|
Name |
Accession |
Description |
Interval |
E-value |
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
99-771 |
0e+00 |
|
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy chain 10 (also called NMMHCB). Mutations in this gene have been associated with May-Hegglin anomaly and developmental defects in brain and heart. Multiple transcript variants encoding different isoforms have been found for this gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276952 [Multi-domain] Cd Length: 673 Bit Score: 1443.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTG 178
Cdd:cd14920 1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 179 ESGAGKTENTKKVIQYLAHVASSHKGRKEHTAPGELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 258
Cdd:cd14920 81 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 259 ANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNGNLPIPGQQDREIFQETMESMKIMGF 338
Cdd:cd14920 161 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMHIMGF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 339 NHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASMPDNTAAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQKAQTKEQAD 418
Cdd:cd14920 241 SHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQAD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 419 FAVEALAKALYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFVLEQEE 498
Cdd:cd14920 321 FAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 499 YQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLSLLDEECWFPKATDKSFVEKVIQELGNHPKFQKPRQLRDKADLCII 578
Cdd:cd14920 401 YQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKDKADFCII 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 579 HYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVDRIVGLDQVSGMGEMSFGSSYKTKKGMFRTVGQLYK 658
Cdd:cd14920 481 HYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTETAFGSAYKTKKGMFRTVGQLYK 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 659 ESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPK 738
Cdd:cd14920 561 ESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPK 640
|
650 660 670
....*....|....*....|....*....|...
gi 1785379719 739 GFMDGKQACAIMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14920 641 GFMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
848-1928 |
0e+00 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 1361.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 848 TRQDEVMQAKVVELQKVKDTQVKTESELKEMANKYQQLFEEKSILAEQLQAETELFAEAEEMRARLASKKQELEEILHDL 927
Cdd:pfam01576 1 TRQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 928 EARVEEEEERTLQLQNEKKKMHQHIQDLEEQLEEEEGARQKLQLEKVTTESRLKKMEEDILLLEDQNAKLAKERKLLDDR 1007
Cdd:pfam01576 81 ESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1008 IGEFTSTMAEEEEKVKSLNKLRNKYEAVIADLEDRLKKEEKGRQEMEKMKRKLDGETTDLQDQLLELQQQIEELKQQLAR 1087
Cdd:pfam01576 161 ISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1088 KEEELQAALARVDDEVGQKNNLLKQLRDLQSQLAELHEDLESEKAARAKAEKQRRDLGEELEALKTELEDTLDSTAAQQE 1167
Cdd:pfam01576 241 KEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1168 LRAKREQEVTDLKKTIEEDVKVRDAQVTEMRQRHNQVVEEISEQLEQARRFKGNLEKVKQTLESENTDLIKEVKNLQAAK 1247
Cdd:pfam01576 321 LRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1248 QDSEQRRKKLEQQVSEFQIRTNESEKVKFELAEKLQKLQAELDGVSGALGSTEGKSIKLTKDLSTVQSQLQDTQELLQEE 1327
Cdd:pfam01576 401 QDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1328 TRQKLNFSSRVRQLEEEKNNLMENLEEEESAKAQLSRQLQALQQQLLESKKRMEDQGGMVEAMEEAKKKSYKELEFLQQR 1407
Cdd:pfam01576 481 TRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQ 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1408 FDEKHQINDKLEKTRNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKNISARYGEERDRAEAEAREKETKALS 1487
Cdd:pfam01576 561 LEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALS 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1488 LSRALEEAIDLKDELDRQNKQLRAEMDDLVSSKDDVGKNVHELERSKRALEQQVQEMKTQIEELEDELQAIEDGKLRLEV 1567
Cdd:pfam01576 641 LARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEV 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1568 NMQAMKAQFERDLQNRDDSNDEKKKLLFKQVREMEVELEEERKQKSQILAAKKKLEMDLQDMESQMDSANKGRDEAVKQL 1647
Cdd:pfam01576 721 NMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQL 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1648 KKLQLQFKEVWREVEETRAARDEIFVQSRDNEKKLKSLEAELLQLQEDLAAAERAKRQAQQERDDLADELSNGVSGKSAL 1727
Cdd:pfam01576 801 KKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSAL 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1728 LDEKRALEMRISQLEEELDEEQSNTELINDRYRKLTLQVETITTELSAERSFSQKAENARQQMERQNKELKVKLNEMDST 1807
Cdd:pfam01576 881 QDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGT 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1808 MRSKYKITIASLEAKISQLEEQMEQESKERIIANKLVRRAEKRLKEVLLQVEEERRNADQFKEQLEKANIRMKQLKRQLE 1887
Cdd:pfam01576 961 VKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLE 1040
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|.
gi 1785379719 1888 EAEEEASRANSNRRRLQRELEDVTESAESMNREVTTLRSRL 1928
Cdd:pfam01576 1041 EAEEEASRANAARRKLQRELDDATESNESMNREVSTLKSKL 1081
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
99-771 |
0e+00 |
|
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. Thus, myosin II has two heads. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276951 [Multi-domain] Cd Length: 662 Bit Score: 1313.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTG 178
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 179 ESGAGKTENTKKVIQYLAHVASSHKGRK-EHTAPGELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIV 257
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASSKKKKeSGKKKGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTGKIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 258 GANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGF-NQYRFLSNGNLPIPGQQDREIFQETMESMKIM 336
Cdd:cd01377 161 GADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDpSYYFFLSQGELTIDGVDDAEEFKLTDEAFDIL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 337 GFNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASMPDNTAAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQKAQTKEQ 416
Cdd:cd01377 241 GFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKGQNKEQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 417 ADFAVEALAKALYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFVLEQ 496
Cdd:cd01377 321 VVFSVGALAKALYERLFLWLVKRINKTLD-TKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMFVLEQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 497 EEYQREGIEWNFIDFGLDLQPCIDLIERPanPPGVLSLLDEECWFPKATDKSFVEKVIQELGNHPK-FQKPRQLRDKADL 575
Cdd:cd01377 400 EEYKKEGIEWTFIDFGLDLQPTIDLIEKP--NMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKnFKKPKPKKSEAHF 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 576 CIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVDRivgldqvsgmgEMSFGSSYKTKKGMFRTVGQ 655
Cdd:cd01377 478 ILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEE-----------SGGGGGKKKKKGGSFRTVSQ 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 656 LYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNA 735
Cdd:cd01377 547 LHKEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNA 626
|
650 660 670
....*....|....*....|....*....|....*.
gi 1785379719 736 IPKGFMDGKQACAIMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd01377 627 IPKGFDDGKAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
99-771 |
0e+00 |
|
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain 18. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276895 [Multi-domain] Cd Length: 676 Bit Score: 1237.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTG 178
Cdd:cd14932 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 179 ESGAGKTENTKKVIQYLAHVASSHKGRKEHTAP----GELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAG 254
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVASSFKTKKDQSSIalshGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 255 YIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNGNLPIPGQQDREIFQETMESMK 334
Cdd:cd14932 161 YIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNVTIPGQQDKELFAETMEAFR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 335 IMGFNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASMPDNTAAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQKAQTK 414
Cdd:cd14932 241 IMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQKAQTQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 415 EQADFAVEALAKALYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFVL 494
Cdd:cd14932 321 EQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 495 EQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLSLLDEECWFPKATDKSFVEKVIQELGNHPKFQKPRQLRDKAD 574
Cdd:cd14932 401 EQEEYQREGIEWSFIDFGLDLQPCIELIEKPNGPPGILALLDEECWFPKATDKSFVEKVVQEQGNNPKFQKPKKLKDDAD 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 575 LCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVDRIVGLDQVSGMGEMSFGsSYKTKKGMFRTVG 654
Cdd:cd14932 481 FCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVDRIVGLDKVAGMGESLHG-AFKTRKGMFRTVG 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 655 QLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 734
Cdd:cd14932 560 QLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 639
|
650 660 670
....*....|....*....|....*....|....*..
gi 1785379719 735 AIPKGFMDGKQACAIMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14932 640 AIPKGFMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
99-771 |
0e+00 |
|
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy chain 9 (also called NMMHCA, NMHC-II-A, MHA, FTNS, EPSTS, and DFNA17). Myosin is a hexameric protein composed of a pair of myosin heavy chains (MYH) and two pairs of nonidentical light chains. The encoded protein is a myosin IIA heavy chain that contains an IQ domain and a myosin head-like domain which is involved in several important functions, including cytokinesis, cell motility and maintenance of cell shape. Defects in this gene have been associated with non-syndromic sensorineural deafness autosomal dominant type 17, Epstein syndrome, Alport syndrome with macrothrombocytopenia, Sebastian syndrome, Fechtner syndrome and macrothrombocytopenia with progressive sensorineural deafness. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276883 [Multi-domain] Cd Length: 670 Bit Score: 1197.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTG 178
Cdd:cd14919 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 179 ESGAGKTENTKKVIQYLAHVASSHKGRKEHtapGELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 258
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHVASSHKSKKDQ---GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 259 ANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNGNLPIPGQQDREIFQETMESMKIMGF 338
Cdd:cd14919 158 ANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 339 NHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASMPDNTAAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQKAQTKEQAD 418
Cdd:cd14919 238 PEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQAD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 419 FAVEALAKALYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFVLEQEE 498
Cdd:cd14919 318 FAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 499 YQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLSLLDEECWFPKATDKSFVEKVIQELGNHPKFQKPRQLRDKADLCII 578
Cdd:cd14919 398 YQREGIEWNFIDFGLDLQPCIDLIEKPAGPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKQLKDKADFCII 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 579 HYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVDRIVGLDQVSGMGEMSFGSSYKTKKGMFRTVGQLYK 658
Cdd:cd14919 478 HYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGMSETALPGAFKTRKGMFRTVGQLYK 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 659 ESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPK 738
Cdd:cd14919 558 EQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPK 637
|
650 660 670
....*....|....*....|....*....|...
gi 1785379719 739 GFMDGKQACAIMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14919 638 GFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
99-771 |
0e+00 |
|
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin heavy chain 11 (also called SMMHC, SMHC). The gene product is a subunit of a hexameric protein that consists of two heavy chain subunits and two pairs of non-identical light chain subunits. It functions as a major contractile protein, converting chemical energy into mechanical energy through the hydrolysis of ATP. The gene encoding a human ortholog of rat NUDE1 is transcribed from the reverse strand of this gene, and its 3' end overlaps with that of the latter. Inversion of the MYH11 locus is one of the most frequent chromosomal aberrations found in acute myeloid leukemia. Alternative splicing generates isoforms that are differentially expressed, with ratios changing during muscle cell maturation. Mutations in MYH11 have been described in individuals with thoracic aortic aneurysms leading to acute aortic dissections with patent ductus arteriosus. MYH11 mutations are also thought to contribute to human colorectal cancer and are also associated with Peutz-Jeghers syndrome. The mutations found in human intestinal neoplasia result in unregulated proteins with constitutive motor activity, similar to the mutant myh11 zebrafish. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276885 [Multi-domain] Cd Length: 673 Bit Score: 1187.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTG 178
Cdd:cd14921 1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 179 ESGAGKTENTKKVIQYLAHVASSHKGRKEHTAPGELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 258
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVVASSHKGKKDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 259 ANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNGNLPIPGQQDREIFQETMESMKIMGF 338
Cdd:cd14921 161 ANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDDEMFQETLEAMSIMGF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 339 NHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASMPDNTAAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQKAQTKEQAD 418
Cdd:cd14921 241 SEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQAD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 419 FAVEALAKALYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFVLEQEE 498
Cdd:cd14921 321 FAIEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 499 YQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLSLLDEECWFPKATDKSFVEKVIQELGNHPKFQKPRQLRDKADLCII 578
Cdd:cd14921 401 YQREGIEWNFIDFGLDLQPCIELIERPNNPPGVLALLDEECWFPKATDKSFVEKLCTEQGNHPKFQKPKQLKDKTEFSII 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 579 HYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVDRIVGLDQVSGMGEMSFGSSYKTKKGMFRTVGQLYK 658
Cdd:cd14921 481 HYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVGLDQMAKMTESSLPSASKTKKGMFRTVGQLYK 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 659 ESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPK 738
Cdd:cd14921 561 EQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANAIPK 640
|
650 660 670
....*....|....*....|....*....|...
gi 1785379719 739 GFMDGKQACAIMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14921 641 GFMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
99-771 |
0e+00 |
|
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain 19. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276899 [Multi-domain] Cd Length: 675 Bit Score: 1173.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTG 178
Cdd:cd15896 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 179 ESGAGKTENTKKVIQYLAHVASSHKGRKEHT----APGELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAG 254
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVASSHKTKKDQNslalSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 255 YIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNGNLPIPGQQDREIFQETMESMK 334
Cdd:cd15896 161 YIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYNNYRFLSNGNVTIPGQQDKDLFTETMEAFR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 335 IMGFNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASMPDNTAAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQKAQTK 414
Cdd:cd15896 241 IMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQKAQTQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 415 EQADFAVEALAKALYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFVL 494
Cdd:cd15896 321 EQAEFAVEALAKATYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 495 EQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLSLLDEECWFPKATDKSFVEKVIQELGNHPKFQKPRQLRDKAD 574
Cdd:cd15896 401 EQEEYQREGIEWSFIDFGLDLQPCIDLIEKPASPPGILALLDEECWFPKATDKSFVEKVLQEQGTHPKFFKPKKLKDEAD 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 575 LCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVDRIVGLDQVSGMGEMSfgSSYKTKKGMFRTVG 654
Cdd:cd15896 481 FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVDRIVGLDKVSGMSEMP--GAFKTRKGMFRTVG 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 655 QLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 734
Cdd:cd15896 559 QLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 638
|
650 660 670
....*....|....*....|....*....|....*..
gi 1785379719 735 AIPKGFMDGKQACAIMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd15896 639 AIPKGFMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
99-771 |
0e+00 |
|
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy chain 14 (also called FLJ13881, KIAA2034, MHC16, MYH17). Its members include mammals, chickens, and turtles. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Some of the data used for this classification were produced by the CyMoBase team at the Max-Planck-Institute for Biophysical Chemistry. The sequence names are composed of the species abbreviation followed by the protein abbreviation and optional protein classifier and variant designations.
Pssm-ID: 276893 [Multi-domain] Cd Length: 670 Bit Score: 1169.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTG 178
Cdd:cd14930 1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 179 ESGAGKTENTKKVIQYLAHVASSHKGRKEHTAPGELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 258
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 259 ANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNGNLPIPGQQdREIFQETMESMKIMGF 338
Cdd:cd14930 161 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQE-RELFQETLESLRVLGF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 339 NHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASMPDNTAAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQKAQTKEQAD 418
Cdd:cd14930 240 SHEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQAD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 419 FAVEALAKALYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFVLEQEE 498
Cdd:cd14930 320 FALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 499 YQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLSLLDEECWFPKATDKSFVEKVIQELGNHPKFQKPRQLRDKADLCII 578
Cdd:cd14930 400 YQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRHLRDQADFSVL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 579 HYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVDRIVGLDQVSGMGEMSFGSsyKTKKGMFRTVGQLYK 658
Cdd:cd14930 480 HYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDGPPGG--RPRRGMFRTVGQLYK 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 659 ESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPK 738
Cdd:cd14930 558 ESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPK 637
|
650 660 670
....*....|....*....|....*....|...
gi 1785379719 739 GFMDGKQACAIMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14930 638 GFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
99-771 |
0e+00 |
|
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle myosin heavy chain 2 (also called MYH2A, MYHSA2, MyHC-IIa, MYHas8, MyHC-2A) in insects and mollusks. This gene encodes a member of the class II or conventional myosin heavy chains, and functions in skeletal muscle contraction. Mutations in this gene results in inclusion body myopathy-3 and familial congenital myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276876 [Multi-domain] Cd Length: 674 Bit Score: 1155.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTG 178
Cdd:cd14911 1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 179 ESGAGKTENTKKVIQYLAHVASShKGRKEHTAP----------GELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 248
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVAAS-KPKGSGAVPhpavnpavliGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 249 NFDVAGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNGNLPIPGQQDREIFQE 328
Cdd:cd14911 160 NFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVPGVDDYAEFQA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 329 TMESMKIMGFNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASMPDNTAAQKLCHLLGLNVTEFSRAILMPRIKVGRDYV 408
Cdd:cd14911 240 TVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 409 QKAQTKEQADFAVEALAKALYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFN 488
Cdd:cd14911 320 TKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 489 HTMFVLEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLSLLDEECWFPKATDKSFVEKVIQELGNHPKFQKpRQ 568
Cdd:cd14911 400 HTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPG---GIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMK-TD 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 569 LRDKADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVDrIVGLDQvSGMGEMSFGSsyKTKKG 648
Cdd:cd14911 476 FRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAE-IVGMAQ-QALTDTQFGA--RTRKG 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 649 MFRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 728
Cdd:cd14911 552 MFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRY 631
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1785379719 729 EILTPNAIPKGFMDGKQACAIMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14911 632 ELLTPNVIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
87-771 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 1108.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 87 VEDMAELTCLNEASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSML 166
Cdd:pfam00063 1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 167 QDREDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKEhtapGELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFI 246
Cdd:pfam00063 81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAGNV----GRLEEQILQSNPILEAFGNAKTVRNNNSSRFGKYI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 247 RINFDVAGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNGN-LPIPGQQDREI 325
Cdd:pfam00063 157 EIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYLSQSGcYTIDGIDDSEE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 326 FQETMESMKIMGFNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASMPDNTAAQKLCHLLGLNVTEFSRAILMPRIKVGR 405
Cdd:pfam00063 237 FKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCKRRIKTGR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 406 DYVQKAQTKEQADFAVEALAKALYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQ 485
Cdd:pfam00063 317 ETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTIEKASFIGVLDIYGFEIFEKNSFEQLCINYVNEKLQQ 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 486 LFNHTMFVLEQEEYQREGIEWNFIDFGlDLQPCIDLIERPanPPGVLSLLDEECWFPKATDKSFVEKVIQELGNHPKFQK 565
Cdd:pfam00063 397 FFNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEKK--PLGILSLLDEECLFPKATDQTFLDKLYSTFSKHPHFQK 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 566 PRQlRDKADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVDRIVGLDQVSGMGEMsfgsSYKT 645
Cdd:pfam00063 474 PRL-QGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESAAANESGKST----PKRT 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 646 KKGMFRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFR 725
Cdd:pfam00063 549 KKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQEFV 628
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 1785379719 726 QRYEILTPNAIPKGFMDGKQACAIMIRALELDPNLYRIGQSKIFFR 771
Cdd:pfam00063 629 QRYRILAPKTWPKWKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
80-783 |
0e+00 |
|
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical interaction between myosin and actin. The core of the myosin structure is similar in fold to that of kinesin.
Pssm-ID: 214580 [Multi-domain] Cd Length: 677 Bit Score: 1014.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 80 NPPKFTKVEDMAELTCLNEASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISE 159
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 160 TAYRSMLQDREDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRkehtapGELEHQLLQANPILEAFGNAKTVKNDNS 239
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNTEV------GSVEDQILESNPILEAFGNAKTLRNNNS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 240 SRFGKFIRINFDVAGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNGNLP-IP 318
Cdd:smart00242 155 SRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSPEDYRYLNQGGCLtVD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 319 GQQDREIFQETMESMKIMGFNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASMPDNT-AAQKLCHLLGLNVTEFSRAIL 397
Cdd:smart00242 235 GIDDAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAASTVKDKeELSNAAELLGVDPEELEKALT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 398 MPRIKVGRDYVQKAQTKEQADFAVEALAKALYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCIN 477
Cdd:smart00242 315 KRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLS-FKDGSTYFIGVLDIYGFEIFEVNSFEQLCIN 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 478 YTNEKLQQLFNHTMFVLEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLSLLDEECWFPKATDKSFVEKVIQEL 557
Cdd:smart00242 394 YANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIE--KKPPGILSLLDEECRFPKGTDQTFLEKLNQHH 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 558 GNHPKFQKPRQlRDKADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDvdrivgldqvsgmgem 637
Cdd:smart00242 471 KKHPHFSKPKK-KGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPS---------------- 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 638 sfGSSYKTKKGMFRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPN 717
Cdd:smart00242 534 --GVSNAGSKKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPY 611
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1785379719 718 RIVFQEFRQRYEILTPNAIPKGFMDGKQACAIMIRALELDPNLYRIGQSKIFFRAGVLAHLEEERD 783
Cdd:smart00242 612 RLPFDEFLQRYRVLLPDTWPPWGGDAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELRE 677
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
35-1245 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 930.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 35 QVWVPSEKHGFEAASIKEERGEEVIVELA---ENGKRVPVAKDDIQ--KMNPPKFTKVEDMAELTCLNEASVLHNLKDRY 109
Cdd:COG5022 11 GCWIPDEEKGWIWAEIIKEAFNKGKVTEEgkkEDGESVSVKKKVLGndRIKLPKFDGVDDLTELSYLNEPAVLHNLEKRY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 110 YSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTGESGAGKTENTK 189
Cdd:COG5022 91 NNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTENAK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 190 KVIQYLAHVASSHkgrkeHTAPGELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVGANIETYLLEKS 269
Cdd:COG5022 171 RIMQYLASVTSSS-----TVEISSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETYLLEKS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 270 RAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNGNLP-IPGQQDREIFQETMESMKIMGFNHEEIMSMLK 348
Cdd:COG5022 246 RVVHQNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLSQGGCDkIDGIDDAKEFKITLDALKTIGIDEEEQDQIFK 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 349 MVSAVLQFGNIVFRKERNtDQASMPDNTAAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQKAQTKEQADFAVEALAKAL 428
Cdd:COG5022 326 ILAAILHIGNIEFKEDRN-GAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALAIRDSLAKAL 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 429 YERLFRWLVHRINKALDRTKRQGaSFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIEWNF 508
Cdd:COG5022 405 YSNLFDWIVDRINKSLDHSAAAS-NFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKEGIEWSF 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 509 IDFgLDLQPCIDLIERpANPPGVLSLLDEECWFPKATDKSFVEKVIQEL--GNHPKFQKPRQLRDKadLCIIHYAGKVDY 586
Cdd:COG5022 484 IDY-FDNQPCIDLIEK-KNPLGILSLLDEECVMPHATDESFTSKLAQRLnkNSNPKFKKSRFRDNK--FVVKHYAGDVEY 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 587 KADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVDRIVgldqvsgmgemsfgssyktKKGMFRTVGQLYKESLSKLMS 666
Cdd:COG5022 560 DVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDEENIE-------------------SKGRFPTLGSRFKESLNSLMS 620
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 667 TLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNA----IPKGFMD 742
Cdd:COG5022 621 TLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSKswtgEYTWKED 700
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 743 GKQACAIMIRALELDPNLYRIGQSKIFFRAGVLAHLEEERDLKITDIIVFFQAAARGYLARRAFYKKQQQMSALKVVQRN 822
Cdd:COG5022 701 TKNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKKIQVIQHG 780
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 823 CAAYLKLRHWQWWRLFTKVKPLLQVTRQDEVMQAKvvelqkvkdtqvkteselKEMANKYQQLFEEKSILAEQLQAETEL 902
Cdd:COG5022 781 FRLRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSY------------------LACIIKLQKTIKREKKLRETEEVEFSL 842
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 903 FAEAEEMRARLASKKQELEEILHDLEARVEEeeertlqLQNEKKKMHQHIQDLEEQLEEEEGARQKLQLEKVTTESRLKK 982
Cdd:COG5022 843 KAEVLIQKFGRSLKAKKRFSLLKKETIYLQS-------AQRVELAERQLQELKIDVKSISSLKLVNLELESEIIELKKSL 915
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 983 MEEDILLLEDQNAKLAKERKLLDDR-IGEFTSTMAEEEEKVKSLNKLRNKYEAVIADLEDRLKKEEKGRQEMEKMKRKLD 1061
Cdd:COG5022 916 SSDLIENLEFKTELIARLKKLLNNIdLEEGPSIEYVKLPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELK 995
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1062 GETTDLQDQLLELQQQIEELKQ--QLARKEEELQAALARV---DDEVGQKNNLLKQLRDLQSQLAELhedlesekAARAK 1136
Cdd:COG5022 996 NFKKELAELSKQYGALQESTKQlkELPVEVAELQSASKIIsseSTELSILKPLQKLKGLLLLENNQL--------QARYK 1067
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1137 AEKQRRDLGEELEALKTELEDT--LDSTAAQQELRAKReqevTDLKKTIEEDVKVRDAQVTemrqrhNQVVEEISEQLEQ 1214
Cdd:COG5022 1068 ALKLRRENSLLDDKQLYQLESTenLLKTINVKDLEVTN----RNLVKPANVLQFIVAQMIK------LNLLQEISKFLSQ 1137
|
1210 1220 1230
....*....|....*....|....*....|...
