVKRVR----ELEVLISELQEDLEAERAAR----GKVEAARRD 1147
Cdd:pfam19220 335 AAKDAALERAEERIASLSDRIAELTKRFEveraALEQANRRLKEELQRERAERalaqGALEIARES 400
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1210-1436 |
1.10e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.83 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1210 EELTEQLEQAKRVRAGLEKAKQALEKESADLSADLRSLASAKQDVEHKKKKVEGQLNELNSRFNEserQRTELGERVSKL 1289
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEE---RREELGERARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1290 TTELDSVTGLLneaegkNIKLSKDVSSLSSQLQDAQELLSEETRQKLNLSGRLRQTEEDRNSLMEQLEEETEAKRAVERQ 1369
Cdd:COG3883 96 YRSGGSVSYLD------VLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1604784239 1370 VSSLNMQLSDSKKKLDEMSGTVEALEEGKKRLQRELEAANSDYEEKASAYDKLEKSRGRMQQELEDV 1436
Cdd:COG3883 170 KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
844-1146 |
1.19e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.91 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 844 KVKPLLQVTRQEEEMG---QKDEELKAAKEvaAKVETELKDITQKHTQLMEE-RAQLEMKLHAEtELYAEAEEMRVRLEA 919
Cdd:PTZ00121 1562 EKKKAEEAKKAEEDKNmalRKAEEAKKAEE--ARIEEVMKLYEEEKKMKAEEaKKAEEAKIKAE-ELKKAEEEKKKVEQL 1638
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 920 KKQELEEVLHEMESRLEEEEDRSNALHNERKEMEQQLQLMEAHiAEEEDARQKLQMEKVSVEGKvKKLEEDILMMEDQNN 999
Cdd:PTZ00121 1639 KKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAK-KAEEDEKKAAEALKKEAEEA-KKAEELKKKEAEEKK 1716
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1000 KLQKERKLLEERLADMSSNLAEEEEKSKNLSKLKtKHESMISELELRMKKEEKGRLDMEKAKRKVEAElgdlqeqhaDLQ 1079
Cdd:PTZ00121 1717 KAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAK-KDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEE---------ELD 1786
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1604784239 1080 AQLAELRAQLAAKEEELQATQARLEEECNQRGAAVKRVRELEVliSELQEDLEAERAARGKVEAARR 1146
Cdd:PTZ00121 1787 EEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMED--SAIKEVADSKNMQLEEADAFEK 1851
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
855-1095 |
1.35e-05 |
|
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: 50.45 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 855 EEEMGQKDEELKAAKEVAAKVETELKDITQKHTQLMEERAQLEMKLHAETELYAEAEEMRVRLEAKKQELEEVLHEMESR 934
Cdd:TIGR02169 790 HSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEE 869
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 935 LEEEEDRSNALHNERKEMEQQLQLMEAHIAEEEDARQklqmekvsvegkvkKLEEDILMMEDQNNKLQKERKLLEERLAD 1014
Cdd:TIGR02169 870 LEELEAALRDLESRLGDLKKERDELEAQLRELERKIE--------------ELEAQIEKKRKRLSELKAKLEALEEELSE 935
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1015 MSSNLAEEEEKSKNLSKLKtKHESMISELELRMKKEEKGRLDMEKAKRKVEAELGDLQEQHADLQAQLAELRAQLAAKEE 1094
Cdd:TIGR02169 936 IEDPKGEDEEIPEEELSLE-DVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEK 1014
|
.
gi 1604784239 1095 E 1095
Cdd:TIGR02169 1015 K 1015
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1346-1547 |
1.37e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.83 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1346 EEDRNSLMEQLEEETEAKRAVERQVSSLNMQLSDSKKKLDEMSGTVEALEEGKKRLQRELEAANSDYEEKASAYDKLEKS 1425
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1426 --RGRMQQELEDVLMDLDSQRQLVSNLEKKQKKFDQ---MLAEERAVSCKFAEERDRAEAEAREKETRVLALARALEENQ 1500
Cdd:COG3883 95 lyRSGGSVSYLDVLLGSESFSDFLDRLSALSKIADAdadLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1604784239 1501 GALEEAEKTMKGLRADMEDLISSKDDVGKSVHDLEKAKRGLEAIVDE 1547
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
850-1344 |
1.42e-05 |
|
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: 50.50 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 850 QVTRQEEEMGQKDEELKAAKEVAAKVETELKDITQKHTQLMEERAQLEMKLHAETELYAEAEEMRVRLEAKKQELEEVlh 929
Cdd:pfam15921 445 QMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKL-- 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 930 emesrleeeedrsnalhneRKEMEQQLQLMEaHIAEEEDARQKLQME----KVSVEGKVKKLE------EDILMMEDQNN 999
Cdd:pfam15921 523 -------------------RSRVDLKLQELQ-HLKNEGDHLRNVQTEcealKLQMAEKDKVIEilrqqiENMTQLVGQHG 582
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1000 K----LQKERKLLEERLADMSSNLAEeeeksknLSKLKTKHESMISELELRMKKEEKGRLDMEKAKRKVEAELGDLQEQH 1075
Cdd:pfam15921 583 RtagaMQVEKAQLEKEINDRRLELQE-------FKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQER 655
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1076 ADLQAQLAELRAQLAAKEEELQATQARLEeecnqrgaavKRVRELEVLISELQEDLeaeRAARGKVEAARRDLGEELNAL 1155
Cdd:pfam15921 656 DQLLNEVKTSRNELNSLSEDYEVLKRNFR----------NKSEEMETTTNKLKMQL---KSAQSELEQTRNTLKSMEGSD 722
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1156 RTELEDSLGTtaaQQELRAKReqevsmlkkamedegrsheAQVQDLRQKhsqaVEELTEQLEQAKrvragleKAKQALEK 1235
Cdd:pfam15921 723 GHAMKVAMGM---QKQITAKR-------------------GQIDALQSK----IQFLEEAMTNAN-------KEKHFLKE 769
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1236 ESADLSADLRSLASakqdvehKKKKVEGQLNELNSrfneserQRTELGERVSKLTTELDSVTglLNEAEGKNIKLSKDVS 1315
Cdd:pfam15921 770 EKNKLSQELSTVAT-------EKNKMAGELEVLRS-------QERRLKEKVANMEVALDKAS--LQFAECQDIIQRQEQE 833
|
490 500 510
....*....|....*....|....*....|..
gi 1604784239 1316 SLSSQLQ---DAQELLSEETRQKLNLSGRLRQ 1344
Cdd:pfam15921 834 SVRLKLQhtlDVKELQGPGYTSNSSMKPRLLQ 865
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
854-1250 |
1.44e-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: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 854 QEEEMGQKDEELKAAKEVAAKVETELKDITQKHTQLMEERAQLEMKLHAE----TELYAEAEEMRVRLEAKKQELEEVLH 929
Cdd:COG4913 329 EAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASaeefAALRAEAAALLEALEEELEALEEALA 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 930 EMESRLEEEEDRSNALHNERKEMEQQLQLMEAHIAEEEDA-RQKLQMEKVSV-----EGKVKKLEED------------- 990
Cdd:COG4913 409 EAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDAlAEALGLDEAELpfvgeLIEVRPEEERwrgaiervlggfa 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 991 -ILMMEDQN--------NKLQKERKLLEERLADMSSNLAEEEEKSKNLS-KLKTK----HESMISEL------------- 1043
Cdd:COG4913 489 lTLLVPPEHyaaalrwvNRLHLRGRLVYERVRTGLPDPERPRLDPDSLAgKLDFKphpfRAWLEAELgrrfdyvcvdspe 568
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1044 ELR----------MKKEEKGR--LDMEKAKRKV-------EAELGDLQEQHADLQAQLAELRAQLAAKEEELQATQARLE 1104
Cdd:COG4913 569 ELRrhpraitragQVKGNGTRheKDDRRRIRSRyvlgfdnRAKLAALEAELAELEEELAEAEERLEALEAELDALQERRE 648
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1105 --EECNQRGAAVKRVRELEVLISELQEDLEAERAARGKVEAARR---DLGEELNALRTELEDSLGT-TAAQQELRAKREQ 1178
Cdd:COG4913 649 alQRLAEYSWDEIDVASAEREIAELEAELERLDASSDDLAALEEqleELEAELEELEEELDELKGEiGRLEKELEQAEEE 728
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1604784239 1179 EVSMLKKAMEDEGRSHEAQVQDLRQKHSQAVEElteqlEQAKRVRAGLEKAKQALEKESADLSADLRSLASA 1250
Cdd:COG4913 729 LDELQDRLEAAEDLARLELRALLEERFAAALGD-----AVERELRENLEERIDALRARLNRAEEELERAMRA 795
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
910-1216 |
1.55e-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: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 910 AEEMRVRLEAKKQELEEVLHEMESRLEEEEDRSNALHNERkemeQQLQLMEAHIAEEEDARQkLQMEKVSVEGKVKKLEE 989
Cdd:COG4913 608 NRAKLAALEAELAELEEELAEAEERLEALEAELDALQERR----EALQRLAEYSWDEIDVAS-AEREIAELEAELERLDA 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 990 ---DILMMEDQNNKLQKERKLLEERLADMSSNLAEEEEKSKNLSKLKTKHESMISELELRMKKEEKGRLDmekAKRKVEA 1066
Cdd:COG4913 683 ssdDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLE---ERFAAAL 759
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1067 ELGDLQEQHADLQAQLAELRAQLAAKEEELQATQARL----EEECNQRGAAVKRVRELEVLISELQED-LEA--ERAARG 1139
Cdd:COG4913 760 GDAVERELRENLEERIDALRARLNRAEEELERAMRAFnrewPAETADLDADLESLPEYLALLDRLEEDgLPEyeERFKEL 839
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1140 KVEAARRDLGEELNALRTELED----------SLGTTAAQQ------ELRAKREQEVSMLKKAMEDEGRSHEAQVQDLRQ 1203
Cdd:COG4913 840 LNENSIEFVADLLSKLRRAIREikeridplndSLKRIPFGPgrylrlEARPRPDPEVREFRQELRAVTSGASLFDEELSE 919
|
330
....*....|...
gi 1604784239 1204 KHSQAVEELTEQL 1216
Cdd:COG4913 920 ARFAALKRLIERL 932
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1195-1420 |
1.67e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.44 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1195 EAQVQDLRQKHSQAVEELTEQLEQAKRVRAGLEKAKQALEKESADLSADLRSLASAKQDVEHKKKKVEGQLNELNSRFNE 1274
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1275 SERQRTELG---------------ERVSKLTTELDSVTGLLNEAEGKNIKLSKDVSSLSSQLQDAQELLSEETRQKLNLS 1339
Cdd:COG3883 95 LYRSGGSVSyldvllgsesfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1340 GRLRQTEEDRNSLMEQLEEETEAKRAVERQVSSLNMQLSDSKKKLDEMSGTVEALEEGKKRLQRELEAANSDYEEKASAY 1419
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGA 254
|
.
gi 1604784239 1420 D 1420
Cdd:COG3883 255 A 255
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1383-1875 |
1.75e-05 |
|
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: 50.22 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1383 KLDEMSGTVEALEEGKKRLQRELEAANSDYEEK-ASAYDKLEKSRGRMQQELEDVLMDLDSQRQLVSNLEKKQKKFDQML 1461
Cdd:pfam12128 259 RLSHLHFGYKSDETLIASRQEERQETSAELNQLlRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDAD 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1462 AEERAVSckfAEERDRAEAEAREKETRVlalaRALEENQGALEEAEKTMKGLRADmedlisskddvgKSVHDLEKAKRGL 1541
Cdd:pfam12128 339 IETAAAD---QEQLPSWQSELENLEERL----KALTGKHQDVTAKYNRRRSKIKE------------QNNRDIAGIKDKL 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1542 EAIVDEMRTQMEELEDELQVAEDAkLRLDVNTQALRAQHERELHArDELGEEKrkqllkqvreleaeleeERKQRGQASg 1621
Cdd:pfam12128 400 AKIREARDRQLAVAEDDLQALESE-LREQLEAGKLEFNEEEYRLK-SRLGELK-----------------LRLNQATAT- 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1622 skkklEGELKDMEDQLEATSRGRDEavkqLRKIQGQVKDLQRDLEDSRAAQKEVLASARESERRSKAMEADIVQLHEMLA 1701
Cdd:pfam12128 460 -----PELLLQLENFDERIERAREE----QEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLF 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1702 A-----VERARKQAEVERDelseelasnSSGKSLMSDEKRRLDTkISQLEEELEEEQANVESLNDRLRKSQ-----QLVE 1771
Cdd:pfam12128 531 PqagtlLHFLRKEAPDWEQ---------SIGKVISPELLHRTDL-DPEVWDGSVGGELNLYGVKLDLKRIDvpewaASEE 600
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1772 QLGAELAAERSTSQSREGSRQQLERQNRELKAKMQEMEGQGRSKLKASIAALEAKLREAEEQLEIESRERQANGKNLRQK 1851
Cdd:pfam12128 601 ELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSA 680
|
490 500
....*....|....*....|....
gi 1604784239 1852 EKKLKDLTIQMEDERKQAQQYKDQ 1875
Cdd:pfam12128 681 NERLNSLEAQLKQLDKKHQAWLEE 704
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1245-1452 |
2.06e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 49.63 E-value: 2.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1245 RSLASAKQDVEHKKKKVEGQLNELNsrfnESERQRTELGERVSKLTTELDSVTGLLNEAEGKNIKLSKDVSSLS------ 1318
Cdd:PHA02562 206 EQRKKNGENIARKQNKYDELVEEAK----TIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQkvikmy 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1319 ----------SQLQDAQELLSEETRQKLNLSGRLRQTEEDRNSLMEQLEEETEAKraverqvsslnMQLSDSKKKLDEMS 1388
Cdd:PHA02562 282 ekggvcptctQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQS-----------KKLLELKNKISTNK 350
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1604784239 1389 GTVEALEEGKKRLQRELEAANSDYEEKASAYDKLEKSRGRMQQELEDVLMDLDsQRQLVSNLEK 1452
Cdd:PHA02562 351 QSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEKY-HRGIVTDLLK 413
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
850-1027 |
2.25e-05 |
|
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: 48.99 E-value: 2.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 850 QVTRQEEEMGQKDEELKAAKEVAAKVETELKDITQKHTQLMEERAQLEMKLHAETELYAE----------AEEMRVRLEA 919
Cdd:COG4942 49 EEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEllralyrlgrQPPLALLLSP 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 920 KK--------QELEEVLHEMESRLEEEEDRSNALHNERKEMEQQLQLMEAHIAEEEDARQKLQMEKVSVEGKVKKLEEDI 991
Cdd:COG4942 129 EDfldavrrlQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKEL 208
|
170 180 190
....*....|....*....|....*....|....*.
gi 1604784239 992 LMMEDQNNKLQKERKLLEERLADMSSNLAEEEEKSK 1027
Cdd:COG4942 209 AELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1387-1625 |
2.41e-05 |
|
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: 48.99 E-value: 2.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1387 MSGTVEALEEGKKRLQRELEAANSDYEEKASAYDKLEKSRGRMQQELEDVLMDLDSQRQLVSNLEKKQKKFDQMLAEera 1466
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1467 vsckFAEERDRAEAEAREKETRVLALARALEE-----------NQGALEEAEKTMKGLRADMEDLISSKDDVGKSVHDLE 1535
Cdd:COG4942 88 ----LEKEIAELRAELEAQKEELAELLRALYRlgrqpplalllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1536 KAKRGLEAIVDEMRTQMEELEDELQVAEDAKLRLDVNTQALRAQHERELHARDELgEEKRKQLLKQVRELEAELEEERKQ 1615
Cdd:COG4942 164 ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAEL-QQEAEELEALIARLEAEAAAAAER 242
|
250
....*....|
gi 1604784239 1616 RGQASGSKKK 1625
Cdd:COG4942 243 TPAAGFAALK 252
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1618-1921 |
2.42e-05 |
|
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: 49.35 E-value: 2.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1618 QASGSKKKLEGELKDME-DQLEATSRGRDEAVKQLRKIQGQVKDLQRDLEDSRA--AQKEVLASARESE-----RRSKAM 1689
Cdd:pfam17380 281 QKAVSERQQQEKFEKMEqERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAiyAEQERMAMERERElerirQEERKR 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1690 EADIVQLHEMLAAVERARkqaEVERDELSEELASNSSGKSLMSDEKRRLDTKISQ---LEEELEEEQANVESLNDRLRKS 1766
Cdd:pfam17380 361 ELERIRQEEIAMEISRMR---ELERLQMERQQKNERVRQELEAARKVKILEEERQrkiQQQKVEMEQIRAEQEEARQREV 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1767 QQLVEQLGAELAAERSTSQSREGSRQQLERQNRELKAKMQEMEgqgrsklkasiaaleaklREAEEQLEIESRERQANGK 1846
Cdd:pfam17380 438 RRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELE------------------KEKRDRKRAEEQRRKILEK 499
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1604784239 1847 NLRQKEKKLkdltiqMEDERKQAQQYKDQAEKGNVRVKQLKHQLEEAEEEAQRMAAARRKLQRELDEATEANDTL 1921
Cdd:pfam17380 500 ELEERKQAM------IEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRL 568
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
849-1126 |
2.48e-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: 49.25 E-value: 2.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 849 LQVTRQEEEMGQKDEELKAAKEVAAKVETELKDITQKHTQLMEERAQLEMKLHAETELYAEAEEMRVRLEAKKQELE--- 925
Cdd:TIGR04523 398 SKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSrsi 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 926 ----EVLHEMESRLEEEEDRSNALHNERKEMEQQLQLMEAHIAEEEDARQKLQMEKVSVEGKVKKLEEDILMMEDQNNK- 1000
Cdd:TIGR04523 478 nkikQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKe 557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1001 -----LQKERKLLEERLADMSSNLAEEEEKSKNLSKLKTKHESMISELELRMKKEEkgrldmekakrKVEAELGDLQEQH 1075
Cdd:TIGR04523 558 nlekeIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKIS-----------SLEKELEKAKKEN 626
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1604784239 1076 ADLQAQLAELRAQLAAKEEELQATQARLEEECNQRGAAVKRVRELEVLISE 1126
Cdd:TIGR04523 627 EKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDD 677
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
945-1288 |
3.31e-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: 48.86 E-value: 3.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 945 LHNERKEMEQQLQLMEAHIAEEEDARQKLQMEKVSVEGKVKKLEEDILMMEDQNNKLQKERKLLEERLADMSSNLAEEEE 1024
Cdd:TIGR04523 361 KQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNS 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1025 KSKNLSKLKTKHESMISELELRMKKEEKGRLDMEKAKRKVEAELGDLQEQHADLQAQLAELRAQLAAKEEElqatqarle 1104
Cdd:TIGR04523 441 EIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEK--------- 511
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1105 eecnqrgaavkrVRELEVLISELQEDLEAERAARGKVEAARRDLGEELNALRTELEDSLGTTAAQQelrakREQEVSMLK 1184
Cdd:TIGR04523 512 ------------VKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDE-----KNKEIEELK 574
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1185 KAMEDEGRSHEaQVQDLRQKHSQAVEELTEQLEQAKRVRAGLEKAKQALEKESADLSADLRSLASAKQDVEHKKKKVEGQ 1264
Cdd:TIGR04523 575 QTQKSLKKKQE-EKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKET 653
|
330 340
....*....|....*....|....