gi 1785379719 1215 ArrfKGNLEKVKQTLESENTDL--IKEVKNLQA 1245
Cdd:COG5022 1138 L---VNTLEPVFQKLSVLQLELdgLFWEANLEA 1167
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
99-771 |
0e+00 |
|
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276950 [Multi-domain] Cd Length: 633 Bit Score: 859.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRH-EIPPHIYAISETAYRSMLQDREDQSILCT 177
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 178 GESGAGKTENTKKVIQYLAHVASSHKGRKEHTApGELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIV 257
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAALSGSGSSKSSSSA-SSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPTGRLV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 258 GANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFL-----SNGNLPIPGQQDREIFQETMES 332
Cdd:cd00124 160 GASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYYYLndylnSSGCDRIDGVDDAEEFQELLDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 333 MKIMGFNHEEIMSMLKMVSAVLQFGNIVF--RKERNTDQASMPDNTAAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQK 410
Cdd:cd00124 240 LDVLGFSDEEQDSIFRILAAILHLGNIEFeeDEEDEDSSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGETITK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 411 AQTKEQADFAVEALAKALYERLFRWLVHRINKALDRTKRQ-GASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNH 489
Cdd:cd00124 320 PLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAeSTSFIGILDIFGFENFEVNSFEQLCINYANEKLQQFFNQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 490 TMFVLEQEEYQREGIEWNFIDFgLDLQPCIDLIERPanPPGVLSLLDEECWFPKATDKSFVEKVIQELGNHPKFQKPRQL 569
Cdd:cd00124 400 HVFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEGK--PLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFFSKKRK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 570 RDKAdLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDkytaelwkdvdrivgldqvsgmgemsfgssyktkkgm 649
Cdd:cd00124 477 AKLE-FGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSGSQ------------------------------------- 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 650 frtvgqlYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 729
Cdd:cd00124 519 -------FRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYR 591
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1785379719 730 ILTPNAIPKGFMDGKQACAIMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd00124 592 ILAPGATEKASDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
99-771 |
0e+00 |
|
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta myosin heavy chain 7b (also called KIAA1512, dJ756N5.1, MYH14, MHC14). MYH7B is a slow-twitch myosin. Mutations in this gene result in one form of autosomal dominant hearing impairment. Multiple transcript variants encoding different isoforms have been found for this gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276953 [Multi-domain] Cd Length: 676 Bit Score: 773.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTG 178
Cdd:cd14927 1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 179 ESGAGKTENTKKVIQYLAHVASSHKGRKEHTAP------GELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDV 252
Cdd:cd14927 81 ESGAGKTVNTKRVIQYFAIVAALGDGPGKKAQFlatktgGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 253 AGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKtDLLLEGFN--QYRFLSNGNLPIPGQQDREIFQETM 330
Cdd:cd14927 161 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQ-DMLLVSMNpyDYHFCSQGVTTVDNMDDGEELMATD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 331 ESMKIMGFNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASMPDNTAAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQK 410
Cdd:cd14927 240 HAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYVTK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 411 AQTKEQADFAVEALAKALYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHT 490
Cdd:cd14927 320 GQSVEQVVYAVGALAKATYDRMFKWLVSRINQTLD-TKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHH 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 491 MFVLEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLSLLDEECWFPKATDKSFVEKVI-QELGNHPKFQKPR-- 567
Cdd:cd14927 399 MFILEQEEYKREGIEWVFIDFGLDLQACIDLIEKPL---GILSILEEECMFPKASDASFKAKLYdNHLGKSPNFQKPRpd 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 568 -QLRDKADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVdriVGLDQVsgmGEMSFGSSYKTK 646
Cdd:cd14927 476 kKRKYEAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYENY---VGSDST---EDPKSGVKEKRK 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 647 KGM-FRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFR 725
Cdd:cd14927 550 KAAsFQTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFK 629
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1785379719 726 QRYEILTPNAIPK-GFMDGKQACAIMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14927 630 QRYRILNPSAIPDdKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
100-771 |
0e+00 |
|
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle myosin heavy chain 3 (MYHC-EMB, MYHSE1, HEMHC, SMHCE) in tetrapods including mammals, lizards, and frogs. This gene is a member of the MYH family and encodes a protein with an IQ domain and a myosin head-like domain. Mutations in this gene have been associated with two congenital contracture (arthrogryposis) syndromes, Freeman-Sheldon syndrome and Sheldon-Hall syndrome. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276878 [Multi-domain] Cd Length: 668 Bit Score: 768.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTGE 179
Cdd:cd14913 2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 180 SGAGKTENTKKVIQYLAHVASSH--KGRKEHTAPGELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIV 257
Cdd:cd14913 82 SGAGKTVNTKRVIQYFATIAATGdlAKKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 258 GANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMkTDLLLEGFNQYR--FLSNGNLPIPGQQDREIFQETMESMKI 335
Cdd:cd14913 162 SADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPEL-IELLLITTNPYDypFISQGEILVASIDDAEELLATDSAIDI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 336 MGFNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASmPDNT-AAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQKAQTK 414
Cdd:cd14913 241 LGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 415 EQADFAVEALAKALYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFVL 494
Cdd:cd14913 320 DQVHHAVNALSKSVYEKLFLWMVTRINQQLD-TKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 495 EQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLSLLDEECWFPKATDKSFVEKVI-QELGNHPKFQKPRQLRDKA 573
Cdd:cd14913 399 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSNNFQKPKVVKGRA 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 574 D--LCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVDrivgldqvSGMGEMSFGSSYKTKKGMFR 651
Cdd:cd14913 476 EahFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFA--------TADADSGKKKVAKKKGSSFQ 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 652 TVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 731
Cdd:cd14913 548 TVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVL 627
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 1785379719 732 TPNAIPKG-FMDGKQACAIMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14913 628 NASAIPEGqFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
99-771 |
0e+00 |
|
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle myosin heavy chain 1 (also called MYHSA1, MYHa, MyHC-2X/D, MGC133384) in insects and crustaceans. Myh1 is a type I skeletal muscle myosin that in Humans is encoded by the MYH1 gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276874 Cd Length: 666 Bit Score: 760.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTG 178
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 179 ESGAGKTENTKKVIQYLAHVASSHKGRKEHTAPGELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 258
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGASKKTDEAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 259 ANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLL-EGFNQYRFLSNGNLPIPGQQDREIFQETMESMKIMG 337
Cdd:cd14909 161 ADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLsDNIYDYYIVSQGKVTVPNVDDGEEFSLTDQAFDILG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 338 FNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASMPDNTAAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQKAQTKEQA 417
Cdd:cd14909 241 FTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNVQQV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 418 DFAVEALAKALYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFVLEQE 497
Cdd:cd14909 321 TNSIGALCKGVFDRLFKWLVKKCNETLD-TQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLEQE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 498 EYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLSLLDEECWFPKATDKSFVEKVI-QELGNHPKFQKPRQLR---DKA 573
Cdd:cd14909 400 EYKREGIDWAFIDFGMDLLACIDLIEKPM---GILSILEEESMFPKATDQTFSEKLTnTHLGKSAPFQKPKPPKpgqQAA 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 574 DLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDvdrivGLDQVSGMGEMSFGSsyKTKKGMFRTV 653
Cdd:cd14909 477 HFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFAD-----HAGQSGGGEQAKGGR--GKKGGGFATV 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 654 GQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTP 733
Cdd:cd14909 550 SSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNP 629
|
650 660 670
....*....|....*....|....*....|....*...
gi 1785379719 734 NAIpKGFMDGKQACAIMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14909 630 AGI-QGEEDPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
99-771 |
0e+00 |
|
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 pseudogene (also called MHC20, MYH16, and myh5), encoding a sarcomeric myosin heavy chain expressed in nonhuman primate masticatory muscles, is inactivated in humans. This cd contains Myh16 in mammals. MYH16 has intermediate fibres between that of slow type 1 and fast 2B fibres, but exert more force than any other fibre type examined. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Some of the data used for this classification were produced by the CyMoBase team at the Max-Planck-Institute for Biophysical Chemistry. The sequence names are composed of the species abbreviation followed by the protein abbreviation and optional protein classifier and variant designations.
Pssm-ID: 276896 [Multi-domain] Cd Length: 659 Bit Score: 730.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTG 178
Cdd:cd14934 1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 179 ESGAGKTENTKKVIQYLAHVASShkGRKEHTAPGELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 258
Cdd:cd14934 81 ESGAGKTENTKKVIQYFANIGGT--GKQSSDGKGSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKLAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 259 ANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAG-EHMKTDLLLEGFNQYRFLSNGNLPIPGQQDREIFQETMESMKIMG 337
Cdd:cd14934 159 ADIESYLLEKSRVISQQAAERGYHIFYQILSNKKpELIESLLLVPNPKEYHWVSQGVTVVDNMDDGEELQITDVAFDVLG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 338 FNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASMPDNTAAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQKAQTKEQA 417
Cdd:cd14934 239 FSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQKGQNMEQC 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 418 DFAVEALAKALYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFVLEQE 497
Cdd:cd14934 319 NNSIGALGKAVYDKMFKWLVVRINKTLD-TKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFVLEQE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 498 EYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLSLLDEECWFPKATDKSFVEKVI-QELGNHPKFQKPRQLRDK---A 573
Cdd:cd14934 398 EYKREGIEWVFIDFGLDLQACIDLLEKPM---GIFSILEEQCVFPKATDATFKAALYdNHLGKSSNFLKPKGGKGKgpeA 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 574 DLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDvdrivgldqvsgmgEMSFGSSYKTKKGM-FRT 652
Cdd:cd14934 475 HFELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSSLGLLALLFKE--------------EEAPAGSKKQKRGSsFMT 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 653 VGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILT 732
Cdd:cd14934 541 VSNFYREQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLN 620
|
650 660 670
....*....|....*....|....*....|....*....
gi 1785379719 733 PNAIPKGFMDGKQACAIMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14934 621 PNVIPQGFVDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
100-771 |
0e+00 |
|
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins that transport a variety of intracellular cargo processively along actin filaments, such as melanosomes, synaptic vesicles, vacuoles, and mRNA. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. It also contains a IQ domain and a globular DIL domain. Myosin V is a class of actin-based motor proteins involved in cytoplasmic vesicle transport and anchorage, spindle-pole alignment and mRNA translocation. The protein encoded by this gene is abundant in melanocytes and nerve cells. Mutations in this gene cause Griscelli syndrome type-1 (GS1), Griscelli syndrome type-3 (GS3) and neuroectodermal melanolysosomal disease, or Elejalde disease. Multiple alternatively spliced transcript variants encoding different isoforms have been reported, but the full-length nature of some variants has not been determined. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Note that the Dictyostelium myoVs are not contained in this child group. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276831 [Multi-domain] Cd Length: 629 Bit Score: 725.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 100 SVLHNLKDRYYSG-LIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTG 178
Cdd:cd01380 2 AVLHNLKVRFCQRnAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 179 ESGAGKTENTKKVIQYLAHVASSHKGrkEHtapgELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 258
Cdd:cd01380 82 ESGAGKTVSAKYAMRYFATVGGSSSG--ET----QVEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYRIIG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 259 ANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNGNLP-IPGQQDREIFQETMESMKIMG 337
Cdd:cd01380 156 ANMRTYLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNQGGSPvIDGVDDAAEFEETRKALTLLG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 338 FNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASMPDNTAAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQKAQTKEQA 417
Cdd:cd01380 236 ISEEEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPLTLQQA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 418 DFAVEALAKALYERLFRWLVHRINKALDRTKRQGA-SFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFVLEQ 496
Cdd:cd01380 316 IVARDALAKHIYAQLFDWIVDRINKALASPVKEKQhSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHVFKLEQ 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 497 EEYQREGIEWNFIDFgLDLQPCIDLIErpaNPPGVLSLLDEECWFPKATDKSFVEKVIQELGNHPK--FQKPRqLRDKAD 574
Cdd:cd01380 396 EEYVKEEIEWSFIDF-YDNQPCIDLIE---GKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKPNkhFKKPR-FSNTAF 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 575 LcIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKytaelwkdvdrivgldqvsgmgemsfgssyktKKgmfrTVG 654
Cdd:cd01380 471 I-VKHFADDVEYQVEGFLEKNRDTVSEEHLNVLKASKNR--------------------------------KK----TVG 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 655 QLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 734
Cdd:cd01380 514 SQFRDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLPS 593
|
650 660 670
....*....|....*....|....*....|....*..
gi 1785379719 735 AIPKGfMDGKQACAIMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd01380 594 KEWLR-DDKKKTCENILENLILDPDKYQFGKTKIFFR 629
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
99-771 |
0e+00 |
|
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy chain 15 in mammals (also called KIAA1000) . MYH15 is a slow-twitch myosin. Myh15 is a ventricular myosin heavy chain. Myh15 is absent in embryonic and fetal muscles and is found in orbital layer of extraocular muscles at birth. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276892 [Multi-domain] Cd Length: 662 Bit Score: 708.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTG 178
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 179 ESGAGKTENTKKVIQYLAHVASSHKGRKEHtapGELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 258
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAMIESKKKL---GALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 259 ANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNGNLPIPGQQDREIFQETMESMKIMGF 338
Cdd:cd14929 158 ADIDIYLLEKSRVIFQQPGERNYHIFYQILSGKKELRDLLLVSANPSDFHFCSCGAVAVESLDDAEELLATEQAMDILGF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 339 NHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASMPDNTAAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQKAQTKEQAD 418
Cdd:cd14929 238 LPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTRSQNIEQVT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 419 FAVEALAKALYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFVLEQEE 498
Cdd:cd14929 318 YAVGALSKSIYERMFKWLVARINRVLD-AKLSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMFVLEQEE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 499 YQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLSLLDEECWFPKATDKSFVEKVI-QELGNHPKFQKPRQLRDK--ADL 575
Cdd:cd14929 397 YRKEGIDWVSIDFGLDLQACIDLIEKPM---GIFSILEEECMFPKATDLTFKTKLFdNHFGKSVHFQKPKPDKKKfeAHF 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 576 CIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKdvdrivglDQVSGMGEMSFGSSYKTKKGMFRTVGQ 655
Cdd:cd14929 474 ELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFE--------NYISTDSAIQFGEKKRKKGASFQTVAS 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 656 LYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNA 735
Cdd:cd14929 546 LHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNPRT 625
|
650 660 670
....*....|....*....|....*....|....*..
gi 1785379719 736 IPKG-FMDGKQACAIMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14929 626 FPKSkFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
100-771 |
0e+00 |
|
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I cardiac muscle myosin heavy chain 7 (also called CMH1, MPD1, and CMD1S). Muscle myosin is a hexameric protein containing 2 heavy chain subunits, 2 alkali light chain subunits, and 2 regulatory light chain subunits. It is expressed predominantly in normal human ventrical and in skeletal muscle tissues rich in slow-twitch type I muscle fibers. Changes in the relative abundance of this protein and the alpha (or fast) heavy subunit of cardiac myosin correlate with the contractile velocity of cardiac muscle. Its expression is also altered during thyroid hormone depletion and hemodynamic overloading. Mutations in this gene are associated with familial hypertrophic cardiomyopathy, myosin storage myopathy, dilated cardiomyopathy, and Laing early-onset distal myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276881 [Multi-domain] Cd Length: 668 Bit Score: 706.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTGE 179
Cdd:cd14917 2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 180 SGAGKTENTKKVIQYLAHVASSHKGRKEHTAPGE--LEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIV 257
Cdd:cd14917 82 SGAGKTVNTKRVIQYFAVIAAIGDRSKKDQTPGKgtLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 258 GANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMkTDLLLEGFN--QYRFLSNGNLPIPGQQDREIFQETMESMKI 335
Cdd:cd14917 162 SADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPEL-LDMLLITNNpyDYAFISQGETTVASIDDAEELMATDNAFDV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 336 MGFNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASmPDNT-AAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQKAQTK 414
Cdd:cd14917 241 LGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAE-PDGTeEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 415 EQADFAVEALAKALYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFVL 494
Cdd:cd14917 320 QQVIYATGALAKAVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 495 EQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLSLLDEECWFPKATDKSFVEKVI-QELGNHPKFQKPRQLRDK- 572
Cdd:cd14917 399 EQEEYKKEGIEWTFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKATDMTFKAKLFdNHLGKSNNFQKPRNIKGKp 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 573 -ADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVdriVGLDQV--SGMGEMSFGSSyktkkgm 649
Cdd:cd14917 476 eAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFANY---AGADAPieKGKGKAKKGSS------- 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 650 FRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 729
Cdd:cd14917 546 FQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYR 625
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1785379719 730 ILTPNAIPKG-FMDGKQACAIMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14917 626 ILNPAAIPEGqFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
101-771 |
0e+00 |
|
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle myosin heavy chain 8 (also called MyHC-peri, MyHC-pn). Myosin is a hexameric protein composed of a pair of myosin heavy chains (MYH) and two pairs of nonidentical light chains. A mutation in this gene results in trismus-pseudocamptodactyly syndrome. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276882 [Multi-domain] Cd Length: 668 Bit Score: 689.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 101 VLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTGES 180
Cdd:cd14918 3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 181 GAGKTENTKKVIQYLAHVASSHKGRKEHTAP--GELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 258
Cdd:cd14918 83 GAGKTVNTKRVIQYFATIAVTGEKKKEESGKmqGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLAS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 259 ANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMkTDLLLEGFN--QYRFLSNGNLPIPGQQDREIFQETMESMKIM 336
Cdd:cd14918 163 ADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDL-IEMLLITTNpyDYAFVSQGEITVPSIDDQEELMATDSAIDIL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 337 GFNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASmPDNT-AAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQKAQTKE 415
Cdd:cd14918 242 GFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 416 QADFAVEALAKALYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFVLE 495
Cdd:cd14918 321 QVYNAVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 496 QEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLSLLDEECWFPKATDKSFVEKVI-QELGNHPKFQKPRQLRDKAD 574
Cdd:cd14918 400 QEEYKKEGIEWTFIDFGMDLAACIELIEKPL---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSANFQKPKVVKGKAE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 575 --LCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVdrivgldqVSGMGEMSFGSSYKTKKGMFRT 652
Cdd:cd14918 477 ahFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTY--------ASAEADSGAKKGAKKKGSSFQT 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 653 VGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILT 732
Cdd:cd14918 549 VSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLN 628
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 1785379719 733 PNAIPKG-FMDGKQACAIMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14918 629 ASAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
100-771 |
0e+00 |
|
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle myosin heavy chain 2 (also called MYH2A, MYHSA2, MyHC-IIa, MYHas8, MyHC-2A) in mammals. Mutations in this gene results in inclusion body myopathy-3 and familial congenital myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276877 [Multi-domain] Cd Length: 673 Bit Score: 687.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTGE 179
Cdd:cd14912 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 180 SGAGKTENTKKVIQYLAHVASSHKGRKEHTAPGE----LEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGY 255
Cdd:cd14912 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEITSGKmqgtLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 256 IVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMkTDLLLEGFN--QYRFLSNGNLPIPGQQDREIFQETMESM 333
Cdd:cd14912 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPEL-IEMLLITTNpyDYPFVSQGEISVASIDDQEELMATDSAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 334 KIMGFNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASmPDNT-AAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQKAQ 412
Cdd:cd14912 241 DILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAE-PDGTeVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 413 TKEQADFAVEALAKALYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMF 492
Cdd:cd14912 320 TVEQVTNAVGALAKAVYEKMFLWMVARINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 493 VLEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLSLLDEECWFPKATDKSFVEKVI-QELGNHPKFQKPRQLRD 571
Cdd:cd14912 399 VLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYeQHLGKSANFQKPKVVKG 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 572 KAD--LCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVDRIVGldQVSGMGEMSFGssyKTKKGM 649
Cdd:cd14912 476 KAEahFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSGAQTAEG--ASAGGGAKKGG---KKKGSS 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 650 FRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 729
Cdd:cd14912 551 FQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYK 630
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1785379719 730 ILTPNAIPKG-FMDGKQACAIMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14912 631 VLNASAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
100-771 |
0e+00 |
|
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac muscle myosin heavy chain 6. Cardiac muscle myosin is a hexamer consisting of two heavy chain subunits, two light chain subunits, and two regulatory subunits. This gene encodes the alpha heavy chain subunit of cardiac myosin. Mutations in this gene cause familial hypertrophic cardiomyopathy and atrial septal defect. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276880 [Multi-domain] Cd Length: 670 Bit Score: 687.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTGE 179
Cdd:cd14916 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 180 SGAGKTENTKKVIQYLAHVAS-SHKGRKE--HTAPGELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYI 256
Cdd:cd14916 82 SGAGKTVNTKRVIQYFASIAAiGDRSKKEnpNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 257 VGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMkTDLLLEGFN--QYRFLSNGNLPIPGQQDREIFQETMESMK 334
Cdd:cd14916 162 ASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPEL-LDMLLVTNNpyDYAFVSQGEVSVASIDDSEELLATDSAFD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 335 IMGFNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASmPDNTA-AQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQKAQT 413
Cdd:cd14916 241 VLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAE-PDGTEdADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 414 KEQADFAVEALAKALYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFV 493
Cdd:cd14916 320 VQQVYYSIGALAKSVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 494 LEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLSLLDEECWFPKATDKSFVEKVI-QELGNHPKFQKPRQLRDK 572
Cdd:cd14916 399 LEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKASDMTFKAKLYdNHLGKSNNFQKPRNVKGK 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 573 --ADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVDRIVGLDQVSGMGEMSFGSSyktkkgmF 650
Cdd:cd14916 476 qeAHFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYASADTGDSGKGKGGKKKGSS-------F 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 651 RTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 730
Cdd:cd14916 549 QTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRI 628
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1785379719 731 LTPNAIPKG-FMDGKQACAIMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14916 629 LNPAAIPEGqFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
100-771 |
0e+00 |
|
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle myosin heavy chain 1 (also called MYHSA1, MYHa, MyHC-2X/D, MGC133384) in mammals. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276875 [Multi-domain] Cd Length: 671 Bit Score: 682.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTGE 179
Cdd:cd14910 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 180 SGAGKTENTKKVIQYLAHVASSHKGRKEHTAPGE----LEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGY 255
Cdd:cd14910 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEATSGKmqgtLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 256 IVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMkTDLLLEGFN--QYRFLSNGNLPIPGQQDREIFQETMESM 333
Cdd:cd14910 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDL-IEMLLITTNpyDYAFVSQGEITVPSIDDQEELMATDSAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 334 KIMGFNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASmPDNT-AAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQKAQ 412
Cdd:cd14910 241 EILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 413 TKEQADFAVEALAKALYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMF 492
Cdd:cd14910 320 TVQQVYNAVGALAKAVYDKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 493 VLEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLSLLDEECWFPKATDKSFVEKVI-QELGNHPKFQKPRQLRD 571
Cdd:cd14910 399 VLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYeQHLGKSNNFQKPKPAKG 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 572 K--ADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVdrivgldqVSGMGEMSFGSSYKTKKG- 648
Cdd:cd14910 476 KveAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGA--------AAAEAEEGGGKKGGKKKGs 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 649 MFRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 728
Cdd:cd14910 548 SFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRY 627
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 1785379719 729 EILTPNAIPKG-FMDGKQACAIMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14910 628 KVLNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
100-771 |
0e+00 |
|
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin heavy chain 13 (also called MyHC-eo) in mammals, chicken, and green anole. Myh13 is a myosin whose expression is restricted primarily to the extrinsic eye muscles which are specialized for function in eye movement. Class II myosins, also called conventional myosins, are the myosin type responsible for producing muscle contraction in muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276887 [Multi-domain] Cd Length: 671 Bit Score: 682.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTGE 179
Cdd:cd14923 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 180 SGAGKTENTKKVIQYLAHVASSHKGRKEHTA---PGELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYI 256
Cdd:cd14923 82 SGAGKTVNTKRVIQYFATIAVTGDKKKEQQPgkmQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 257 VGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMkTDLLLEGFNQYR--FLSNGNLPIPGQQDREIFQETMESMK 334
Cdd:cd14923 162 ASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPEL-IDLLLISTNPFDfpFVSQGEVTVASIDDSEELLATDNAID 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 335 IMGFNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASmPDNT-AAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQKAQT 413
Cdd:cd14923 241 ILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 414 KEQADFAVEALAKALYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFV 493
Cdd:cd14923 320 VQQVTNSVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 494 LEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLSLLDEECWFPKATDKSFVEKVI-QELGNHPKFQKPRQLRDK 572
Cdd:cd14923 399 LEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSNNFQKPKPAKGK 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 573 AD--LCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVdriVGLDQVSGMGEMSFGssyKTKKGMF 650
Cdd:cd14923 476 AEahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNY---AGAEAGDSGGSKKGG---KKKGSSF 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 651 RTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 730
Cdd:cd14923 550 QTVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRI 629
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1785379719 731 LTPNAIPKG-FMDGKQACAIMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14923 630 LNASAIPEGqFIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
100-771 |
0e+00 |
|
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin heavy chain 4 (also called MYH2B, MyHC-2B, MyHC-IIb). Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276879 [Multi-domain] Cd Length: 671 Bit Score: 674.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTGE 179
Cdd:cd14915 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 180 SGAGKTENTKKVIQYLAHVASSHKGRKEHTAPGE----LEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGY 255
Cdd:cd14915 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEAASGKmqgtLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 256 IVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMkTDLLLEGFNQYRF--LSNGNLPIPGQQDREIFQETMESM 333
Cdd:cd14915 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPEL-IEMLLITTNPYDFafVSQGEITVPSIDDQEELMATDSAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 334 KIMGFNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASmPDNT-AAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQKAQ 412
Cdd:cd14915 241 DILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 413 TKEQADFAVEALAKALYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMF 492
Cdd:cd14915 320 TVQQVYNSVGALAKAIYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 493 VLEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLSLLDEECWFPKATDKSFVEKVI-QELGNHPKFQKPRQLRD 571
Cdd:cd14915 399 VLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYeQHLGKSNNFQKPKPAKG 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 572 KAD--LCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVDRIvgldQVSGMGEMSFGssyKTKKGM 649
Cdd:cd14915 476 KAEahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFSGGQTA----EAEGGGGKKGG---KKKGSS 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 650 FRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 729
Cdd:cd14915 549 FQTVSALFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYK 628
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1785379719 730 ILTPNAIPKG-FMDGKQACAIMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14915 629 VLNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
100-771 |
0e+00 |
|
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ motifs such as found in class V, VIII, XI, and XIII myosins. These myosins are defined by two tandem MyTH4 and FERM domains. The apicomplexan, but not diatom myosins contain 4-6 WD40 repeats near the end of the C-terminal tail which suggests a possible function of these myosins in signal transduction and transcriptional regulation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276849 [Multi-domain] Cd Length: 661 Bit Score: 655.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTGE 179
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 180 SGAGKTENTKKVIQYLAHVASSHKgrkehtapgELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVGA 259
Cdd:cd14883 82 SGAGKTETTKLILQYLCAVTNNHS---------WVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGHIKGA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 260 NIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGE--HMKTDLLLEGFNQYRFLS-NGNLPIPGQQDREIFQETMESMKIM 336
Cdd:cd14883 153 IIQDYLLEQSRITFQAPGERNYHVFYQLLAGAKHskELKEKLKLGEPEDYHYLNqSGCIRIDNINDKKDFDHLRLAMNVL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 337 GFNHEEIMSMLKMVSAVLQFGNIVFRK-ERNTDQASMPDNTAAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQKAQTKE 415
Cdd:cd14883 233 GIPEEMQEGIFSVLSAILHLGNLTFEDiDGETGALTVEDKEILKIVAKLLGVDPDKLKKALTIRQINVRGNVTEIPLKVQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 416 QADFAVEALAKALYERLFRWLVHRINKALDRTKRQGaSFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFVLE 495
Cdd:cd14883 313 EARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNS-RFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHYVFKLE 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 496 QEEYQREGIEWNFIDFGlDLQPCIDLIERPanPPGVLSLLDEECWFPKATDKSFVEKVIQELGNHPKFQKPRQLRDKADL 575
Cdd:cd14883 392 QEEYEKEGINWSHIVFT-DNQECLDLIEKP--PLGILKLLDEECRFPKGTDLTYLEKLHAAHEKHPYYEKPDRRRWKTEF 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 576 CIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVDrIVGLDQVSGMGEMSfGSSYKTKKGMfRTVGQ 655
Cdd:cd14883 469 GVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFTYPD-LLALTGLSISLGGD-TTSRGTSKGK-PTVGD 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 656 LYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNA 735
Cdd:cd14883 546 TFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCLDPRA 625
|
650 660 670
....*....|....*....|....*....|....*.