gi 1604784239 1265 LNELNSRFNESERQRTELGERVSK 1288
Cdd:TIGR04523 654 IKEIRNKWPEIIKKIKESKTKIDD 677
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
900-1461 |
3.52e-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: 48.98 E-value: 3.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 900 LHAETELYAEAEEMRVRLEAKKQELEEVLHEMESRLEEEEDRSNALHNERKEMEQQLQLMEAHIAEEEDARQKLQmekvs 979
Cdd:pfam07111 61 LSQQAELISRQLQELRRLEEEVRLLRETSLQQKMRLEAQAMELDALAVAEKAGQAEAEGLRAALAGAEMVRKNLE----- 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 980 vEGKVKKLEEDILMMEDQNNKLQKERkllEERLADMSSNlAEEEEKSknLSKLKTKHESMISELELRMKKEEKGRLDMEK 1059
Cdd:pfam07111 136 -EGSQRELEEIQRLHQEQLSSLTQAH---EEALSSLTSK-AEGLEKS--LNSLETKRAGEAKQLAEAQKEAELLRKQLSK 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1060 AKRKVEAELGDLQEQHADLQAQ-LAELRAQLAAKE-EELQATQARLEEECNQRGAAVK----RVRELEVLISELQEDL-- 1131
Cdd:pfam07111 209 TQEELEAQVTLVESLRKYVGEQvPPEVHSQTWELErQELLDTMQHLQEDRADLQATVEllqvRVQSLTHMLALQEEELtr 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1132 ----------EAERAARGKVEAARRD---LGEELNALRTELEDSL----GTTAAQQELRAKREQEVSMLKKAMEDEGRSH 1194
Cdd:pfam07111 289 kiqpsdslepEFPKKCRSLLNRWREKvfaLMVQLKAQDLEHRDSVkqlrGQVAELQEQVTSQSQEQAILQRALQDKAAEV 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1195 EA-------------QVQDLRQKHSQAVEELTEQLE----QAKRVRAGLEKAKQALEKESADLSADLRSLASAKQDVEHK 1257
Cdd:pfam07111 369 EVermsakglqmelsRAQEARRRQQQQTASAEEQLKfvvnAMSSTQIWLETTMTRVEQAVARIPSLSNRLSYAVRKVHTI 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1258 KKKVEGQLNELNSRFNES-------------ERQRTELGERVSKLTTELDSVTGLLN--------EAEGKNIKLSKDVSS 1316
Cdd:pfam07111 449 KGLMARKVALAQLRQESCpppppappvdadlSLELEQLREERNRLDAELQLSAHLIQqevgrareQGEAERQQLSEVAQQ 528
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1317 LSSQLQDAQELLSEETRQ-KLNLSGRLRQTEEDRNSLMEQLEEETEAKRAVERQVSS----LNMQLSDSKKKLD----EM 1387
Cdd:pfam07111 529 LEQELQRAQESLASVGQQlEVARQGQQESTEEAASLRQELTQQQEIYGQALQEKVAEvetrLREQLSDTKRRLNearrEQ 608
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1604784239 1388 SGTVEALEEGKKRLQRELEAANSDYEEKASAYDKLEKSRGRMQQELE-DVLMDLDSQRQLVSNLEKKQKKFDQML 1461
Cdd:pfam07111 609 AKAVVSLRQIQHRATQEKERNQELRRLQDEARKEEGQRLARRVQELErDKNLMLATLQQEGLLSRYKQQRLLAVL 683
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1322-1598 |
3.89e-05 |
|
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: 48.58 E-value: 3.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1322 QDAQELLSE-ETRQKLNLSGRLRQTEEDRNSLMEQLEEeteaKRAVERQVSSLNMQLSDSKKKLDEMSGTVEALEEGK-- 1398
Cdd:pfam17380 303 QEKEEKAREvERRRKLEEAEKARQAEMDRQAAIYAEQE----RMAMERERELERIRQEERKRELERIRQEEIAMEISRmr 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1399 --KRLQRELEAANSDYE---EKASAYDKLEKSRGRMQQELEDVLMDLDS------QRQLVSNLEKKQKKFDQMLAEE--- 1464
Cdd:pfam17380 379 elERLQMERQQKNERVRqelEAARKVKILEEERQRKIQQQKVEMEQIRAeqeearQREVRRLEEERAREMERVRLEEqer 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1465 ---------------RAVSCKFAEERDRAEAEarekETRVLALARALEENQGALEEAEKTMKGLRADMEDLisskddvGK 1529
Cdd:pfam17380 459 qqqverlrqqeeerkRKKLELEKEKRDRKRAE----EQRRKILEKELEERKQAMIEEERKRKLLEKEMEER-------QK 527
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1604784239 1530 SVHDLEKAKrgleaIVDEMRTQMEELEDELQVAEDAKLRLDVNTQALRAQHERELHARDELGEEKRKQL 1598
Cdd:pfam17380 528 AIYEEERRR-----EAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAEY 591
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1054-1252 |
3.95e-05 |
|
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: 47.92 E-value: 3.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1054 RLDMEKAKRKVEAELGDLQEQHADL-------QAQLAELRAQLAAKEEELQATQARLEEECNQRGAAVKRVRELEvlisE 1126
Cdd:TIGR02794 56 QQQKKPAAKKEQERQKKLEQQAEEAekqraaeQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAA----E 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1127 LQEDLEAERAARGKVEAARRdlgEELNALRTELEDSlgtTAAQQELRAKREQEVsmLKKAMEDEGRSHEAQVQDLRQKHS 1206
Cdd:TIGR02794 132 AKAKAEAEAERKAKEEAAKQ---AEEEAKAKAAAEA---KKKAEEAKKKAEAEA--KAKAEAEAKAKAEEAKAKAEAAKA 203
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1604784239 1207 QAVEELTEQLEQAKRVRAGLEKAKQALEKESADLSADLRSLASAKQ 1252
Cdd:TIGR02794 204 KAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQ 249
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1190-1586 |
4.08e-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: 48.80 E-value: 4.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1190 EGRSHEAQVQDLRQKHSQAVEELTEQLEQAKRVRAGLEKakqaLEKESADLSADLRS----LASAKQDVEHKKK--KVEG 1263
Cdd:COG3096 279 ERRELSERALELRRELFGARRQLAEEQYRLVEMARELEE----LSARESDLEQDYQAasdhLNLVQTALRQQEKieRYQE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1264 QLNELNSRFNESERQRTELGERVSkltteldsvtgllnEAEGKNIKLSKDVSSLSSQLQDAQELLSE-ETR-----QKLN 1337
Cdd:COG3096 355 DLEELTERLEEQEEVVEEAAEQLA--------------EAEARLEAAEEEVDSLKSQLADYQQALDVqQTRaiqyqQAVQ 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1338 LSGRLRQTEEDRNSLMEQLEEETEAKRAVERQVSSlnmQLSDSKKKLDEMSGTVEALEEGKKRLQR-----ELEAANSDY 1412
Cdd:COG3096 421 ALEKARALCGLPDLTPENAEDYLAAFRAKEQQATE---EVLELEQKLSVADAARRQFEKAYELVCKiagevERSQAWQTA 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1413 EEKASAYDKLEKSRGRMQQ---ELEDVLMDLDSQRQLVSNLEKKQKKFDQMLAEERAVSCKFAE---ERDRAEAEAREKE 1486
Cdd:COG3096 498 RELLRRYRSQQALAQRLQQlraQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAEleaQLEELEEQAAEAV 577
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1487 TRVLALARALEENQGALEEAEKTMKGLRADMEDLISSKDDVGKSVHDLEKakrgleaiVDEMRTQMEELEDELQVAEDak 1566
Cdd:COG3096 578 EQRSELRQQLEQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQE--------VTAAMQQLLEREREATVERD-- 647
|
410 420
....*....|....*....|
gi 1604784239 1567 lRLDVNTQALRAQHERELHA 1586
Cdd:COG3096 648 -ELAARKQALESQIERLSQP 666
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1081-1867 |
4.10e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.80 E-value: 4.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1081 QLAELRAQLAAKEEELQATQARLEEecnqrgaavkRVRELEVLI---SELQEDLEAERAARGKVEAARRDLG------EE 1151
Cdd:PRK04863 287 EALELRRELYTSRRQLAAEQYRLVE----------MARELAELNeaeSDLEQDYQAASDHLNLVQTALRQQEkieryqAD 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1152 LNALRTELEDSLGTTAAQQELRAKREQEVSmlkkAMEDEGRSHEAQVQDlrqkHSQAVEELTE---QLEQAKRVragLEK 1228
Cdd:PRK04863 357 LEELEERLEEQNEVVEEADEQQEENEARAE----AAEEEVDELKSQLAD----YQQALDVQQTraiQYQQAVQA---LER 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1229 AKQALEKesADLSADlrSLASAKQDVEHKKKKVEGQLNELNSRFNESE---RQRTELGERVSKLTTELDSvtgllNEAEG 1305
Cdd:PRK04863 426 AKQLCGL--PDLTAD--NAEDWLEEFQAKEQEATEELLSLEQKLSVAQaahSQFEQAYQLVRKIAGEVSR-----SEAWD 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1306 KNIKLSKDVSSLSSQLQDAQELlseetRQKLnlsGRLRQTEEDRNSLMEQLEEETEAKRAVERQVSSLNMQLSDSKKKLD 1385
Cdd:PRK04863 497 VARELLRRLREQRHLAEQLQQL-----RMRL---SELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLE 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1386 EMSGTVEALEEGKKRLQRELEAANSDYEEKAS-------AYDKLEKSRGRMQQELEDVlMDLDSQRQlvsnlekkqkkfd 1458
Cdd:PRK04863 569 SLSESVSEARERRMALRQQLEQLQARIQRLAArapawlaAQDALARLREQSGEEFEDS-QDVTEYMQ------------- 634
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1459 QMLAEERAVSckfaEERDRAEAEAREKETRVLALAraleenQGALEEAEkTMKGLRADMEDLISSK--DDV--------- 1527
Cdd:PRK04863 635 QLLERERELT----VERDELAARKQALDEEIERLS------QPGGSEDP-RLNALAERFGGVLLSEiyDDVsledapyfs 703
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1528 ---GKSVH-----DLEKAKRGLEAI----------------VDEMRTQMEELEDELQVaedaklrlDVNTQALRAQHERE 1583
Cdd:PRK04863 704 alyGPARHaivvpDLSDAAEQLAGLedcpedlyliegdpdsFDDSVFSVEELEKAVVV--------KIADRQWRYSRFPE 775
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1584 L-----HARDELGEEKRKQLLKQVRELEAELEEERK-QRGQASGSK-------------------------KKLEGELKD 1632
Cdd:PRK04863 776 VplfgrAAREKRIEQLRAEREELAERYATLSFDVQKlQRLHQAFSRfigshlavafeadpeaelrqlnrrrVELERALAD 855
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1633 MEDQ-LEATSRGRD--EAVKQLRKIQGQVKDLQRDLEDSRAAQ-KEVLASARESERRSKAMEADIVQLHEMLAAVERARK 1708
Cdd:PRK04863 856 HESQeQQQRSQLEQakEGLSALNRLLPRLNLLADETLADRVEEiREQLDEAEEAKRFVQQHGNALAQLEPIVSVLQSDPE 935
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1709 Q-AEVERD-ELSEELASNSSGK-----SLM--------SDEKRRL---DTKISQLEEELEEEQANVESLNDRLRKSQQLV 1770
Cdd:PRK04863 936 QfEQLKQDyQQAQQTQRDAKQQafaltEVVqrrahfsyEDAAEMLaknSDLNEKLRQRLEQAEQERTRAREQLRQAQAQL 1015
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1771 EQLGAELAAERSTSQSREGSRQQLERQNREL----KAKMQEMEGQGRSKLKASIAALEAKLREAEEQLEIESRERQANGK 1846
Cdd:PRK04863 1016 AQYNQVLASLKSSYDAKRQMLQELKQELQDLgvpaDSGAEERARARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTK 1095
|
890 900
....*....|....*....|.
gi 1604784239 1847 NLRQKEKKLKDLTIQMEDERK 1867
Cdd:PRK04863 1096 KLRKLERDYHEMREQVVNAKA 1116
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1076-1220 |
4.34e-05 |
|
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: 47.80 E-value: 4.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1076 ADLQAQLAELRAQLAAkeeeLQATQARLEEECNQRGAAVKRVRELEVLISELQEDLEAERAARGKVEAARRDLGEELNAL 1155
Cdd:pfam00529 54 TDYQAALDSAEAQLAK----AQAQVARLQAELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARR 129
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1604784239 1156 RTELEDSLG-------TTAAQQELRAKREQEVSMLKKAMEDEGRSHEAQVQDLRQKHSQA---VEELTEQLEQAK 1220
Cdd:pfam00529 130 RVLAPIGGIsreslvtAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSGAqlqIAEAEAELKLAK 204
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1079-1438 |
4.39e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 48.90 E-value: 4.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1079 QAQLAELRAQLAAKEEeLQATQARLEE--ECNQRGAAVKRV-RELEVLISELQEDLEAERAARGKVEA--ARRDLGEELN 1153
Cdd:PRK10929 34 QAKAAKTPAQAEIVEA-LQSALNWLEErkGSLERAKQYQQViDNFPKLSAELRQQLNNERDEPRSVPPnmSTDALEQEIL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1154 ALRTELEDSlgTTAAQQELRAKREQEVSMLKkamedegrsheaqvqdLRQKHSQAVEELTE-------------QLEQAK 1220
Cdd:PRK10929 113 QVSSQLLEK--SRQAQQEQDRAREISDSLSQ----------------LPQQQTEARRQLNEierrlqtlgtpntPLAQAQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1221 RVRAGLEKAKQAL---EKESADLSADLRS-LASAKQDVeHKKK--KVEGQLNELNSRFNeSERQRTelGERVSKLTTELD 1294
Cdd:PRK10929 175 LTALQAESAALKAlvdELELAQLSANNRQeLARLRSEL-AKKRsqQLDAYLQALRNQLN-SQRQRE--AERALESTELLA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1295 SVTGLLNEAEGKNIKLSKDVSSLSSQLQDAQELLSEETRQKLNLSGRLRQTeedRNSLMEQ---LEEET---EAKRAver 1368
Cdd:PRK10929 251 EQSGDLPKSIVAQFKINRELSQALNQQAQRMDLIASQQRQAASQTLQVRQA---LNTLREQsqwLGVSNalgEALRA--- 324
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1604784239 1369 QVSslnmQLSDSKK--KLD-EMSG-TVEAL--EEGKKRLQRELEAANSDYEEKASAYDKLEKSRGRMQQELEDVLM 1438
Cdd:PRK10929 325 QVA----RLPEMPKpqQLDtEMAQlRVQRLryEDLLNKQPQLRQIRQADGQPLTAEQNRILDAQLRTQRELLNSLL 396
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1672-1917 |
4.81e-05 |
|
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: 48.58 E-value: 4.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1672 QKEVLASARESERRSKAMEADIV--QLHEMLAAVERARKQAEVE--RDELSEELASNSSGKSLMSDEKRRLDTKISQLEE 1747
Cdd:pfam17380 279 QHQKAVSERQQQEKFEKMEQERLrqEKEEKAREVERRRKLEEAEkaRQAEMDRQAAIYAEQERMAMERERELERIRQEER 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1748 ELEEEQANVESLNDRLRKSQQLVE-QLGAELAAERSTSQSREGSRQQLERQNRELKAKMQEMEGQGRSKLKASIAALEAK 1826
Cdd:pfam17380 359 KRELERIRQEEIAMEISRMRELERlQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVR 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1827 LREAE-----EQLEIESRERQANGKNLRQKEKKLKDLTIQMEDERKQAQQYKDQaekgnvRVKQLKHQLEEAEEEAQRMA 1901
Cdd:pfam17380 439 RLEEEraremERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQ------RRKILEKELEERKQAMIEEE 512
|
250
....*....|....*.