gi 1785379719 736 IPKGFMDGKQACAIMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14883 626 RSADHKETCGAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
100-771 |
0e+00 |
|
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated with endocytosis, cytokinesis, cell-to-cell coupling and gating at plasmodesmata. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. It also contains IQ domains Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276834 Cd Length: 647 Bit Score: 648.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRgkKRHEIPPHIYAISETAYRSMLQDREDQSILCTGE 179
Cdd:cd01383 2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYR--QKLLDSPHVYAVADTAYREMMRDEINQSIIISGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 180 SGAGKTENTKKVIQYLAHVASSHKGrkehtapgeLEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVGA 259
Cdd:cd01383 80 SGAGKTETAKIAMQYLAALGGGSSG---------IENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKICGA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 260 NIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNGN-LPIPGQQDREIFQETMESMKIMGF 338
Cdd:cd01383 151 KIQTYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKSASEYKYLNQSNcLTIDGVDDAKKFHELKEALDTVGI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 339 NHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASMPDNTAAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQKAQTKEQAD 418
Cdd:cd01383 231 SKEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKLTLQQAI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 419 FAVEALAKALYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFVLEQEE 498
Cdd:cd01383 311 DARDALAKAIYASLFDWLVEQINKSLEVGKRRTGRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLFKLEQEE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 499 YQREGIEWNFIDFgLDLQPCIDLIERpaNPPGVLSLLDEECWFPKATDKSFVEKVIQELGNHPKFQKPrqlRDKAdLCII 578
Cdd:cd01383 391 YELDGIDWTKVDF-EDNQECLDLIEK--KPLGLISLLDEESNFPKATDLTFANKLKQHLKSNSCFKGE---RGGA-FTIR 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 579 HYAGKVDYKADEWLMKNMDPLNDNVATLLhQSTDKYTAELWKDVDRIVGLDQVSGMGEMSFGSsyktkkgMFRTVGQLYK 658
Cdd:cd01383 464 HYAGEVTYDTSGFLEKNRDLLHSDLIQLL-SSCSCQLPQLFASKMLDASRKALPLTKASGSDS-------QKQSVATKFK 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 659 ESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIpK 738
Cdd:cd01383 536 GQLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLPEDV-S 614
|
650 660 670
....*....|....*....|....*....|...
gi 1785379719 739 GFMDGKQACAIMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd01383 615 ASQDPLSTSVAILQQFNILPEMYQVGYTKLFFR 647
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
100-771 |
0e+00 |
|
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, and class I myosins have been implicated in phagocytosis and vesicle transport. Myosin I, an unconventional myosin, does not form dimers. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. There are 5 myosin subclasses with subclasses c/h, d/g, and a/b have an IQ domain and a TH1 domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276829 Cd Length: 652 Bit Score: 644.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTGE 179
Cdd:cd01378 2 AINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 180 SGAGKTENTKKVIQYLAHVASSHKGRKEHTapgelEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVGA 259
Cdd:cd01378 82 SGAGKTEASKRIMQYIAAVSGGSESEVERV-----KDMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEPVGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 260 NIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNGN-LPIPGQQDREIFQETMESMKIMGF 338
Cdd:cd01378 157 HITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGcFDVDGIDDAADFKEVLNAMKVIGF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 339 NHEEIMSMLKMVSAVLQFGNIVFrKERNTDQASMPDNTAAQKLCHLLGLNVTEFSRAILMPRIKVG---RDYVQKAQTKE 415
Cdd:cd01378 237 TEEEQDSIFRILAAILHLGNIQF-AEDEEGNAAISDTSVLDFVAYLLGVDPDQLEKALTHRTIETGgggRSVYEVPLNVE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 416 QADFAVEALAKALYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFnhTMFVL- 494
Cdd:cd01378 316 QAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKKKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIF--IELTLk 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 495 -EQEEYQREGIEWNFIDFgLDLQPCIDLIErpANPPGVLSLLDEECWFP-KATDKSFVEKVIQELGNHPKFQKPRQLRDK 572
Cdd:cd01378 394 aEQEEYVREGIEWTPIKY-FNNKIICDLIE--EKPPGIFAILDDACLTAgDATDQTFLQKLNQLFSNHPHFECPSGHFEL 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 573 ADLC--IIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVDRivgldqvsgmgemsfgssyKTKKGMF 650
Cdd:cd01378 471 RRGEfrIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEGVD-------------------LDSKKRP 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 651 RTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 730
Cdd:cd01378 532 PTAGTKFKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYKL 611
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 1785379719 731 LTPNAIPKGFMDGKQACAIMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd01378 612 LSPKTWPAWDGTWQGGVESILKDLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
99-771 |
0e+00 |
|
class VII myosin, motor domain; These monomeric myosins have been associated with functions in sensory systems such as vision and hearing. Mammalian myosin VII has a tail with 2 MyTH4 domains, 2 FERM domains, and a SH3 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276832 Cd Length: 648 Bit Score: 614.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTG 178
Cdd:cd01381 1 AGILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 179 ESGAGKTENTKKVIQYLAHVASSHKgrkehtapgELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 258
Cdd:cd01381 81 ESGAGKTESTKLILQYLAAISGQHS---------WIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIEG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 259 ANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNGN-LPIPGQQDREIFQETMESMKIMG 337
Cdd:cd01381 152 AKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDASDYYYLTQGNcLTCEGRDDAAEFADIRSAMKVLM 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 338 FNHEEIMSMLKMVSAVLQFGNIVFRK--ERNTDQASMPDNTAAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQKAQTKE 415
Cdd:cd01381 232 FTDEEIWDIFKLLAAILHLGNIKFEAtvVDNLDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSPLSAE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 416 QADFAVEALAKALYERLFRWLVHRINKALDRTKRQGAS--FIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFV 493
Cdd:cd01381 312 QALDVRDAFVKGIYGRLFIWIVNKINSAIYKPRGTDSSrtSIGVLDIFGFENFEVNSFEQLCINFANENLQQFFVRHIFK 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 494 LEQEEYQREGIEWNFIDFgLDLQPCIDLI-ERPANppgVLSLLDEECWFPKATDKSFVEKVIQELGNHPKFQKPRQLRDK 572
Cdd:cd01381 392 LEQEEYDKEGINWQHIEF-VDNQDVLDLIaLKPMN---IMSLIDEESKFPKGTDQTMLEKLHSTHGNNKNYLKPKSDLNT 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 573 AdLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDvdrivgldqvsgmgEMSFGSSYKTKKgmfRT 652
Cdd:cd01381 468 S-FGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNE--------------DISMGSETRKKS---PT 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 653 VGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILT 732
Cdd:cd01381 530 LSSQFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVLV 609
|
650 660 670
....*....|....*....|....*....|....*....
gi 1785379719 733 PNAIPKGFMDGKQACAIMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd01381 610 PGIPPAHKTDCRAATRKICCAVLGGDADYQLGKTKIFLK 648
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
99-771 |
0e+00 |
|
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle transport. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle.
Pssm-ID: 276835 Cd Length: 647 Bit Score: 613.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCT 177
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 178 GESGAGKTENTKKVIQYLAHVAsshkGRKE-HTAPgeLEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYI 256
Cdd:cd01384 81 GESGAGKTETTKMLMQYLAYMG----GRAVtEGRS--VEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAGRI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 257 VGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNGN-LPIPGQQDREIFQETMESMKI 335
Cdd:cd01384 155 SGAAIRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKDPKQFHYLNQSKcFELDGVDDAEEYRATRRAMDV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 336 MGFNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASMPDNTAAQKL---CHLLGLNVTEFSRAiLMPRIKVGRD-YVQKA 411
Cdd:cd01384 235 VGISEEEQDAIFRVVAAILHLGNIEFSKGEEDDSSVPKDEKSEFHLkaaAELLMCDEKALEDA-LCKRVIVTPDgIITKP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 412 QTKEQADFAVEALAKALYERLFRWLVHRINKALDRTKRQgASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTM 491
Cdd:cd01384 314 LDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNS-KRLIGVLDIYGFESFKTNSFEQFCINLANEKLQQHFNQHV 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 492 FVLEQEEYQREGIEWNFIDFgLDLQPCIDLIERpaNPPGVLSLLDEECWFPKATDKSFVEKVIQELGNHPKFQKPRqlRD 571
Cdd:cd01384 393 FKMEQEEYTKEEIDWSYIEF-VDNQDVLDLIEK--KPGGIIALLDEACMFPRSTHETFAQKLYQTLKDHKRFSKPK--LS 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 572 KADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVDRivgldqvsgmGEMSfgSSYKtkkgmFR 651
Cdd:cd01384 468 RTDFTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLFPPLPR----------EGTS--SSSK-----FS 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 652 TVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 731
Cdd:cd01384 531 SIGSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGLL 610
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 1785379719 732 TPNAiPKGFMDGKQACAIMIRALELDPnlYRIGQSKIFFR 771
Cdd:cd01384 611 APEV-LKGSDDEKAACKKILEKAGLKG--YQIGKTKVFLR 647
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
99-771 |
0e+00 |
|
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the minus-end of actin filaments, in contrast to most other myosins which moves towards the plus-end of actin filaments. It is thought that myosin VI, unlike plus-end directed myosins, does not use a pure lever arm mechanism, but instead steps with a mechanism analogous to the kinesin neck-linker uncoupling model. It has been implicated in a myriad of functions including: the transport of cytoplasmic organelles, maintenance of normal Golgi morphology, endocytosis, secretion, cell migration, border cell migration during development, and in cancer metastasis playing roles in deafness and retinal development among others. While how this is accomplished is largely unknown there are several interacting proteins that have been identified such as disabled homolog 2 (DAB2), GIPC1, synapse-associated protein 97 (SAP97; also known as DLG1) and optineurin, which have been found to target myosin VI to different cellular compartments. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the minus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276833 Cd Length: 649 Bit Score: 575.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCT 177
Cdd:cd01382 1 ATLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 178 GESGAGKTENTKKVIQYLAHVASSHKGrkehtapgELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIV 257
Cdd:cd01382 81 GESGAGKTESTKYILRYLTESWGSGAG--------PIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 258 GANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLegfnqyrflsngnlpIPGQQDREIFQETMESMKIMG 337
Cdd:cd01382 153 GGFVSHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLLK---------------DPLLDDVGDFIRMDKAMKKIG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 338 FNHEEIMSMLKMVSAVLQFGNIVFRKERNT-------DQASMPDNTAAQKlchLLGLNVTEF-----SRAILMPRIKVGR 405
Cdd:cd01382 218 LSDEEKLDIFRVVAAVLHLGNIEFEENGSDsgggcnvKPKSEQSLEYAAE---LLGLDQDELrvsltTRVMQTTRGGAKG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 406 DYVQKAQTKEQADFAVEALAKALYERLFRWLVHRINKALDRTKrqGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQ 485
Cdd:cd01382 295 TVIKVPLKVEEANNARDALAKAIYSKLFDHIVNRINQCIPFET--SSYFIGVLDIAGFEYFEVNSFEQFCINYCNEKLQQ 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 486 LFNHTMFVLEQEEYQREGIEWNFIDFgLDLQPCIDLIERPANppGVLSLLDEECWFPKATDKSFVEKVIQELGNHPKFQK 565
Cdd:cd01382 373 FFNERILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEAKLV--GILDLLDEESKLPKPSDQHFTSAVHQKHKNHFRLSI 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 566 PRQ--------LRDKADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVDRIVGldqvsgmgem 637
Cdd:cd01382 450 PRKsklkihrnLRDDEGFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFESSTNNNK---------- 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 638 sfGSSYKTKKGMFRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPN 717
Cdd:cd01382 520 --DSKQKAGKLSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPS 597
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 1785379719 718 RIVFQEFRQRYEILTPNAIPKgfMDGKQACAIMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd01382 598 RTSFHDLYNMYKKYLPPKLAR--LDPRLFCKALFKALGLNENDFKFGLTKVFFR 649
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
99-771 |
7.72e-180 |
|
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: 560.16 E-value: 7.72e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTG 178
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 179 ESGAGKTENTKKVIQYLAHVASSHKGrkehtapgeLEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 258
Cdd:cd14872 81 ESGAGKTEATKQCLSFFAEVAGSTNG---------VEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRICG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 259 ANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGfnQYRFLSNGN-LPIPGQQDREIFQETMESMKIMG 337
Cdd:cd14872 152 ASTENYLLEKSRVVYQIKGERNFHIFYQLLASPDPASRGGWGSSA--AYGYLSLSGcIEVEGVDDVADFEEVVLAMEQLG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 338 FNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASMPDNTAAQKLCH---LLGLNVTEFSRAILMPRIKV-GRDYVQKAQT 413
Cdd:cd14872 230 FDDADINNVMSLIAAILKLGNIEFASGGGKSLVSGSTVANRDVLKEvatLLGVDAATLEEALTSRLMEIkGCDPTRIPLT 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 414 KEQADFAVEALAKALYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFV 493
Cdd:cd14872 310 PAQATDACDALAKAAYSRLFDWLVKKINESMRPQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEKLQQHFNQYTFK 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 494 LEQEEYQREGIEWNFIDFgLDLQPCIDLIERpaNPPGVLSLLDEECWFPKATDKSFVEKVIQELGNHPKFQKPRQLRDKA 573
Cdd:cd14872 390 LEEALYQSEGVKFEHIDF-IDNQPVLDLIEK--KQPGLMLALDDQVKIPKGSDATFMIAANQTHAAKSTFVYAEVRTSRT 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 574 DLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWkdvdrivgldqvsgmgEMSFGSSyKTKKGmfrTV 653
Cdd:cd14872 467 EFIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLF----------------PPSEGDQ-KTSKV---TL 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 654 GQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILtP 733
Cdd:cd14872 527 GGQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKRYRFL-V 605
|
650 660 670
....*....|....*....|....*....|....*....
gi 1785379719 734 NAIPKGFM-DGKQACAIMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14872 606 KTIAKRVGpDDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
99-771 |
9.77e-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: 552.46 E-value: 9.77e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQ----DREDQS 173
Cdd:cd14890 1 ASLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQsgvlDPSNQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 174 ILCTGESGAGKTENTKKVIQYLAHVASSHKGRKEH----------TAPGELEHQLLQANPILEAFGNAKTVKNDNSSRFG 243
Cdd:cd14890 81 IIISGESGAGKTEATKIIMQYLARITSGFAQGASGegeaaseaieQTLGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 244 KFIRINFDVAGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNGNLPIPGQQDR 323
Cdd:cd14890 161 KFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPVEYFYLRGECSSIPSCDDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 324 EIFQETMESMKIMGFNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASmpDNTAAQKLCH---LLGLNVTEFSRAILMPR 400
Cdd:cd14890 241 KAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTVLE--DATTLQSLKLaaeLLGVNEDALEKALLTRQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 401 IKVGRDYVQKAQTKEQADFAVEALAKALYERLFRWLVHRINKALDRTKRQgASFIGILDIAGFEIFELNSFEQLCINYTN 480
Cdd:cd14890 319 LFVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDK-WGFIGVLDIYGFEKFEWNTFEQLCINYAN 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 481 EKLQQLFNHTMFVLEQEEYQREGIEWNFIDFGlDLQPCIDLIE-RPANPPGVLSLLDeECWFPKAT--DKSFVEKVIQEL 557
Cdd:cd14890 398 EKLQRHFNQHMFEVEQVEYSNEGIDWQYITFN-DNQACLELIEgKVNGKPGIFITLD-DCWRFKGEeaNKKFVSQLHASF 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 558 G-------------NHPKFQKPRQLRDKAdLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTdkytaelwkdvdr 624
Cdd:cd14890 476 GrksgsggtrrgssQHPHFVHPKFDADKQ-FGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSR------------- 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 625 ivgldqvSGMGEMSFGSSYKTkkgmfrtvgqlykeSLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGV 704
Cdd:cd14890 542 -------RSIREVSVGAQFRT--------------QLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGM 600
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1785379719 705 LEGIRICRQGFPNRIVFQEFRQRYEILTPNAipkgfMDGKQACAIMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14890 601 MEAIQIRQQGFALREEHDSFFYDFQVLLPTA-----ENIEQLVAVLSKMLGLGKADWQIGSSKIFLK 662
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
99-771 |
6.32e-174 |
|
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: 544.73 E-value: 6.32e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTG 178
Cdd:cd01387 1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 179 ESGAGKTENTKKVIQYLAHVASShkgrkehtAPGELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDvAGYIVG 258
Cdd:cd01387 81 ESGSGKTEATKLIMQYLAAVNQR--------RNNLVTEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFFE-GGVIVG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 259 ANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNG-NLPIPGQQDREIFQETMESMKIMG 337
Cdd:cd01387 152 AITSQYLLEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQEAEKYFYLNQGgNCEIAGKSDADDFRRLLAAMQVLG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 338 FNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQ---ASMPDNTAAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQKAQTK 414
Cdd:cd01387 232 FSSEEQDSIFRILASVLHLGNVYFHKRQLRHGqegVSVGSDAEIQWVAHLLQISPEGLQKALTFKVTETRRERIFTPLTI 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 415 EQADFAVEALAKALYERLFRWLVHRINkALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFVL 494
Cdd:cd01387 312 DQALDARDAIAKALYALLFSWLVTRVN-AIVYSGTQDTLSIAILDIFGFEDLSENSFEQLCINYANENLQYYFNKHVFKL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 495 EQEEYQREGIEWNFIDFgLDLQPCIDLIERpaNPPGVLSLLDEECWFPKATDKSFVEKVIQELGNHPKFQKPRQlrDKAD 574
Cdd:cd01387 391 EQEEYIREQIDWTEIAF-ADNQPVINLISK--KPVGILHILDDECNFPQATDHSFLEKCHYHHALNELYSKPRM--PLPE 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 575 LCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVdrivgLDQVSGMGEMSFGSSYKTKKGMFRTVG 654
Cdd:cd01387 466 FTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSSH-----RAQTDKAPPRLGKGRFVTMKPRTPTVA 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 655 QLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 734
Cdd:cd01387 541 ARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYRCLVAL 620
|
650 660 670
....*....|....*....|....*....|....*...
gi 1785379719 735 AIPKGfMDGKQACAIMIRALELDP-NLYRIGQSKIFFR 771
Cdd:cd01387 621 KLPRP-APGDMCVSLLSRLCTVTPkDMYRLGATKVFLR 657
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
99-771 |
2.33e-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: 529.73 E-value: 2.33e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCT 177
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 178 GESGAGKTENTKKVIQYLAHVAsshkgrkehtapGELEH----QLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVA 253
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIA------------GGLNDstikKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKN 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 254 GYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAgeHMKTDLLLEGFNQYRFL-SNGNLPIPGQQDREIFQETMES 332
Cdd:cd14903 149 GTLVGAKCRTYLLEKTRVISHERPERNYHIFYQLLASP--DVEERLFLDSANECAYTgANKTIKIEGMSDRKHFARTKEA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 333 MKIMGFNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASM--PDNTAAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQK 410
Cdd:cd14903 227 LSLIGVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSAiaPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDVYTV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 411 AQTKEQADFAVEALAKALYERLFRWLVHRINKALDRTKRQgASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHT 490
Cdd:cd14903 307 PLKKDQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKM-ANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFTQD 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 491 MFVLEQEEYQREGIEWNFIDFgLDLQPCIDLIErpaNPPGVLSLLDEECWFPKATDKSFVEKVIqelGNHPKFQK----P 566
Cdd:cd14903 386 VFKTVQIEYEEEGIRWAHIDF-ADNQDVLAVIE---DRLGIISLLNDEVMRPKGNEESFVSKLS---SIHKDEQDviefP 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 567 RQlrDKADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDvdrIVGLDQVSGMGEMSFGSSYKTK 646
Cdd:cd14903 459 RT--SRTQFTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKE---KVESPAAASTSLARGARRRRGG 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 647 KGMFRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQ 726
Cdd:cd14903 534 ALTTTTVGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLD 613
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 1785379719 727 RYEILTPNAiPKGFMDGKQACAIMIRALELD-PNLYRIGQSKIFFR 771
Cdd:cd14903 614 KFWLFLPEG-RNTDVPVAERCEALMKKLKLEsPEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
99-771 |
1.10e-167 |
|
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: 528.87 E-value: 1.10e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTG 178
Cdd:cd01385 1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 179 ESGAGKTENTKKVIQYLahVASSHKGrkehTAPGeLEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 258
Cdd:cd01385 81 ESGSGKTESTNFLLHHL--TALSQKG----YGSG-VEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 259 ANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLS-NGNLPIPGQQDREIFQETMESMKIMG 337
Cdd:cd01385 154 AVVEKYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHYLNqSDCYTLEGEDEKYEFERLKQAMEMVG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 338 FNHEEIMSMLKMVSAVLQFGNIVFRKER-NTDQASMPDNTAAQKL-CHLLGLNVTEFSRAILMPRIKVGRDYVQKAQTKE 415
Cdd:cd01385 234 FLPETQRQIFSVLSAVLHLGNIEYKKKAyHRDESVTVGNPEVLDIiSELLRVKEETLLEALTTKKTVTVGETLILPYKLP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 416 QADFAVEALAKALYERLFRWLVHRINKAL----DRTKRQGASfIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTM 491
Cdd:cd01385 314 EAIATRDAMAKCLYSALFDWIVLRINHALlnkkDLEEAKGLS-IGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQHI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 492 FVLEQEEYQREGIEWNFIDFgLDLQPCIDLIERpaNPPGVLSLLDEECWFPKATDKSFVEKVIQELGNHPKFQKPrQLRD 571
Cdd:cd01385 393 FKLEQEEYKKEGISWHNIEY-TDNTGCLQLISK--KPTGLLCLLDEESNFPGATNQTLLAKFKQQHKDNKYYEKP-QVME 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 572 KAdLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELwkdvdriVGLDQV-------------------- 631
Cdd:cd01385 469 PA-FIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVREL-------IGIDPVavfrwavlrafframaafre 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 632 SGM----------------GEMSFGSSYKTKKGMfrTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLV 695
Cdd:cd01385 541 AGRrraqrtaghsltlhdrTTKSLLHLHKKKKPP--SVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELV 618
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1785379719 696 LDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILtpnaIPKGFMDGKQACAIMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd01385 619 LRQLRYTGMLETVRIRRSGYSVRYTFQEFITQFQVL----LPKGLISSKEDIKDFLEKLNLDRDNYQIGKTKVFLK 690
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
99-769 |
1.34e-165 |
|
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: 522.04 E-value: 1.34e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMY------RGKKRHEIPPHIYAISETAYRSMLQDRE-- 170
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 171 --DQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKEHTAPGELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 248
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLASVSSATTHGQNATERENVRDRVLESNPILEAFGNARTNRNNNSSRFGKFIRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 249 NFDVAGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNGNLPI--PGQQDREIF 326
Cdd:cd14901 161 GFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYLNSSQCYDrrDGVDDSVQY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 327 QETMESMKIMGFNHEEIMSMLKMVSAVLQFGNIVF-RKERNTDQASMPDNTAAQKLCHLLGLNVTEFSRAILMPRIKVGR 405
Cdd:cd14901 241 AKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFvKKDGEGGTFSMSSLANVRAACDLLGLDMDVLEKTLCTREIRAGG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 406 DYVQKAQTKEQADFAVEALAKALYERLFRWLVHRINKALDRTKRQGAS-FIGILDIAGFEIFELNSFEQLCINYTNEKLQ 484
Cdd:cd14901 321 EYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSESTGASrFIGIVDIFGFEIFATNSLEQLCINFANEKLQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 485 QLFNHTMFVLEQEEYQREGIEWNFIDFgldlqP----CIDLIErpANPPGVLSLLDEECWFPKATDKSFVEKVIQELGNH 560
Cdd:cd14901 401 QLFGKFVFEMEQDEYVAEAIPWTFVEY-----PnndaCVAMFE--ARPTGLFSLLDEQCLLPRGNDEKLANKYYDLLAKH 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 561 PKFQKPRQLRDKADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAElwkdvdrivgldqvsgmgemsfg 640
Cdd:cd14901 474 ASFSVSKLQQGKRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLSS----------------------- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 641 ssyktkkgmfrTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIV 720
Cdd:cd14901 531 -----------TVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFP 599
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 1785379719 721 FQEFRQRYEILTPNAIPKGFMDGKQACAIMIRA------LELDPNLYrIGQSKIF 769
Cdd:cd14901 600 HDAFVHTYSCLAPDGASDTWKVNELAERLMSQLqhselnIEHLPPFQ-VGKTKVF 653
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
99-771 |
1.04e-163 |
|
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: 516.17 E-value: 1.04e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKK-RHEIPPHIYAISETAYRSMLQDREDQSILCT 177
Cdd:cd14897 1 NTIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 178 GESGAGKTENTKKVIQYLAHVASShkgrkehtAPGELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIV 257
Cdd:cd14897 81 GESGAGKTESTKYMIKHLMKLSPS--------DDSDLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQLL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 258 GANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNGNLPIPGQQD-------REIFQETM 330
Cdd:cd14897 153 GAKIDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDPDCHRILRDDNRNRPVFNDseeleyyRQMFHDLT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 331 ESMKIMGFNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASMPDNTAAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQK 410
Cdd:cd14897 233 NIMKLIGFSEEDISVIFTILAAILHLTNIVFIPDEDTDGVTVADEYPLHAVAKLLGIDEVELTEALISNVNTIRGERIQS 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 411 AQTKEQADFAVEALAKALYERLFRWLVHRINKAL----DRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQL 486
Cdd:cd14897 313 WKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLwpdkDFQIMTRGPSIGILDMSGFENFKINSFDQLCINLSNERLQQY 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 487 FNHTMFVLEQEEYQREGIEWNFIDFGlDLQPCIDLIERpaNPPGVLSLLDEECWFPKATDKSFVEKVIQELGNHPKFQKP 566
Cdd:cd14897 393 FNDYVFPRERSEYEIEGIEWRDIEYH-DNDDVLELFFK--KPLGILPLLDEESTFPQSTDSSLVQKLNKYCGESPRYVAS 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 567 rqLRDKADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWkdvdrivgldqvsgmgemsfgSSYktk 646
Cdd:cd14897 470 --PGNRVAFGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLF---------------------TSY--- 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 647 kgmfrtvgqlYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQ 726
Cdd:cd14897 524 ----------FKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYEDFVK 593
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 1785379719 727 RYEILTPNAiPKGFMDGKQACAIMIRALELDPnlYRIGQSKIFFR 771
Cdd:cd14897 594 RYKEICDFS-NKVRSDDLGKCQKILKTAGIKG--YQFGKTKVFLK 635
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
99-733 |
3.25e-163 |
|
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: 516.17 E-value: 3.25e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYTEQIVEMYRgKKRHEIPPHIYAISETAYRSMLQDREDQSILCT 177
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 178 GESGAGKTENTKKVIQYLAHVASSHKGRKEhtapgELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD------ 251
Cdd:cd14888 80 GESGAGKTESTKYVMKFLACAGSEDIKKRS-----LVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFSklkskr 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 252 ---VAGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNGNLP------------ 316
Cdd:cd14888 155 msgDRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAREAKNTGLSYEENDEKLAKGADAKPisidmssfephl 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 317 ------------IPGQQDREIFQETMESMKIMGFNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASMPDNTAAQKL--- 381
Cdd:cd14888 235 kfryltksscheLPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFENNEACSEGAVVSASCTDDLekv 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 382 CHLLGLNVTEFSRAILMPRIKVGRDYVQKAQTKEQADFAVEALAKALYERLFRWLVHRINKALDRTKRQGASFIGILDIA 461
Cdd:cd14888 315 ASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGYSKDNSLLFCGVLDIF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 462 GFEIFELNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLSLLDEECWF 541
Cdd:cd14888 395 GFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVDLLQ--EKPLGIFCMLDEECFV 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 542 PKATDKSFVEKVIQELGNHPKFQKPRQlrDKADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKD 621
Cdd:cd14888 472 PGGKDQGLCNKLCQKHKGHKRFDVVKT--DPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKNPFISNLFSA 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 622 -VDRIVGLdqvsgmgemsfgssyKTKKGMFRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLR 700
Cdd:cd14888 550 yLRRGTDG---------------NTKKKKFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQLK 614
|
650 660 670
....*....|....*....|....*....|...
gi 1785379719 701 CNGVLEGIRICRQGFPNRIVFQEFRQRYEILTP 733
Cdd:cd14888 615 YGGVLQAVQVSRAGYPVRLSHAEFYNDYRILLN 647
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
100-771 |
3.86e-163 |
|
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: 514.52 E-value: 3.86e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTGE 179
Cdd:cd01379 2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 180 SGAGKTENTKKVIQYLAHVASShkgrkehtAPGELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVGA 259
Cdd:cd01379 82 SGAGKTESANLLVQQLTVLGKA--------NNRTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAVTGA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 260 NIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTD---LLLEGFNQYRFLSNGNLPIPGQQD--REIFQETMESMK 334
Cdd:cd01379 154 RISEYLLEKSRVVHQAIGERNFHIFYYIYAGLAEDKKLAkykLPENKPPRYLQNDGLTVQDIVNNSgnREKFEEIEQCFK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 335 IMGFNHEEIMSMLKMVSAVLQFGNIVFR---KERNTDQASM-PDNTAAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQK 410
Cdd:cd01379 234 VIGFTKEEVDSVYSILAAILHIGDIEFTeveSNHQTDKSSRiSNPEALNNVAKLLGIEADELQEALTSHSVVTRGETIIR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 411 AQTKEQADFAVEALAKALYERLFRWLVHRINKAL--DRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFN 488
Cdd:cd01379 314 NNTVEEATDARDAMAKALYGRLFSWIVNRINSLLkpDRSASDEPLSIGILDIFGFENFQKNSFEQLCINIANEQIQYYFN 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 489 HTMFVLEQEEYQREGIEWNFIDFGlDLQPCID-LIERPAnppGVLSLLDEECWFPKATDKSFVEKVIQELGNHPkFQKPR 567
Cdd:cd01379 394 QHIFAWEQQEYLNEGIDVDLIEYE-DNRPLLDmFLQKPM---GLLALLDEESRFPKATDQTLVEKFHNNIKSKY-YWRPK 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 568 qlRDKADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAElwkdvdrivgldqvsgmgemsfgssyktkk 647
Cdd:cd01379 469 --SNALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVRQ------------------------------ 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 648 gmfrTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQR 727
Cdd:cd01379 517 ----TVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRILFADFLKR 592
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 1785379719 728 YEILTPNAIPKGFMDgKQACAIMIRALELDPnlYRIGQSKIFFR 771
Cdd:cd01379 593 YYFLAFKWNEEVVAN-RENCRLILERLKLDN--WALGKTKVFLK 633
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
99-771 |
8.51e-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: 511.65 E-value: 8.51e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCT 177
Cdd:cd14873 1 GSIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 178 GESGAGKTENTKKVIQYLAHVASSHKGRKEHTAPGELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIV 257
Cdd:cd14873 81 GESGAGKTESTKLILKFLSVISQQSLELSLKEKTSCVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 258 GANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLS-NGNLPIPGQQDREIFQETMESMKIM 336
Cdd:cd14873 161 GGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTPENYHYLNqSGCVEDKTISDQESFREVITAMEVM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 337 GFNHEEIMSMLKMVSAVLQFGNIVFrkeRNTDQASMPDNTAAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQKAQTKEQ 416
Cdd:cd14873 241 QFSKEEVREVSRLLAGILHLGNIEF---ITAGGAQVSFKTALGRSAELLGLDPTQLTDALTQRSMFLRGEEILTPLNVQQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 417 ADFAVEALAKALYERLFRWLVHRINKaldRTKRQGA-SFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFVLE 495
Cdd:cd14873 318 AVDSRDSLAMALYARCFEWVIKKINS---RIKGKEDfKSIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKHIFSLE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 496 QEEYQREGIEWNFIDFgLDLQPCIDLIERPAnppGVLSLLDEECWFPKATDKSFVEKVIQELGNHPKFQKPRQLRDkaDL 575
Cdd:cd14873 395 QLEYSREGLVWEDIDW-IDNGECLDLIEKKL---GLLALINEESHFPQATDSTLLEKLHSQHANNHFYVKPRVAVN--NF 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 576 CIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVDrivgldqvSGMGEMSFGSSYKTKKgmfRTVGQ 655
Cdd:cd14873 469 GVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEHVS--------SRNNQDTLKCGSKHRR---PTVSS 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 656 LYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNA 735
Cdd:cd14873 538 QFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMRNL 617
|
650 660 670
....*....|....*....|....*....|....*.
gi 1785379719 736 IPKGFMDGKqaCAIMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14873 618 ALPEDVRGK--CTSLLQLYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
99-771 |
2.68e-160 |
|
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: 507.76 E-value: 2.68e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEI---PPHIYAISETAYRSMLQDR----ED 171
Cdd:cd14892 1 APLLDVLRRRYERDAIYTFTADILISINPYKSIPLLYDVPGFDSQRKEEATAsspPPHVFSIAERAYRAMKGVGkgqgTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 172 QSILCTGESGAGKTENTKKVIQYLA----HVASSHKGRKEHTAPGELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIR 247
Cdd:cd14892 81 QSIVVSGESGAGKTEASKYIMKYLAtaskLAKGASTSKGAANAHESIEECVLLSNLILEAFGNAKTIRNDNSSRFGKYIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 248 INFDVAGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNGN-LPIPGQQDREIF 326
Cdd:cd14892 161 IHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAESFLFLNQGNcVEVDGVDDATEF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 327 QETMESMKIMGFNHEEIMSMLKMVSAVLQFGNIVFrkERNTDQ----ASMPDNTAAQKLCHLLGLNVTEFSRAILMPRIK 402
Cdd:cd14892 241 KQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRF--EENADDedvfAQSADGVNVAKAAGLLGVDAAELMFKLVTQTTS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 403 VGRDYV-QKAQTKEQADFAVEALAKALYERLFRWLVHRINKALDRTKRQ---------GASFIGILDIAGFEIFELNSFE 472
Cdd:cd14892 319 TARGSVlEIKLTAREAKNALDALCKYLYGELFDWLISRINACHKQQTSGvtggaasptFSPFIGILDIFGFEIMPTNSFE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 473 QLCINYTNEKLQQLFNHTMFVLEQEEYQREGIEWNFIDFGlDLQPCIDLIERPanPPGVLSLLDEECWFP-KATDKSFVE 551
Cdd:cd14892 399 QLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQ-DNQDCLDLIQKK--PLGLLPLLEEQMLLKrKTTDKQLLT 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 552 KVIQE-LGNHPKFQKPrqlRDKADLCII-HYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDkytaelwkdvdrivgld 629
Cdd:cd14892 476 IYHQThLDKHPHYAKP---RFECDEFVLrHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSSSK----------------- 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 630 qvsgmgemsfgssyktkkgmFRTvgqlykeSLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIR 709
Cdd:cd14892 536 --------------------FRT-------QLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVR 588
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1785379719 710 ICRQGFPNRIVFQEFRQRYEIL---------TPNAIPkGFMDGKQACAIMIRALEldPNLYRIGQSKIFFR 771
Cdd:cd14892 589 IRREGFPIRRQFEEFYEKFWPLarnkagvaaSPDACD-ATTARKKCEEIVARALE--RENFQLGRTKVFLR 656
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
100-731 |
9.41e-148 |
|
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: 472.10 E-value: 9.41e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYTEQIVEMY-----------RGKKRHEIPPHIYAISETAYRSM-- 165
Cdd:cd14900 2 TILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssstRNKGSDPMPPHIYQVAGEAYKAMml 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 166 --LQDREDQSILCTGESGAGKTENTKKVIQYLAHvASSHKGRKEHTAPGELE---HQLLQANPILEAFGNAKTVKNDNSS 240
Cdd:cd14900 82 glNGVMSDQSILVSGESGSGKTESTKFLMEYLAQ-AGDNNLAASVSMGKSTSgiaAKVLQTNILLESFGNARTLRNDNSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 241 RFGKFIRINFDVAGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEhmktdlllegfnqyrflsngnlpipGQ 320
Cdd:cd14900 161 RFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASE-------------------------AA 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 321 QDREIFQETMESMKIMGFNHEEIMSMLKMVSAVLQFGNIVFRKERNTD-QASMPDNTAAQKL------CHLLGLNVTEFS 393
Cdd:cd14900 216 RKRDMYRRVMDAMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDrLGQLKSDLAPSSIwsrdaaATLLSVDATKLE 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 394 RAILMPRIKVGRDYVQKAQTKEQADFAVEALAKALYERLFRWLVHRINKAL---DRTKRQGAS-FIGILDIAGFEIFELN 469
Cdd:cd14900 296 KALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLkmdDSSKSHGGLhFIGILDIFGFEVFPKN 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 470 SFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLSLLDEECWFPKATDKSF 549
Cdd:cd14900 376 SFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFC-DNQDCVNLIS--QRPTGILSLIDEECVMPKGSDTTL 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 550 VEKVIQELGNHPKFQKPRQLRDKADLCIIHYAGKVDYKADEWLMKNMDplndnvatLLHQSTdkytaelwkdVDrivgld 629
Cdd:cd14900 453 ASKLYRACGSHPRFSASRIQRARGLFTIVHYAGHVEYSTDGFLEKNKD--------VLHQEA----------VD------ 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 630 qvsgmgemsfgssyktkkgMFRTVGQlYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIR 709
Cdd:cd14900 509 -------------------LFVYGLQ-FKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVMEAVR 568
|
650 660
....*....|....*....|..
gi 1785379719 710 ICRQGFPNRIVFQEFRQRYEIL 731
Cdd:cd14900 569 VARAGFPIRLLHDEFVARYFSL 590
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
101-771 |
1.37e-142 |
|
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: 458.99 E-value: 1.37e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 101 VLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSML----QDREDQSILC 176
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 177 TGESGAGKTENTKKVIQYLAHVASSHKgrkehtapgELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDvAGYI 256
Cdd:cd14889 83 SGESGAGKTESTKLLLRQIMELCRGNS---------QLEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRFR-NGHV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 257 VGANIETYLLEKSRAIRQAKDERTFHVFYQLLAG--AGEHMKTDLLLEGFnqYRFLSN--GNLPIPgQQDREIFQETMES 332
Cdd:cd14889 153 KGAKINEYLLEKSRVVHQDGGEENFHIFYYMFAGisAEDRENYGLLDPGK--YRYLNNgaGCKREV-QYWKKKYDEVCNA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 333 MKIMGFNHEEIMSMLKMVSAVLQFGNIVFrkERNTDQASMPDNTAAQKL---CHLLGLNVTEFSRAILMPRIKVGRDYVQ 409
Cdd:cd14889 230 MDMVGFTEQEEVDMFTILAGILSLGNITF--EMDDDEALKVENDSNGWLkaaAGQFGVSEEDLLKTLTCTVTFTRGEQIQ 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 410 KAQTKEQADFAVEALAKALYERLFRWLVHRINKALDRTKRQG--ASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLF 487
Cdd:cd14889 308 RHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLLAPKDDSSveLREIGILDIFGFENFAVNRFEQACINLANEQLQYFF 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 488 NHTMFVLEQEEYQREGIEWNFIDFgLDLQPCIDLIErpANPPGVLSLLDEECWFPKATDKSFVEKVIQELGNHPKFQKPR 567
Cdd:cd14889 388 NHHIFLMEQKEYKKEGIDWKEITY-KDNKPILDLFL--NKPIGILSLLDEQSHFPQATDESFVDKLNIHFKGNSYYGKSR 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 568 qlRDKADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWK-DVDRIVGLDQVSGM---GEMSFGSSY 643
Cdd:cd14889 465 --SKSPKFTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFTaTRSRTGTLMPRAKLpqaGSDNFNSTR 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 644 KtkkgmfRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQE 723
Cdd:cd14889 543 K------QSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFSWRPSFAE 616
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 1785379719 724 FRQRYEIL--TPNaIPKgfmdGKQACAIMIRALELDPnlYRIGQSKIFFR 771
Cdd:cd14889 617 FAERYKILlcEPA-LPG----TKQSCLRILKATKLVG--WKCGKTRLFFK 659
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
99-734 |
3.08e-141 |
|
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: 455.64 E-value: 3.08e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYTEQIVEMYRGKKRH--------EIPPHIYAISETAYRSMLQDR 169
Cdd:cd14907 1 AELLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEQIIQngeyfdikKEPPHIYAIAALAFKQLFENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 170 EDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKEHTAPGE-----------LEHQLLQANPILEAFGNAKTVKNDN 238
Cdd:cd14907 81 KKQAIVISGESGAGKTENAKYAMKFLTQLSQQEQNSEEVLTLTSsiratskstksIEQKILSCNPILEAFGNAKTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 239 SSRFGKFIRINFD-VAGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEG---FNQYRFLS-NG 313
Cdd:cd14907 161 SSRFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLKNqlsGDRYDYLKkSN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 314 NLPIPGQQDREIFQETMESMKIMGFNHEEIMSMLKMVSAVLQFGNIVF--RKERNTDQASMPDNTAAQKLCHLLGLNVTE 391
Cdd:cd14907 241 CYEVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFddSTLDDNSPCCVKNKETLQIIAKLLGIDEEE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 392 FSRAILMPRIKVGRDYVQKAQTKEQADFAVEALAKALYERLFRWLVHRINKAL-------DRTKRQGASFIGILDIAGFE 464
Cdd:cd14907 321 LKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpkdekdQQLFQNKYLSIGLLDIFGFE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 465 IFELNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIE--WNFIDFgLDLQPCIDLIERPanPPGVLSLLDEECWFP 542
Cdd:cd14907 401 VFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEdyLNQLSY-TDNQDVIDLLDKP--PIGIFNLLDDSCKLA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 543 KATDKSFVEKVIQELGNHPKFQKPRQLRdKADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWkdv 622
Cdd:cd14907 478 TGTDEKLLNKIKKQHKNNSKLIFPNKIN-KDTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIF--- 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 623 driVGLDQVSGMGEMSFGSSYKTKKgmfrTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCN 702
Cdd:cd14907 554 ---SGEDGSQQQNQSKQKKSQKKDK----FLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYL 626
|
650 660 670
....*....|....*....|....*....|..
gi 1785379719 703 GVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 734
Cdd:cd14907 627 GVLESIRVRKQGYPYRKSYEDFYKQYSLLKKN 658
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
99-771 |
5.14e-138 |
|
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: 445.93 E-value: 5.14e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCT 177
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 178 GESGAGKTENTKKVIQYLAHVASshkGRKEHTAPgelehQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIV 257
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVAG---GRKDKTIA-----KVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRGKLI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 258 GANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFL--SNGNLPIPGQQDREIFQETMESMKI 335
Cdd:cd14904 153 GAKCETYLLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQYLgdSLAQMQIPGLDDAKLFASTQKSLSL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 336 MGFNHEEIMSMLKMVSAVLQFGNIVFrKERNTDQASMPDNTAAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQKAQTKE 415
Cdd:cd14904 233 IGLDNDAQRTLFKILSGVLHLGEVMF-DKSDENGSRISNGSQLSQVAKMLGLPTTRIEEALCNRSVVTRNESVTVPLAPV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 416 QADFAVEALAKALYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFVLE 495
Cdd:cd14904 312 EAEENRDALAKAIYSKLFDWMVVKINAAISTDDDRIKGQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDVFKTV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 496 QEEYQREGIEWNFIDFGlDLQPCIDLIErpaNPPGVLSLLDEECWFPKATDKSFVEKV---IQELGNHPKFQKPRQLRDK 572
Cdd:cd14904 392 EEEYIREGLQWDHIEYQ-DNQGIVEVID---GKMGIIALMNDHLRQPRGTEEALVNKIrtnHQTKKDNESIDFPKVKRTQ 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 573 adLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVDrivgldqvsGMGEMSFGSSYKTKKGMfRT 652
Cdd:cd14904 468 --FIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFGSSE---------APSETKEGKSGKGTKAP-KS 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 653 VGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILT 732
Cdd:cd14904 536 LGSQFKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAIMF 615
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 1785379719 733 PNAIPKGfmDGKQACAIMIRAL-ELDPNLYRIGQSKIFFR 771
Cdd:cd14904 616 PPSMHSK--DVRRTCSVFMTAIgRKSPLEYQIGKSLIYFK 653
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
99-771 |
1.25e-137 |
|
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: 444.49 E-value: 1.25e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 99 ASVLHNLKDRyySGLI----YTYSGLFCVVINPYKNLPiytEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDRE---D 171
Cdd:cd14891 1 AGILHNLEER--SKLDnqrpYTFMANVLIAVNPLRRLP---EPDKSDYINTPLDPCPPHPYAIAEMAYQQMCLGSGrmqN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 172 QSILCTGESGAGKTENTKKVIQYLAH------------VASSHKGRKEHTApgELEHQLLQANPILEAFGNAKTVKNDNS 239
Cdd:cd14891 76 QSIVISGESGAGKTETSKIILRFLTTravggkkasgqdIEQSSKKRKLSVT--SLDERLMDTNPILESFGNAKTLRNHNS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 240 SRFGKFIRINFDVAGY-IVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNGNLPI- 317
Cdd:cd14891 154 SRFGKFMKLQFTKDKFkLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSPEDFIYLNQSGCVSd 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 318 PGQQDREIFQETMESMKIMGFNHEEIMSMLKMVSAVLQFGNIVFRK----ERNTDQASMPDNTAAQKLCHLLGLNVTEFS 393
Cdd:cd14891 234 DNIDDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEedtsEGEAEIASESDKEALATAAELLGVDEEALE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 394 RAILMPRIkVGRDYVQKAQ-TKEQADFAVEALAKALYERLFRWLVHRINKALDRtKRQGASFIGILDIAGFEIFEL-NSF 471
Cdd:cd14891 314 KVITQREI-VTRGETFTIKrNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGH-DPDPLPYIGVLDIFGFESFETkNDF 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 472 EQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLSLLDEECWFPKATDKSFVE 551
Cdd:cd14891 392 EQLLINYANEALQATFNQQVFIAEQELYKSEGIDVGVITWP-DNRECLDLIA--SKPNGILPLLDNEARNPNPSDAKLNE 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 552 KVIQELGNHPKFQKPRQlRDKADLCII-HYAGKVDYKADEWLMKNMDPLNDNVATLLHQStdkytaelwkdvdrivgldq 630
Cdd:cd14891 469 TLHKTHKRHPCFPRPHP-KDMREMFIVkHYAGTVSYTIGSFIDKNNDIIPEDFEDLLASS-------------------- 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 631 vsgmgemsfgssyktkkgmfrtvgQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRI 710
Cdd:cd14891 528 ------------------------AKFSDQMQELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEV 583
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1785379719 711 CRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQA-CAIMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14891 584 LKVGLPTRVTYAELVDVYKPVLPPSVTRLFAENDRTlTQAILWAFRVPSDAYRLGRTRVFFR 645
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
99-771 |
3.65e-135 |
|
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: 438.96 E-value: 3.65e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYR--GKKRHE-------IPPHIYAISETAYRSMLQD- 168
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSQgiespqaLGPHVFAIADRSYRQMMSEi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 169 REDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKEHTAPGE---LEHQLLQANPILEAFGNAKTVKNDNSSRFGKF 245
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLTTLGNGEEGAPNEGEELGklsIMDRVLQSNPILEAFGNARTLRNDNSSRFGKF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 246 IRINFDVAGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGE--------HMKTDLLLEGFNQYRFLSNGNLPI 317
Cdd:cd14908 161 IELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEeehekyefHDGITGGLQLPNEFHYTGQGGAPD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 318 PGQ-QDREIFQETMESMKIMGFNHEEIMSMLKMVSAVLQFGNIVFRKERNtDQASMPDNTAAQK----LCHLLGLNVTEF 392
Cdd:cd14908 241 LREfTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEE-DGAAEIAEEGNEKclarVAKLLGVDVDKL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 393 SRAILMPRIKVGRDYVQKAQTKEQADFAVEALAKALYERLFRWLVHRINKAL--DRTKRQGASfIGILDIAGFEIFELNS 470
Cdd:cd14908 320 LRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSInwENDKDIRSS-VGVLDIFGFECFAHNS 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 471 FEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLSLLDEECWFP-KATDKSF 549
Cdd:cd14908 399 FEQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQ--AKKKGILTMLDDECRLGiRGSDANY 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 550 VEKVI--------QELGNHPKFQKPRQLRDKADLCIIHYAGKVDYKADEWLM-KNMDPLNdnvatllhqstdkytaelwk 620
Cdd:cd14908 476 ASRLYetylpeknQTHSENTRFEATSIQKTKLIFAVRHFAGQVQYTVETTFCeKNKDEIP-------------------- 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 621 dvdrivgldqvsgmgemsfgssyKTKKGMFRTvGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLR 700
Cdd:cd14908 536 -----------------------LTADSLFES-GQQFKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLR 591
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 701 CNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPnAIPKGFM-------DGKQACA--------------IMIRALELDPN 759
Cdd:cd14908 592 YGGVLEAVRVARSGYPVRLPHKDFFKRYRMLLP-LIPEVVLswsmerlDPQKLCVkkmckdlvkgvlspAMVSMKNIPED 670
|
730
....*....|..
gi 1785379719 760 LYRIGQSKIFFR 771
Cdd:cd14908 671 TMQLGKSKVFMR 682
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
99-771 |
2.01e-134 |
|
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 domains, a single FERM domain, and an SH3 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276861 [Multi-domain] Cd Length: 644 Bit Score: 435.36 E-value: 2.01e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTG 178
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 179 ESGAGKTENTKKVIQYLAHV---ASSHKGRkehtapgelehQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDvAGY 255
Cdd:cd14896 81 HSGSGKTEAAKKIVQFLSSLyqdQTEDRLR-----------QPEDVLPILESFGHAKTILNANASRFGQVLRLHLQ-HGV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 256 IVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNGNL-PIPGQQDREIFQETMESMK 334
Cdd:cd14896 149 IVGASVSHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQGPETYYYLNQGGAcRLQGKEDAQDFEGLLKALQ 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 335 IMGFNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQ--ASMPDNTAAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQKAQ 412
Cdd:cd14896 229 GLGLCAEELTAIWAVLAAILQLGNICFSSSERESQevAAVSSWAEIHTAARLLQVPPERLEGAVTHRVTETPYGRVSRPL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 413 TKEQADFAVEALAKALYERLFRWLVHRINKALDRTKRQGA-SFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTM 491
Cdd:cd14896 309 PVEGAIDARDALAKTLYSRLFTWLLKRINAWLAPPGEAESdATIGVVDAYGFEALRVNGLEQLCINLASERLQLFSSQTL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 492 FVLEQEEYQREGIEWNFIDfGLDLQPCIDLIErpANPPGVLSLLDEECWFPKATDKSFVEKVIQELGNHPKFQKPRQlrD 571
Cdd:cd14896 389 LAQEEEECQRELLPWVPIP-QPPRESCLDLLV--DQPHSLLSILDDQTWLSQATDHTFLQKCHYHHGDHPSYAKPQL--P 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 572 KADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVDRIVGLDQvsgmgemsfGSSyktkkgmfr 651
Cdd:cd14896 464 LPVFTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQEAEPQYGLGQ---------GKP--------- 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 652 TVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 731
Cdd:cd14896 526 TLASRFQQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGAL 605
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 1785379719 732 TpNAIPKGFMDGKQACAIMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14896 606 G-SERQEALSDRERCGAILSQVLGAESPLYHLGATKVLLK 644
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
97-824 |
2.58e-134 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 441.39 E-value: 2.58e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 97 NEASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEI-PPHIYAISETAYRSMLQDREDQSIL 175
Cdd:PTZ00014 108 NIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYRDAKDSDKlPPHVFTTARRALENLHGVKKSQTII 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 176 CTGESGAGKTENTKKVIQYLAHVASSHKGRKEHTApgelehqLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGY 255
Cdd:PTZ00014 188 VSGESGAGKTEATKQIMRYFASSKSGNMDLKIQNA-------IMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEEGG 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 256 IVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNGNLPIPGQQDREIFQETMESMKI 335
Cdd:PTZ00014 261 IRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKLKSLEEYKYINPKCLDVPGIDDVKDFEEVMESFDS 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 336 MGFNHEEIMSMLKMVSAVLQFGNIVF--RKERNTDQASM--PDNTAA-QKLCHLLGLNVTEFSRAILMPRIKVGRDYVQK 410
Cdd:PTZ00014 341 MGLSESQIEDIFSILSGVLLLGNVEIegKEEGGLTDAAAisDESLEVfNEACELLFLDYESLKKELTVKVTYAGNQKIEG 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 411 AQTKEQADFAVEALAKALYERLFRWLVHRINKALDRTKRQGAsFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHT 490
Cdd:PTZ00014 421 PWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGFKV-FIGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFVDI 499
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 491 MFVLEQEEYQREGIEWNFIDFgLDLQPCIDLIERPANppGVLSLLDEECWFPKATDKSFVEKVIQELGNHPKFqKPRQLR 570
Cdd:PTZ00014 500 VFERESKLYKDEGISTEELEY-TSNESVIDLLCGKGK--SVLSILEDQCLAPGGTDEKFVSSCNTNLKNNPKY-KPAKVD 575
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 571 DKADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVdrivgldqvsgmgEMSFGssyKTKKGMF 650
Cdd:PTZ00014 576 SNKNFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLFEGV-------------EVEKG---KLAKGQL 639
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 651 rtVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 730
Cdd:PTZ00014 640 --IGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKY 717
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 731 LTPNAIPKGFMDGKQACAIMIRALELDPNLYRIGQSKIFFR---AGVLAHLEEERDLKITDIIVFFQAAARGYLARRAFy 807
Cdd:PTZ00014 718 LDLAVSNDSSLDPKEKAEKLLERSGLPKDSYAIGKTMVFLKkdaAKELTQIQREKLAAWEPLVSVLEALILKIKKKRKV- 796
|
730
....*....|....*..