gi 1604784239 1902 AARRKLQRELDEATEA 1917
Cdd:pfam17380 513 RKRKLLEKEMEERQKA 528
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1493-1933 |
4.94e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.80 E-value: 4.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1493 ARALEENQGALEEAEKtmkgLRADmedLISSKDDVGKSVHDLEKAKRGLEAIVDEMRtqmeELEDELQVAEDaklRLDVN 1572
Cdd:PRK04863 275 MRHANERRVHLEEALE----LRRE---LYTSRRQLAAEQYRLVEMARELAELNEAES----DLEQDYQAASD---HLNLV 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1573 TQALRAQhERELHARDELgEEKRKQLLKQvreleaeleeerkqrgqasgskKKLEGELKDMEDQLEATSRGRDEAVKQLR 1652
Cdd:PRK04863 341 QTALRQQ-EKIERYQADL-EELEERLEEQ----------------------NEVVEEADEQQEENEARAEAAEEEVDELK 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1653 kiqGQVKDLQR--DLEDSRAAQ----KEVLASARESerrSKAMEADIVQLHEMLAAVERARKQAEVERDELSEELASNSS 1726
Cdd:PRK04863 397 ---SQLADYQQalDVQQTRAIQyqqaVQALERAKQL---CGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQA 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1727 GKSLMsDEKRRLDTKISQLEEELEEEQANVESLNdRLRKSQQLVEQLGAeLAAERSTSQSREGSRQQLERQNRELKAKMQ 1806
Cdd:PRK04863 471 AHSQF-EQAYQLVRKIAGEVSRSEAWDVARELLR-RLREQRHLAEQLQQ-LRMRLSELEQRLRQQQRAERLLAEFCKRLG 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1807 EMEgQGRSKLKASIAALEAKLREAEEQLEiESRERQANgknLRQKEKKLKDLTIQMEDERKQAQQYKDqaekgnvRVKQL 1886
Cdd:PRK04863 548 KNL-DDEDELEQLQEELEARLESLSESVS-EARERRMA---LRQQLEQLQARIQRLAARAPAWLAAQD-------ALARL 615
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1604784239 1887 KHQLEEAEEEAQRMAAARRKLQRELDEATEANDTLSRDMASLRSKLR 1933
Cdd:PRK04863 616 REQSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALDEEIE 662
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
848-1396 |
6.32e-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: 47.81 E-value: 6.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 848 LLQVTRQEEEMGQKDEELKAAKEVAAKVETELKDIT-------QKHTQLMEER-AQLEMKLHAETELYAEAEEMRVRLEA 919
Cdd:pfam05557 11 LSQLQNEKKQMELEHKRARIELEKKASALKRQLDREsdrnqelQKRIRLLEKReAEAEEALREQAELNRLKKKYLEALNK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 920 KKQELEEVLHEMESRLEEEEDRSNALH--------------NERKEMEQQLQLMEAHIAEEEDARQKLQMEKVSV---EG 982
Cdd:pfam05557 91 KLNEKESQLADAREVISCLKNELSELRrqiqraelelqstnSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLaeaEQ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 983 KVKKLEEDILMMEDQNNKLQKERKLLeERLADMSSNLAEEEEKSKNLSKLKTKHESMISE---LELRMKKEEKGRLDMEK 1059
Cdd:pfam05557 171 RIKELEFEIQSQEQDSEIVKNSKSEL-ARIPELEKELERLREHNKHLNENIENKLLLKEEvedLKRKLEREEKYREEAAT 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1060 AKRKVEAELGDLQEQHADLQAQLAELRA--QLAAKEEELQATQARLEEecnQRGAAVKRVRELEVLISELQEDLeaeRAA 1137
Cdd:pfam05557 250 LELEKEKLEQELQSWVKLAQDTGLNLRSpeDLSRRIEQLQQREIVLKE---ENSSLTSSARQLEKARRELEQEL---AQY 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1138 RGKVEAARRDLgEELNALRTELEDSLGTTAAQQE-LRAKRE---QEVSMLKKAMEDEGRSHEAqvQDLRQKHSQAVEELT 1213
Cdd:pfam05557 324 LKKIEDLNKKL-KRHKALVRRLQRRVLLLTKERDgYRAILEsydKELTMSNYSPQLLERIEEA--EDMTQKMQAHNEEME 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1214 EQLEQAKRVRAGLEKAKQALEKESADL--SADLRSLASAKQDVEHKKKKVEgqlnelnsrfnESERQRTELGERVSKLTT 1291
Cdd:pfam05557 401 AQLSVAEEELGGYKQQAQTLERELQALrqQESLADPSYSKEEVDSLRRKLE-----------TLELERQRLREQKNELEM 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1292 ELDSVTgLLNEAEGKNIKLskdvsslssqLQDAQELLSEETRQKLNLSGRLRQTEEDRNSLMEQLEEETEAKRAVERQVS 1371
Cdd:pfam05557 470 ELERRC-LQGDYDPKKTKV----------LHLSMNPAAEAYQQRKNQLEKLQAEIERLKRLLKKLEDDLEQVLRLPETTS 538
|
570 580
....*....|....*....|....*.
gi 1604784239 1372 SLNMQ-LSDSKKKLDEMSGTVEALEE 1396
Cdd:pfam05557 539 TMNFKeVLDLRKELESAELKNQRLKE 564
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1323-1871 |
7.01e-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: 7.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1323 DAQELLSEETRQKLNLSGRLRQTEEdrnSLMEQLEEeteaKRAVERQVSSLNMQLSDSKKKLDEMSGTVEALEEGKKRLQ 1402
Cdd:pfam07111 42 DGQGPGRRGRSLELEGSQALSQQAE---LISRQLQE----LRRLEEEVRLLRETSLQQKMRLEAQAMELDALAVAEKAGQ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1403 RELEAANSDYEEKASAYDKLEKSRGRMQQELEDVlmdldSQRQLVSNLEKKQKKFDQMLAEERAVSCKFAEERDRAEAEA 1482
Cdd:pfam07111 115 AEAEGLRAALAGAEMVRKNLEEGSQRELEEIQRL-----HQEQLSSLTQAHEEALSSLTSKAEGLEKSLNSLETKRAGEA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1483 REketrvlaLARALEENQGALEEAEKTMKGLRADMEDLISSKDDVGKSV-HDLEKAKRGLE--AIVDEMRTQMEELEDEL 1559
Cdd:pfam07111 190 KQ-------LAEAQKEAELLRKQLSKTQEELEAQVTLVESLRKYVGEQVpPEVHSQTWELErqELLDTMQHLQEDRADLQ 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1560 QVAEDAKLRLDVNTQALRAQHE---RELHARDELGEE---KRKQLLKQVRELEAELEEERK-QRGQASGSKKKLEGELKD 1632
Cdd:pfam07111 263 ATVELLQVRVQSLTHMLALQEEeltRKIQPSDSLEPEfpkKCRSLLNRWREKVFALMVQLKaQDLEHRDSVKQLRGQVAE 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1633 MEDQLeaTSRGRDEAVKQlRKIQGQVKDLQRDLEDSRAAQKEvLASARESERRSK---------------AMEADIVQLH 1697
Cdd:pfam07111 343 LQEQV--TSQSQEQAILQ-RALQDKAAEVEVERMSAKGLQME-LSRAQEARRRQQqqtasaeeqlkfvvnAMSSTQIWLE 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1698 EMLAAVERARKQAEVERDELSEELASNSSGKSLMS----------------------------------DEKRRLDTKIS 1743
Cdd:pfam07111 419 TTMTRVEQAVARIPSLSNRLSYAVRKVHTIKGLMArkvalaqlrqescpppppappvdadlsleleqlrEERNRLDAELQ 498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1744 ------QLEEELEEEQANVE---------SLNDRLRKSQQLVEQLGAEL-AAERSTSQSREGS---RQQLERQNRELKAK 1804
Cdd:pfam07111 499 lsahliQQEVGRAREQGEAErqqlsevaqQLEQELQRAQESLASVGQQLeVARQGQQESTEEAaslRQELTQQQEIYGQA 578
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1604784239 1805 MQEMEGQGRSKLKASIAALEAKLREA-EEQLEIESRERQANGKNLRQKEKKLKDLTIQMEDERKQAQQ 1871
Cdd:pfam07111 579 LQEKVAEVETRLREQLSDTKRRLNEArREQAKAVVSLRQIQHRATQEKERNQELRRLQDEARKEEGQR 646
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1629-1933 |
7.95e-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: 7.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1629 ELKDMEDQLEATSRGRDEAVKQLRKIQGQVKDLQRDLEDSRAAQKEVLASARESERRSKAMEADIVQLHEMLA----AVE 1704
Cdd:pfam07888 42 ERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSeekdALL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1705 RARKQAEVERDELSEELASNSSGKSLMSDEKRRLDTKISQLEEELEEEQANVESLNDRLRKSQQLVEQLGAELAAERSTS 1784
Cdd:pfam07888 122 AQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1785 QSREGSRQQLERQNRELKAKMQEMEgqgrsKLKASIAALEAKLREAEEQLEIESRERQANGKNLR--------------- 1849
Cdd:pfam07888 202 AQRDTQVLQLQDTITTLTQKLTTAH-----RKEAENEALLEELRSLQERLNASERKVEGLGEELSsmaaqrdrtqaelhq 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1850 ------QKEKKLKDLTIQMEDERKQAQQYKD----QAEKGNVRVKQLKHQLEEAEEEAQRMAAARRKLQRELDEATEAN- 1918
Cdd:pfam07888 277 arlqaaQLTLQLADASLALREGRARWAQEREtlqqSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNr 356
|
330
....*....|....*...
gi 1604784239 1919 ---DTLSRDMASLRSKLR 1933
Cdd:pfam07888 357 vqlSESRRELQELKASLR 374
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1613-1856 |
8.03e-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: 8.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1613 RKQRGQASGSKKKLEGELKDMEDQLEATSRGRDEAVKQLRKIQGQVKDLQRDLEdsraaqkevlasareserrskAMEAD 1692
Cdd:COG3883 22 QKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIA---------------------EAEAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1693 IVQLHEMLAAVERARKQAEVERDELSEELASNSsgkslmsdekrrLDTKISQLEEELEEEQANVESLNDrLRKSQQLVEQ 1772
Cdd:COG3883 81 IEERREELGERARALYRSGGSVSYLDVLLGSES------------FSDFLDRLSALSKIADADADLLEE-LKADKAELEA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1773 LGAELAAErstsqsregsRQQLERQNRELKAKMQEMEGQgRSKLKASIAALEAKLREAEEQLEIESRERQANGKNLRQKE 1852
Cdd:COG3883 148 KKAELEAK----------LAELEALKAELEAAKAELEAQ-QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
....
gi 1604784239 1853 KKLK 1856
Cdd:COG3883 217 AAAA 220
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1208-1468 |
9.05e-05 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 47.26 E-value: 9.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1208 AVEELTEQLEQAKRVRAGLEKAKQALEKESADLSADLRSLASAKQDVEHKKKKVEGQLNELNSRFNESE-----RQRTEL 1282
Cdd:COG5185 234 ALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTksidiKKATES 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1283 GERVSKLTTELDSVTGLLNEAEGKNIKLSKDVSSLSSQLQDAQELLSEEtRQKLNLSGRLRQTEEDRNSLMEQLEEETE- 1361
Cdd:COG5185 314 LEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEE-IENIVGEVELSKSSEELDSFKDTIESTKEs 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1362 ---AKRAVERQVSSLNMQLSDSKKKLDEMSgtvealeegkKRLQRELEAANSDYEEKASAYDKLEKSRGRMQQELEDVLM 1438
Cdd:COG5185 393 ldeIPQNQRGYAQEILATLEDTLKAADRQI----------EELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQ 462
|
250 260 270
....*....|....*....|....*....|
gi 1604784239 1439 DLDSQRQLVSNLEKKQKKFDQMLAEERAVS 1468
Cdd:COG5185 463 SRLEEAYDEINRSVRSKKEDLNEELTQIES 492
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1062-1716 |
1.05e-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: 47.44 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1062 RKVEAELGDLQEQHADLQA-QLAELRaqlaakeeelqatqaRLEEECNQ-RGAAVKRVRELEVLISELQEDLEAERAARG 1139
Cdd:pfam07111 51 RSLELEGSQALSQQAELISrQLQELR---------------RLEEEVRLlRETSLQQKMRLEAQAMELDALAVAEKAGQA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1140 KVEAARRDL-GEELnaLRTELEDslGTTAAQQELRAKREQEVSMLKKAMED-------EGRSHEAQVQDLRQKHSQAVEE 1211
Cdd:pfam07111 116 EAEGLRAALaGAEM--VRKNLEE--GSQRELEEIQRLHQEQLSSLTQAHEEalssltsKAEGLEKSLNSLETKRAGEAKQ 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1212 LTEQLEQAKRVRAGLEKAKQALEKEsADLSADLRSLASAKQDVEHKKKKVEGQLNELNSRFNESERQRTELGERVSKLTT 1291
Cdd:pfam07111 192 LAEAQKEAELLRKQLSKTQEELEAQ-VTLVESLRKYVGEQVPPEVHSQTWELERQELLDTMQHLQEDRADLQATVELLQV 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1292 ELDSVTGLLNEAEGKNIKLSKDVSSLSSQL-QDAQELLSEETRQKLNLSGRLRQTEEDRNSLMEQLEEETEAkraVERQV 1370
Cdd:pfam07111 271 RVQSLTHMLALQEEELTRKIQPSDSLEPEFpKKCRSLLNRWREKVFALMVQLKAQDLEHRDSVKQLRGQVAE---LQEQV 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1371 SSLNMQLSDSKKKLDEMSGTVEALEEGKKRLQRELeaansdyeekasayDKLEKSRGRMQQELEDVLMDLdsqRQLVSNL 1450
Cdd:pfam07111 348 TSQSQEQAILQRALQDKAAEVEVERMSAKGLQMEL--------------SRAQEARRRQQQQTASAEEQL---KFVVNAM 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1451 EKKQKKFDQMLAEERAVSCKFAEERDRAEAEAREKETRVLALARALEENQGALEEAEKTMKGLRADMEdlisskddvgks 1530
Cdd:pfam07111 411 SSTQIWLETTMTRVEQAVARIPSLSNRLSYAVRKVHTIKGLMARKVALAQLRQESCPPPPPAPPVDAD------------ 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1531 vhdlekakrgleaivdemrtqmeeLEDELQVAEDAKLRLDVNTQALRAQHERELHARDELGEEKRKQLLKQVRELEAELe 1610
Cdd:pfam07111 479 ------------------------LSLELEQLREERNRLDAELQLSAHLIQQEVGRAREQGEAERQQLSEVAQQLEQEL- 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1611 eerkQRGQASGSK--KKLEGELKDMEDQLEATSRGRDEAVKQLR---------------KIQGQVKDLQRDLEDSRAAQK 1673
Cdd:pfam07111 534 ----QRAQESLASvgQQLEVARQGQQESTEEAASLRQELTQQQEiygqalqekvaevetRLREQLSDTKRRLNEARREQA 609
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 1604784239 1674 EVLASARESERRS---KAMEADIVQLHEMLAAVER---ARKQAEVERDE 1716
Cdd:pfam07111 610 KAVVSLRQIQHRAtqeKERNQELRRLQDEARKEEGqrlARRVQELERDK 658
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
661-685 |
1.06e-04 |
|
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: 44.64 E-value: 1.06e-04
10 20
....*....|....*....|....*
gi 1604784239 661 YKESLGKLMTTLHNTQPNFVRCIIP 685
Cdd:cd01363 146 INESLNTLMNVLRATRPHFVRCISP 170
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1543-1934 |
1.22e-04 |
|
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: 47.27 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1543 AIVDEMRTQMEELEDELQVAED-AKLRLDVNTQALRAQHERELHARDELGEEKRKQ-LLKQVRELEAELEEERKQRGQAS 1620
Cdd:TIGR00618 187 AKKKSLHGKAELLTLRSQLLTLcTPCMPDTYHERKQVLEKELKHLREALQQTQQSHaYLTQKREAQEEQLKKQQLLKQLR 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1621 GSKKKLEGELKDMEDQLEATSRGRDEA-----VKQLRKIQGQVKDLQRDLEDSRAAQKEVLASARESERRSKAMEADIVQ 1695
Cdd:TIGR00618 267 ARIEELRAQEAVLEETQERINRARKAAplaahIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1696 LHEMLAAVERARKQAEVE---RDELSEELASNSSGKSLMSDEKRRLDTK--ISQLEEELEEEQANVESLNDRLR------ 1764
Cdd:TIGR00618 347 LQTLHSQEIHIRDAHEVAtsiREISCQQHTLTQHIHTLQQQKTTLTQKLqsLCKELDILQREQATIDTRTSAFRdlqgql 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1765 ---KSQQLVEQLGAELAAERSTSQS-----REGSRQQLERQNRELKAKMQEMEGQGRSKLKASIAALEAKLREAEEQLEI 1836
Cdd:TIGR00618 427 ahaKKQQELQQRYAELCAAAITCTAqceklEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPL 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1837 ESRERQANGK-------------------NLRQKEKKLKDLTIQMEDERKQAQQYKDQAEKGNVRVKQLKHQLEEAEEEA 1897
Cdd:TIGR00618 507 CGSCIHPNPArqdidnpgpltrrmqrgeqTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDI 586
|
410 420 430
....*....|....*....|....*....|....*..
gi 1604784239 1898 QRMAAARRKLQRELDEATEANDTLSRDMASLRSKLRH 1934
Cdd:TIGR00618 587 PNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQP 623
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1115-1268 |
1.27e-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: 45.69 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1115 KRVRELEVLISELQEDLEAERAARGKVEAARRDLGEELNALRTELEDSLGTTAAQQELRAKREQEVSMLKKAMEDEGRSH 1194
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEALQK 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1604784239 1195 EaqVQDLRQKHSQAVEELTEQLEQAKRVRAGLEKAKQALEKESADLSADLRSLASAKQDVEHKKKKVEGQLNEL 1268
Cdd:COG1579 97 E--IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREEL 168
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1042-1157 |
1.31e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 46.77 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1042 ELELRMKKEEKGRLDMEKAKRKVEAELGDLQEQHADLQAQLAELRAQLAAKEEELQATQARLEEECNQRGAAVKRVRELE 1121
Cdd:COG2433 389 ELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREIRKDREIS 468
|
90 100 110
....*....|....*....|....*....|....*.
gi 1604784239 1122 VLISELqEDLEAERAargKVEAARRDLGEELNALRT 1157
Cdd:COG2433 469 RLDREI-ERLERELE---EERERIEELKRKLERLKE 500
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1065-1218 |
1.46e-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: 45.90 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1065 EAELGDLQEQHADLQAQLAELRAQLAAKEEELQATQARLEEEcnqrgaavkrVRELEVLISELQEDLEAERAARGKVEAA 1144
Cdd:pfam09787 46 TLELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQEE----------AESSREQLQELEEQLATERSARREAEAE 115
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1604784239 1145 RRDLGEELNALRTELEDSLGTTaaqQELRAKREQEVSMLKKAMEDEGRSHEAQvQDLRQKhsqaVEELTEQLEQ 1218
Cdd:pfam09787 116 LERLQEELRYLEEELRRSKATL---QSRIKDREAEIEKLRNQLTSKSQSSSSQ-SELENR----LHQLTETLIQ 181
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1459-1780 |
1.48e-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: 46.21 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1459 QMLAEERAVSCKFAEERDRAEAEAREKETRVLALARALEENQGALEEAEKTMKGLRADMEDLISSKDDVGKSVHDLEKAK 1538
Cdd:pfam19220 55 ALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDKTAQAEALERQLAAETEQN 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1539 RGLEAIVDEMRTQMEELEDELQVAE----DAKLRLDVNTQALRAQHER---------ELHARDELGEEKRKQLLKQVREL 1605
Cdd:pfam19220 135 RALEEENKALREEAQAAEKALQRAEgelaTARERLALLEQENRRLQALseeqaaelaELTRRLAELETQLDATRARLRAL 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1606 EAELEEERKQRGQASG----SKKKLEGELKDMEDQLEATSrGRDEAVKQLrkiQGQVKDLQRDLEDS-RAAQ---KEVLA 1677
Cdd:pfam19220 215 EGQLAAEQAERERAEAqleeAVEAHRAERASLRMKLEALT-ARAAATEQL---LAEARNQLRDRDEAiRAAErrlKEASI 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1678 SARESERRSKAMEADIVQLHEMLAAVERARKQAEVERDELSEELASNssgkslmsdekrrlDTKISQLEEELEEEQANVE 1757
Cdd:pfam19220 291 ERDTLERRLAGLEADLERRTQQFQEMQRARAELEERAEMLTKALAAK--------------DAALERAEERIASLSDRIA 356
|
330 340
....*....|....*....|...