gi 1785379719 808 kkqqqMSALKVVQRNCA 824
Cdd:PTZ00014 797 -----RKNIKSLVRIQA 808
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
100-771 |
1.53e-132 |
|
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: 432.45 E-value: 1.53e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPiyteqivEMYRGKKRHE-------IPPHIYAISETAYRSMLQ----- 167
Cdd:cd14895 2 AFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIP-------GLYDLHKYREempgwtaLPPHVFSIAEGAYRSLRRrlhep 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 168 --DREDQSILCTGESGAGKTENTKKVIQYLA----HVASSHKGRKEHTAPGElehQLLQANPILEAFGNAKTVKNDNSSR 241
Cdd:cd14895 75 gaSKKNQTILVSGESGAGKTETTKFIMNYLAesskHTTATSSSKRRRAISGS---ELLSANPILESFGNARTLRNDNSSR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 242 FGKFIRINF-----DVAGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFN--QYRFLSNGN 314
Cdd:cd14895 152 FGKFVRMFFeghelDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQLELLSaqEFQYISGGQ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 315 LPI--PGQQDREIFQETMESMKIMGFNHEEIMSMLKMVSAVLQFGNIVFRKERNTD---------------QASMPDNTA 377
Cdd:cd14895 232 CYQrnDGVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEgeedngaasapcrlaSASPSSLTV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 378 AQKL---CHLLGLNVTEFSRAILMPRIKVGRDYVQKAQTKEQADFAVEALAKALYERLFRWLVHRINKALDRTK------ 448
Cdd:cd14895 312 QQHLdivSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASPQRQfalnpn 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 449 ----RQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIEWNFIDFGLDlQPCIDLIEr 524
Cdd:cd14895 392 kaanKDTTPCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDN-SVCLEMLE- 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 525 pANPPGVLSLLDEECWFPKATDKSFVEKVIQELGNHPKFQKPRqlRDKADLC--IIHYAGKVDYKADEWLMKNMDPLNDN 602
Cdd:cd14895 470 -QRPSGIFSLLDEECVVPKGSDAGFARKLYQRLQEHSNFSASR--TDQADVAfqIHHYAGAVRYQAEGFCEKNKDQPNAE 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 603 VATLLHQSTDKYTAELWKDVDRIVGLDQVSGMGEMSFGSSYKTKKGmfrtVGQLYKESLSKLMSTLRNTNPNFVRCIIPN 682
Cdd:cd14895 547 LFSVLGKTSDAHLRELFEFFKASESAELSLGQPKLRRRSSVLSSVG----IGSQFKQQLASLLDVVQQTQTHYIRCIKPN 622
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 683 HEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACAIMIRALELdpnlyr 762
Cdd:cd14895 623 DESASDQFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLVAAKNASDATASALIETLKVDHAEL------ 696
|
....*....
gi 1785379719 763 iGQSKIFFR 771
Cdd:cd14895 697 -GKTRVFLR 704
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
99-733 |
2.09e-130 |
|
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: 427.00 E-value: 2.09e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYTEQIVEMYR--------GKKRHEIPPHIYAISETAYRSMLQ-D 168
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLKpE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 169 REDQSILCTGESGAGKTENTKKVIQYLAHV-ASSHKGRKEHTAPGELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIR 247
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLTSVgRDQSSTEQEGSDAVEIGKRILQTNPILESFGNAQTIRNDNSSRFGKFIK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 248 INFDVAGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFL-----SNGNLPIPGQQD 322
Cdd:cd14902 161 IQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKGGKYELLnsygpSFARKRAVADKY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 323 REIFQETMESMKIMGFNHEEIMSMLKMVSAVLQFGNIVFRKE-RNTDQASMPDNTAAQ--KLCHLLGLNVTEFSRAILMP 399
Cdd:cd14902 241 AQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAEnGQEDATAVTAASRFHlaKCAELMGVDVDKLETLLSSR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 400 RIKVGRDYVQKAQTKEQADFAVEALAKALYERLFRWLVHRINKALD--------RTKRQGASFIGILDIAGFEIFELNSF 471
Cdd:cd14902 321 EIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINyfdsavsiSDEDEELATIGILDIFGFESLNRNGF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 472 EQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIEWNFIDFGlDLQPCIDLIERPANppGVLSLLDEECWFPKATDKSFVE 551
Cdd:cd14902 401 EQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYP-SNAACLALFDDKSN--GLFSLLDQECLMPKGSNQALST 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 552 KVIQELGNHPKFqkprqlrdkadlCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDkytaelwkDVDRIVGLDQV 631
Cdd:cd14902 478 KFYRYHGGLGQF------------VVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSN--------EVVVAIGADEN 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 632 SGMGEMSFGSSYKTKKGMFRT--VGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIR 709
Cdd:cd14902 538 RDSPGADNGAAGRRRYSMLRApsVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLEAVR 617
|
650 660
....*....|....*....|....
gi 1785379719 710 ICRQGFPNRIVFQEFRQRYEILTP 733
Cdd:cd14902 618 IARHGYSVRLAHASFIELFSGFKC 641
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
99-769 |
2.26e-126 |
|
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: 412.84 E-value: 2.26e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRH-EIPPHIYAISETAYRSMLQDREDQSILCT 177
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDAPDLtKLPPHVFYTARRALENLHGVNKSQTIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 178 GESGAGKTENTKKVIQYLAHVASSHKGRKEHTApgelehqLLQANPILEAFGNAKTVKNDNSSRFGKFIRInfDVA--GY 255
Cdd:cd14876 81 GESGAGKTEATKQIMRYFASAKSGNMDLRIQTA-------IMAANPVLEAFGNAKTIRNNNSSRFGRFMQL--DVAseGG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 256 IVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNGNLPIPGQQDREIFQETMESMKI 335
Cdd:cd14876 152 IRYGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLGLKEYKFLNPKCLDVPGIDDVADFEEVLESLKS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 336 MGFNHEEIMSMLKMVSAVLQFGNIVFRKErntDQASMPDntAA----------QKLCHLLGLNVTEFSRAILMPRIKVGR 405
Cdd:cd14876 232 MGLTEEQIDTVFSIVSGVLLLGNVKITGK---TEQGVDD--AAaisneslevfKEACSLLFLDPEALKRELTVKVTKAGG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 406 DYVQKAQTKEQADFAVEALAKALYERLFRWLVHRINKALDrtKRQG-ASFIGILDIAGFEIFELNSFEQLCINYTNEKLQ 484
Cdd:cd14876 307 QEIEGRWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIE--PPGGfKNFMGMLDIFGFEVFKNNSLEQLFINITNEMLQ 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 485 QLFNHTMFVLEQEEYQREGIEWNFIDFgLDLQPCIDLIERPANppGVLSLLDEECWFPKATDKSFVEKVIQELGNHPKFq 564
Cdd:cd14876 385 KNFIDIVFERESKLYKDEGIPTAELEY-TSNAEVIDVLCGKGK--SVLSILEDQCLAPGGSDEKFVSACVSKLKSNGKF- 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 565 KPRQLRDKADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVdrivgldqvsgmgEMSFGssyK 644
Cdd:cd14876 461 KPAKVDSNINFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEGV-------------VVEKG---K 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 645 TKKGMFrtVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEF 724
Cdd:cd14876 525 IAKGSL--IGSQFLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEF 602
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 1785379719 725 RQRYEILTPNAIPKGFMDGKQACAIMIRALELDPNLYRIGQSKIF 769
Cdd:cd14876 603 LYQFKFLDLGIANDKSLDPKVAALKLLESSGLSEDEYAIGKTMVF 647
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
99-771 |
3.38e-124 |
|
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: 408.24 E-value: 3.38e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTG 178
Cdd:cd01386 1 SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 179 ESGAGKTENTKKVIQYLAHVASSHKGRkehtapgeLEHQLLQA-NPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIV 257
Cdd:cd01386 81 RSGSGKTTNCRHILEYLVTAAGSVGGV--------LSVEKLNAaLTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQLA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 258 GANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNqyrflSNGNLPIPGQQDREIFQETM------- 330
Cdd:cd01386 153 SASIQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLA-----ESNSFGIVPLQKPEDKQKAAaafsklq 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 331 ESMKIMGFNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASMPDNTAAQKLCHLLGLNVTEFSRAILMP----------- 399
Cdd:cd01386 228 AAMKTLGISEEEQRAIWSILAAIYHLGAAGATKAASAGRKQFARPEWAQRAAYLLGCTLEELSSAIFKHhlsggpqqstt 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 400 -RIKVGRDYVQKAQTKEQADFAVEALAKALYERLFRWLVHRINKALDRTKRQGASfIGILDIAGFEIFELN------SFE 472
Cdd:cd01386 308 sSGQESPARSSSGGPKLTGVEALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSS-ITIVDTPGFQNPAHSgsqrgaTFE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 473 QLCINYTNEKLQQLFNHTMFVLEQEEYQREGIEWNFIDFGLDLQPCIDLIERP---ANPP---------GVLSLLDEECW 540
Cdd:cd01386 387 DLCHNYAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQApqqALVRsdlrdedrrGLLWLLDEEAL 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 541 FPKATDKSFVEKVIQELG--NHPKFQKPRQLRDKADLCII-HYAGK--VDYKADEWLMK-NMDPLNDNVATLLHQSTDKY 614
Cdd:cd01386 467 YPGSSDDTFLERLFSHYGdkEGGKGHSLLRRSEGPLQFVLgHLLGTnpVEYDVSGWLKAaKENPSAQNATQLLQESQKET 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 615 TAelwkdvdrivgldqvsgmgemsfgssyKTKKGMFRTVgqlyKESLSKLMSTLRNTNPNFVRCIIPNHE------KKAG 688
Cdd:cd01386 547 AA---------------------------VKRKSPCLQI----KFQVDALIDTLRRTGLHFVHCLLPQHNagkderSTSS 595
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 689 KLEPHLVLD------QLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGF-----MDGKQACAIMIRALELD 757
Cdd:cd01386 596 PAAGDELLDvpllrsQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPLTKKLGlnsevADERKAVEELLEELDLE 675
|
730
....*....|....
gi 1785379719 758 PNLYRIGQSKIFFR 771
Cdd:cd01386 676 KSSYRIGLSQVFFR 689
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
99-733 |
4.61e-119 |
|
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: 392.68 E-value: 4.61e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYTEQIVEMYRGKKR-HEIPPHIYAISETAYRSMLQDRE--DQSI 174
Cdd:cd14880 1 ETVLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQpQKLKPHIFTVGEQTYRNVKSLIEpvNQSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 175 LCTGESGAGKTENTKKVIQYLAHVASSHKGRKEHTAPGELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAG 254
Cdd:cd14880 81 VVSGESGAGKTWTSRCLMKFYAVVAASPTSWESHKIAERIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQLNRAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 255 YIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSN--GNLpipgqqDREIFQETMES 332
Cdd:cd14880 161 QMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAAFSWLPNpeRNL------EEDCFEVTREA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 333 MKIMGFNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASMPDNTA---AQKLCHLLGLNVTEFSRAILMPRIKVGRDYV- 408
Cdd:cd14880 235 MLHLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPCQPMDDTkesVRTSALLLKLPEDHLLETLQIRTIRAGKQQQv 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 409 -QKAQTKEQADFAVEALAKALYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLF 487
Cdd:cd14880 315 fKKPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSICADTDSWTTFIGLLDVYGFESFPENSLEQLCINYANEKLQQHF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 488 NHTMFVLEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLSLLDEECWFPKATDKSFVEKVIQE-LGNHPKFQKP 566
Cdd:cd14880 395 VAHYLRAQQEEYAVEGLEWSFINYQ-DNQTCLDLIE--GSPISICSLINEECRLNRPSSAAQLQTRIESaLAGNPCLGHN 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 567 RqLRDKADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVDRIVGLDQVSGmgemsfgssykTK 646
Cdd:cd14880 472 K-LSREPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPANPEEKTQEEPSG-----------QS 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 647 KGMFRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQ 726
Cdd:cd14880 540 RAPVLTVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQNFVE 619
|
....*..
gi 1785379719 727 RYEILTP 733
Cdd:cd14880 620 RYKLLRR 626
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
99-734 |
9.39e-117 |
|
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds Dictyostelium and Polysphondylium. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276871 [Multi-domain] Cd Length: 715 Bit Score: 387.80 E-value: 9.39e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYTEQIVEMYRGKKR-HEIPPHIYAISETAYRSMLQDREDQSILC 176
Cdd:cd14906 1 AIILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 177 TGESGAGKTENTKKVIQYLAHVASSHKGRKEH--TAPGELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAG 254
Cdd:cd14906 81 SGESGSGKTEASKTILQYLINTSSSNQQQNNNnnNNNNSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFRSSD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 255 YIV-GANIETYLLEKSR-AIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEG-FNQYRFL--------------SNGNLPI 317
Cdd:cd14906 161 GKIdGASIETYLLEKSRiSHRPDNINLSYHIFYYLVYGASKDERSKWGLNNdPSKYRYLdarddvissfksqsSNKNSNH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 318 PGQQDR-EIFQETMESMKIMGFNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQAS--MPDNTAA-QKLCHLLGLNVTEFS 393
Cdd:cd14906 241 NNKTESiESFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSDFSKYAyqKDKVTASlESVSKLLGYIESVFK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 394 RAILMPRIKV-GRDYVQ-KAQTKEQADFAVEALAKALYERLFRWLVHRINKALDR----------TKRQGASFIGILDIA 461
Cdd:cd14906 321 QALLNRNLKAgGRGSVYcRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRKFNQntqsndlaggSNKKNNLFIGVLDIF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 462 GFEIFELNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIEWNFIDFgLDLQPCIDLIERPANppGVLSLLDEECWF 541
Cdd:cd14906 401 GFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELIEKKSD--GILSLLDDECIM 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 542 PKATDKSFVEKVIQELGNHPKFQKpRQLrDKADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELwkd 621
Cdd:cd14906 478 PKGSEQSLLEKYNKQYHNTNQYYQ-RTL-AKGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFLKKSL--- 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 622 vdrivgldqvSGMGEMSFGSSYKTKKGMFRTVGQlYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRC 701
Cdd:cd14906 553 ----------FQQQITSTTNTTKKQTQSNTVSGQ-FLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLSQLRN 621
|
650 660 670
....*....|....*....|....*....|...
gi 1785379719 702 NGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 734
Cdd:cd14906 622 VGVLNTIKVRKMGYSYRRDFNQFFSRYKCIVDM 654
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
99-771 |
1.14e-112 |
|
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: 373.84 E-value: 1.14e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYTEQIVEMYRGKKRH-----EIPPHIYAISETAYRSMLQDREDQ 172
Cdd:cd14886 1 AVVIDILRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 173 SILCTGESGAGKTENTKKVIQYLAHVASshkgrkehTAPGELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDV 252
Cdd:cd14886 81 SCIVSGESGAGKTETAKQLMNFFAYGHS--------TSSTDVQSLILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 253 AGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNGN-LPIPGQQDREIFQETME 331
Cdd:cd14886 153 DGGLKGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLESYNFLNASKcYDAPGIDDQKEFAPVRS 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 332 SMKIMgFNHEEIMSMLKMVSAVLQFGNIVFRKERN--TDQASMPDNTAA-QKLCHLLGLNVTEFSRAILMPRIKVGRDYV 408
Cdd:cd14886 233 QLEKL-FSKNEIDSFYKCISGILLAGNIEFSEEGDmgVINAAKISNDEDfGKMCELLGIESSKAAQAIITKVVVINNETI 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 409 QKAQTKEQADFAVEALAKALYERLFRWLVHRINKAL---DRTKRqgasFIGILDIAGFEIFELNSFEQLCINYTNEKLQQ 485
Cdd:cd14886 312 ISPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEIIqfdADARP----WIGILDIYGFEFFERNTYEQLLINYANERLQQ 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 486 LFNHTMFVLEQEEYQREGIEWNFIDFGlDLQPCIDLIERPANppGVLSLLDEECWFPKATDKSFVEKVIQELGNHpkfqk 565
Cdd:cd14886 388 YFINQVFKSEIQEYEIEGIDHSMITFT-DNSNVLAVFDKPNL--SIFSFLEEQCLIQTGSSEKFTSSCKSKIKNN----- 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 566 pRQLRDKADLC---IIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVDRIVGLdqvsgmgemsfgss 642
Cdd:cd14886 460 -SFIPGKGSQCnftIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNKAFSDIPNEDGN-------------- 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 643 yktKKGMFrtVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQ 722
Cdd:cd14886 525 ---MKGKF--LGSTFQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFE 599
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 1785379719 723 EFRQRYEILT--PNAIPKGFMDGKQACAIMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14886 600 EFFHRNKILIshNSSSQNAGEDLVEAVKSILENLGIPCSDYRIGKTKVFLR 650
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
99-771 |
1.40e-110 |
|
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: 368.37 E-value: 1.40e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 99 ASVLHNLKDRYYS-GLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRG-KKRHEIPPHIYAISETAYRSM-LQDREDQSIL 175
Cdd:cd14875 1 ATLLHCIKERFEKlHQQYSLMGEMVLSVNPFRLMPFNSEEERKKYLAlPDPRLLPPHIWQVAHKAFNAIfVQGLGNQSVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 176 CTGESGAGKTENTKKVIQYLAHVASSHKGR-KEHTAPGELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD-VA 253
Cdd:cd14875 81 ISGESGSGKTENAKMLIAYLGQLSYMHSSNtSQRSIADKIDENLKWSNPVMESFGNARTVRNDNSSRFGKYIKLYFDpTS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 254 GYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDL-LLEGFNQYRFLSNGNL----PIPGQ--QDREIF 326
Cdd:cd14875 161 GVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELgGLKTAQDYKCLNGGNTfvrrGVDGKtlDDAHEF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 327 QETMESMKIMGFNHEEIMSMLKMVSAVLQFGNIVFRKERNtDQASMPDNTAAQKLCHLLGLNVTEFSRAILmprIKVGRD 406
Cdd:cd14875 241 QNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQN-DKAQIADETPFLTACRLLQLDPAKLRECFL---VKSKTS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 407 YVQKAQTKEQADFAVEALAKALYERLFRWLVHRINKALD-RTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQ 485
Cdd:cd14875 317 LVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNASITpQGDCSGCKYIGLLDIFGFENFTRNSFEQLCINYANESLQN 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 486 LFNHTMFVLEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLSLLDEECWFPKATDKSFVEKVIQELGNH----- 560
Cdd:cd14875 397 HYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNMFD--QKRTGIFSMLDEECNFKGGTTERFTTNLWDQWANKspyfv 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 561 -PKFQKPRQLRdkadlcIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELwkdvdrivgldqvsgmgemsf 639
Cdd:cd14875 474 lPKSTIPNQFG------VNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTL--------------------- 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 640 gssYKTKKGMFR---TVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFP 716
Cdd:cd14875 527 ---LSTEKGLARrkqTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYP 603
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1785379719 717 NRIVFQEFRQRYEILTPNAIPKGFMDGK---QACAIMIRALEL----DPNlYRIGQSKIFFR 771
Cdd:cd14875 604 VRRPIEQFCRYFYLIMPRSTASLFKQEKyseAAKDFLAYYQRLygwaKPN-YAVGKTKVFLR 664
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
99-728 |
1.18e-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: 355.94 E-value: 1.18e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYTEQIVEMY----------RGKKRHEIPPHIYAISETAYRSMLQ 167
Cdd:cd14899 1 ASILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYaydhnsqfgdRVTSTDPREPHLFAVARAAYIDIVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 168 DREDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKEHTAPGE---------LEHQLLQANPILEAFGNAKTVKNDN 238
Cdd:cd14899 81 NGRSQSILISGESGAGKTEATKIIMTYFAVHCGTGNNNLTNSESISppaspsrttIEEQVLQSNPILEAFGNARTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 239 SSRFGKFIRINF-DVAGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAG----AGEHMKTDLLLEGFNQYRFLSNG 313
Cdd:cd14899 161 SSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSAdnncVSKEQKQVLALSGGPQSFRLLNQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 314 NLPIP---GQQDREIFQETMESMKIMGFNHEEIMSMLKMVSAVLQFGNIVF-----RKERNT--DQASMPDNTAA----- 378
Cdd:cd14899 241 SLCSKrrdGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFeqiphKGDDTVfaDEARVMSSTTGafdhf 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 379 QKLCHLLGLNVTEFSRAILMPRIKVGRDYVQKAQTKEQADFAVEALAKALYERLFRWLVHRINKALDRT----------- 447
Cdd:cd14899 321 TKAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLQRQasapwgadesd 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 448 ---KRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIEWNFIDFGlDLQPCIDLIER 524
Cdd:cd14899 401 vddEEDATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFP-NNRACLELFEH 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 525 paNPPGVLSLLDEECWFPKATDKSFVEKVIQEL---GNHPKFQKPRQLRDKADLCIIHYAGKVDYKADEWLMKNMDPLND 601
Cdd:cd14899 480 --RPIGIFSLTDQECVFPQGTDRALVAKYYLEFekkNSHPHFRSAPLIQRTTQFVVAHYAGCVTYTIDGFLAKNKDSFCE 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 602 NVATLLHQSTDKYTAELWKDVDRIVGLDQVSGMGEMSFGSSYKTKKGMFRTVGQLYKESLSKLMSTLRNTNPNFVRCIIP 681
Cdd:cd14899 558 SAAQLLAGSSNPLIQALAAGSNDEDANGDSELDGFGGRTRRRAKSAIAAVSVGTQFKIQLNELLSTVRATTPRYVRCIKP 637
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1785379719 682 NHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 728
Cdd:cd14899 638 NDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRY 684
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
99-771 |
2.45e-102 |
|
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: 346.64 E-value: 2.45e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 99 ASVLHNLKDRYYS--------GLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDRE 170
Cdd:cd14887 1 PNLLENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 171 DQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKEHTapgeLEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 250
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTYLAAVSDRRHGADSQG----LEARLLQSGPVLEAFGNAHTVLNANSSRFGKMLLLHF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 251 DVAGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLlegfnqyrflsngnlpiPGQQDREIFQ--- 327
Cdd:cd14887 157 TGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAVAAATQKSS-----------------AGEGDPESTDlrr 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 328 --ETMESMKIMGFNHEEImsmLKMVSAVLQFGNIVFRKERNTDQASMPDNTA--------AQKLCHLL-------GLNVT 390
Cdd:cd14887 220 itAAMKTVGIGGGEQADI---FKLLAAILHLGNVEFTTDQEPETSKKRKLTSvsvgceetAADRSHSSevkclssGLKVT 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 391 EFSRAIL--------MPRIKVGRDYV------------QKAQTKEQADFAVEALAKALYERLFRWLVHRINKALDRTKR- 449
Cdd:cd14887 297 EASRKHLktvarllgLPPGVEGEEMLrlalvsrsvretRSFFDLDGAAAARDAACKNLYSRAFDAVVARINAGLQRSAKp 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 450 ------------QGASFIGILDIAGFEIFE---LNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIEWNFI--DFG 512
Cdd:cd14887 377 sesdsdedtpstTGTQTIGILDLFGFEDLRnhsKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGVFQNQDcsAFP 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 513 LDLQPCIDLIERPAN---------------------PPGVLSLLDE------ECWFPKATDKSFVEKVIQELGNHPKFQK 565
Cdd:cd14887 457 FSFPLASTLTSSPSStspfsptpsfrsssafatspsLPSSLSSLSSslssspPVWEGRDNSDLFYEKLNKNIINSAKYKN 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 566 --PRQLRDKADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLhQSTDKYTaelwkdvdRIVGLDQVSGMgemsfgSSY 643
Cdd:cd14887 537 itPALSRENLEFTVSHFACDVTYDARDFCRANREATSDELERLF-LACSTYT--------RLVGSKKNSGV------RAI 601
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 644 KTKKgmfRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQE 723
Cdd:cd14887 602 SSRR---STLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVE 678
|
730 740 750 760
....*....|....*....|....*....|....*....|....*...