gi 1604784239 1758 SLNDRLRKSQQLVEQLGAELAAE 1780
Cdd:pfam19220 357 ELTKRFEVERAALEQANRRLKEE 379
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1306-1887 |
1.49e-04 |
|
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: 46.94 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1306 KNIKLSKD--VSSLSSQLQDAQELLSEETRQKLNLSGRLRQTEEDRNSLMEQLEEeteakraVERQVSSLNMQLSDSKKK 1383
Cdd:TIGR04523 25 KNIANKQDteEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKI-------LEQQIKDLNDKLKKNKDK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1384 LDEmsgtveaLEEGKKRLQRELEAANSDYEEKASAYDKLEKSRGRMQQELEDVLMDLdsqRQLVSNLEKKQKKFDQMLAE 1463
Cdd:TIGR04523 98 INK-------LNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEI---KKKEKELEKLNNKYNDLKKQ 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1464 ERAVSckfaEERDRAEAEAREKETRVLALA---RALEENQGALEEAEKTMKGLRADMEDLISSKDDVGKSVHDLEKAKRG 1540
Cdd:TIGR04523 168 KEELE----NELNLLEKEKLNIQKNIDKIKnklLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1541 LEAIVDEMRTQMEELEDELQvaedaklrlDVNTQALRAQHERELHardelgEEKRKQLLKQVRELEAELEEERKQRGQas 1620
Cdd:TIGR04523 244 KTTEISNTQTQLNQLKDEQN---------KIKKQLSEKQKELEQN------NKKIKELEKQLNQLKSEISDLNNQKEQ-- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1621 GSKKKLEGELKDMEDQLEATSRGRDEAVKQLRKIQGQVKDLQRDLEDSraaqkevlasarESERRSKAMeadivQLHEML 1700
Cdd:TIGR04523 307 DWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNS------------ESENSEKQR-----ELEEKQ 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1701 AAVERARKQAEVERDELseelasnssgKSLMSdEKRRLDTKISQLEEELEEEQANVESLNDRLRKSQQLVEQLGAELAAE 1780
Cdd:TIGR04523 370 NEIEKLKKENQSYKQEI----------KNLES-QINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKN 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1781 RSTSQSregsrqqLERQNRELKAKMQEmegqgrskLKASIAALEAKLREAEEQLEIESRERQANGKNLRQKEKKLKDLTI 1860
Cdd:TIGR04523 439 NSEIKD-------LTNQDSVKELIIKN--------LDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNE 503
|
570 580
....*....|....*....|....*..
gi 1604784239 1861 QMEDERKQAQQYKDQAEKGNVRVKQLK 1887
Cdd:TIGR04523 504 EKKELEEKVKDLTKKISSLKEKIEKLE 530
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1058-1507 |
1.73e-04 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 46.44 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1058 EKAKRKVEAELGDLQEQHAD---LQAQLAELRAQLAAKEEELQATQARLEEECNQRGAAVKRVRELEVLISELQEDLEAE 1134
Cdd:COG5278 82 EEARAEIDELLAELRSLTADnpeQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1135 RAARGKVEAARRDLGEELNALRTELEDSLGTTAAQQELRAKREQEVSMLKKAMEDEGRSHEAQVQDLRQKHSQAVEELTE 1214
Cdd:COG5278 162 ALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALA 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1215 QLEQAKRVRAGLEKAKQALEKESADLSADLRSLASAKQDVEhkkkKVEGQLNELNSRFNESERQRTELGERVSKLTTELD 1294
Cdd:COG5278 242 LALLLAALLLALLAALALAALLAAALLALAALLLALAAAAA----LAAAAALELAAAEALALAELELELLLAAAAAAAAA 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1295 SVTGLLNEAEGKNIKLSKDVSSLSSQLQDAQELLSEETRQKLNLSGRLRQTEEDRNSLMEQLEEETEAKRAVERQVSSLN 1374
Cdd:COG5278 318 AAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAA 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1375 MQLSDSKKKLDEMSGTVEALEEGKKRLQRELEAANSDYEEKASAYDKLEKSRGRMQQELEDVLMDLDSQRQLVSNLEKKQ 1454
Cdd:COG5278 398 AAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAAL 477
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1604784239 1455 KKFDQMLAEERAVSCKFAEERDRAEAEAREKETRVLALARALEENQGALEEAE 1507
Cdd:COG5278 478 AAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAALASAEL 530
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1001-1126 |
1.81e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 45.73 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1001 LQKERKL-LEERLADMSSNLAEEEEKSKNLSKLKTKHESMISELELRmKKEEKGRLDMEKAkrkVEAELgdlQEQHADLQ 1079
Cdd:PRK09039 71 LERQGNQdLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGR-AGELAQELDSEKQ---VSARA---LAQVELLN 143
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1604784239 1080 AQLAELRAQLAAKEEELQATQARLEEECNQ--------RGAAVKRVRELEVLISE 1126
Cdd:PRK09039 144 QQIAALRRQLAALEAALDASEKRDRESQAKiadlgrrlNVALAQRVQELNRYRSE 198
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
1042-1417 |
2.02e-04 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 46.25 E-value: 2.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1042 ELELRMKKEEKGRLDMEKAKRKVEAELGDlqeqhadlqaQLAELRAQLAAKEEELQATQARLEEecnqrgaAVKRVRELE 1121
Cdd:pfam03528 5 DLQQRVAELEKENAEFYRLKQQLEAEFNQ----------KRAKFKELYLAKEEDLKRQNAVLQE-------AQVELDALQ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1122 VLISELQEDLE--------AERAARGKVEAARRDLGEELNALRTELEDSLGTTAAQQELRAkrEQEVSMLKKAMEdegrS 1193
Cdd:pfam03528 68 NQLALARAEMEnikavatvSENTKQEAIDEVKSQWQEEVASLQAIMKETVREYEVQFHRRL--EQERAQWNQYRE----S 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1194 HEAQVQDLRQKHSQAVEE--LTEQLEQAKRVRAGLEKAKQALEKESADLSADLRSLASAKQDVEHKKKKvegqlnELNSR 1271
Cdd:pfam03528 142 AEREIADLRRRLSEGQEEenLEDEMKKAQEDAEKLRSVVMPMEKEIAALKAKLTEAEDKIKELEASKMK------ELNHY 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1272 FNESERQRTELGERVSKLTTElDSVtgllneaegknikLSKDVSSLSSQLQDAQELLSEETRQKlnlsGRLRQTEEDRNs 1351
Cdd:pfam03528 216 LEAEKSCRTDLEMYVAVLNTQ-KSV-------------LQEDAEKLRKELHEVCHLLEQERQQH----NQLKHTWQKAN- 276
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1604784239 1352 lmeqlEEETEAKRAVERQVSSLNMQLSDSKKKLDEMSGTVEALEEGKKRLQRELEAANSDYEEKAS 1417
Cdd:pfam03528 277 -----DQFLESQRLLMRDMQRMESVLTSEQLRQVEEIKKKDQEEHKRARTHKEKETLKSDREHTVS 337
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1478-1932 |
2.09e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.60 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1478 AEAEAREKETRVLALARALEENQGALEEAEKTMKGLRADMEDLISSKDDVGKsvhdLEKAKRGLEAIVDEMRTQMEELED 1557
Cdd:PRK03918 198 KEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELES----LEGSKRKLEEKIRELEERIEELKK 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1558 ELQVAEDAKLRLdvntqalraqheRELHARDELGEEKRKQLLKQVRELEAELEEERKQRGQASGSKKKLEgELKDMEDQL 1637
Cdd:PRK03918 274 EIEELEEKVKEL------------KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIK-ELEEKEERL 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1638 EATSRGRDEAVKQLRKIQGQVKDLQRdledsraaQKEVLASARESERRSKAMEADivQLHEMLAAVERARKQAEVERDEL 1717
Cdd:PRK03918 341 EELKKKLKELEKRLEELEERHELYEE--------AKAKKEELERLKKRLTGLTPE--KLEKELEELEKAKEEIEEEISKI 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1718 SEELASNSS----------------------GKSLMSDEKRRLDTKISQLEEELEEEQANVESLNDRLRKSQQLVEQL-- 1773
Cdd:PRK03918 411 TARIGELKKeikelkkaieelkkakgkcpvcGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVlk 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1774 -GAELAAERSTSQSREGSRQQLERQNRE-LKAKMQEMEGQGRS--KLKASIAALEAKLREAEEqLEIESRERQANGKNLR 1849
Cdd:PRK03918 491 kESELIKLKELAEQLKELEEKLKKYNLEeLEKKAEEYEKLKEKliKLKGEIKSLKKELEKLEE-LKKKLAELEKKLDELE 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1850 QK----EKKLKDLTIQMEDERKQAQQYKDQAEKGNVRVKQLKHQLeeaeeeaQRMAAARRKLQRELDEATEANDTLSRDM 1925
Cdd:PRK03918 570 EElaelLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKEL-------EREEKELKKLEEELDKAFEELAETEKRL 642
|
....*..
gi 1604784239 1926 ASLRSKL 1932
Cdd:PRK03918 643 EELRKEL 649
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1046-1255 |
2.37e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 45.57 E-value: 2.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1046 RMKKEEKGRLDMEKAKRKVEAELGD-LQEQHADLQAQLAELRAQ-LAAKEEELQATQARLEEECNQRGAAVKRVRELEV- 1122
Cdd:PRK09510 66 RQQQQQKSAKRAEEQRKKKEQQQAEeLQQKQAAEQERLKQLEKErLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAa 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1123 -LISELQEDLEAERAARGKVEAARRDLGEelnalrteledslgtTAAQQELRAKREQEVSMLKKAMEDEgrshEAQVQDL 1201
Cdd:PRK09510 146 kAKAEAEAKRAAAAAKKAAAEAKKKAEAE---------------AAKKAAAEAKKKAEAEAAAKAAAEA----KKKAEAE 206
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1604784239 1202 RQKHSQAVEELTEQLEQAKRVRAGLEKAKQALEKESADLSADLRSLASAKQDVE 1255
Cdd:PRK09510 207 AKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEVD 260
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1217-1366 |
2.68e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.92 E-value: 2.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1217 EQAKRVRAGLEKAKQALEKESadlsadlrsLASAKQDVEHKKKKVEgqlNELNSRFNESERQRTELGERVSKLTTELDSV 1296
Cdd:PRK12704 38 EEAKRILEEAKKEAEAIKKEA---------LLEAKEEIHKLRNEFE---KELRERRNELQKLEKRLLQKEENLDRKLELL 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1297 TGLLNEAEGKNIKLSKDVSSLSSQLQDAQELLSEETRQKLNLSGRlrQTEEDRNSLMEQLEEETEAKRAV 1366
Cdd:PRK12704 106 EKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGL--TAEEAKEILLEKVEEEARHEAAV 173
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1188-1603 |
2.71e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.10 E-value: 2.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1188 EDEGRSHEAQVQDLRQKHSQAVEELTEQLEQAKRVRAGLEkakqALEKESADLSADLRS----LASAKQDVEHKKK--KV 1261
Cdd:PRK04863 278 ANERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELA----ELNEAESDLEQDYQAasdhLNLVQTALRQQEKieRY 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1262 EGQLNELNSRFNESERQRTELGERVSKLTTELDsvtgllnEAEgkniklsKDVSSLSSQLQDAQELLSE-ETR-----QK 1335
Cdd:PRK04863 354 QADLEELEERLEEQNEVVEEADEQQEENEARAE-------AAE-------EEVDELKSQLADYQQALDVqQTRaiqyqQA 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1336 LNLSGRLRQTEEDRNSLMEQLEEETEAKRAVERQVSslnmqlsdskkkldemsgtvEALEEGKKRLqRELEAANSDYEEK 1415
Cdd:PRK04863 420 VQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEAT--------------------EELLSLEQKL-SVAQAAHSQFEQA 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1416 ASAYDKL--EKSRGRMQQELEDVLMDLDSQRQL---VSNLEKKQKKFDQMLAEERAVsckfaeERDRAEAEAR--EKETR 1488
Cdd:PRK04863 479 YQLVRKIagEVSRSEAWDVARELLRRLREQRHLaeqLQQLRMRLSELEQRLRQQQRA------ERLLAEFCKRlgKNLDD 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1489 VLALARALEENQGALEEAEKTMKGLRADMEDLISSKDDVGKSVHDLEK---AKRGLEAIVDEMRTQM-EELEDELQVAEd 1564
Cdd:PRK04863 553 EDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAArapAWLAAQDALARLREQSgEEFEDSQDVTE- 631
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1604784239 1565 akLRLDVntqalrAQHERELH-ARDELgEEKRKQLLKQVR 1603
Cdd:PRK04863 632 --YMQQL------LERERELTvERDEL-AARKQALDEEIE 662
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1681-1933 |
2.74e-04 |
|
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: 46.21 E-value: 2.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1681 ESERRSKAMEADIVQLHEMLAAVERARKQAEvERDELSEELASN-----SSGKSLMSDEKRRLDTKISQLEEELEEEQAN 1755
Cdd:TIGR02169 181 EVEENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEKREYegyelLKEKEALERQKEAIERQLASLEEELEKLTEE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1756 VESLNDRLRKSQQLVEQLGAELAAERSTSQSR--------EGSRQQLERQNRELKAKMQEMEGQgRSKLKASIAALEAKL 1827
Cdd:TIGR02169 260 ISELEKRLEEIEQLLEELNKKIKDLGEEEQLRvkekigelEAEIASLERSIAEKERELEDAEER-LAKLEAEIDKLLAEI 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1828 REAEEQLEIESRERQANGKNLRQKEKKLKDLTIQMEDERKQAQQYKDQAekgnvrvkqlkhqleeaeeeaqrmaaarRKL 1907
Cdd:TIGR02169 339 EELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDEL----------------------------KDY 390
|
250 260
....*....|....*....|....*.
gi 1604784239 1908 QRELDEATEANDTLSRDMASLRSKLR 1933
Cdd:TIGR02169 391 REKLEKLKREINELKRELDRLQEELQ 416
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1319-1505 |
2.94e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 45.45 E-value: 2.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1319 SQLQDAQELLSEETRqklnlsgRLRQTEEDRNSLMEQLEEETEAKRAVERQVSSLNMQLSDSKKKLDEMSGTVEALEEGK 1398
Cdd:PRK11637 47 DQLKSIQQDIAAKEK-------SVRQQQQQRASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQIDELNASIAKLEQQQ 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1399 KR----LQRELEAA----------------NSDYEEKASAY-DKLEKSRGRMQQELEDVLMDLDSQRQLvsnLEKKQKKF 1457
Cdd:PRK11637 120 AAqerlLAAQLDAAfrqgehtglqlilsgeESQRGERILAYfGYLNQARQETIAELKQTREELAAQKAE---LEEKQSQQ 196
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1604784239 1458 DQMLAEERAVSCKFAEERDraeaeAREKEtrVLALARALEENQGALEE 1505
Cdd:PRK11637 197 KTLLYEQQAQQQKLEQARN-----ERKKT--LTGLESSLQKDQQQLSE 237
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1592-1887 |
3.00e-04 |
|
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: 45.66 E-value: 3.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1592 EEKRKQLLKQVRELEAELEEERKQRGQASGSKKKLEGELKDMEDQLEATSRGRDEAVKQLRKIQGQVKDLQRDLEDSRAA 1671
Cdd:pfam07888 37 EECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1672 QKEVLASARESERRSKAMEADI-----------VQLHEMLAAVERA---RKQAEVERDELSEELASNSSGKSLMSDEKRR 1737
Cdd:pfam07888 117 KDALLAQRAAHEARIRELEEDIktltqrvlereTELERMKERAKKAgaqRKEEEAERKQLQAKLQQTEEELRSLSKEFQE 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1738 LDTKISQLEEELEEEQANVESLNDRLRKSQQLVEQLGAELAAERSTSQSREGSRQQLERQNRELkAKMQEMEGQGRSKL- 1816
Cdd:pfam07888 197 LRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEEL-SSMAAQRDRTQAELh 275
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1604784239 1817 KASIAALEAKLREAEEQLEIE------SRERQANGKNLRQKEKKLKDLTIQMEDERKQAQQYKDQAEKGNVRVKQLK 1887
Cdd:pfam07888 276 QARLQAAQLTLQLADASLALRegrarwAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELGREK 352
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
882-1332 |
3.08e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 45.95 E-value: 3.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 882 ITQKHTQLMEERAQLEMKLHAETELYAEAEEMRVRLEAKKQELEEVLHEmesrleeeedrsnalHNERKEMEQQLQLMEA 961
Cdd:PRK10246 306 LAHTRQQIEEVNTRLQSTMALRARIRHHAAKQSAELQAQQQSLNTWLAE---------------HDRFRQWNNELAGWRA 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 962 HIAEEEDARQKLQMEKVSVEGKVKKLE-----------EDILMMEDQNNKLQKERK---LLEERLADMSSNLAEEEEKSK 1027
Cdd:PRK10246 371 QFSQQTSDREQLRQWQQQLTHAEQKLNalpaitltltaDEVAAALAQHAEQRPLRQrlvALHGQIVPQQKRLAQLQVAIQ 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1028 NLSKLKTKHESMISELELRMKKEEKGRLDMeKAKRKVEAELGDLQEQHADLQA-QLAELRAqlAAKEEELQATQArLEEE 1106
Cdd:PRK10246 451 NVTQEQTQRNAALNEMRQRYKEKTQQLADV-KTICEQEARIKDLEAQRAQLQAgQPCPLCG--STSHPAVEAYQA-LEPG 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1107 CNQRgaavkRVRELEVLISELQEDleaERAARGKVEAARRDLGEELNALRTELEDSLGTTAAQQELRA------KREQEV 1180
Cdd:PRK10246 527 VNQS-----RLDALEKEVKKLGEE---GAALRGQLDALTKQLQRDESEAQSLRQEEQALTQQWQAVCAslnitlQPQDDI 598
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1181 SMLKKAMEDegrsHEAQVQDLRQKHS-QAveELTEQLEQAKRVRAGLEKAKQALEkesADLSAdlRSLASAKQDVEhkkk 1259
Cdd:PRK10246 599 QPWLDAQEE----HERQLRLLSQRHElQG--QIAAHNQQIIQYQQQIEQRQQQLL---TALAG--YALTLPQEDEE---- 663
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1260 kvEGQLNELNSRFNESERQRTELG---ERVSKLTTELDSV--TGLLNEAEGKNI-----KLSKDVSSLSSQLQDAQELLS 1329
Cdd:PRK10246 664 --ASWLATRQQEAQSWQQRQNELTalqNRIQQLTPLLETLpqSDDLPHSEETVAldnwrQVHEQCLSLHSQLQTLQQQDV 741
|
...
gi 1604784239 1330 EET 1332
Cdd:PRK10246 742 LEA 744
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1552-1929 |
3.14e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.90 E-value: 3.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1552 MEELEdELQVAEDAKLRLDVNTQALRAQHERELHARDELGEEKRkqlLKQVRELEAELEEERKQRGQASGSKKKLEGELK 1631
Cdd:PTZ00121 1029 IEELT-EYGNNDDVLKEKDIIDEDIDGNHEGKAEAKAHVGQDEG---LKPSYKDFDFDAKEDNRADEATEEAFGKAEEAK 1104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1632 DMEDQLEATSRGRDEAVKQLRKIqgqvkdlqRDLEDSRAAQKevlasARESERRSKAMEADIVqlhEMLAAVERARKQAE 1711
Cdd:PTZ00121 1105 KTETGKAEEARKAEEAKKKAEDA--------RKAEEARKAED-----ARKAEEARKAEDAKRV---EIARKAEDARKAEE 1168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1712 VERDELSEELASNSSGKSLMSDEKRRldtKISQLEEELEEEQANVESLNDRLRKSQQlVEQLGAELAAERSTSQSREGSR 1791
Cdd:PTZ00121 1169 ARKAEDAKKAEAARKAEEVRKAEELR---KAEDARKAEAARKAEEERKAEEARKAED-AKKAEAVKKAEEAKKDAEEAKK 1244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1792 QQLERQNRELKaKMQEMEGQGRSKLKASIAALEAK----------LREAEEQLEIESRERQANGKNLRQKEKKLKDLTIQ 1861
Cdd:PTZ00121 1245 AEEERNNEEIR-KFEEARMAHFARRQAAIKAEEARkadelkkaeeKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKK 1323
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1604784239 1862 MEDERKQAQQYKDQAEKGNVRVKQLKHQLEEAEEEAQRMAAARRKLQRELDEATEANDTLSRDMASLR 1929
Cdd:PTZ00121 1324 AEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKK 1391
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
885-1367 |
3.16e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 45.95 E-value: 3.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 885 KHTQLMEERAQLE---MKLHAE-TELYAEAEEMRVRLEAKKQELEEVlhemeSRLEEEEDRSNALHNERKEME--QQLQL 958
Cdd:PRK10246 434 QIVPQQKRLAQLQvaiQNVTQEqTQRNAALNEMRQRYKEKTQQLADV-----KTICEQEARIKDLEAQRAQLQagQPCPL 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 959 --------MEAHIAEEEDARQ--KLQMEKvsvegKVKKLEEDILMMEDQNNKLQKERklleERLADMSSNLAEEEEKskn 1028
Cdd:PRK10246 509 cgstshpaVEAYQALEPGVNQsrLDALEK-----EVKKLGEEGAALRGQLDALTKQL----QRDESEAQSLRQEEQA--- 576
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1029 lskLKTKHESMISELELRMKKEEKGRLDMEKAKRKvEAELGDLQEQHAdLQAQLAELRAQLAAKEEELQATQARLEEECN 1108
Cdd:PRK10246 577 ---LTQQWQAVCASLNITLQPQDDIQPWLDAQEEH-ERQLRLLSQRHE-LQGQIAAHNQQIIQYQQQIEQRQQQLLTALA 651
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1109 QRGAAVKRVRELEVLISELQEdlEAERAARGKVEAARrdLGEELNALRTELEdslgTTAAQQELRAKREQEVSMLKKAME 1188
Cdd:PRK10246 652 GYALTLPQEDEEASWLATRQQ--EAQSWQQRQNELTA--LQNRIQQLTPLLE----TLPQSDDLPHSEETVALDNWRQVH 723
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1189 DEGRSHEAQVQDLRQkhsqaveELTEQLEQAKRVRAGLEKAKQAleKESADLSADLRSL--ASAKQDVEHKKKKVEGQLN 1266
Cdd:PRK10246 724 EQCLSLHSQLQTLQQ-------QDVLEAQRLQKAQAQFDTALQA--SVFDDQQAFLAALldEETLTQLEQLKQNLENQRQ 794
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1267 ELNSRFNESERQrtelgervskLTTELDSVTGLLNEAegkniklsKDVSSLSSQLQDAQELLSEETRQKLNLSGRLRQTE 1346
Cdd:PRK10246 795 QAQTLVTQTAQA----------LAQHQQHRPDGLDLT--------VTVEQIQQELAQLAQQLRENTTRQGEIRQQLKQDA 856
|
490 500
....*....|....*....|.
gi 1604784239 1347 EDRNSLMEQLEEETEAKRAVE 1367
Cdd:PRK10246 857 DNRQQQQALMQQIAQATQQVE 877
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1753-1933 |
3.32e-04 |
|
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: 45.14 E-value: 3.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1753 QANVESLNDRLRKSQQLVEQLGAELAAERSTSQSREGSRQQLERQNRELKA---KMQEMEGQgRSKLKASIAALEAKLRE 1829
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAAlarRIRALEQE-LAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1830 AEEQLEIESRERQA------------------NGKNLRQKEKKLKDLTIQMEDERKQAQQYKDQAEKGNVRVKQLKHQLE 1891
Cdd:COG4942 95 LRAELEAQKEELAEllralyrlgrqpplalllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1604784239 1892 EAEEEAQRMAAARRKLQRELDEATEANDTLSRDMASLRSKLR 1933
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELA 216
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1341-1498 |
3.62e-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: 3.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1341 RLRQTEEDRNSLMEQLEEETEAKRAVERQVSSLNMQLSDSKKKLDEMSGTVEALEEGKKRLQRELEAANS--DYEEKASA 1418
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNnkEYEALQKE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1419 YDKLEKSRGRMQQELEDVLMDLDSQRQLVSNLEKKQKKFDQMLAEERAvsckfaeERDRAEAEAREKETRVLALARALEE 1498
Cdd:COG1579 98 IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKA-------ELDEELAELEAELEELEAEREELAA 170
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1076-1235 |
4.11e-04 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 44.65 E-value: 4.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1076 ADLQAQLAELRAQLAAKEEELQATQARLeeecnqrgaavkrvrelevlisELQEDLEAERAARGKVEAARRDLGEELNAL 1155
Cdd:COG1566 79 TDLQAALAQAEAQLAAAEAQLARLEAEL----------------------GAEAEIAAAEAQLAAAQAQLDLAQRELERY 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1156 RTELEDSLGTTAAQQELRAKREQEVSMLKKAmedegrshEAQVQDLRQKHSQAvEELTEQLEQAKRVRAGLEKAKQALEK 1235
Cdd:COG1566 137 QALYKKGAVSQQELDEARAALDAAQAQLEAA--------QAQLAQAQAGLREE-EELAAAQAQVAQAEAALAQAELNLAR 207
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1376-1622 |
4.75e-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: 4.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1376 QLSDSKKKLDEMSGTVEALEEGKKRLQRELEAANSDYEEKASAYDKLEKSRGRMQQELEDVLMDLDSQRQLVSNLEKKQK 1455
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1456 KFDQMLAEERAV--SCKFAEERDRAEAeareketrvlaLARALEENQGALEEAEKTMKglradmedlisskddvgksvhD 1533
Cdd:COG3883 97 RSGGSVSYLDVLlgSESFSDFLDRLSA-----------LSKIADADADLLEELKADKA---------------------E 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1534 LEKAKRGLEAIVDEMRTQMEELEDELQVAEDAKLRLDVNTQALRAQHERELHARDELGEEKRKQLLKQVRELEAELEEER 1613
Cdd:COG3883 145 LEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
|
....*....
gi 1604784239 1614 KQRGQASGS 1622
Cdd:COG3883 225 AAAAAAAAA 233
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1030-1159 |
4.77e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 45.07 E-value: 4.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1030 SKLKTKHESMISELElrmkkeekgrlDMEKAKRKVEAELGDL-QEQHADLQAQLAELRAQLAAKEEELQATQARLEEEcn 1108
Cdd:COG0542 400 ARVRMEIDSKPEELD-----------ELERRLEQLEIEKEALkKEQDEASFERLAELRDELAELEEELEALKARWEAE-- 466
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1604784239 1109 qrgaavkrvRELEVLISELQEDLEAERAARGKVEAARRDLGEELNALRTEL 1159
Cdd:COG0542 467 ---------KELIEEIQELKEELEQRYGKIPELEKELAELEEELAELAPLL 508
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
853-1220 |
5.61e-04 |
|
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: 44.89 E-value: 5.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 853 RQEEEMGQKDEELKAAKEVAAKVETELKDITQKHTQLMEERAQLEMKLHAETELYAEAEEMRVRLEAKKQELEEVLHEME 932
Cdd:pfam07888 63 RYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLT 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 933 SrleeeedRSNALHNERKEMEQQLQLMEAHIAEEEDARQKLQMEKVSVEGKVKKLEEDILMMEDQNNKLQKERKLLEERL 1012
Cdd:pfam07888 143 Q-------RVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTI 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1013 ADMSSNLAEEEEKSKNLSKLKTKHESMISELELRMKKEEKGRLD---MEKAKRKVEAELGDLQEQHADLQAQLAELRaqL 1089
Cdd:pfam07888 216 TTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEElssMAAQRDRTQAELHQARLQAAQLTLQLADAS--L 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1090 AAKEEELQATQarlEEECNQRGAAVKRVR--ELEVLISELQEDLEAERAARGKVEAarrDLGEELNALRTELEDSlgtTA 1167
Cdd:pfam07888 294 ALREGRARWAQ---ERETLQQSAEADKDRieKLSAELQRLEERLQEERMEREKLEV---ELGREKDCNRVQLSES---RR 364
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1604784239 1168 AQQELRAKReqevsmlkKAMEDEGRSHEAQVQDLRQkHSQAVEELTEQLEQAK 1220
Cdd:pfam07888 365 ELQELKASL--------RVAQKEKEQLQAEKQELLE-YIRQLEQRLETVADAK 408
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1016-1313 |
7.09e-04 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 44.03 E-value: 7.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1016 SSNLAEEEEKSKNLSKLKTKHESMISELELRMKKEEKGRLDMEKAKRKVEAELGDLQEQHADLQAQLAELRAQLAAKEEE 1095
Cdd:pfam15905 58 SLELKKKSQKNLKESKDQKELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQLLELTRV 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1096 LQATQARLEEECNQrgaavKRVRELEVLISELQEDLEAERAArgkVEAARRDLGEELNALRTELEDSLGTTAAQQElrak 1175
Cdd:pfam15905 138 NELLKAKFSEDGTQ-----KKMSSLSMELMKLRNKLEAKMKE---VMAKQEGMEGKLQVTQKNLEHSKGKVAQLEE---- 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1176 reQEVSMLKKAMEDEGRsheaqvqdlrqkhsqaVEELTEQLEQAKRVRAGLEKAKQALEKESADLSADLRSLASAKQDVE 1255
Cdd:pfam15905 206 --KLVSTEKEKIEEKSE----------------TEKLLEYITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLE 267
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1604784239 1256 HKKKKVEGQLNELNSRF----NESERQRTELGERVSKLTTELDSVTGLLNEAEGKNIKLSKD 1313
Cdd:pfam15905 268 EKEQELSKQIKDLNEKCklleSEKEELLREYEEKEQTLNAELEELKEKLTLEEQEHQKLQQK 329
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1178-1349 |
7.29e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 43.80 E-value: 7.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1178 QEVSMLKKAMEDEGRsheaQVQDLRQKHS---QAVEELTEQLEQakrVRAGLEKAkqalEKESADLSADLRSLASAKQDV 1254
Cdd:PRK09039 46 REISGKDSALDRLNS----QIAELADLLSlerQGNQDLQDSVAN---LRASLSAA----EAERSRLQALLAELAGAGAAA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1255 EHKKKKVEGQLNELNSRFNESERQRTELGERVSKLTTELDSVTGLLNEAEGKNIKLSKDVSSLSSQL-----QDAQELls 1329
Cdd:PRK09039 115 EGRAGELAQELDSEKQVSARALAQVELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADLGRRLnvalaQRVQEL-- 192
|
170 180
....*....|....*....|
gi 1604784239 1330 eeTRQKLNLSGRLRQTEEDR 1349
Cdd:PRK09039 193 --NRYRSEFFGRLREILGDR 210
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
866-1252 |
7.68e-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: 44.36 E-value: 7.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 866 KAAKEVAAKVETELKDITQKHTQLMEERAQLEMKLHAETELYAEAEemrvrLEAKKQELEEVLHEMESRLEEEEDRSNAL 945
Cdd:pfam09731 100 EVAEEEKEATKDAAEAKAQLPKSEQEKEKALEEVLKEAISKAESAT-----AVAKEAKDDAIQAVKAHTDSLKEASDTAE 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 946 HNERKEMEQQLQLMEAHIAE-EEDARQKLQMEKVSVEGKVKKLEEDIL-MMEDQNNKLQKERKLLEERLADMSSNLAEEE 1023
Cdd:pfam09731 175 ISREKATDSALQKAEALAEKlKEVINLAKQSEEEAAPPLLDAAPETPPkLPEHLDNVEEKVEKAQSLAKLVDQYKELVAS 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1024 EKSKNLSKLKTKHESMISEL-ELRMKKEEKGRLDMEKAKRKVEAelgdlqeqhadLQAQLAELRAQlaAKEEELQATQAR 1102
Cdd:pfam09731 255 ERIVFQQELVSIFPDIIPVLkEDNLLSNDDLNSLIAHAHREIDQ-----------LSKKLAELKKR--EEKHIERALEKQ 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1103 LEEECNQRGAAVKRVrELEVLISELQEDLEAERAARGKVEAARRDLGEELNALRTELEDSLGTTAAQQELRAKREQEVSm 1182
Cdd:pfam09731 322 KEELDKLAEELSARL-EEVRAADEAQLRLEFEREREEIRESYEEKLRTELERQAEAHEEHLKDVLVEQEIELQREFLQD- 399
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1604784239 1183 LKKAMEDEGRSHEAQVQDLRQK---HSQAVEELTEQLEQAKRVRAgLEKAKQALEKESADLSADLRSLASAKQ 1252
Cdd:pfam09731 400 IKEKVEEERAGRLLKLNELLANlkgLEKATSSHSEVEDENRKAQQ-LWLAVEALRSTLEDGSADSRPRPLVRE 471
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1083-1267 |
8.56e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 44.17 E-value: 8.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1083 AELRAQlaaKEEELQATQARLE-EECNQRgaavkrvrelevliselQEDLEAERAARGKVEAARRDlGEELNALRTELED 1161
Cdd:PRK05035 436 AEIRAI---EQEKKKAEEAKARfEARQAR-----------------LEREKAAREARHKKAAEARA-AKDKDAVAAALAR 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1162 SLGTTAAQQELRAKREQEVSMLKKAMEDEGRSHEAQVQDLRQKHSQAVEELTEQLEQAKRVRAGLEKAKQALEKESADLS 1241
Cdd:PRK05035 495 VKAKKAAATQPIVIKAGARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANAEAEEE 574
|
170 180
....*....|....*....|....*.
gi 1604784239 1242 ADLRSLASAKQDVEHKKKKVEGQLNE 1267
Cdd:PRK05035 575 VDPKKAAVAAAIARAKAKKAAQQAAS 600
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
870-1012 |
9.00e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 44.30 E-value: 9.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 870 EVAAKV-------ETELKDITQKHTQLMEERAQLEMklHAETELYAEAEEmrvrLEAKKQELEEVLHEMESRLEEEEDRS 942
Cdd:COG0542 397 EAAARVrmeidskPEELDELERRLEQLEIEKEALKK--EQDEASFERLAE----LRDELAELEEELEALKARWEAEKELI 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 943 NALHNERKEMEQQLQLMEAHIAEEEDARQKLQMEKVSVEGKVKklEEDIL-------------MMEDQNNKLQKerklLE 1009
Cdd:COG0542 471 EEIQELKEELEQRYGKIPELEKELAELEEELAELAPLLREEVT--EEDIAevvsrwtgipvgkLLEGEREKLLN----LE 544
|
...
gi 1604784239 1010 ERL 1012
Cdd:COG0542 545 EEL 547
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
879-1050 |
9.10e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.00 E-value: 9.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 879 LKDITQKHTQLMEERAQLEMKlhaETELYAEAEEMRVRLEAKkqelEEVLHEMESRLEEEEDRSNALhnerKEMEQQLQL 958
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILE---EAKKEAEAIKKEALLEAK----EEIHKLRNEFEKELRERRNEL----QKLEKRLLQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 959 MEAHIAEEEDARQKLQMEKVSVEGKVKKLEEDILMMEDQ-NNKLQKERKLLEErladmSSNLAEEEEKSKNLSKLK--TK 1035
Cdd:PRK12704 94 KEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEElEELIEEQLQELER-----ISGLTAEEAKEILLEKVEeeAR 168
|
170
....*....|....*..
gi 1604784239 1036 HE--SMISELELRMKKE 1050
Cdd:PRK12704 169 HEaaVLIKEIEEEAKEE 185
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
863-1177 |
1.04e-03 |
|
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: 43.86 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 863 EELKAAKEVAAKVETELKDITQKHTQLMEERAQL-----------EMKLHAETELYAEAEEMRVRLEAKKQELEEVlhem 931
Cdd:pfam05701 124 AQLEVAKARHAAAVAELKSVKEELESLRKEYASLvserdiaikraEEAVSASKEIEKTVEELTIELIATKESLESA---- 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 932 esrleeeedrsNALHNERKEmeqqlQLMEAHIAEEEDaRQKLQMEKVSVEGKVKKLEEDILMMEDQNNKLQKERKLL--- 1008
Cdd:pfam05701 200 -----------HAAHLEAEE-----HRIGAALAREQD-KLNWEKELKQAEEELQRLNQQLLSAKDLKSKLETASALLldl 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1009 -EERLADMSSNLAEEEEKSKNlsklKTKHESMISELELRMKKE-EKGRLDMEKAKRKVEAelgdlqeqhadLQAQLAELR 1086
Cdd:pfam05701 263 kAELAAYMESKLKEEADGEGN----EKKTSTSIQAALASAKKElEEVKANIEKAKDEVNC-----------LRVAAASLR 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1087 AQLAAKEEELQATQARleeecnqRGAAVKRVRELEVLISELQEDLEAERAARGKVEAARRDLGEELNALRTELEDS-LGT 1165
Cdd:pfam05701 328 SELEKEKAELASLRQR-------EGMASIAVSSLEAELNRTKSEIALVQAKEKEAREKMVELPKQLQQAAQEAEEAkSLA 400
|
330
....*....|..
gi 1604784239 1166 TAAQQELRAKRE 1177
Cdd:pfam05701 401 QAAREELRKAKE 412
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1614-1842 |
1.06e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 43.37 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1614 KQRGQASGSKKKLEGELKDMEDQLEATSRGRDEAVKQLRKIQGQVKDLQRDLEDSRAAQKEVlasareserrskamEADI 1693
Cdd:pfam00038 40 KKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLRTSA--------------ENDL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1694 VQLHEMLAAVERARKQAEVERDELSEELA----------------SNSSGKSLMSDEKRRLD-TKISQLEEELEEEQAN- 1755
Cdd:pfam00038 106 VGLRKDLDEATLARVDLEAKIESLKEELAflkknheeevrelqaqVSDTQVNVEMDAARKLDlTSALAEIRAQYEEIAAk 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1756 ------------VESLNDRLRKSQQLVEQLGAELAAERSTSQSREGSRQQLERQNRELKAKMQEMEGQG---RSKLKASI 1820
Cdd:pfam00038 186 nreeaeewyqskLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKASLERQLAETEERYelqLADYQELI 265
|
250 260
....*....|....*....|..