gi 1785379719 724 FRQRYEILTPNAIpKGFMDGKQACAIMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14887 679 LWRRYETKLPMAL-REALTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
100-735 |
6.07e-100 |
|
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: 334.56 E-value: 6.07e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNlpIYTEQIVEMYRGKKRHeIPPHIYAISETAYRSMLQdREDQSILCTGE 179
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYET--IYGAGAMKAYLKNYSH-VEPHVYDVAEASVQDLLV-HGNQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 180 SGAGKTENTKKVIQYLAhvasshkgrkEHTAPGE-LEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDvaGYIVG 258
Cdd:cd14898 78 SGSGKTENAKLVIKYLV----------ERTASTTsIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKFD--GKITG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 259 ANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDlllegFNQYRF-LSNGNLPIPGQQDREIFQETMESMKIMG 337
Cdd:cd14898 146 AKFETYLLEKSRVTHHEKGERNFHIFYQFCASKRLNIKND-----FIDTSStAGNKESIVQLSEKYKMTCSAMKSLGIAN 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 338 FnhEEIMSMLkmvSAVLQFGNIVFRKERNTDQASmpdNTAAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQKAQTKEQA 417
Cdd:cd14898 221 F--KSIEDCL---LGILYLGSIQFVNDGILKLQR---NESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIEVFNTLKQA 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 418 DFAVEALAKALYERLFRWLVHRINKALDRTkrqGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFVLEQE 497
Cdd:cd14898 293 RTIRNSMARLLYSNVFNYITASINNCLEGS---GERSISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMFRAKQG 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 498 EYQREGIEWNFIDFgLDLQPCIDLIERPAnppGVLSLLDEECWFPKATDKSFVEKvIQELGNHpkfqkprQLRDKADLCI 577
Cdd:cd14898 370 MYKEEGIEWPDVEF-FDNNQCIRDFEKPC---GLMDLISEESFNAWGNVKNLLVK-IKKYLNG-------FINTKARDKI 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 578 I--HYAGKVDYKADEWLMKNMDplndnvatllhqstdkytaelwkdvdrivgldqvsGMGEMSFGSSYKTKKGMFRTVGQ 655
Cdd:cd14898 438 KvsHYAGDVEYDLRDFLDKNRE-----------------------------------KGQLLIFKNLLINDEGSKEDLVK 482
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 656 LYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNA 735
Cdd:cd14898 483 YFKDSMNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRILGITL 562
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
96-770 |
8.89e-95 |
|
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase uses its motor domain to tether its vesicular cargo to peripheral actin. It works in opposition to dynein, contributing to the retention of Mcs1 vesicles at the site of cell growth and increasing vesicle fusion necessary for polarized growth. Class 17 myosins consist of a N-terminal myosin motor domain with Cyt-b5, chitin synthase 2, and a DEK_C domains at it C-terminus. The chitin synthase region contains several transmembrane domains by which myosin 17 is thought to bind secretory vesicles. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276845 [Multi-domain] Cd Length: 647 Bit Score: 321.81 E-value: 8.89e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 96 LNEASVLHNLKDRYYSGLIYTY---SGLfcVVINPYKNLPIYTEQIVEMYR-------GKKRHEIPPHIYAISETAYRSM 165
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRlgsSAL--VAVNPYKYLSSNSDASLGEYGseyydttSGSKEPLPPHAYDLAARAYLRM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 166 LQDREDQSILCTGESGAGKTENTKKVIQYLAHV-ASSHKGRKehtapgeLEHQLLQANPILEAFGNAKTVKNDNSSRFGK 244
Cdd:cd14879 79 RRRSEDQAVVFLGETGSGKSESRRLLLRQLLRLsSHSKKGTK-------LSSQISAAEFVLDSFGNAKTLTNPNASRFGR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 245 FIRINFDVAGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNGNL----PIPGQ 320
Cdd:cd14879 152 YTELQFNERGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPSDYALLASYGChplpLGPGS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 321 QDREIFQETMESMKIMGFNHEEIMSMLKMVSAVLQFGNIVFR--KERNTDQASMpDNTAA-QKLCHLLGLNVTEFsRAIL 397
Cdd:cd14879 232 DDAEGFQELKTALKTLGFKRKHVAQICQLLAAILHLGNLEFTydHEGGEESAVV-KNTDVlDIVAAFLGVSPEDL-ETSL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 398 MPRIK-VGRD----YVQKAQTKEQADfaveALAKALYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIF---ELN 469
Cdd:cd14879 310 TYKTKlVRKElctvFLDPEGAAAQRD----ELARTLYSLLFAWVVETINQKLCAPEDDFATFISLLDFPGFQNRsstGGN 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 470 SFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIEWNFIDFgLDLQPCIDLIERPanPPGVLSLLDEEC-WFPKATDKS 548
Cdd:cd14879 386 SLDQFCVNFANERLHNYVLRSFFERKAEELEAEGVSVPATSY-FDNSDCVRLLRGK--PGGLLGILDDQTrRMPKKTDEQ 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 549 FVEKVIQELGNHPKF---QKPRQLRDKADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLhqstdkytaelwkdvdri 625
Cdd:cd14879 463 MLEALRKRFGNHSSFiavGNFATRSGSASFTVNHYAGEVTYSVEGFLERNGDVLSPDFVNLL------------------ 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 626 vgldqvsgmgemsfgssyktkkgmfRTVGQLyKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVL 705
Cdd:cd14879 525 -------------------------RGATQL-NAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQIRSLGLP 578
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1785379719 706 EGIRICRQGFPNRIVFQEFRQRYEILTPnaipkgFMDGKQACAIMIRALELDPNLYRIGQSKIFF 770
Cdd:cd14879 579 ELAARLRVEYVVSLEHAEFCERYKSTLR------GSAAERIRQCARANGWWEGRDYVLGNTKVFL 637
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
99-771 |
6.64e-92 |
|
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: 313.68 E-value: 6.64e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYR---GKKRHEIPPHIYAISETAYRSMLQDREDQSIL 175
Cdd:cd14878 1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYLsssGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 176 CTGESGAGKTENTKKVIQYLAHVASSHKGrkehtapgELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF-DVAG 254
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLTCRASSSRT--------TFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFcERKK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 255 YIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNGnlpIPGQ-------QDREIFQ 327
Cdd:cd14878 153 HLTGARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQT---MREDvstaersLNREKLA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 328 ETMESMKIMGFNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASMPDNTAAQKLCHLLGLNVTEFSRAILMPRIKVGRDY 407
Cdd:cd14878 230 VLKQALNVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDM 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 408 VQKAQTKEQADFAVEALAKALYERLFRWLVHRINKAL---DRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQ 484
Cdd:cd14878 310 IIRRHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLqsqDEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMH 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 485 QLFNHTMFVLEQEEYQREGIewnfidfgldlqpCIDLIERPAN-----------PPGVLSLLDEECWFPKATDKSFVEKV 553
Cdd:cd14878 390 HYINEVLFLQEQTECVQEGV-------------TMETAYSPGNqtgvldfffqkPSGFLSLLDEESQMIWSVEPNLPKKL 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 554 --IQELGNHPKFQKPRQ-------LRDK-ADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELwkdvd 623
Cdd:cd14878 457 qsLLESSNTNAVYSPMKdgngnvaLKDQgTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHL----- 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 624 rivgldqvsgmgemsFGSSYKTkkgmfrTVGQLYKeSLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNG 703
Cdd:cd14878 532 ---------------FQSKLVT------IASQLRK-SLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIG 589
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1785379719 704 VLEGIRICRQGFPNRIVFQEFRQRYEILTPNAI-PKGFMDGKQACAIMIRALELDPnlYRIGQSKIFFR 771
Cdd:cd14878 590 VLEMVKIFRYGYPVRLSFSDFLSRYKPLADTLLgEKKKQSAEERCRLVLQQCKLQG--WQMGVRKVFLK 656
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
99-771 |
1.58e-91 |
|
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: 312.33 E-value: 1.58e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQivemYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTG 178
Cdd:cd14937 1 AEVLNMLALRYKKNYIYTIAEPMLISINPYQVIDVDINE----YKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 179 ESGAGKTENTKKVIQYLAhvasshKGRKEHTapgELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 258
Cdd:cd14937 77 ESGSGKTEASKLVIKYYL------SGVKEDN---EISNTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIVS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 259 ANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNGNLPIPGQQDREIFQETMESMKIMGF 338
Cdd:cd14937 148 SSIEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSENEYKYIVNKNVVIPEIDDAKDFGNLMISFDKMNM 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 339 nHEEIMSMLKMVSAVLQFGNIVFR---KERNTDQASMPDNT--AAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQKAQT 413
Cdd:cd14937 228 -HDMKDDLFLTLSGLLLLGNVEYQeieKGGKTNCSELDKNNleLVNEISNLLGINYENLKDCLVFTEKTIANQKIEIPLS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 414 KEQADFAVEALAKALYERLFRWLVHRINKALDRTKrQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFV 493
Cdd:cd14937 307 VEESVSICKSISKDLYNKIFSYITKRINNFLNNNK-ELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIHSIYLYIVYE 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 494 LEQEEYQREGIEWNFIDFGLDlQPCIDLIERPANppgVLSLLDEECWFPKATDKSFVEKVIQELGNHPKFQKPRQLRDKa 573
Cdd:cd14937 386 KETELYKAEDILIESVKYTTN-ESIIDLLRGKTS---IISILEDSCLGPVKNDESIVSVYTNKFSKHEKYASTKKDINK- 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 574 DLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVDRIVGLDQVSGMgemsfgsSYKtkkgmfrtv 653
Cdd:cd14937 461 NFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDVEVSESLGRKNLI-------TFK--------- 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 654 gqlYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRIcRQGFPNRIVFQEFRQRYEILTP 733
Cdd:cd14937 525 ---YLKNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNI-SFFFQYKYTFDVFLSYFEYLDY 600
|
650 660 670
....*....|....*....|....*....|....*...
gi 1785379719 734 NAIPKGFMDGKQACAIMIRAlELDPNLYRIGQSKIFFR 771
Cdd:cd14937 601 STSKDSSLTDKEKVSMILQN-TVDPDLYKVGKTMVFLK 637
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
99-723 |
5.52e-78 |
|
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: 274.09 E-value: 5.52e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYTEQIVEMYRGKKRHE-------IPPHIYAISETAYRSMLQDRE 170
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSaasaapfPKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 171 DQSILCTGESGAGKTENTKKVIQYLAHVasshKGRKEHTapgELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 250
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYFHYI----QTDSQMT---ERIDKLIYINNILESMSNATTIKNNNSSRCGRINLLIF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 251 D---------VAGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAG-AGEHMKTDLLLEGFNQYRFLSN-------- 312
Cdd:cd14884 154 EeventqknmFNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGlSDEDLARRNLVRNCGVYGLLNPdeshqkrs 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 313 --GNLPIPG----------QQDREIFQETMESMKIMGFNHEEIMSMLKMVSAVLQFGNIVFRKerntdqasmpdntaaqk 380
Cdd:cd14884 234 vkGTLRLGSdsldpseeekAKDEKNFVALLHGLHYIKYDERQINEFFDIIAGILHLGNRAYKA----------------- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 381 LCHLLGLNVTEFSRAILMPRIKVGRDYVQKAQTKEQADFAVEALAKALYERLFRWLVHRINKALDRTKRQGA-------- 452
Cdd:cd14884 297 AAECLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNVLKCKEKDEsdnediys 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 453 ---SFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIEWNFIDFGlDLQPCIDLIERpanpp 529
Cdd:cd14884 377 ineAIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDVAP-SYSDTLIFIAK----- 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 530 gVLSLLDE-----ECWFPKATDKSFV-----EKVIQELGNH------PKFQK---PRQLRDKADLCIIHYAGKVDYKADE 590
Cdd:cd14884 451 -IFRRLDDitklkNQGQKKTDDHFFRyllnnERQQQLEGKVsygfvlNHDADgtaKKQNIKKNIFFIRHYAGLVTYRINN 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 591 WLMKNMDPLNDNVATLLHQSTDKYTAElwkdvdrivgldqvsgmgemsfgSSYKTKKGMFRTVGQLYKESLSKLMSTLRN 670
Cdd:cd14884 530 WIDKNSDKIETSIETLISCSSNRFLRE-----------------------ANNGGNKGNFLSVSKKYIKELDNLFTQLQS 586
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 1785379719 671 TNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQE 723
Cdd:cd14884 587 TDMYYIRCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIPKKE 639
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
100-758 |
1.26e-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: 268.52 E-value: 1.26e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYknlpiyteqiveMYRGKKRHEIPPHIYA-------ISETAYRSMLQDREDQ 172
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPY------------RDVGNPLTLTSTRSSPlapqllkVVQEAVRQQSETGYPQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 173 SILCTGESGAGKTENTKKVIQYLAHVASshkGRKEHTApgeLEHqLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFdV 252
Cdd:cd14881 70 AIILSGTSGSGKTYASMLLLRQLFDVAG---GGPETDA---FKH-LAAAFTVLRSLGSAKTATNSESSRIGHFIEVQV-T 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 253 AGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFN--QYRFLSNGNLPIPGQQDREIFQETM 330
Cdd:cd14881 142 DGALYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDGYSpaNLRYLSHGDTRQNEAEDAARFQAWK 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 331 ESMKIMGFNHEEIMSMLkmvSAVLQFGNIVFrKERNTDQASMPDNTAAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQK 410
Cdd:cd14881 222 ACLGILGIPFLDVVRVL---AAVLLLGNVQF-IDGGGLEVDVKGETELKSVAALLGVSGAALFRGLTTRTHNARGQLVKS 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 411 AQTKEQADFAVEALAKALYERLFRWLVHRINKaldrTKRQGAS--------FIGILDIAGFEIFELNSFEQLCINYTNEK 482
Cdd:cd14881 298 VCDANMSNMTRDALAKALYCRTVATIVRRANS----LKRLGSTlgthatdgFIGILDMFGFEDPKPSQLEHLCINLCAET 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 483 LQQLFNHTMFVLEQEEYQREGIEWNF-IDFgLDLQPCIDLIErpANPPGVLSLLDEECwFPKATDKSFVEKVIQELGNHP 561
Cdd:cd14881 374 MQHFYNTHIFKSSIESCRDEGIQCEVeVDY-VDNVPCIDLIS--SLRTGLLSMLDVEC-SPRGTAESYVAKIKVQHRQNP 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 562 KFQKPRQLRDKAdLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTdkytaelwkdvdrivgldqvsgmgeMSFGs 641
Cdd:cd14881 450 RLFEAKPQDDRM-FGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYKQN-------------------------CNFG- 502
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 642 syktkkgmFRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVF 721
Cdd:cd14881 503 --------FATHTQDFHTRLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAGGYPHRMRF 574
|
650 660 670
....*....|....*....|....*....|....*....
gi 1785379719 722 QEFRQRYEILTPNAIPKGFMDGKQACA--IMIRALELDP 758
Cdd:cd14881 575 KAFNARYRLLAPFRLLRRVEEKALEDCalILQFLEAQPP 613
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
100-724 |
4.32e-73 |
|
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: 259.25 E-value: 4.32e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYTEQIVEMYrgKKRHEIPPHIYAISETAYRSMLQDREDQSILCTG 178
Cdd:cd14905 2 TLINIIQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNY--NQRRGLPPHLFALAAKAISDMQDFRRDQLIFIGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 179 ESGAGKTENTKKVIQYLAhvaSSHKGRKEHtapgeLEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 258
Cdd:cd14905 80 ESGSGKSENTKIIIQYLL---TTDLSRSKY-----LRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 259 ANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSN-GNLPIPGQQDREIFQETMESMKIMG 337
Cdd:cd14905 152 AKLYSYFLDENRVTYQNKGERNFHIFYQFLKGITDEEKAAYQLGDINSYHYLNQgGSISVESIDDNRVFDRLKMSFVFFD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 338 FNHEEIMSMLKMVSAVLQFGNIVFRKERNtdQASMPDNTAAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQKAqtkeqa 417
Cdd:cd14905 232 FPSEKIDLIFKTLSFIIILGNVTFFQKNG--KTEVKDRTLIESLSHNITFDSTKLENILISDRSMPVNEAVENR------ 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 418 dfavEALAKALYERLFRWLVHRINKALDRTkrQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFVLEQE 497
Cdd:cd14905 304 ----DSLARSLYSALFHWIIDFLNSKLKPT--QYSHTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVLKQEQR 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 498 EYQREGIEW-NFIDFGlDLQPCIDLIERpanppgVLSLLDEECWFPKATDKSFVEKVIQELGNHPKF-QKPRQLRdkadl 575
Cdd:cd14905 378 EYQTERIPWmTPISFK-DNEESVEMMEK------IINLLDQESKNINSSDQIFLEKLQNFLSRHHLFgKKPNKFG----- 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 576 cIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKY-------------TAELWKDVD----------RIV------ 626
Cdd:cd14905 446 -IEHYFGQFYYDVRGFIIKNRDEILQRTNVLHKNSITKYlfsrdgvfninatVAELNQMFDakntakksplSIVkvllsc 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 627 ------------------GLDQVSGMGEMSFGSSYKTKKGMFRTVGQlykeslsklmstlRNTNPNFVRCIIPNHEKKAG 688
Cdd:cd14905 525 gsnnpnnvnnpnnnsgggGGGGNSGGGSGSGGSTYTTYSSTNKAINN-------------SNCDFHFIRCIKPNSKKTHL 591
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 1785379719 689 KLEPHLVLDQLRCNGVLEGIRICRQGFP----NRIVFQEF 724
Cdd:cd14905 592 TFDVKSVNEQIKSLCLLETTRIQRFGYTihynNKIFFDRF 631
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
99-736 |
3.80e-70 |
|
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: 249.40 E-value: 3.80e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYrgkkrheippHIYAISETAYRSMLQDRED-QSILCT 177
Cdd:cd14874 1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 178 GESGAGKTENTKKVIQYLAHVASSHKGRKEHTApgelehqllqANPILEAFGNAKTVKNDNSSRFGKFIRINFDvAGYIV 257
Cdd:cd14874 71 GESGSGKSYNAFQVFKYLTSQPKSKVTTKHSSA----------IESVFKSFGCAKTLKNDEATRFGCSIDLLYK-RNVLT 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 258 GANIE-TYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNGNLPIPGQQDREIFQETMESMKIM 336
Cdd:cd14874 140 GLNLKyTVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGLQKFFYINQGNSTENIQSDVNHFKHLEDALHVL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 337 GFNHEEIMSMLKMVSAVLQFGNIVFRKERNTD---QASMPDNTAAQK-LCHLLGLNVTEFSrAILMPRIKVGrdyvqKAQ 412
Cdd:cd14874 220 GFSDDHCISIYKIISTILHIGNIYFRTKRNPNveqDVVEIGNMSEVKwVAFLLEVDFDQLV-NFLLPKSEDG-----TTI 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 413 TKEQADFAVEALAKALYERLFRWLVHRINKALDRTKRQGAsfIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMF 492
Cdd:cd14874 294 DLNAALDNRDSFAMLIYEELFKWVLNRIGLHLKCPLHTGV--ISILDHYGFEKYNNNGVEEFLINSVNERIENLFVKHSF 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 493 VLEQEEYQREGIEWNF-IDFGLDLQPCIDLIERpaNPPGVLSLLDEECWFPKATDKSFVEKVIQELGNHPKFQKPRQlRD 571
Cdd:cd14874 372 HDQLVDYAKDGISVDYkVPNSIENGKTVELLFK--KPYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRSSYGKARN-KE 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 572 KADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELwkdvdrivgldqvsgmgemsFGSSYKTKKGMFR 651
Cdd:cd14874 449 RLEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLL--------------------FESYSSNTSDMIV 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 652 TVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 731
Cdd:cd14874 509 SQAQFILRGAQEIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYRCL 588
|
....*
gi 1785379719 732 TPNAI 736
Cdd:cd14874 589 LPGDI 593
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
102-729 |
9.07e-66 |
|
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: 239.10 E-value: 9.07e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 102 LHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYT----------EQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDRED 171
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTpdhmqaynksREQTPLYEKDTVNDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 172 QSILCTGESGAGKTENTKKVIQYLAHVASS----HKGRKEHTAPGELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIR 247
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQYLCEIGDEteprPDSEGASGVLHPIGQQILHAFTILEAFGNAATRQNRNSSRFAKMIS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 248 INFDVAGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAgEH---MKTDLLL-EGFNQYRFLSN-----GNLPIp 318
Cdd:cd14893 164 VEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGV-QHdptLRDSLEMnKCVNEFVMLKQadplaTNFAL- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 319 gqqDREIFQETMESMKIMGFNHEEIMSMLKMVSAVLQFGNIVF-------------RKERNTDQASMPDNTAAQKL--CH 383
Cdd:cd14893 242 ---DARDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFvpdpeggksvggaNSTTVSDAQSCALKDPAQILlaAK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 384 LLGLNVTEFSRaILMPRIKVGRDYVQ-----KAQTKEQADFAVEALAKALYERLFRWLVHRINKAL----DRTKRQG--- 451
Cdd:cd14893 319 LLEVEPVVLDN-YFRTRQFFSKDGNKtvsslKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILggifDRYEKSNivi 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 452 -ASFIGILDIAGFEIFE--LNSFEQLCINYTNEKLQQLF-NHTMFV----LEQEEYQREG--IEWNFIDFGLDLQPCIDL 521
Cdd:cd14893 398 nSQGVHVLDMVGFENLTpsQNSFDQLCFNYWSEKVHHFYvQNTLAInfsfLEDESQQVENrlTVNSNVDITSEQEKCLQL 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 522 IERPanPPGVLSLLDEECWFPKATDKSFVEKVIQ-----------ELGNHPKFQKPRQLRDKADLCII-HYAGKVDYKAD 589
Cdd:cd14893 478 FEDK--PFGIFDLLTENCKVRLPNDEDFVNKLFSgneavgglsrpNMGADTTNEYLAPSKDWRLLFIVqHHCGKVTYNGK 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 590 EWLMKNMDPLNDNVATLLHQSTDKytaelwkdVDRIVGLDQVSGMGEMSFGSSY---KTKKGMFRTVGQLYKESLS---- 662
Cdd:cd14893 556 GLSSKNMLSISSTCAAIMQSSKNA--------VLHAVGAAQMAAASSEKAAKQTeerGSTSSKFRKSASSARESKNitds 627
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1785379719 663 ----------KLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 729
Cdd:cd14893 628 aatdvynqadALLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRYK 704
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
100-771 |
3.07e-65 |
|
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: 235.02 E-value: 3.07e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTGE 179
Cdd:cd14882 2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 180 SGAGKTENTKKVIQYLAHVASSHKGRKEhtapgelehQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVGA 259
Cdd:cd14882 82 SYSGKTTNARLLIKHLCYLGDGNRGATG---------RVESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMSGA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 260 NIETYLLEKSRAIRQAKDERTFHVFYQLLAG--AGEHMKTDLLLEGFNqYRFL--SNGNLPIPGQQDR-------EIFQE 328
Cdd:cd14882 153 IFWMYQLEKLRVSTTDGNQSNFHIFYYFYDFieAQNRLKEYNLKAGRN-YRYLriPPEVPPSKLKYRRddpegnvERYKE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 329 TMESMKIMGFNHEEIMSMLKMVSAVLQFGNIVFRKerNTDQASMPDNTAAQKLCHLLGLNVTEFSRAILMPRIKVGRDYV 408
Cdd:cd14882 232 FEEILKDLDFNEEQLETVRKVLAAILNLGEIRFRQ--NGGYAELENTEIASRVAELLRLDEKKFMWALTNYCLIKGGSAE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 409 QKAQTKEQADFAVEALAKALYERLFRWLVHRINKALDRTKrqgASF-----IGILDIAGFEIFELNSFEQLCINYTNEKL 483
Cdd:cd14882 310 RRKHTTEEARDARDVLASTLYSRLVDWIINRINMKMSFPR---AVFgdkysISIHDMFGFECFHRNRLEQLMVNTLNEQM 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 484 QQLFNHTMFV---LEQEEYQREGIEWNFIDFGLDLQPCIdlierpANPPGVLSLLDEECwfPKATDKSFVEKVIQElgNH 560
Cdd:cd14882 387 QYHYNQRIFIsemLEMEEEDIPTINLRFYDNKTAVDQLM------TKPDGLFYIIDDAS--RSCQDQNYIMDRIKE--KH 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 561 PKFQKPRQlrdKADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDvdrivglDQVSGMgemsfg 640
Cdd:cd14882 457 SQFVKKHS---AHEFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTN-------SQVRNM------ 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 641 ssyKTKKGMFRTVgqlykeSLSKLMSTLRNTNP---NFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPN 717
Cdd:cd14882 521 ---RTLAATFRAT------SLELLKMLSIGANSggtHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSY 591
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 1785379719 718 RIVFQEFRQRYEILTPNAIPKGFMDgKQACAIMIRALELDPnlYRIGQSKIFFR 771
Cdd:cd14882 592 RIPFQEFLRRYQFLAFDFDETVEMT-KDNCRLLLIRLKMEG--WAIGKTKVFLK 642
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
121-255 |
2.91e-59 |
|
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: 201.80 E-value: 2.91e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 121 FCVVINPYKNLPIYTEQIV-EMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTGESGAGKTENTKKVIQYLAHVA 199
Cdd:cd01363 1 VLVRVNPFKELPIYRDSKIiVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1785379719 200 SSHKGRKEHTA-------PGELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGY 255
Cdd:cd01363 81 FNGINKGETEGwvylteiTVTLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEILLDIAGF 143
|
|
| MYSc_Myo24B |
cd14938 |
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
100-769 |
2.62e-55 |
|
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: 207.00 E-value: 2.62e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYR-GKKRHEIPPHIYAISETAYRSMLQDREDQSILCTG 178
Cdd:cd14938 2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKcIDCIEDLSLNEYHVVHNALKNLNELKRNQSIIISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 179 ESGAGKTENTKKVIQYLAHVASSHKGRKEHTAP---------------GELEHQLLQANPILEAFGNAKTVKNDNSSRFG 243
Cdd:cd14938 82 ESGSGKSEIAKNIINFIAYQVKGSRRLPTNLNDqeednihneentdyqFNMSEMLKHVNVVMEAFGNAKTVKNNNSSRFS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 244 KFIRINFDvAGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNGNLPIPGQQDR 323
Cdd:cd14938 162 KFCTIHIE-NEEIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIENYSMLNNEKGFEKFSDYS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 324 EIFQETMESMKIMGFNHEEIMSMLKMVSAVLQFGNI----VFRKE----------------------RNTDQASMPDNTA 377
Cdd:cd14938 241 GKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNTeivkAFRKKsllmgknqcgqninyetilselENSEDIGLDENVK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 378 AQKL-CHLLGLNVTEFSRAILMPRIkVGRDYVQKAQTKEQADFAVEALAKALYERLFRWLVHRINKALDRTKR--QGASF 454
Cdd:cd14938 321 NLLLaCKLLSFDIETFVKYFTTNYI-FNDSILIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEKCTQLQNinINTNY 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 455 IGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANppGVLSL 534
Cdd:cd14938 400 INVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLYNLLVGPTE--GSLFS 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 535 LDEECWFPKATDKS-FVEKVIQELGNHPKF-QKPRQLRDKADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTD 612
Cdd:cd14938 478 LLENVSTKTIFDKSnLHSSIIRKFSRNSKYiKKDDITGNKKTFVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQSEN 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 613 KYTAELWKDVDRIVGLDQVSGMGEMSFGSSYKTKKGMFRTVGQ----LYKESLSKLMSTLRNTNPNFVRCIIPNHEKKA- 687
Cdd:cd14938 558 EYMRQFCMFYNYDNSGNIVEEKRRYSIQSALKLFKRRYDTKNQmavsLLRNNLTELEKLQETTFCHFIVCMKPNESKREl 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 688 GKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPnaipkgfmDGKQACAIMIRALELDPNLYRIGQSK 767
Cdd:cd14938 638 CSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIKNE--------DLKEKVEALIKSYQISNYEWMIGNNM 709
|
..
gi 1785379719 768 IF 769
Cdd:cd14938 710 IF 711
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
861-1713 |
2.00e-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: 2.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 861 LQKVKD------TQVKTESELKEMANKYQQLFEEKSILaeQLQAETELFAEAEEMRARLASKKQELEEILHDLEARVEEE 934
Cdd:TIGR02168 188 LDRLEDilneleRQLKSLERQAEKAERYKELKAELREL--ELALLVLRLEELREELEELQEELKEAEEELEELTAELQEL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 935 EERTLQLQNEKKKMHQHIQDLEEQLEEEEGARQKLQLEKVTTESRLKKMEEDILLLEDQNAKLAKERKLLddrigeftst 1014
Cdd:TIGR02168 266 EEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDEL---------- 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1015 maeeEEKVKSLNKLRNKYEAVIADLEDRLKKEEKGRQEMEKMKRKLDGETTDLQDQLLELQQQIEELKQQLARKEEELQA 1094
Cdd:TIGR02168 336 ----AEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLER 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1095 ALARVDDEVGQKNNLLKQLRDlqSQLAELHEDLESEKAARAKAEKQRRDLGEELEALKTELEdtldstAAQQELRAKREQ 1174
Cdd:TIGR02168 412 LEDRRERLQQEIEELLKKLEE--AELKELQAELEELEEELEELQEELERLEEALEELREELE------EAEQALDAAERE 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1175 evtdlkktiEEDVKVRDAQVTEMRQRHNQVVEEISEQLEQARRFKGNLEKVKQTLESEN--------------TDLIkeV 1240
Cdd:TIGR02168 484 ---------LAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEgyeaaieaalggrlQAVV--V 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1241 KNLQAAKQDSEQRRKKLEQQVSEFQIRTNESEKVKFELAEKLQklqaELDGVSGALGSTEGKSIKLTKDLSTVQSQLQDT 1320
Cdd:TIGR02168 553 ENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILK----NIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVV 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1321 QELLQE-ETRQKLNFSSRVRQLEEEKNNLMENLeeeesakaqlsrqlqalqqqlleSKKRMEDQGGMVEAMEEAKKKSyK 1399
Cdd:TIGR02168 629 DDLDNAlELAKKLRPGYRIVTLDGDLVRPGGVI-----------------------TGGSAKTNSSILERRREIEELE-E 684
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1400 ELEFLQQRFDEKHQINDKLEKTRNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKNISARYGEERDRAEAEAR 1479
Cdd:TIGR02168 685 KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIE 764
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1480 EKETKALSLSRALEEAIDLKDELDRQNKQLRAEMDDLVSSKDDVGKNVHELERSKRALEQQVQEMKTQIEELEDELQAIE 1559
Cdd:TIGR02168 765 ELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLE 844
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1560 DGKLRLEVNMQAMKAQFERDLQNRDDSNDEKKKLLfkqvremeveleeerKQKSQILAAKKKLEMDLQDMESQMDSANKG 1639
Cdd:TIGR02168 845 EQIEELSEDIESLAAEIEELEELIEELESELEALL---------------NERASLEEALALLRSELEELSEELRELESK 909
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1785379719 1640 RDEAVKQLKKLQLQFKEVWREVEETRAARDEIFVQSRDNEK-KLKSLEAELLQLQEDLAAAERAKRQAQQERDDL 1713
Cdd:TIGR02168 910 RSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSlTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
218-712 |
7.08e-26 |
|
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: 116.38 E-value: 7.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 218 LLQANPILEAFGNAKTVKNDNSSRFGKF--IRINFDVAGY---IVGANIETYLLEKSRAIRQA------KDERTFHVFYQ 286
Cdd:cd14894 249 VLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPWefqICGCHISPFLLEKSRVTSERgresgdQNELNFHILYA 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 287 LLAGAGEH-----MKTDLLLEGFN--QYRFLSNGNLPIPG--------QQDREIFQETMESMKIMGFNHEEIMSMLKMVS 351
Cdd:cd14894 329 MVAGVNAFpfmrlLAKELHLDGIDcsALTYLGRSDHKLAGfvskedtwKKDVERWQQVIDGLDELNVSPDEQKTIFKVLS 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 352 AVLQFGNIVFRKERNTDQASMPDN---TAAQKLCHLLGLNVTEFSRAILMPR---IKVGRDYVQKAQTKEQADFAVEALA 425
Cdd:cd14894 409 AVLWLGNIELDYREVSGKLVMSSTgalNAPQKVVELLELGSVEKLERMLMTKsvsLQSTSETFEVTLEKGQVNHVRDTLA 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 426 KALYERLFRWLVHRINKAL-------DRTKRQ---------GASFIGILDIAGFEIFELNSFEQLCINYTNEKLQqlfnh 489
Cdd:cd14894 489 RLLYQLAFNYVVFVMNEATkmsalstDGNKHQmdsnasapeAVSLLKIVDVFGFEDLTHNSLDQLCINYLSEKLY----- 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 490 tmfvleQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLSLLDEECWFPKAT----------DKSFVEKVIQElgN 559
Cdd:cd14894 564 ------AREEQVIAVAYSSRPHLTARDSEKDVLFIYEHPLGVFASLEELTILHQSEnmnaqqeekrNKLFVRNIYDR--N 635
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 560 HPKFQKPRQLRDKAD-----------LCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVDRivgL 628
Cdd:cd14894 636 SSRLPEPPRVLSNAKrhtpvllnvlpFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNSSHFCRMLNESSQ---L 712
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 629 DQVSGMGEMSFGSSYKTKKGMFRTVGQlYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGI 708
Cdd:cd14894 713 GWSPNTNRSMLGSAESRLSGTKSFVGQ-FRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCRSQRLIRQM 791
|
....
gi 1785379719 709 RICR 712
Cdd:cd14894 792 EICR 795
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
968-1719 |
3.37e-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: 108.22 E-value: 3.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 968 KLQLEKVTTESRLKKMEEDILLLEDQNAKLAKERKLLDdrigeftstmaEEEEKVKSLNKLRNKYEAV-IADLEDRLKKE 1046
Cdd:TIGR02168 169 KYKERRKETERKLERTRENLDRLEDILNELERQLKSLE-----------RQAEKAERYKELKAELRELeLALLVLRLEEL 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1047 EKGRQEMEKMKRKLDGETTDLQDQLLELQQQIEELKQQLARKEEELQAALARVDDEVGQKNNLLKQLRDLQSQLAELHED 1126
Cdd:TIGR02168 238 REELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQ 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1127 LESEKAARAKAEKQRRDLGEELEALKTELEDTLDSTAAQQELRAKREQEVTDLKKTIEEDVKVRDAQVTEMRQRHNQvVE 1206
Cdd:TIGR02168 318 LEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ-IA 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1207 EISEQLEQarrfkgnlekvkqtLESENTDLIKEVKNLQAakQDSEQRRKKLEQQVSEFQIRTNESEKVKFELAEKLQKLQ 1286
Cdd:TIGR02168 397 SLNNEIER--------------LEARLERLEDRRERLQQ--EIEELLKKLEEAELKELQAELEELEEELEELQEELERLE 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1287 AELDGVSGALGSTEGKSIKLTKDLSTVQSQLQDTQELLQEetrqKLNFSSRVRQLEEEKNNLMENLEEEES--------A 1358
Cdd:TIGR02168 461 EALEELREELEEAEQALDAAERELAQLQARLDSLERLQEN----LEGFSEGVKALLKNQSGLSGILGVLSElisvdegyE 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1359 KAQLSRQLQALQQQLLESKkrmEDQGGMVEAMEEAK---------------KKSYKELEFLQQRFDEKHQINDkLEKTRN 1423
Cdd:TIGR02168 537 AAIEAALGGRLQAVVVENL---NAAKKAIAFLKQNElgrvtflpldsikgtEIQGNDREILKNIEGFLGVAKD-LVKFDP 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1424 RLQQELDDL-----MVD-----------LDHQRQIVS----------NLEKKQKKFDQMLAEEKNISARYGEERDRAEAE 1477
Cdd:TIGR02168 613 KLRKALSYLlggvlVVDdldnalelakkLRPGYRIVTldgdlvrpggVITGGSAKTNSSILERRREIEELEEKIEELEEK 692
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1478 AREKETKALSLSRALEEAIDLKDELDRQNKQLRAEMDDLVSSKDDVGKNVHELERSKRALEQQVQEMKTQIEELEDELQA 1557
Cdd:TIGR02168 693 IAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEE 772
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1558 IEDGKLRLEVNMQAMKAQFERDLQN-----------RDDSNDEKKKLLFKQVREMEVELEEERKQKS--QILAAKKKLEM 1624
Cdd:TIGR02168 773 AEEELAEAEAEIEELEAQIEQLKEElkalrealdelRAELTLLNEEAANLRERLESLERRIAATERRleDLEEQIEELSE 852
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1625 DLQDMESQMDSANKGRDEAVKQLKKLQLQFKEVWREVEETRAARDEIFVQSRDNEKKLKSLEAELLQLQEDLAAAERAKR 1704
Cdd:TIGR02168 853 DIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLE 932
|
810
....*....|....*
gi 1785379719 1705 QAQQERDDLADELSN 1719
Cdd:TIGR02168 933 GLEVRIDNLQERLSE 947
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
970-1738 |
3.60e-23 |
|
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: 108.23 E-value: 3.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 970 QLEKVTTEsRLKKMEEDILLLEDQNAK---LAKERKLLDDRIGEFTSTMAEEEEKVKSLNKLRNKYEAVIADLEDRLkke 1046
Cdd:TIGR02169 199 QLERLRRE-REKAERYQALLKEKREYEgyeLLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLL--- 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1047 ekgRQEMEKMKRKLDGETTDLQDQLLELQQQIEELKQQLARKEEELQAALARVddevgqkNNLLKQLRDLQSQLAELHED 1126
Cdd:TIGR02169 275 ---EELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERL-------AKLEAEIDKLLAEIEELERE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1127 LESEKAARAKAEKQRRDLGEELEALKTELEDTLDSTAAQQELRAKREQEVTDLKKTIEEDVKVRDAQVTEMRQRHNQVvE 1206
Cdd:TIGR02169 345 IEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEEL-A 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1207 EISEQLEQARrfkgnlEKVKQtLESENTDLIKEVK----NLQAAKQDSEQRRKKLEQQVSEFQIRTNESEKVKFELAEKL 1282
Cdd:TIGR02169 424 DLNAAIAGIE------AKINE-LEEEKEDKALEIKkqewKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAE 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1283 QKLQAELDGVSGALGSTE--GKSIK----LTKDLSTVQSQLQDTQE-----------------------LLQEETRQKLN 1333
Cdd:TIGR02169 497 AQARASEERVRGGRAVEEvlKASIQgvhgTVAQLGSVGERYATAIEvaagnrlnnvvveddavakeaieLLKRRKAGRAT 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1334 FS--SRVRQLEEEKNNLMENLEEEES----------AKAQLSRQLQALQQQLLESKKRMEDQGGMVE----------AME 1391
Cdd:TIGR02169 577 FLplNKMRDERRDLSILSEDGVIGFAvdlvefdpkyEPAFKYVFGDTLVVEDIEAARRLMGKYRMVTlegelfeksgAMT 656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1392 EAKKKSYKELEFLQQRFDEKHQINDKLEKtrnrLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKNISARYGEER 1471
Cdd:TIGR02169 657 GGSRAPRGGILFSRSEPAELQRLRERLEG----LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEE 732
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1472 DRAEAEAREKETKALSLSRALEEAIDLKDELD-------RQNKQLRAEMDDLVSSKDDVGknVHELERSKRALEQQVQEM 1544
Cdd:TIGR02169 733 EKLKERLEELEEDLSSLEQEIENVKSELKELEarieeleEDLHKLEEALNDLEARLSHSR--IPEIQAELSKLEEEVSRI 810
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1545 KTQIEELEDELQAIEDGKLRLEVNMQAMKAQfERDLQNRDDSNDEKKKLLFKQVREMEVELEEERKQKSQILAAKKKLEM 1624
Cdd:TIGR02169 811 EARLREIEQKLNRLTLEKEYLEKEIQELQEQ-RIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKK 889
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1625 DLQDMESQMDSANKGRDEA---VKQLKKLQLQFKEVWREVEETRAARDEIF---VQSRDNEKKLKSLEAELLQLQEDLAA 1698
Cdd:TIGR02169 890 ERDELEAQLRELERKIEELeaqIEKKRKRLSELKAKLEALEEELSEIEDPKgedEEIPEEELSLEDVQAELQRVEEEIRA 969
|
810 820 830 840
....*....|....*....|....*....|....*....|
gi 1785379719 1699 AERAKRQAQQERDDLADELSNGVSGKSALLDEKRALEMRI 1738
Cdd:TIGR02169 970 LEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERI 1009
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1082-1930 |
8.26e-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: 8.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1082 KQQLARKEEELQAALARVDDEVgqkNNLLKQLRDLQSQ------LAELHEDLESEKAARAKAEKQrrDLGEELEALKTEL 1155
Cdd:TIGR02168 174 RKETERKLERTRENLDRLEDIL---NELERQLKSLERQaekaerYKELKAELRELELALLVLRLE--ELREELEELQEEL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1156 EDTLDSTAAQQELRAKREQEVTDLKKTIEEDvkvrDAQVTEMRQRHNQVVEEISEQLEQARRFKGNLEKVKQTLESENTD 1235
Cdd:TIGR02168 249 KEAEEELEELTAELQELEEKLEELRLEVSEL----EEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQ 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1236 LIKEVKNLQAAKQDSEQRRKKLEQ---QVSEFQIRTNESEKVKFELAEKLQKLQAELDGVSGALGSTEGKSIKLTKDLST 1312
Cdd:TIGR02168 325 LEELESKLDELAEELAELEEKLEElkeELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIER 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1313 VQSQLQDTQELLQeetrqklNFSSRVRQLEEEKNNLMENLEEEESAkaqlsrqlqalqqqllESKKRMEDQGGMVEAMEE 1392
Cdd:TIGR02168 405 LEARLERLEDRRE-------RLQQEIEELLKKLEEAELKELQAELE----------------ELEEELEELQEELERLEE 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1393 AkkksykeLEFLQQRFDEKHQINDKLEKTRNRLQQELDDLmvdldhqRQIVSNLEKKQKKFDQMLAEEKNISARYGEERD 1472
Cdd:TIGR02168 462 A-------LEELREELEEAEQALDAAERELAQLQARLDSL-------ERLQENLEGFSEGVKALLKNQSGLSGILGVLSE 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1473 RAEAEAReketkalsLSRALEEAidlkdeldrqnkqLRAEMDDLV-SSKDDVGKNVHELERS---KRALEQQVQEMKTQI 1548
Cdd:TIGR02168 528 LISVDEG--------YEAAIEAA-------------LGGRLQAVVvENLNAAKKAIAFLKQNelgRVTFLPLDSIKGTEI 586
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1549 EELEDELQAIEDGKLRLEVNMQAMKAQFERDLQNR----------DDSNDEKKKLLFKQV---------REMEVELEEER 1609
Cdd:TIGR02168 587 QGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLlggvlvvddlDNALELAKKLRPGYRivtldgdlvRPGGVITGGSA 666
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1610 KQKSQILAAK---KKLEMDLQDMESQMDSANKGRDEAVKQLKKLQLQFKEVWREVEETRAARDEIFVQSRDNEKKLKSLE 1686
Cdd:TIGR02168 667 KTNSSILERRreiEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE 746
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1687 AELLQLQEDLAAAERAKRQAQQERDDLADELSNGVSGKSALLDEKRALEMRISQLEEELDEEQSNTELINDRYRKLTLQV 1766
Cdd:TIGR02168 747 ERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERL 826
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1767 ETITTELSAERsfsQKAENARQQMERQNKELkvklnemdstmrSKYKITIASLEAKISQLEEQMEQESKERIIANKLVRR 1846
Cdd:TIGR02168 827 ESLERRIAATE---RRLEDLEEQIEELSEDI------------ESLAAEIEELEELIEELESELEALLNERASLEEALAL 891
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1847 AEKRLKEVLLQVEEERRNADQFKEQLEKANIRMKQLKRQLeeaEEEASRANSNRRRLQRELEDVTESAESMNREVTTLRS 1926
Cdd:TIGR02168 892 LRSELEELSEELRELESKRSELRRELEELREKLAQLELRL---EGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEE 968
|
....
gi 1785379719 1927 RLRR 1930
Cdd:TIGR02168 969 EARR 972
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1112-1881 |
6.25e-20 |
|
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: 97.50 E-value: 6.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1112 QLRDLQSQLAELHEdlesekaaraKAEKQRRDLGEELEALKTELEDTLDSTAAQQELRAKREQEVTDLKKTIEEDVKVRD 1191
Cdd:pfam15921 86 QVKDLQRRLNESNE----------LHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1192 AQvtemRQRHNQVVEEISEQLEQARRFKGNLEKVKQTLESENTDLiKEVKNLQAAKQDS-------------EQRRKKLE 1258
Cdd:pfam15921 156 AA----KCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDF-EEASGKKIYEHDSmstmhfrslgsaiSKILRELD 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1259 QQVSEFQIRT----NESEKVKFELAEKLQKL-QAELDGVSGALGSTEGKSIKLTKDLSTVQSQ---LQDTQELLQEETRQ 1330
Cdd:pfam15921 231 TEISYLKGRIfpveDQLEALKSESQNKIELLlQQHQDRIEQLISEHEVEITGLTEKASSARSQansIQSQLEIIQEQARN 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1331 KlnFSSRVRQLEEeknnlmenleeeesakaqLSRQLQALQQQLLESKKRMEDQggmVEAMEeakkksyKELEFLQQRFDE 1410
Cdd:pfam15921 311 Q--NSMYMRQLSD------------------LESTVSQLRSELREAKRMYEDK---IEELE-------KQLVLANSELTE 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1411 KHQINDKLEKTRNRLQQELDDLMVDLdHQRQIVSNLEKKQKK--FDQMLAEEKNIsarygeERDRAEAEAREKETKALsl 1488
Cdd:pfam15921 361 ARTERDQFSQESGNLDDQLQKLLADL-HKREKELSLEKEQNKrlWDRDTGNSITI------DHLRRELDDRNMEVQRL-- 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1489 sRALEEAidLKDELDRQNKQLRAEMDDLVSSKDDVGKNVHELERSKRALEQQVQEMKTQIEELEDELQAIEDGKLRLEVN 1568
Cdd:pfam15921 432 -EALLKA--MKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEK 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1569 MQAMKAQFER--DLQNRDDSNDEKKKLLFKQVREMEVELEEERKQKSQILAAKKKLEMDLQDMESQMDSANK-GRDEAVK 1645
Cdd:pfam15921 509 ERAIEATNAEitKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQhGRTAGAM 588
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1646 QLKKLQLQfKEV---WREVEETRAARDEIFVQSRDNEKKLKSLEAELLQLQEDLAAAERAKRQAQQERDDLADELSNGVS 1722
Cdd:pfam15921 589 QVEKAQLE-KEIndrRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRN 667
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1723 GKSALLDEKRALEMRISQLeeeldeeqsnTELINDRYRKLTLQVETITTELSAERSFSQKAENArqqmerQNKELKVKLN 1802
Cdd:pfam15921 668 ELNSLSEDYEVLKRNFRNK----------SEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGS------DGHAMKVAMG 731
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1785379719 1803 eMDSTMRSKyKITIASLEAKISQLEEQMEQESKERiianKLVRRAEKRLKEVLLQVEEERRNADQFKEQLEKANIRMKQ 1881
Cdd:pfam15921 732 -MQKQITAK-RGQIDALQSKIQFLEEAMTNANKEK----HFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKE 804
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
998-1822 |
6.46e-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: 97.45 E-value: 6.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 998 AKERKLLDDRI---GEFTSTMAEEEEKVKSLNKLRNKYEAVIADLEDRLKKEEKGRQEMEKM------------------ 1056
Cdd:TIGR02169 152 PVERRKIIDEIagvAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYqallkekreyegyellke 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1057 KRKLDGETTDLQDQLLELQQQIEELKQQLARKEEELQAALARVDDEV--------GQKNNLLKQLRDLQSQLAELhEDLE 1128
Cdd:TIGR02169 232 KEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNkkikdlgeEEQLRVKEKIGELEAEIASL-ERSI 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1129 SEKAARAK-AEKQRRDLGEELEALKTELEDTLDSTAAQQELRAKREQEVTDLKKTIEE---DVKVRDAQVTEMRQRHNQV 1204
Cdd:TIGR02169 311 AEKERELEdAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDlraELEEVDKEFAETRDELKDY 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1205 VEEIseqlEQARRFKGNLEKVKQTLESENTDLIKEVKNLQAAKQDSEQRRKKLEQQVSEFQIRTNESEKVKFELAEKLQK 1284
Cdd:TIGR02169 391 REKL----EKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSK 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1285 LQAELDGVSGALGSTEGKSIKLTKDLSTVQSQLQDTQELLQEETRQKLNFSSR-------VRQLEEEKNNLMENLEEEES 1357
Cdd:TIGR02169 467 YEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASiqgvhgtVAQLGSVGERYATAIEVAAG 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1358 AKAQLSRqlqalqqqlleskkrMEDQGGMVEAMEEAKKKSYKELEFLQQRfdekhQINDK-LEKTRNRLQQELDDLM--V 1434
Cdd:TIGR02169 547 NRLNNVV---------------VEDDAVAKEAIELLKRRKAGRATFLPLN-----KMRDErRDLSILSEDGVIGFAVdlV 606
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1435 DLDHQRQ-----------IVSNLEKKQKKFDQ--MLAEEKNISARYG------EERDRAEAEAREKETKALSLSRALEEA 1495
Cdd:TIGR02169 607 EFDPKYEpafkyvfgdtlVVEDIEAARRLMGKyrMVTLEGELFEKSGamtggsRAPRGGILFSRSEPAELQRLRERLEGL 686
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1496 IDLKDELDRQNKQLRAEMDDLVSSKDDVGKNVHELERSKRALEQQVQEMKTQIEELEDELQAIEDGKLRLEVNMQ---AM 1572
Cdd:TIGR02169 687 KRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKeleAR 766
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1573 KAQFERDLQN-RDDSNDEKKKLLFKQVREMEVELEEERKQKSQILAAKKKLEMDLQDMESQMDSANKGRDEAVKQLKKLQ 1651
Cdd:TIGR02169 767 IEELEEDLHKlEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLK 846
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1652 LQFKEVWREVEETRAARDEIFVQSRDNEKKLKSLEAELLQLQEDLAAAERAKRQAQQERDDLADELSNGVSGKSALLDEK 1731
Cdd:TIGR02169 847 EQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKL 926
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1732 RALEMRISQLEEELDEEQSNTELINDrYRKLTLQVETITTELSAERSFSQKAENARQQMERQNKELKVKLNEMdSTMRSK 1811
Cdd:TIGR02169 927 EALEEELSEIEDPKGEDEEIPEEELS-LEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKL-EEERKA 1004
|
890
....*....|.
gi 1785379719 1812 YKITIASLEAK 1822
Cdd:TIGR02169 1005 ILERIEEYEKK 1015
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
855-1560 |
2.47e-19 |
|
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: 95.51 E-value: 2.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 855 QAKVVELQKVKDTQVKTESELKEMANKYQQLFEEKSILAEQLQAETELFAEAEEMRARLASKKQELEEILHDLEARVEEE 934
Cdd:TIGR02168 305 QILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETL 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 935 EERTLQLQNEKKKMHQHIQDLEEQLEEEEGARQKLQLEKVTTESRLKKMEedillLEDQNAKLAKERKLLDDRIGEFTST 1014
Cdd:TIGR02168 385 RSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE-----LKELQAELEELEEELEELQEELERL 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1015 MAEEEEKVKSLNKLRNKYEAVIADLEdrlkkEEKGRQEM-EKMKRKLDGETTDLQDQLLELQQQIEELKQ--QLARKEEE 1091
Cdd:TIGR02168 460 EEALEELREELEEAEQALDAAERELA-----QLQARLDSlERLQENLEGFSEGVKALLKNQSGLSGILGVlsELISVDEG 534
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1092 LQAALARV------------DDEVGQKNNLLKQLRDLQSQLAEL----HEDLESEKAARAKAEKQRRDLGEELEALKTEL 1155
Cdd:TIGR02168 535 YEAAIEAAlggrlqavvvenLNAAKKAIAFLKQNELGRVTFLPLdsikGTEIQGNDREILKNIEGFLGVAKDLVKFDPKL 614
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1156 E-------------DTLDSTAAQQELRAKREQEVTDLKKTIEED------VKVRDAQVTEMRQRHNQVVEEISEQLEQAR 1216
Cdd:TIGR02168 615 RkalsyllggvlvvDDLDNALELAKKLRPGYRIVTLDGDLVRPGgvitggSAKTNSSILERRREIEELEEKIEELEEKIA 694
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1217 rfkgNLEKVKQTLESENTDLIKEVKNLQAAKQDSEQRRKKLEQQVSEFQIRTNESEKVKFELAEKLQKLQAELDGVSGAL 1296
Cdd:TIGR02168 695 ----ELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERL 770
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1297 GSTEGKSIKLTKDLSTVQSQLQDTQELLQEETRQKLNFSSRVRQLEEEKNNLMENLEEEESAKAQLSRQLQALQQQLLES 1376
Cdd:TIGR02168 771 EEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEEL 850
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1377 KKRMEDQGGMVEAMEEAKKKSYKELEFLQQRFDEkhqindkLEKTRNRLQQELDDLMVDLDhqrqivsNLEKKQKKFDQM 1456
Cdd:TIGR02168 851 SEDIESLAAEIEELEELIEELESELEALLNERAS-------LEEALALLRSELEELSEELR-------ELESKRSELRRE 916
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1457 LAEEKNISARYGEERDRAEAEAREKETKALSL-SRALEEAIDLKDELDRQNKQLRAEMDDLVSSKDDVGkNVHEL-ERSK 1534
Cdd:TIGR02168 917 LEELREKLAQLELRLEGLEVRIDNLQERLSEEySLTLEEAEALENKIEDDEEEARRRLKRLENKIKELG-PVNLAaIEEY 995
|
730 740
....*....|....*....|....*.