gi 1604784239 1821 AALEAKLREAEEQLEIESRERQ 1842
Cdd:pfam00038 266 SELEAELQETRQEMARQLREYQ 287
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1065-1268 |
1.14e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 43.37 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1065 EAELGDLQEQHADLQAQLAELRAQLAAKEEELQATQARLEEECNQRgaavkrvRELEVLISELQEDLEAERAARGKVEAA 1144
Cdd:pfam00038 53 EKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLR-------TSAENDLVGLRKDLDEATLARVDLEAK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1145 RRDLGEELNALRTELEDSLGTTAAQ----------------------QELRAKREQEVSMLKKAMEDEGRSHEAQVQDLR 1202
Cdd:pfam00038 126 IESLKEELAFLKKNHEEEVRELQAQvsdtqvnvemdaarkldltsalAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAA 205
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1604784239 1203 QKHSQAVEELTEQLEQAKRVRAGLEKAKQALEKESADLsadLRSLASAKQDVEHKKKKVEGQLNEL 1268
Cdd:pfam00038 206 ARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKASL---ERQLAETEERYELQLADYQELISEL 268
|
|
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
1076-1150 |
1.24e-03 |
|
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope biogenesis, Defense mechanisms];
Pssm-ID: 440606 [Multi-domain] Cd Length: 324 Bit Score: 43.01 E-value: 1.24e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1604784239 1076 ADLQAQLAELRAQLAAKEEELQATQARLE--EECNQRGAAVKrvRELEVLISELQEDLEAERAARGKVEAARRDLGE 1150
Cdd:COG0845 57 PDLQAALAQAQAQLAAAQAQLELAKAELEryKALLKKGAVSQ--QELDQAKAALDQAQAALAAAQAALEQARANLAY 131
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
980-1406 |
1.28e-03 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 43.74 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 980 VEGKVKKLEEDILMMEDQ-------NNKLQKERK-------LLEERLADMSSNLAEEEEKSKNLSKLKTKHESMISELEL 1045
Cdd:pfam15964 126 LEAEVKFCKEELSEMKQRvqvvvleNEKLQQELKsqtqeetLREQTLLDSSGNMQNSWCTPEDSRVHQTSKRPASHNLAE 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1046 RMK-----KEEKGRLDMEKAKRKVEAELGDLQEQHADLQAQLAELRAQLAAKEEELQATQARLEEECNQR-GAAVKRVRE 1119
Cdd:pfam15964 206 RLKsattgEDEKWRLELEKLKLLYEAKTEVLESQVKSLRKDLAESQKTCEDLKERLKHKESLVAASTSSRvGGLCLKCAQ 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1120 LEVLISELQEDLEAERAARgkVEAARRDLGEELNALRTELEDslgttAAQQELRAKRE--QEVSMLKKAMEDEGRSHeAQ 1197
Cdd:pfam15964 286 HEAVLAQTHTNVHMQTIER--LTKERDDLMSALVSVRSSLAE-----AQQRESSAYEQvkQAVQMTEEANFEKTKAL-IQ 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1198 VQDLRQKHSQAVEELTEQL--EQAKRVRAGlEKAKQALEKESADLSADLRSLASAKQDVEHKKKKVEGQLNELNSRFNES 1275
Cdd:pfam15964 358 CEQLKSELERQKERLEKELasQQEKRAQEK-EALRKEMKKEREELGATMLALSQNVAQLEAQVEKVTREKNSLVSQLEEA 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1276 ERQRTELGERVSKLTTELDSvtgLLNEAEGKNIKLSKDVSSLSSQLQDAQELLSEETRQ-KLNLSG---RLRQTEEDRNS 1351
Cdd:pfam15964 437 QKQLASQEMDVTKVCGEMRY---QLNQTKMKKDEAEKEHREYRTKTGRQLEIKDQEIEKlGLELSEskqRLEQAQQDAAR 513
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1604784239 1352 LMEQLEEETEAKRAVERQvsslnMQLSDSKKKLDEMSGTVEALEEGKKRLQRELE 1406
Cdd:pfam15964 514 AREECLKLTELLGESEHQ-----LHLTRLEKESIQQSFSNEAKAQALQAQQREQE 563
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1113-1307 |
1.30e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1113 AVKRVRELEVLISELQEDLEAERAARGKVEAARRDLGEELNALRTELEDSLGTTAAQQELRAKREQEVSMLKKAMEDEGR 1192
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1193 SheAQVQDLRQKH----------------SQAVEELTEQ----LEQAKRVRAGLEKAKQALEKESADLSADLRSLASAKQ 1252
Cdd:COG3883 94 A--LYRSGGSVSYldvllgsesfsdfldrLSALSKIADAdadlLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1604784239 1253 DVEHKKKKVEGQLNELNSRFNESERQRTELGERVSKLTTELDSVTGLLNEAEGKN 1307
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAA 226
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
855-1044 |
1.38e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 855 EEEMGQKDEELKAAKEVAAKVETELKDITQKHTQLMEERAQLEMKLHA----ETELYAEAEEMRVRLEAKKQELEEVLHE 930
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEAlqaeIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 931 MESRLEEEE---------------DRSNALhneRKEMEQQLQLMEAHiaeeEDARQKLQMEKVSVEGKVKKLEEDILMME 995
Cdd:COG3883 95 LYRSGGSVSyldvllgsesfsdflDRLSAL---SKIADADADLLEEL----KADKAELEAKKAELEAKLAELEALKAELE 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1604784239 996 DQNNKLQKERKLLEERLADMSSNLAEEEEKSKNLSKLKTKHESMISELE 1044
Cdd:COG3883 168 AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1613-1780 |
1.42e-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: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1613 RKQRGQASGSKKKLEGELKDMEDQLEATSRGRDEAVKQLRKIQGQVKDLQRDLEDSRAAQKEVlasarESERRSKAMEAD 1692
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNV-----RNNKEYEALQKE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1693 IVQLHEMLAAVERARKQAEVERDELSEELASNssgKSLMSDEKRRLDTKISQLEEELEEEQANVESLNdrlRKSQQLVEQ 1772
Cdd:COG1579 98 IESLKRRISDLEDEILELMERIEELEEELAEL---EAELAELEAELEEKKAELDEELAELEAELEELE---AEREELAAK 171
|
....*...
gi 1604784239 1773 LGAELAAE 1780
Cdd:COG1579 172 IPPELLAL 179
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1581-1916 |
1.53e-03 |
|
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: 43.79 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1581 ERELHARDELGEEKRKQLLKQVRELEAeleeeRKQRGQASGSKKKLEGELKDMEDQLEATSrgrdEAVKQLRKIQGQVKD 1660
Cdd:COG3096 285 ERALELRRELFGARRQLAEEQYRLVEM-----ARELEELSARESDLEQDYQAASDHLNLVQ----TALRQQEKIERYQED 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1661 LQrDLEDSRAAQKEVLASARE--SERRSKAMEADI-----------------------VQLHEMLAAVERARKQ---AEV 1712
Cdd:COG3096 356 LE-ELTERLEEQEEVVEEAAEqlAEAEARLEAAEEevdslksqladyqqaldvqqtraIQYQQAVQALEKARALcglPDL 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1713 ERDELSEELASNSSGKSLMSDEKRRLDTKISQLeeeleeeqanvESLNDRLRKSQQLVEQLgaelAAERSTSQSREGSRQ 1792
Cdd:COG3096 435 TPENAEDYLAAFRAKEQQATEEVLELEQKLSVA-----------DAARRQFEKAYELVCKI----AGEVERSQAWQTARE 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1793 QLeRQNRELKAkmqemegqgrskLKASIAALEAKLREAEEQLEIESR-ERQANGKNLRQKekklKDLTIQMEDERKQAQQ 1871
Cdd:COG3096 500 LL-RRYRSQQA------------LAQRLQQLRAQLAELEQRLRQQQNaERLLEEFCQRIG----QQLDAAEELEELLAEL 562
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1604784239 1872 ykdqaekgnvrvkqlKHQLEEAEEEAQRMAAARRKLQRELDEATE 1916
Cdd:COG3096 563 ---------------EAQLEELEEQAAEAVEQRSELRQQLEQLRA 592
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
865-1087 |
1.66e-03 |
|
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: 43.30 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 865 LKAAKEVAAKVETELKdiTQKHTQLMEERAqlemklhAETELYA---EAEEMRVRL----EAKKQELEEVLHEMESRLEE 937
Cdd:pfam09726 407 LKAELQASRQTEQELR--SQISSLTSLERS-------LKSELGQlrqENDLLQTKLhnavSAKQKDKQTVQQLEKRLKAE 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 938 EEDRSNA---LHNERK----EMEQQLQLMEAHIAEEEDARQKLQMEKVSVEGKVKKLEEDILMMEDQnnklQKERKLLEE 1010
Cdd:pfam09726 478 QEARASAekqLAEEKKrkkeEEATAARAVALAAASRGECTESLKQRKRELESEIKKLTHDIKLKEEQ----IRELEIKVQ 553
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1011 RLADMSSNLAEEEEKSKNLSKLKTKHESmiseLELRMKKEEKGRLDMEKA----KRKVEAELGDLQEQHA---DLQAQLA 1083
Cdd:pfam09726 554 ELRKYKESEKDTEVLMSALSAMQDKNQH----LENSLSAETRIKLDLFSAlgdaKRQLEIAQGQIYQKDQeikDLKQKIA 629
|
....
gi 1604784239 1084 ELRA 1087
Cdd:pfam09726 630 EVMA 633
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
954-1177 |
1.72e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 43.14 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 954 QQLQLMEAHIAEEEDARQKLQMEKVSVEGKVKKLEEDILMMEDQNNKLQKERKLLEERLADMSSNLAEEEEKSKNLSKLK 1033
Cdd:PRK11637 47 DQLKSIQQDIAAKEKSVRQQQQQRASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQIDELNASIAKLEQQQAAQERLL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1034 TKHESMI------SELELRMKKEEKGRldmekaKRKVEAELGDLQEQHADLQAQLAELRAQLAAKEEELQATQAR----L 1103
Cdd:PRK11637 127 AAQLDAAfrqgehTGLQLILSGEESQR------GERILAYFGYLNQARQETIAELKQTREELAAQKAELEEKQSQqktlL 200
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1604784239 1104 EEECNQR----GAAVKRVRELEVLISELQEDleaeraargkveaaRRDLGeELNALRTELEDSLGTTAAQQELRAKRE 1177
Cdd:PRK11637 201 YEQQAQQqkleQARNERKKTLTGLESSLQKD--------------QQQLS-ELRANESRLRDSIARAEREAKARAERE 263
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1245-1508 |
1.78e-03 |
|
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: 43.19 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1245 RSLASAKQDVEHKKKKVEGQLNELNSRFNESERQRtELGERVSKLTTELDSVTGLLNEAEGKNIKLSKDVS--SLSSQLQ 1322
Cdd:pfam17380 282 KAVSERQQQEKFEKMEQERLRQEKEEKAREVERRR-KLEEAEKARQAEMDRQAAIYAEQERMAMERERELEriRQEERKR 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1323 DAQELLSEETRQKLNLSGRLRQTEEDRNSLMEQLEEETEAKRAVERQVSSLNMQLSDSKKkldEMSGTVEALEEGKKRLQ 1402
Cdd:pfam17380 361 ELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKV---EMEQIRAEQEEARQREV 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1403 RELEaansdyEEKASAYDKLEKSRGRMQQELEDVLMDLDSQRQLVSNLEKKQKKFDQMLAEERAVSCKFAEERDRAEAEA 1482
Cdd:pfam17380 438 RRLE------EERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEE 511
|
250 260
....*....|....*....|....*.
gi 1604784239 1483 REKETrvlALARALEENQGALEEAEK 1508
Cdd:pfam17380 512 ERKRK---LLEKEMEERQKAIYEEER 534
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1634-1880 |
1.88e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1634 EDQLEATSRGRDEAVKQLRKIQGQVKDLQRDLEDSRAAQKEVLASARESERRSKAMEADIvqlhemlaavERARKQAEVE 1713
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEI----------AEAEAEIEER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1714 RDELSEELASNSSGKSLMSDEKRRLDTKisqleeeleeeqaNVESLNDRLRKSQQLVEQLGAELAAERSTsqsregsRQQ 1793
Cdd:COG3883 85 REELGERARALYRSGGSVSYLDVLLGSE-------------SFSDFLDRLSALSKIADADADLLEELKAD-------KAE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1794 LERQNRELKAKMQEmegqgrskLKASIAALEAKLREAEEQLEiesrERQANGKNLRQKEKKLKDLTIQMEDERKQAQQYK 1873
Cdd:COG3883 145 LEAKKAELEAKLAE--------LEALKAELEAAKAELEAQQA----EQEALLAQLSAEEAAAEAQLAELEAELAAAEAAA 212
|
....*..
gi 1604784239 1874 DQAEKGN 1880
Cdd:COG3883 213 AAAAAAA 219
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
853-1159 |
2.18e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 42.97 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 853 RQEEEMGQKDEELKAAKEVAAKVETELKDI------TQKHTQLMEErAQLEMKLHAETELY-AEAEEMRVR-LEAKKQEL 924
Cdd:PLN02939 104 RDEAIAAIDNEQQTNSKDGEQLSDFQLEDLvgmiqnAEKNILLLNQ-ARLQALEDLEKILTeKEALQGKINiLEMRLSET 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 925 EEVLHEMESRLEEEEDRSNALHNERKEMEQQLQLMEAHIAEEEDARQKLQMEKVSVEGKVKKLEEDILMMEDQNN---KL 1001
Cdd:PLN02939 183 DARIKLAAQEKIHVEILEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAELIEVAETEErvfKL 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1002 QKERKLLEERLADMSSNLAEEEEKSKNLSKLKtkhesmiseLELRMKKEEKGRLDMEKAKRKVEAELGDLQeQHADLQAQ 1081
Cdd:PLN02939 263 EKERSLLDASLRELESKFIVAQEDVSKLSPLQ---------YDCWWEKVENLQDLLDRATNQVEKAALVLD-QNQDLRDK 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1082 LAELRAQLAA--------KEEELQATQARLEEECNQRGAA--VKRVRELEVLISELQEDLEaeraaRGKVEAARRDLGEE 1151
Cdd:PLN02939 333 VDKLEASLKEanvskfssYKVELLQQKLKLLEERLQASDHeiHSYIQLYQESIKEFQDTLS-----KLKEESKKRSLEHP 407
|
....*...
gi 1604784239 1152 LNALRTEL 1159
Cdd:PLN02939 408 ADDMPSEF 415
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1753-1921 |
2.19e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.08 E-value: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1753 QANVESLNDRLR--KSQQLVEQLGAELAAERSTSQSREGSRQQLERQNRELKAKMQEMEGQGRSKLKAS--------IAA 1822
Cdd:COG3206 188 RKELEEAEAALEefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALpellqspvIQQ 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1823 LEAKLREAEEQLEIESRERQANGKNLRQKEKKLKDLTIQMEDERKQA-QQYKDQAEKGNVRVKQLKHQLEEAEEEAQRMA 1901
Cdd:COG3206 268 LRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRIlASLEAELEALQAREASLQAQLAQLEARLAELP 347
|
170 180
....*....|....*....|...
gi 1604784239 1902 AARRK---LQRELDEATEANDTL 1921
Cdd:COG3206 348 ELEAElrrLEREVEVARELYESL 370
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
863-1155 |
2.20e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.97 E-value: 2.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 863 EELKAAKEVAAKVETELKDITQKHTQLMEERAQLEMKLHAETELYAEaeemrvRLEAKKQELEEVLhEMESRLEEEEDRS 942
Cdd:PRK01156 476 EKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYN------KIESARADLEDIK-IKINELKDKHDKY 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 943 NALHNERKEMEqqlqlmeahiAEEEDARQKLQMEKVSVEGKVkkleeDILMMEDQNNKLQKERKLLEERLADMSSNLaeE 1022
Cdd:PRK01156 549 EEIKNRYKSLK----------LEDLDSKRTSWLNALAVISLI-----DIETNRSRSNEIKKQLNDLESRLQEIEIGF--P 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1023 EEKSKNLSKLKtKHESMISELELRMKKEEKGRLDMEKAKRKVE------AELGDLQEQHADLQAQLAELRAQLAAKEEEL 1096
Cdd:PRK01156 612 DDKSYIDKSIR-EIENEANNLNNKYNEIQENKILIEKLRGKIDnykkqiAEIDSIIPDLKEITSRINDIEDNLKKSRKAL 690
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1604784239 1097 QATQARLEEECNQRGAAVKRVRELEVLISELQEDLEAERaargKVEAARRDLGEELNAL 1155
Cdd:PRK01156 691 DDAKANRARLESTIEILRTRINELSDRINDINETLESMK----KIKKAIGDLKRLREAF 745
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
965-1066 |
2.87e-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: 2.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 965 EEEDARQKLQMEKVSV-EGKVKKLEEDILMMEDQNNKLQKERKLLEERLADMSSNLAEEEEKSKNLSKLKTKHESMISEL 1043
Cdd:COG2433 402 EHEERELTEEEEEIRRlEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREIRKDREISRLDREIERLEREL 481
|
90 100
....*....|....*....|....*
gi 1604784239 1044 -ELRMKKEE-KGRLDMEKAKRKVEA 1066
Cdd:COG2433 482 eEERERIEElKRKLERLKELWKLEH 506
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1382-1554 |
3.06e-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: 3.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1382 KKLDEMSGTVEALEEGKKRLQRELEAANSDYEEKASAYDKLEKSRGRMQQELEDVLMDLDSQRQLVSNLeKKQKKFDQML 1461
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNV-RNNKEYEALQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1462 AEEravsckfaeerDRAEAEAREKETRVLALARALEENQGALEEAEKTMKGLRADMEDLISSKDDVgksVHDLEKAKRGL 1541
Cdd:COG1579 96 KEI-----------ESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEE---LAELEAELEEL 161
|
170
....*....|...
gi 1604784239 1542 EAIVDEMRTQMEE 1554
Cdd:COG1579 162 EAEREELAAKIPP 174
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1005-1465 |
3.55e-03 |
|
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: 42.32 E-value: 3.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1005 RKLLEERLADMSSNLAE--------EEEKSKNLSKLK-TKHEsmISELELRMKK----EEKGRLDMEKAKRKV-EAELGD 1070
Cdd:pfam05701 37 RKLVELELEKVQEEIPEykkqseaaEAAKAQVLEELEsTKRL--IEELKLNLERaqteEAQAKQDSELAKLRVeEMEQGI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1071 LQEQHADLQAQLAELRAQLAAKEEELQATQARLE---EE----CNQRGAAVKRVRElevLISELQEdleaeraargkVEA 1143
Cdd:pfam05701 115 ADEASVAAKAQLEVAKARHAAAVAELKSVKEELEslrKEyaslVSERDIAIKRAEE---AVSASKE-----------IEK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1144 ARRDLGEELNALRTELEDSLGT--TAAQQELRA--KREQEVSMLKKAMEDEgrshEAQVQDLRQKHSqAVEELTEQLEQA 1219
Cdd:pfam05701 181 TVEELTIELIATKESLESAHAAhlEAEEHRIGAalAREQDKLNWEKELKQA----EEELQRLNQQLL-SAKDLKSKLETA 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1220 KRVRAGLEK-----AKQALEKESADLSADLRS-------LASAKQDVEHKKKKVEGQLNELN-------SRFNESERQRT 1280
Cdd:pfam05701 256 SALLLDLKAelaayMESKLKEEADGEGNEKKTstsiqaaLASAKKELEEVKANIEKAKDEVNclrvaaaSLRSELEKEKA 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1281 ELGE----------RVSKLTTELDSVTGLLNEAEGKNIKLSKDVSSLSSQLQDAQE------LLSEETRQKLNLS-GRLR 1343
Cdd:pfam05701 336 ELASlrqregmasiAVSSLEAELNRTKSEIALVQAKEKEAREKMVELPKQLQQAAQeaeeakSLAQAAREELRKAkEEAE 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1344 QTEEDRNSLMEQLEE---ETEAKRAVER----QVSSLNMQLSDSKKKLDEMSG-----TVEALEEGKKRLQRELEAANSD 1411
Cdd:pfam05701 416 QAKAAASTVESRLEAvlkEIEAAKASEKlalaAIKALQESESSAESTNQEDSPrgvtlSLEEYYELSKRAHEAEELANKR 495
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1604784239 1412 YEEKASAYDKLEKSRGRMQQELEDVLMDLDSQRQ-LVSNLEKKQKKFDQMLAEER 1465
Cdd:pfam05701 496 VAEAVSQIEEAKESELRSLEKLEEVNREMEERKEaLKIALEKAEKAKEGKLAAEQ 550
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1020-1358 |
3.93e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 3.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1020 AEEEEKSKNLSKLKTKHESMISELELRMKKEEKGRLDMEKAKRKVEAELGDLQEQHADLQAQLAELRAQLAAKEEELQAT 1099
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1100 QARLEEECNQRGAAVKRVRELEVLISELQEDLEAERAARGKVEAARRDLGEELNALRTELEDSLGTTAAQQELRAKREQE 1179
Cdd:COG4372 86 NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1180 VSMLKKAMEDEGRSHEAQVQDLRQKHSQAVEELTEQLEQAKRVRAGLEKAKQALEKESADLSADLRSLASAKQDVEHKKK 1259
Cdd:COG4372 166 LAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1260 KVEGQLNELNSRFNESERQRTELGERVSKLTTELDSVTGLLNEAEGKNIKLSKDVSSLSSQLQDAQELLSEETRQKLNLS 1339
Cdd:COG4372 246 EDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELA 325
|
330
....*....|....*....
gi 1604784239 1340 GRLRQTEEDRNSLMEQLEE 1358
Cdd:COG4372 326 KKLELALAILLAELADLLQ 344
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1443-1739 |
4.20e-03 |
|
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: 42.03 E-value: 4.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1443 QRQLVSNLEKKQKKFDQMlaeeravsckfAEERDRAEAE--AREKETRvlalaRALEENQGALEEAEKTMKGLRADMEDL 1520
Cdd:pfam17380 279 QHQKAVSERQQQEKFEKM-----------EQERLRQEKEekAREVERR-----RKLEEAEKARQAEMDRQAAIYAEQERM 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1521 ISSKDDVGKSVHdLEKAKRGLEAIVDEM------------RTQMEE------LEDELQVAEDAKL----------RLDVN 1572
Cdd:pfam17380 343 AMERERELERIR-QEERKRELERIRQEEiameisrmreleRLQMERqqknerVRQELEAARKVKIleeerqrkiqQQKVE 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1573 TQALRAQHERELHARDELGEEKRKQLLKQVRELEAeleeerkQRGQASGSKKKLEGELKDMEDQLEATSRGRDEAVKQLR 1652
Cdd:pfam17380 422 MEQIRAEQEEARQREVRRLEEERAREMERVRLEEQ-------ERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRR 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1653 KIqgqvkdLQRDLEDSRAAQKevlasarESERRSKAMEADIVQLHEMLAAVERARKQAEVERDELS-EELASNSSGKSLM 1731
Cdd:pfam17380 495 KI------LEKELEERKQAMI-------EEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEmEERRRIQEQMRKA 561
|
....*...
gi 1604784239 1732 SDEKRRLD 1739
Cdd:pfam17380 562 TEERSRLE 569
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1264-1440 |
4.84e-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: 4.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1264 QLNELNSRFNESERQRTELGERVSKLTTELDSVTGLLNEAEGKNIKLSKDVSSLSSQLQDAQELLsEETRQKLNLSgrlr 1343
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARI-KKYEEQLGNV---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1344 QTEEDRNSLMEQLEEETEAKRAVERQVSSLNMQLSDSKKKLDEMSgtvEALEEGKKRLQRELEAANSDYEEKASAYDKLE 1423
Cdd:COG1579 86 RNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELE---AELAELEAELEEKKAELDEELAELEAELEELE 162
|
170
....*....|....*..
gi 1604784239 1424 KSRGRMQQELEDVLMDL 1440
Cdd:COG1579 163 AEREELAAKIPPELLAL 179
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
1071-1405 |
4.94e-03 |
|
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: 41.97 E-value: 4.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1071 LQEQHADLQAQLAELRAQLAAKEEELQATQARLEEECNQRGAAVKRVRE--LEVLISELQEDL-EAERAARGKVEAARRD 1147
Cdd:pfam13166 87 LGEESIEIQEKIAKLKKEIKDHEEKLDAAEANLQKLDKEKEKLEADFLDecWKKIKRKKNSALsEALNGFKYEANFKSRL 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1148 LGEELNALRTE----LEDSLGTTAAQQELRAKREQEVSMLKKAMEDEGRSHEAQVQDLRQKhSQAVEELTEQLEQAKRVR 1223
Cdd:pfam13166 167 LREIEKDNFNAgvllSDEDRKAALATVFSDNKPEIAPLTFNVIDFDALEKAEILIQKVIGK-SSAIEELIKNPDLADWVE 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1224 AGLEKAKQ------------------ALE----KESADLSADLRSLASakqDVEHKKKKVEGQLN---ELNSRFNESERQ 1278
Cdd:pfam13166 246 QGLELHKAhldtcpfcgqplpaerkaALEahfdDEFTEFQNRLQKLIE---KVESAISSLLAQLPavsDLASLLSAFELD 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1279 RTELGERVSKLTTELDSVTGLLNEAEG---KNIKLSK---DVSSLSSQLQDAQELLSEETRQKLNLSGRLRQTEED-RNS 1351
Cdd:pfam13166 323 VEDIESEAEVLNSQLDGLRRALEAKRKdpfKSIELDSvdaKIESINDLVASINELIAKHNEITDNFEEEKNKAKKKlRLH 402
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1604784239 1352 LMEQLEEE----TEAKRAVERQVSSLNMQLSDSKKKLdemsgtvEALEEGKKRLQREL 1405
Cdd:pfam13166 403 LVEEFKSEideyKDKYAGLEKAINSLEKEIKNLEAEI-------KKLREEIKELEAQL 453
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
948-1221 |
5.13e-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: 41.55 E-value: 5.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 948 ERKEMEQQL--QLMEAHIAEEEDARQKLQmekvsveGKVKKLEEDI--LMMEDQNNKLQ--KERKLLEERLADMSSNLAE 1021
Cdd:pfam05667 218 AAQEWEEEWnsQGLASRLTPEEYRKRKRT-------KLLKRIAEQLrsAALAGTEATSGasRSAQDLAELLSSFSGSSTT 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1022 EEEKSKNLSKLKTKHESMISELELRMKKEEKGRLDMEKAKRKVEAELGDLQEQHADLQAQLAELRAQLAAKE-------- 1093
Cdd:pfam05667 291 DTGLTKGSRFTHTEKLQFTNEAPAATSSPPTKVETEEELQQQREEELEELQEQLEDLESSIQELEKEIKKLEssikqvee 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1094 --EELQATQARLEEECNQRGAAVKRVRELEVLISELQEDLEAErAAR-----GKVEAARRDLGEELNALRTEledslgtt 1166
Cdd:pfam05667 371 elEELKEQNEELEKQYKVKKKTLDLLPDAEENIAKLQALVDAS-AQRlvelaGQWEKHRVPLIEEYRALKEA-------- 441
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1604784239 1167 AAQQELRAKRE-QEVSMLKKAMEDegrsheaQVQDLRQKhSQAVEELTEQLEQAKR 1221
Cdd:pfam05667 442 KSNKEDESQRKlEEIKELREKIKE-------VAEEAKQK-EELYKQLVAEYERLPK 489
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1690-1835 |
5.82e-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: 40.87 E-value: 5.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1690 EADIVQLHEMLAAVERARKQAEVERDELSEELASNSSGKSLM---SDEKRRLDTKISQLEEELEEEQANVESLNDRLRK- 1765
Cdd:pfam00529 57 QAALDSAEAQLAKAQAQVARLQAELDRLQALESELAISRQDYdgaTAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPIg 136
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1604784239 1766 --SQQLVEQLGAELAAERSTSQSREGSRQQLERQNRELKAKMQEMEGQGRSKLKASIAALEAKLREAEEQLE 1835
Cdd:pfam00529 137 giSRESLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSGAQLQIAEAEAELKLAKLDLE 208
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
856-1262 |
6.43e-03 |
|
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: 41.38 E-value: 6.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 856 EEMGQKDEELKAAKEVAAKVETELKDITQKHTQLMEERAQLEMK-------LHAETELYAEAEEmrvrleakkqELEEVL 928
Cdd:pfam06160 86 KALDEIEELLDDIEEDIKQILEELDELLESEEKNREEVEELKDKyrelrktLLANRFSYGPAID----------ELEKQL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 929 HEMESRLEEEEDRSNA-LHNERKEmeqQLQLMEAHIAEEEDarqklQMEKV---------SVEGKVKKLEEDILMMEDQN 998
Cdd:pfam06160 156 AEIEEEFSQFEELTESgDYLEARE---VLEKLEEETDALEE-----LMEDIpplyeelktELPDQLEELKEGYREMEEEG 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 999 -----NKLQKERKLLEERLADMSSNLA--EEEEKSKNLSKLKTKHESMISELElrmkKEEKGRLDMEKAKRKVEAELGDL 1071
Cdd:pfam06160 228 yalehLNVDKEIQQLEEQLEENLALLEnlELDEAEEALEEIEERIDQLYDLLE----KEVDAKKYVEKNLPEIEDYLEHA 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1072 QEQHADLQAQLAELRA--QLAAKE-EELQATQARLEEECNQRGAAVKRVRELEVLISELQEDLEAERAARGKVEAARRDL 1148
Cdd:pfam06160 304 EEQNKELKEELERVQQsyTLNENElERVRGLEKQLEELEKRYDEIVERLEEKEVAYSELQEELEEILEQLEEIEEEQEEF 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1149 GEELNALRTELEDslgttaAQQELrAKREQEVSMLKKAMEdegRSH----EAQVQDLRQKHSQAVEELTEQLEQakrVRA 1224
Cdd:pfam06160 384 KESLQSLRKDELE------AREKL-DEFKLELREIKRLVE---KSNlpglPESYLDYFFDVSDEIEDLADELNE---VPL 450
|
410 420 430
....*....|....*....|....*....|....*...
gi 1604784239 1225 GLEKAKQALEKesadlsadlrslasAKQDVEHKKKKVE 1262
Cdd:pfam06160 451 NMDEVNRLLDE--------------AQDDVDTLYEKTE 474
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1001-1155 |
6.44e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 41.23 E-value: 6.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1001 LQKERKLLEERLADMSSNLAEEEEKSKNLSKlktkhESMISELELRMKKEEKGRLDMEKAKRKVEaELGDLQEQHADLQA 1080
Cdd:PRK12705 25 LKKRQRLAKEAERILQEAQKEAEEKLEAALL-----EAKELLLRERNQQRQEARREREELQREEE-RLVQKEEQLDARAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1081 QLAELRAQLAAKEEELQATQARLEEECNQRGAAVKRVREL------EVLISELQEDLEAERAARGKVEAARRDLGEELNA 1154
Cdd:PRK12705 99 KLDNLENQLEEREKALSARELELEELEKQLDNELYRVAGLtpeqarKLLLKLLDAELEEEKAQRVKKIEEEADLEAERKA 178
|
.
gi 1604784239 1155 L 1155
Cdd:PRK12705 179 Q 179
|
|
| PRK05431 |
PRK05431 |
seryl-tRNA synthetase; Provisional |
1754-1835 |
6.59e-03 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 235461 [Multi-domain] Cd Length: 425 Bit Score: 41.21 E-value: 6.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1754 ANVESLNDRLRKSQQLVEqlgaELAAERStsqsrEGSRQ--QLERQNRELKAKMQEMEgqgrsKLKASIAALEAKLREAE 1831
Cdd:PRK05431 28 DELLELDEERRELQTELE----ELQAERN-----ALSKEigQAKRKGEDAEALIAEVK-----ELKEEIKALEAELDELE 93
|
....
gi 1604784239 1832 EQLE 1835
Cdd:PRK05431 94 AELE 97
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1581-1931 |
6.72e-03 |
|
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: 41.64 E-value: 6.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1581 ERELHARDELGEEKRKQLLKQVRELEAELEEERKQRGQASGSKKKLEGELKDMEDQLEATSRGRDEAvkqlrkiqgqvKD 1660
Cdd:pfam15921 91 QRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAA-----------KC 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1661 LQRDLEDSRAAQKEVLASARESErrskamEADIVQLHEMLAAVERARKQAEVERDELSeELASNSSGkSLMSDEKRRLDT 1740
Cdd:pfam15921 160 LKEDMLEDSNTQIEQLRKMMLSH------EGVLQEIRSILVDFEEASGKKIYEHDSMS-TMHFRSLG-SAISKILRELDT 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1741 KISQLEEELEEEQANVESLNDR--------LRKSQQLVEQLGAE-------LAAERSTSQSREGS--------RQQLERQ 1797
Cdd:pfam15921 232 EISYLKGRIFPVEDQLEALKSEsqnkiellLQQHQDRIEQLISEheveitgLTEKASSARSQANSiqsqleiiQEQARNQ 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1798 NRELKAKMQEME---GQGRSKLKASIAALEAKLREAEEQLEIESRE-----------RQANGKNLRQKEKKLKDLTIQME 1863
Cdd:pfam15921 312 NSMYMRQLSDLEstvSQLRSELREAKRMYEDKIEELEKQLVLANSEltearterdqfSQESGNLDDQLQKLLADLHKREK 391
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1604784239 1864 D---ERKQAQQYKDQAEKGNVRVKQLKHQLEEAEEEAQRMAAARRKLQreldeaTEANDTLSRDMASLRSK 1931
Cdd:pfam15921 392 ElslEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMK------SECQGQMERQMAAIQGK 456
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1299-1890 |
6.83e-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: 41.26 E-value: 6.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1299 LLNEAEGKNIKLSKDVSSLSSQLQDAQELLSEETRQKLNLSGRLRQTEEDRNSLMEQLEEETEAKRAVERQVSSLNMQLS 1378
Cdd:pfam05557 14 LQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1379 DSKKKLDEMSGTVEALEEGKKRLQRELEAANSDYEEKASaydKLEksrgRMQQELEDVLMDLDSQRQLVSNLEKKQKkfd 1458
Cdd:pfam05557 94 EKESQLADAREVISCLKNELSELRRQIQRAELELQSTNS---ELE----ELQERLDLLKAKASEAEQLRQNLEKQQS--- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1459 qmlaeeravSCKFAEERDRAEAEAREKETRVLALARALEENQGALEEAEKTMKGLRADMEDLISSKDDVGKsvhdLEKAK 1538
Cdd:pfam05557 164 ---------SLAEAEQRIKELEFEIQSQEQDSEIVKNSKSELARIPELEKELERLREHNKHLNENIENKLL----LKEEV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1539 RGLEAIVDEMRTQMEELEDeLQVaEDAKLRLDVNTQALRAQHERELHARDELGEEKRKQLLKQVRELEAELEEERKQRGQ 1618
Cdd:pfam05557 231 EDLKRKLEREEKYREEAAT-LEL-EKEKLEQELQSWVKLAQDTGLNLRSPEDLSRRIEQLQQREIVLKEENSSLTSSARQ 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1619 ASGSKKKLEGELKDMEDQLEATSRGRDEAVKQLRKIQGQVKDLQRDLEDSRAAQKEVLASARESERRSKAMEAdIVQLHE 1698
Cdd:pfam05557 309 LEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAILESYDKELTMSNYSPQLLER-IEEAED 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1699 MLAAVERARKQAEVERDELSEELASNssgKSLMSDEKRRLDTKISQleeeleeeqanvESLNDRlRKSQQLVEQLGAELa 1778
Cdd:pfam05557 388 MTQKMQAHNEEMEAQLSVAEEELGGY---KQQAQTLERELQALRQQ------------ESLADP-SYSKEEVDSLRRKL- 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1779 aerstsQSREGSRQQLERQNRELKAKMQEMEGQGRSKLKASiaaleaKLREAEEQLEIESRERQANGKNLRQKE-KKLKD 1857
Cdd:pfam05557 451 ------ETLELERQRLREQKNELEMELERRCLQGDYDPKKT------KVLHLSMNPAAEAYQQRKNQLEKLQAEiERLKR 518
|
570 580 590
....*....|....*....|....*....|....
gi 1604784239 1858 LTIQMEDERKQAQQYKDQAEKGNVR-VKQLKHQL 1890
Cdd:pfam05557 519 LLKKLEDDLEQVLRLPETTSTMNFKeVLDLRKEL 552
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
972-1106 |
7.04e-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: 7.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 972 KLQMEKVSVEGKVKKLEEDILMMEDQNNKLQKERKLL-EERLADMSSNLAEEEEKsknlsklktkhesmISELELRMKKE 1050
Cdd:COG0542 401 RVRMEIDSKPEELDELERRLEQLEIEKEALKKEQDEAsFERLAELRDELAELEEE--------------LEALKARWEAE 466
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1604784239 1051 ekgrldmekakRKVEAELGDLQEQHADLQAQLAELRAQLAAKEEELQATQARLEEE 1106
Cdd:COG0542 467 -----------KELIEEIQELKEELEQRYGKIPELEKELAELEEELAELAPLLREE 511
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
950-1092 |
7.95e-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: 40.60 E-value: 7.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 950 KEMEQQLQLMEAHIAEEEDARQKLQMEKVSVEGKVKKLEEdilmmedqnnKLQKERKLLEERLADMSSNLAEEEEKSKN- 1028
Cdd:TIGR02794 92 KELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAE----------AKAKAEAEAERKAKEEAAKQAEEEAKAKAa 161
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1604784239 1029 -LSKLKTKHESMISELELRMKKEEKGRLDMEKAKRKVEAELGDLQEQHADLQAQLAELRAQLAAK 1092
Cdd:TIGR02794 162 aEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAE 226
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
1070-1217 |
8.29e-03 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 39.17 E-value: 8.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1070 DLQEQHADLQAQLAELRAQLAAKEEELQAT-QARLEEecnqrgaavkRVRELEVLISELQEDLEAeraargKVEAARRDL 1148
Cdd:pfam01442 34 ETEALRERLQKDLEEVRAKLEPYLEELQAKlGQNVEE----------LRQRLEPYTEELRKRLNA------DAEELQEKL 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1604784239 1149 GEELNALRTELEDSLGTTAAQ-----QELRAKREQEVSMLKKAMEDEGRSHEAQ----VQDLRQKHSQAVEELTEQLE 1217
Cdd:pfam01442 98 APYGEELRERLEQNVDALRARlapyaEELRQKLAERLEELKESLAPYAEEVQAQlsqrLQELREKLEPQAEDLREKLD 175
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1119-1436 |
8.35e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 40.97 E-value: 8.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1119 ELEVLISELQEDLEAERAARGKVEAAR---RDLGEELNALRteleDSLGTTAAqqELRAKREQEVSMLKKAME--DEGRS 1193
Cdd:PRK04778 120 DIEQILEELQELLESEEKNREEVEQLKdlyRELRKSLLANR----FSFGPALD--ELEKQLENLEEEFSQFVEltESGDY 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1194 HEAQvqdlrqKHSQAVEELTEQLEQ-AKRVRAGLEKAKQALEKESADLSADLRSLASAKQDVEHKKkkVEGQLNELNSRF 1272
Cdd:PRK04778 194 VEAR------EILDQLEEELAALEQiMEEIPELLKELQTELPDQLQELKAGYRELVEEGYHLDHLD--IEKEIQDLKEQI 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1273 NESERQRTEL-----GERVSKLTTELDSVTGLL-NEAEGKN--IKLSKDVSSLSSQLQDAQELLSEETrQKLNLSGRLRq 1344
Cdd:PRK04778 266 DENLALLEELdldeaEEKNEEIQERIDQLYDILeREVKARKyvEKNSDTLPDFLEHAKEQNKELKEEI-DRVKQSYTLN- 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1345 teedrnslmeqlEEETEAKRAVERQVSSLNMQLSDSKKKLDEMSGTVEALEEGKKRLQRELEAANSDYEEKASAYDKLEK 1424
Cdd:PRK04778 344 ------------ESELESVRQLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEEIEKEQEKLSEMLQGLRK 411
|
330
....*....|....*....
gi 1604784239 1425 SR-------GRMQQELEDV 1436
Cdd:PRK04778 412 DEleareklERYRNKLHEI 430
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1177-1388 |
8.63e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.77 E-value: 8.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1177 EQEVSMLKKAMEDEGRSHEAQVQDLRQKHSQAVEElteqleqAKRVRAGLEKAKQAL---EKESADLSADLRSLASAKQD 1253
Cdd:PHA02562 194 QQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEE-------AKTIKAEIEELTDELlnlVMDIEDPSAALNKLNTAAAK 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1254 VEHKKKkvegQLNELNSRFNESE------RQRTELGERVSKLTTELDSVTGLLNEAEGKNIKLSKDVSSLSSQLQDAQEL 1327
Cdd:PHA02562 267 IKSKIE----QFQKVIKMYEKGGvcptctQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLEL 342
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1604784239 1328 LSEETRQKLNLSgRLRQTEEDRNSLMEQLEEE----TEAKRAVERQVSSLNMQLSDSKKKLDEMS 1388
Cdd:PHA02562 343 KNKISTNKQSLI-TLVDKAKKVKAAIEELQAEfvdnAEELAKLQDELDKIVKTKSELVKEKYHRG 406
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1080-1465 |
8.65e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 40.83 E-value: 8.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1080 AQLAELRAQLAAKEEELQATQARLEEECNQRGAAVKRVRELEVLISELQEDLEAERAARG----KVEAARRDLGE----- 1150
Cdd:pfam05622 24 SLLQEEKNSLQQENKKLQERLDQLESGDDSGTPGGKKYLLLQKQLEQLQEENFRLETARDdyriKCEELEKEVLElqhrn 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1151 -ELNALRTE---LEDSLGTTAAQQELRAKREQEVSMLKKAMEDEG--RSHEAQVQDLRQKHSQAVEELTEQLEQAKRVRA 1224
Cdd:pfam05622 104 eELTSLAEEaqaLKDEMDILRESSDKVKKLEATVETYKKKLEDLGdlRRQVKLLEERNAEYMQRTLQLEEELKKANALRG 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1225 GLEKAKqaleKESADLSADLRSLASAKQDVEHKKKKVEGQLNELnsrfnESERQRTeLGERVSKLTTELDSVTGLLNEAE 1304
Cdd:pfam05622 184 QLETYK----RQVQELHGKLSEESKKADKLEFEYKKLEEKLEAL-----QKEKERL-IIERDTLRETNEELRCAQLQQAE 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1305 GKNIKLSKDVSSLSSQLQdAQELLSEETRQKL------NLSGRLRQTEEDRNSLME---QLEEETEAK-------RAVER 1368
Cdd:pfam05622 254 LSQADALLSPSSDPGDNL-AAEIMPAEIREKLirlqheNKMLRLGQEGSYRERLTElqqLLEDANRRKneletqnRLANQ 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1369 QVSSLNMQLSDSKKKLDEMSGTVEALEEGKKRLQRELEAANSDYEEkasaydkleksRGRMQQELEDVLMDLDSQRQL-V 1447
Cdd:pfam05622 333 RILELQQQVEELQKALQEQGSKAEDSSLLKQKLEEHLEKLHEAQSE-----------LQKKKEQIEELEPKQDSNLAQkI 401
|
410 420
....*....|....*....|
gi 1604784239 1448 SNLEKK-QKKFDQMLA-EER 1465
Cdd:pfam05622 402 DELQEAlRKKDEDMKAmEER 421
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
989-1243 |
8.73e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 41.04 E-value: 8.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 989 EDILMMEDQNNKLQKERKLLEERLADMSSNLAEEEEKSKNLSKLKTKHESMISELELRMKKEEKGRLDMEKakrkveaEL 1068
Cdd:PLN02939 156 EDLEKILTEKEALQGKINILEMRLSETDARIKLAAQEKIHVEILEEQLEKLRNELLIRGATEGLCVHSLSK-------EL 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1069 GDLQEQHADLQAQLAELRAQLAakeeELQATQAR---LEEECNQRGAAvkrVRELEVLISELQED------LEAErAARG 1139
Cdd:PLN02939 229 DVLKEENMLLKDDIQFLKAELI----EVAETEERvfkLEKERSLLDAS---LRELESKFIVAQEDvsklspLQYD-CWWE 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1140 KVEaarrDLGEELNALRTELEDSLGTTAAQQELRAKreqeVSMLKKAMEDEGRSHEA-QVQDLRQKHSQAVEELTE---- 1214
Cdd:PLN02939 301 KVE----NLQDLLDRATNQVEKAALVLDQNQDLRDK----VDKLEASLKEANVSKFSsYKVELLQQKLKLLEERLQasdh 372
|
250 260 270
....*....|....*....|....*....|....*..
gi 1604784239 1215 ------QLEQ--AKRVRAGLEKAKQALEKESADLSAD 1243
Cdd:PLN02939 373 eihsyiQLYQesIKEFQDTLSKLKEESKKRSLEHPAD 409
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1080-1190 |
9.00e-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: 9.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1080 AQLAELRAQLAAKEEELQAtqarLEEEcnQRGAAVKRVRELEVLISELQEDLEAERAArgkvEAARRDLGEELNALRTEL 1159
Cdd:COG0542 411 EELDELERRLEQLEIEKEA----LKKE--QDEASFERLAELRDELAELEEELEALKAR----WEAEKELIEEIQELKEEL 480
|
90 100 110
....*....|....*....|....*....|.
gi 1604784239 1160 EDSLGTTAAQQELRAKREQEVSMLKKAMEDE 1190
Cdd:COG0542 481 EQRYGKIPELEKELAELEEELAELAPLLREE 511
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1023-1155 |
9.03e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.97 E-value: 9.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1023 EEKSKNLSKLKTKHESMISELE-LRMKKEEKgRLDMEKAKRKVEAELGDLQEQHADLQAQLAELRaqlaakeeelqatqA 1101
Cdd:PRK00409 505 EEAKKLIGEDKEKLNELIASLEeLERELEQK-AEEAEALLKEAEKLKEELEEKKEKLQEEEDKLL--------------E 569
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1604784239 1102 RLEEECNQRGAAVKrvRELEVLISELQEDLEAERAA--RGKVEAARRDLGEELNAL 1155
Cdd:PRK00409 570 EAEKEAQQAIKEAK--KEADEIIKELRQLQKGGYASvkAHELIEARKRLNKANEKK 623
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
964-1304 |
9.12e-03 |
|
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: 40.99 E-value: 9.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 964 AEEEDARQKLQmekvSVEGKVKKLEEDILMMEDQNNKLQKERKLLEERLADMSSNLAEeeeKSKNLSKLKTKHESMISEL 1043
Cdd:pfam06160 86 KALDEIEELLD----DIEEDIKQILEELDELLESEEKNREEVEELKDKYRELRKTLLA---NRFSYGPAIDELEKQLAEI 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1044 ELRMKK--EEKGRLDMEKAKR---KVEAELGDLQEQHADLQAQLAELRAQLAAKEEELQATQARLEEE------------ 1106
Cdd:pfam06160 159 EEEFSQfeELTESGDYLEAREvleKLEEETDALEELMEDIPPLYEELKTELPDQLEELKEGYREMEEEgyalehlnvdke 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1107 ----CNQRGAAVKRVRELEV------------LISELQEDLEAERAARGKVEAARRDLGEELNALR---TELEDSLGTTA 1167
Cdd:pfam06160 239 iqqlEEQLEENLALLENLELdeaeealeeieeRIDQLYDLLEKEVDAKKYVEKNLPEIEDYLEHAEeqnKELKEELERVQ 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1168 AQQELRAKREQEVsmlkKAMEDEGRSHEAQVQDLRQK---HSQAVEELTEQLEQakrvragLEKAKQALEKESADLSADL 1244
Cdd:pfam06160 319 QSYTLNENELERV----RGLEKQLEELEKRYDEIVERleeKEVAYSELQEELEE-------ILEQLEEIEEEQEEFKESL 387
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1604784239 1245 RSLASAKQDVEHKKKKVEGQLNELNSR----------------FNESERQRTELGERVSKLTTELDSVTGLLNEAE 1304
Cdd:pfam06160 388 QSLRKDELEAREKLDEFKLELREIKRLveksnlpglpesyldyFFDVSDEIEDLADELNEVPLNMDEVNRLLDEAQ 463
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1416-1683 |
9.18e-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: 9.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1416 ASAYdkLEKSRGRMQQELEDVLMDLDSQ-RQLVSNLEKKQKKFDQMLAEERAVSckfaeerdrAEAEAREKETRVLALAR 1494
Cdd:COG3206 158 AEAY--LEQNLELRREEARKALEFLEEQlPELRKELEEAEAALEEFRQKNGLVD---------LSEEAKLLLQQLSELES 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1495 ALEENQGALEEAEKTMKGLRADMEDLISSKDDVGKSvhdlekakrgleAIVDEMRTQMEELEDELQvaeDAKLRLDVNTQ 1574
Cdd:COG3206 227 QLAEARAELAEAEARLAALRAQLGSGPDALPELLQS------------PVIQQLRAQLAELEAELA---ELSARYTPNHP 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1575 ALRAQherelhardelgEEKRKQLLKQVRELEAELEEERKQRGQASGSKkklEGELKDMEDQLEAtsrgrdeAVKQLRKI 1654
Cdd:COG3206 292 DVIAL------------RAQIAALRAQLQQEAQRILASLEAELEALQAR---EASLQAQLAQLEA-------RLAELPEL 349
|
250 260
....*....|....*....|....*....
gi 1604784239 1655 QGQVKDLQRDLEDSRAAQKEVLASARESE 1683
Cdd:COG3206 350 EAELRRLEREVEVARELYESLLQRLEEAR 378
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1426-1841 |
9.37e-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: 40.65 E-value: 9.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1426 RGRMQQELEDVLMDLDSQRQLVSNLEKKQKKFDQMLAEERAVSCKFAEERDRAEAEAREKETRVLALARALEEnqgalee 1505
Cdd:pfam07888 12 ESHGEEGGTDMLLVVPRAELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAE------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1506 AEKTMKGLRADMEDLISSKDDVGKSVHDLEKAKRGLEAIVDEMRTQMEELEDELQVAEDAKLRLDVNTQALRAQHERELH 1585
Cdd:pfam07888 85 LKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1586 ARDElGEEKRKQLLKQVRELEAELEEERKQRGQASGSKKKLEGELKDMEDQLEATSRGRDEAvkqlrkiQGQVKDLQRDL 1665
Cdd:pfam07888 165 QRKE-EEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTA-------HRKEAENEALL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1666 EDSRAAQKEVLASARESERRSKAMEADIVQLHEMLAAVERARKQAEVERDELSEELASNSSGKSLMSDEKRRLDTKISQL 1745
Cdd:pfam07888 237 EELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEAD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1746 EEELEEEQANVESLNDRLRKSQQLVEQLGAELAAERSTSQSREGSRQqleRQNRELKAKMQEMEGQgRSKLKASIAALEA 1825
Cdd:pfam07888 317 KDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESR---RELQELKASLRVAQKE-KEQLQAEKQELLE 392
|
410
....*....|....*.
gi 1604784239 1826 KLREAEEQLEIESRER 1841
Cdd:pfam07888 393 YIRQLEQRLETVADAK 408
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1259-1916 |
9.64e-03 |
|
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: 40.77 E-value: 9.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1259 KKVEGQLNELNSRFNESERQRTELGERVSKLTTELDSVTGLLNEAEGKNIKLSKDVSSLSSQLQDAQEllseetrQKLNL 1338
Cdd:TIGR04523 50 KNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKE-------QKNKL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1339 sgrlrqtEEDRNSLMEQLEEETEAKRAVERQVSSLNMQLSDSKKKLDEMSGTVEALEEGKKRLQRELEAANSDYEEKASA 1418
Cdd:TIGR04523 123 -------EVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNK 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1419 YDKLE------KSRGRMQQELEDVLMDLDSQR-QLVSNLEKKQKKFDQMLAE-----ERAVSCKFAEERDRAEAEAREKE 1486
Cdd:TIGR04523 196 LLKLElllsnlKKKIQKNKSLESQISELKKQNnQLKDNIEKKQQEINEKTTEisntqTQLNQLKDEQNKIKKQLSEKQKE 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1487 trvlalaraLEENQGALEEAEKTMKGLRADMEDLISSKD-----DVGKSVHDLEKAKRGLEAIVDEMRTQMEELEDELQV 1561
Cdd:TIGR04523 276 ---------LEQNNKKIKELEKQLNQLKSEISDLNNQKEqdwnkELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQ 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1562 AEDAKLRLDVNTQALRaqheRELhardelgEEKRKQLLKqvreleaeleeERKQRGQASGSKKKLEGELKDMEDQLEats 1641
Cdd:TIGR04523 347 LKKELTNSESENSEKQ----REL-------EEKQNEIEK-----------LKKENQSYKQEIKNLESQINDLESKIQ--- 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1642 rgrdEAVKQLRKIQGQVKDLQRDLEDSRAAQKEVLASARESERRSKAMEADIVQLHEMLAAVERARKQAEVERDELSEEL 1721
Cdd:TIGR04523 402 ----NQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSI 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1722 ASNssgKSLMSDEKRRLDTKISQleeeleeeqanVESLNDRLRKSQQLVEQLGAELAAERSTSQSREGSRQQLERQNREL 1801
Cdd:TIGR04523 478 NKI---KQNLEQKQKELKSKEKE-----------LKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDL 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1802 KAKMQEME-GQGRSKLKASIAALEAKLREAEEqleiesrerqaNGKNLRQKEKKLKDLTIQMEDERKQaqqYKDQAEKGN 1880
Cdd:TIGR04523 544 EDELNKDDfELKKENLEKEIDEKNKEIEELKQ-----------TQKSLKKKQEEKQELIDQKEKEKKD---LIKEIEEKE 609
|
650 660 670
....*....|....*....|....*....|....*.
gi 1604784239 1881 VRVKQLKHQLEEAEEEAQRMAAARRKLQRELDEATE 1916
Cdd:TIGR04523 610 KKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQ 645
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1784-1890 |
9.74e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 40.33 E-value: 9.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1784 SQSREGSRQQLERQNRELK--AKMQEMEGQGRSKLKASIAALEAKLREAE---EQLEIESRERQANGKNLrqkEKKLKDL 1858
Cdd:PRK09039 45 SREISGKDSALDRLNSQIAelADLLSLERQGNQDLQDSVANLRASLSAAEaerSRLQALLAELAGAGAAA---EGRAGEL 121
|
90 100 110
....*....|....*....|....*....|..
gi 1604784239 1859 TIQMEDERKQAQQYKDQAEKGNVRVKQLKHQL 1890
Cdd:PRK09039 122 AQELDSEKQVSARALAQVELLNQQIAALRRQL 153
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1131-1292 |
9.77e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.53 E-value: 9.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1131 LEAERAARGKVEAARRdlgeELNALRTEledslgttaaqQELRAKreQEVSMLKKAMEDEGRSHEAQVQDLRQKHSQAVE 1210
Cdd:PRK12704 34 KEAEEEAKRILEEAKK----EAEAIKKE-----------ALLEAK--EEIHKLRNEFEKELRERRNELQKLEKRLLQKEE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604784239 1211 ELTEQLEQakrvragLEKAKQALEKESADLSADLRSLASAKQDVEHKKKKvegqlnelnsrfneserQRTELgERVSKLT 1290
Cdd:PRK12704 97 NLDRKLEL-------LEKREEELEKKEKELEQKQQELEKKEEELEELIEE-----------------QLQEL-ERISGLT 151
|
..
gi 1604784239 1291 TE 1292
Cdd:PRK12704 152 AE 153
|
|
| |