gi 1785379719 1535 RALEQQVQEMKTQIEELEDELQAIED 1560
Cdd:TIGR02168 996 EELKERYDFLTAQKEDLTEAKETLEE 1021
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
897-1516 |
4.05e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 94.62 E-value: 4.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 897 QAET-----ELFAEAEEMRARLASKK-QELEEILHDLEARVEEEEERTLQLQNEKKKMHQHIQDLEEQLEEEEGARQKLQ 970
Cdd:COG1196 208 QAEKaeryrELKEELKELEAELLLLKlRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 971 LEKVTTESRLKKMEEDILLLEDQNAKLAKERKLLDDRIGEFTSTMAEEEEKVKSLNKLRNKYEAVIADLEDRLKKEEKGR 1050
Cdd:COG1196 288 AEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1051 QEMEKMKRKLDGETTDLQDQLLELQQQIEELKQQLARKEEELQAALARVDDEVGQKNNLLKQLRDLQSQLAELHEDLESE 1130
Cdd:COG1196 368 LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEA 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1131 KAARAKAEKQRRDLGEELEALKTELEDTLDSTAAQQELRAKREQEVtDLKKTIEEDVKVRDAQVTEMRQRHNQvvEEISE 1210
Cdd:COG1196 448 AEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARL-LLLLEAEADYEGFLEGVKAALLLAGL--RGLAG 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1211 QLEQARRFKGNLEKVKQTLESENTDLIkEVKNLQAAKQDSEQRRKKLEQQVSEFQIRTNESEKVKFELAEKLQKLQAELD 1290
Cdd:COG1196 525 AVAVLIGVEAAYEAALEAALAAALQNI-VVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDL 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1291 GVSgalgstegksikLTKDLSTVQSQLQDTQELLQEETRQKLNFSSRVRQLEEEKNNLMENLEEEESAKAQLSRQLQALQ 1370
Cdd:COG1196 604 VAS------------DLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELL 671
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1371 QQLLESKKRMEDQggmveamEEAKKKSYKELEFLQQRFDEKHQINDKLEKTRNRLQQELDDLMVDLDHQRQIVSNLEkkq 1450
Cdd:COG1196 672 AALLEAEAELEEL-------AERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEEL--- 741
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1785379719 1451 kkFDQMLAEEKNISARYGEERDRAEAEAREKETKAlSLSR-------ALEEAIDLK---DELDRQNKQLRAEMDDL 1516
Cdd:COG1196 742 --LEEEELLEEEALEELPEPPDLEELERELERLER-EIEAlgpvnllAIEEYEELEeryDFLSEQREDLEEARETL 814
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
867-1719 |
4.20e-19 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 95.21 E-value: 4.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 867 TQVKTESELKEMANKYQQLFEEKSILAEQLQAETELFAEA---EEMRARLASKKQE----LEEILHDLEARVEEEEERTL 939
Cdd:PTZ00121 1064 AHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAkktETGKAEEARKAEEakkkAEDARKAEEARKAEDARKAE 1143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 940 QLQNEKKKMHQHIQDLEEQLEEEEGARQKLQLEKVTTESRLKKMEEDILLLEDQNAKLAKERKllddrigeftstMAEEE 1019
Cdd:PTZ00121 1144 EARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAAR------------KAEEE 1211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1020 EKVKSLNKLRN--KYEAVIADLEDRLKKEEKGRQEMEkmkRKLDGETTDLQDQLLELQQQIEELKQQLARKEEELQAALA 1097
Cdd:PTZ00121 1212 RKAEEARKAEDakKAEAVKKAEEAKKDAEEAKKAEEE---RNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEE 1288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1098 RVDDEVGQKNNLLKQLRDLQSQLAELHEDLESEKAARAKAEKQRRDLGEELEALKTELEDTLDSTAAQQELRAKREQEVT 1177
Cdd:PTZ00121 1289 KKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEA 1368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1178 DLKKTIEEDVKVRDA-QVTEMRQRHNQVVEEISEQLEQARRFKGNLEKVKQTLESENTdlIKEVKNLQAAKQDSEQRRKK 1256
Cdd:PTZ00121 1369 AEKKKEEAKKKADAAkKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKK--AEEKKKADEAKKKAEEAKKA 1446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1257 LEQQVSEFQIRTNESEKVKFELAEKLQKL--QAELDGVSGALGSTEGKSIKLTKDLSTVQSQLQDTQELLQEETRQKlnf 1334
Cdd:PTZ00121 1447 DEAKKKAEEAKKAEEAKKKAEEAKKADEAkkKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKK--- 1523
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1335 SSRVRQLEE----EKNNLMENLEEEESAKAQLSRQLQALQQQLLESKKRMEDQGGMVEAMEEAKKKSYKELEFLQQRFDE 1410
Cdd:PTZ00121 1524 ADEAKKAEEakkaDEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEE 1603
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1411 KHQINDKLEKTRNRLQQELDDLMVDLDHQR---QIVSNLEKKQKKFDQMLAEEKNISARYGEERDRAEAEAREKET--KA 1485
Cdd:PTZ00121 1604 EKKMKAEEAKKAEEAKIKAEELKKAEEEKKkveQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEakKA 1683
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1486 LSLSRALEEAIDLKDELDRQNKQLRAEMDDLVSSKDDVGKNVHELERSKRALEQQVQEMKTQIEEL---EDELQAIEDGK 1562
Cdd:PTZ00121 1684 EEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAkkdEEEKKKIAHLK 1763
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1563 LRLEVNMQAMKAQFERDLQNRDDSNDEKKKLLFKQVREMEVELEEERKQ--KSQILAAKKKLEMDLQDMESQMDSANKGR 1640
Cdd:PTZ00121 1764 KEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEggKEGNLVINDSKEMEDSAIKEVADSKNMQL 1843
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1785379719 1641 DEAvkqlkklqlqfkevwREVEETRAARDEIFVQSRDNEKKLKSleaELLQLQEDLAAAERAKRQAQQERDDLADELSN 1719
Cdd:PTZ00121 1844 EEA---------------DAFEKHKFNKNNENGEDGNKEADFNK---EKDLKEDDEEEIEEADEIEKIDKDDIEREIPN 1904
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
860-1433 |
1.78e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 89.23 E-value: 1.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 860 ELQKVKDTQVKTESELKEMANKYQQLFEEKSILAEQLQAETELFAEAEEMRARLASKKQELEEILHDLEARVEEEEERTL 939
Cdd:COG1196 240 ELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 940 QLQNEKKKMHQHIQDLEEQLEEEEGARQKLQLEKVTTESRLKKMEEDILLLEDQNAKLAKERKLLDDRIGEFTSTMAEEE 1019
Cdd:COG1196 320 ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELA 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1020 EKVKSLNKLRNKYEAVIADLEDRLKKEEKGRQEMEKMKRKLDGETTDLQDQLLELQQQIEELKQQLARKEEELQAALARV 1099
Cdd:COG1196 400 AQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAAL 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1100 DDEVGQKNNLLKQLRDLQSQLAELHEDLESEKAARAKAEKQRRDLGEELEALKTELEDTLDSTAAQQELRAKREQEVTDL 1179
Cdd:COG1196 480 AELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVA 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1180 KKTIEEDVKVRDAQVT-----EMRQRHNQVVEEISEQLEQARRFkgnLEKVKQTLESENTDLIKEVKNLQAAKQDSEQRR 1254
Cdd:COG1196 560 AAAIEYLKAAKAGRATflpldKIRARAALAAALARGAIGAAVDL---VASDLREADARYYVLGDTLLGRTLVAARLEAAL 636
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1255 KKLEQQVSEFQIRTNESEKVKFELAEKLQKLQAELDGVSGALGSTEGKSIKLTKDLSTVQSQLQDTQELLQEETRQKLNF 1334
Cdd:COG1196 637 RRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEER 716
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1335 SSRVRQLEEEKNNLMENLEEEESAKAQLSRQLQALQQQLLESKKRMEDQGGMVEAMEEAKKK-------SYKELEFLQQR 1407
Cdd:COG1196 717 LEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAlgpvnllAIEEYEELEER 796
|
570 580 590
....*....|....*....|....*....|
gi 1785379719 1408 FDE-KHQINDkLEKTRNRLQQ---ELDDLM 1433
Cdd:COG1196 797 YDFlSEQRED-LEEARETLEEaieEIDRET 825
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
844-1555 |
2.60e-17 |
|
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: 88.97 E-value: 2.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 844 LLQVTRQDEVMQAKVVElqkvKDTQVKTESELKEMANKYQQLFEEK-----SILAEQLQAeteLFAEAEEMRARLASKKQ 918
Cdd:TIGR02169 179 LEEVEENIERLDLIIDE----KRQQLERLRREREKAERYQALLKEKreyegYELLKEKEA---LERQKEAIERQLASLEE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 919 ELEEI---LHDLEARVEEEEERTLQLQNEKKKMHQHIQdleeqleeeegARQKLQLEKVTTEsrLKKMEEDILLLEDQNA 995
Cdd:TIGR02169 252 ELEKLteeISELEKRLEEIEQLLEELNKKIKDLGEEEQ-----------LRVKEKIGELEAE--IASLERSIAEKERELE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 996 KLAKERKLLDDRIGEFTSTMAEEEEKVKSLNKLRNKYEAVIADLEDRL-----------KKEEKGRQEMEKMKRKLDgET 1064
Cdd:TIGR02169 319 DAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELedlraeleevdKEFAETRDELKDYREKLE-KL 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1065 TDLQDQLLELQQQIEELKQQLARKEEELQAALARVDDevgQKNNLLKQLRDLQSQLAELHEDLESEKAARAKAEKQRRDL 1144
Cdd:TIGR02169 398 KREINELKRELDRLQEELQRLSEELADLNAAIAGIEA---KINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDL 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1145 GEELEALKTELE------DTLDSTAAQQELRAKREQEVTDLKKTIEEDVKVRDAQVTEMRQRH-------------NQVV 1205
Cdd:TIGR02169 475 KEEYDRVEKELSklqrelAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYataievaagnrlnNVVV 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1206 EEIS---EQLEQARRFKGN------LEKVKQtlESENTDLIKE------------------------------VKNLQAA 1246
Cdd:TIGR02169 555 EDDAvakEAIELLKRRKAGratflpLNKMRD--ERRDLSILSEdgvigfavdlvefdpkyepafkyvfgdtlvVEDIEAA 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1247 K-QDSEQRRKKLEQQVSEFQ-------IRTNESEKVKFELAEKLQKLQAELDGVSGALGStegksikLTKDLSTVQSQLQ 1318
Cdd:TIGR02169 633 RrLMGKYRMVTLEGELFEKSgamtggsRAPRGGILFSRSEPAELQRLRERLEGLKRELSS-------LQSELRRIENRLD 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1319 DTQELLQEETRQKLNFSSRVRQLEEEKNNLMENLEEEESAKAQLSRQLQALQQQLLESKKRMEDQGGMVEAMEEAKKKSY 1398
Cdd:TIGR02169 706 ELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLE 785
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1399 KELefLQQRFDEKHQINDKLEKTRNRLQQELDDLMVDLdhqrqivsnlekKQKKFDQMLAEEKnisaRYGEERDRAEAEA 1478
Cdd:TIGR02169 786 ARL--SHSRIPEIQAELSKLEEEVSRIEARLREIEQKL------------NRLTLEKEYLEKE----IQELQEQRIDLKE 847
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1785379719 1479 REKETKalslsRALEEAIDLKDELDRQNKQLRAEMDDLVSSKDDVGKNVHELERSKRALEQQVQEMKTQIEELEDEL 1555
Cdd:TIGR02169 848 QIKSIE-----KEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRL 919
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1087-1583 |
4.46e-17 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 87.79 E-value: 4.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1087 RKEEELQAALARVDDEVGQKN--NLLKQLRDLQSQLAELHEDLESEKAARAKAEKQRRDLG----------EELEALKTE 1154
Cdd:PRK02224 180 RVLSDQRGSLDQLKAQIEEKEekDLHERLNGLESELAELDEEIERYEEQREQARETRDEADevleeheerrEELETLEAE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1155 LEDTLDSTAAQQELRAKREQEVTDLKKTIEE-----------------DVKVRDAQVTEMRQRHNQVVEEISEQLEQARR 1217
Cdd:PRK02224 260 IEDLRETIAETEREREELAEEVRDLRERLEEleeerddllaeaglddaDAEAVEARREELEDRDEELRDRLEECRVAAQA 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1218 FKGNLEKVKQ---TLESENTDLIKEVKNLQAAKQDSEQRRKKLEQQVSEFQIRTNESEKVKFELAEKLQKLQAELDGVSG 1294
Cdd:PRK02224 340 HNEEAESLREdadDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELRE 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1295 ALGSTEGKSIKLTKDLSTVQSQLQDTQELLQE----ETRQKLNFSSRVRQLEEEKNNLMENLEEEESAKAQLSRQLQA-- 1368
Cdd:PRK02224 420 ERDELREREAELEATLRTARERVEEAEALLEAgkcpECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERle 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1369 LQQQLLESKKRMEDQGGMVEAMEEAKKKSYKELEFLQQRFDEKHQINDKLEKTRNRLQQELDDLMVDLDHQRQIVSNLEK 1448
Cdd:PRK02224 500 RAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNS 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1449 KQKKFDQ----------MLAEEKNISARYGEERDRAEAEAREKETKALSLSRALEEAIDLKDELDRQN-KQLRAEMDDLV 1517
Cdd:PRK02224 580 KLAELKErieslerirtLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEARiEEAREDKERAE 659
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1785379719 1518 SSKDDVGKNVHELERSKRALEQQVQEMKTQIEELE---DELQAIEDGKLRLEV------NMQAMKAQFERDLQNR 1583
Cdd:PRK02224 660 EYLEQVEEKLDELREERDDLQAEIGAVENELEELEelrERREALENRVEALEAlydeaeELESMYGDLRAELRQR 734
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1184-1909 |
2.34e-16 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 85.89 E-value: 2.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1184 EEDVKVRDA-----QVTEMRQRHNQVVEEISEQLEQARRFKGNLEKVKQTL----ESENTDLIKEVKNLQAAKQDSEQRR 1254
Cdd:TIGR02169 167 EFDRKKEKAleeleEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLkekrEYEGYELLKEKEALERQKEAIERQL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1255 KKLEQQVSEFQIRTNESEKVKFELAEKLQKLQAELDGVsgalgsTEGKSIKLTKDLSTVQSQLQDTQELLQEETRQKLNF 1334
Cdd:TIGR02169 247 ASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDL------GEEEQLRVKEKIGELEAEIASLERSIAEKERELEDA 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1335 SSRVRQLEEEKNNLMENLEEEESAKAQLSRQLQALQQQLLESKKRMEDQGGMVEAMEEAKKKSYKELEFLQQRFDE-KHQ 1413
Cdd:TIGR02169 321 EERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKlKRE 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1414 INDkLEKTRNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDqmlaeeknisarygEERDRAEAEAREKETKalslsraLE 1493
Cdd:TIGR02169 401 INE-LKRELDRLQEELQRLSEELADLNAAIAGIEAKINELE--------------EEKEDKALEIKKQEWK-------LE 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1494 EAIDLKDELDRQNKQLRAEMDDLVSSKDDVGKNVHELERSKRALEQQVQEMKTQIEELEDELQAI-----------EDGK 1562
Cdd:TIGR02169 459 QLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVhgtvaqlgsvgERYA 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1563 LRLEV--------------------------------------NMQAMKA------------------QFERDLQN---- 1582
Cdd:TIGR02169 539 TAIEVaagnrlnnvvveddavakeaiellkrrkagratflplnKMRDERRdlsilsedgvigfavdlvEFDPKYEPafky 618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1583 --RD----DSNDEKKKL------------LFKQVREMEVELEEERKQKSQILAAKKKLEM---DLQDMESQMDSANKGRD 1641
Cdd:TIGR02169 619 vfGDtlvvEDIEAARRLmgkyrmvtlegeLFEKSGAMTGGSRAPRGGILFSRSEPAELQRlreRLEGLKRELSSLQSELR 698
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1642 EAVKQLKKLQLQFKEVWREVEETRAARDEIfvqsrdnEKKLKSLEAELLQLQEDLAAAERAKRQAQQERDDLADELSNGV 1721
Cdd:TIGR02169 699 RIENRLDELSQELSDASRKIGEIEKEIEQL-------EQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELE 771
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1722 SGKSALLDEKRALEMRISQLEEELDEEQSNTelINDRYRKLTLQVETITTELSAERSFSQKAENARQQMERQNKELKVKL 1801
Cdd:TIGR02169 772 EDLHKLEEALNDLEARLSHSRIPEIQAELSK--LEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQI 849
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1802 N------EMDSTMRSKYKITIASLEAKISQLEEQMEQESKERIIANKLVRRAEKRLKEVLLQVEEERRNADQFKEQLEKA 1875
Cdd:TIGR02169 850 KsiekeiENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEAL 929
|
810 820 830 840
....*....|....*....|....*....|....*....|
gi 1785379719 1876 NIRMKQLKRQLEEAEEEASRANS------NRRRLQRELED 1909
Cdd:TIGR02169 930 EEELSEIEDPKGEDEEIPEEELSledvqaELQRVEEEIRA 969
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
999-1871 |
3.83e-16 |
|
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: 85.02 E-value: 3.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 999 KERKLLDDRIGEFTSTMAEEE------EKVKSLNKLRNKYEAVIADLEDRLKKEEKGRQEMEKMKRKLDGETTDLQDQLL 1072
Cdd:pfam02463 153 ERRLEIEEEAAGSRLKRKKKEalkkliEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1073 ELQQQIEELKQQLARKEEELQAALARVDDEVGQKNNLLKQLRDLQSQLAELHEDLESEKAARAKAEKQRRDLGEELEALK 1152
Cdd:pfam02463 233 KLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDD 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1153 TELEDTLDSTAAQQELRAKREQEVTDLKKTIEEDVKVRdaqvtemRQRHNQVVEEISEQLEQARRFKGNLEKvKQTLESE 1232
Cdd:pfam02463 313 EEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIK-------REAEEEEEEELEKLQEKLEQLEEELLA-KKKLESE 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1233 NTDLIKEVKNLQAAKQDSEQRRKKLEQQVSE-----FQIRTNESEKVKFELAEKLQKLQAELDGVSGALGSTEGKSIKLT 1307
Cdd:pfam02463 385 RLSSAAKLKEEELELKSEEEKEAQLLLELARqledlLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDE 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1308 KDLSTVQSQLQDTQELLQEETRQKLNFSS---RVRQLEEEKNNLMENLEEEESAKAQLSRQLQALQQQLLESKKRMEDQG 1384
Cdd:pfam02463 465 LELKKSEDLLKETQLVKLQEQLELLLSRQkleERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVA 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1385 GMVEAMEEAKKKSyKELEFLQQRFDEKHQINDKLEKTRNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKNIS 1464
Cdd:pfam02463 545 ISTAVIVEVSATA-DEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAK 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1465 ARYGEERDRAEAEAREKETKALSLSRA---LEEAIDLKDELDRQNKQLRAEMDDLVSSKDDVGKNVHELERSKRALEQQV 1541
Cdd:pfam02463 624 VVEGILKDTELTKLKESAKAKESGLRKgvsLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKK 703
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1542 QEMKTQIEELEDELQAIEDGKLRLEVNMQAMKAQFERDLQNRDDSNDEKKKLLFKQVREMEVELEEERKQKSQIL-AAKK 1620
Cdd:pfam02463 704 KEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEeREKT 783
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1621 KLEMDLQDMESQMDSANKGRDEAVKQLKKLQLQFKEVWREVEETRAARDEIFVQSRDNEKKL----KSLEAELLQLQEDL 1696
Cdd:pfam02463 784 EKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEqkleKLAEEELERLEEEI 863
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1697 AAAERAKRQAQQERDDLADELSNGVSGKSALLDEKRALEMRISQLEEELDEEQSNTELINDRYRKLTLQVETITTELSAE 1776
Cdd:pfam02463 864 TKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLE 943
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1777 RSFSQKAENARQQMERQNKELKVKLNEMDSTMRSKYKITIASLEAKISQLEEQMEQESKERIIANKLVRRAEKRLKEVLL 1856
Cdd:pfam02463 944 EADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFL 1023
|
890
....*....|....*
gi 1785379719 1857 QVEEERRNADQFKEQ 1871
Cdd:pfam02463 1024 ELFVSINKGWNKVFF 1038
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
857-1665 |
1.04e-15 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 84.04 E-value: 1.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 857 KVVELQKVKDTQVKTESELKEMANKYQQLFEEKSILAEQLQAETELFAEAEEMR-----ARLASKKQELEEILHDLEARV 931
Cdd:PTZ00121 1183 KAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKkdaeeAKKAEEERNNEEIRKFEEARM 1262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 932 EEEEERTLQLQNEKKKMHQHIQDleeqleeeegARQKLQLEKVTTESRLKKMEEdiLLLEDQNAKLAKERKllddrigef 1011
Cdd:PTZ00121 1263 AHFARRQAAIKAEEARKADELKK----------AEEKKKADEAKKAEEKKKADE--AKKKAEEAKKADEAK--------- 1321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1012 tstmAEEEEKVKSLNKLRNKYEAVIADLEDRLKKEEKGRQEMEKMKRKLDGEttdlqdqllelqqqieELKQQLARKEEE 1091
Cdd:PTZ00121 1322 ----KKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAA----------------EKKKEEAKKKAD 1381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1092 lqaALARVDDEVGQKNNLLKQLRDLQSQLAELHEDLESEKAA---RAKAEKQRRdlgeeLEALKTELEDTLDSTAAQQEL 1168
Cdd:PTZ00121 1382 ---AAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKAdeaKKKAEEKKK-----ADEAKKKAEEAKKADEAKKKA 1453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1169 RAKREQEvtDLKKTIEEDVKVRDAQVTEMRQRH----NQVVEEISEQLEQARRFKGNLEKVKQTLESENTDLIKEVKNLQ 1244
Cdd:PTZ00121 1454 EEAKKAE--EAKKKAEEAKKADEAKKKAEEAKKadeaKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAE 1531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1245 AAKQDSEQRR----KKLEQQVSEFQIRTNEsEKVKFELAEKLQKLQAELDGVSGALGSTEGKSIKLTKDLSTVQSQLQDT 1320
Cdd:PTZ00121 1532 EAKKADEAKKaeekKKADELKKAEELKKAE-EKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAE 1610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1321 QELLQEETRQKlnfSSRVRQLEEEKNNLMENLEEEESAKAQLSRQLQALQQQL---LESKKRMEDQGGMVEAMEEAKKKS 1397
Cdd:PTZ00121 1611 EAKKAEEAKIK---AEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKikaAEEAKKAEEDKKKAEEAKKAEEDE 1687
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1398 YKELEFLQQRFDEKHqindKLEKTRNRLQQELD--DLMVDLDHQRQIVSNLEKKQKKFDQMLAEEknisARYGEERDRAE 1475
Cdd:PTZ00121 1688 KKAAEALKKEAEEAK----KAEELKKKEAEEKKkaEELKKAEEENKIKAEEAKKEAEEDKKKAEE----AKKDEEEKKKI 1759
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1476 AEAREKETKALSLSRALEEAIdLKDELDRQNKQLRAEMDDLVSSKDDVGKNVHELERSKRALEQQVQEMktqieELEDEL 1555
Cdd:PTZ00121 1760 AHLKKEEEKKAEEIRKEKEAV-IEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEM-----EDSAIK 1833
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1556 QAIEDGKLRLEVNMQAMKAQFERDLQNRDDSNDEKKkllfkqvreMEVELEEERKQKSQILAAKKKLEMDLQDMESQMDS 1635
Cdd:PTZ00121 1834 EVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEAD---------FNKEKDLKEDDEEEIEEADEIEKIDKDDIEREIPN 1904
|
810 820 830
....*....|....*....|....*....|.
gi 1785379719 1636 AN-KGRDEAVKQLKKLQLQFKEvwREVEETR 1665
Cdd:PTZ00121 1905 NNmAGKNNDIIDDKLDKDEYIK--RDAEETR 1933
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
870-1674 |
2.46e-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: 82.42 E-value: 2.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 870 KTESELKEMANKYQQLFEEKSILAEQLQAETELFAEAEEMRARLASKKQELEEILHDLEARVEEE-EERTLQLQNEKKKM 948
Cdd:TIGR02169 220 KREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGEL 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 949 H--------------QHIQDLEEQleeeegaRQKLQLEKVTTESRLKKMEEDIlllEDQNAKLAKerkllddrigeftsT 1014
Cdd:TIGR02169 300 EaeiaslersiaekeRELEDAEER-------LAKLEAEIDKLLAEIEELEREI---EEERKRRDK--------------L 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1015 MAEEEEKVKSLNKLRNKYEAVIADLEDRLKKEEKGRQEMEKMKRKLDgettdlqdQLLELQQQIEELKQQLARKEEELQA 1094
Cdd:TIGR02169 356 TEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREIN--------ELKRELDRLQEELQRLSEELADLNA 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1095 ALARVDDevgQKNNLLKQLRDLQSQLAELHEDLESEKAARAKAEKQRRDLGEELEALKTELEDtldstaAQQELRAKREQ 1174
Cdd:TIGR02169 428 AIAGIEA---KINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSK------LQRELAEAEAQ 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1175 evtdlKKTIEEDVKVRDAQVTEMRQRHNQVVEEISEQLEQARRFKGNLEKV-----------KQTLESENTDLIKEVKN- 1242
Cdd:TIGR02169 499 -----ARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEVAagnrlnnvvveDDAVAKEAIELLKRRKAg 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1243 ------LQAAKQDSEQRRKKLEQQVSEFQIRTNESEKvKFELAeklqklqaeldgVSGALGST-------EGKSIKLTKD 1309
Cdd:TIGR02169 574 ratflpLNKMRDERRDLSILSEDGVIGFAVDLVEFDP-KYEPA------------FKYVFGDTlvvedieAARRLMGKYR 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1310 LSTVQSQLQDTQELLQEETRQKLNFSSRVRQLEEEKNNLMENLEEEESAKAQLSRQLQALQQQLLESKKRMEDQGGMVEA 1389
Cdd:TIGR02169 641 MVTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGE 720
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1390 MEEAKKKSYKELEFLQQRFDEKHQINDKLEKTRNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKniSARYGE 1469
Cdd:TIGR02169 721 IEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSR--IPEIQA 798
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1470 ERDRAEAEAREKETKALSLSRALEEAIDLKDELDRQNKQLRAEMDDLVSSKDDVGKNVHELERSKRALEQQVQEMKTQIE 1549
Cdd:TIGR02169 799 ELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALR 878
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1550 ELEDELQAIEDGKLRLEVNMQAMKAQFERDLQNRDDSNDEKKKLLFKQVREMEVELEEERKQKS------------QILA 1617
Cdd:TIGR02169 879 DLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEdeeipeeelsleDVQA 958
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1785379719 1618 AKKKLEMDLQDMES-------QMDSANKGRDEAVKQLKKLQLQFKEVWREVEETRAARDEIFVQ 1674
Cdd:TIGR02169 959 ELQRVEEEIRALEPvnmlaiqEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREVFME 1022
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1211-1882 |
6.89e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 80.75 E-value: 6.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1211 QLEQARRfkgNLEKVkqtlesenTDLIKEVknlqaakqdsEQRRKKLEQQVSE----FQIRTNESEKVKFELAEKLQKLQ 1286
Cdd:COG1196 180 KLEATEE---NLERL--------EDILGEL----------ERQLEPLERQAEKaeryRELKEELKELEAELLLLKLRELE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1287 AELDGVSGALGSTEGKSIKLTKDLSTVQSQLQDTQELLQEETRQKLNFSSRVRQLEEEKNNLMENLEEEESAKAQLSRQL 1366
Cdd:COG1196 239 AELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1367 QALQQQLLESKKRMEDQGGMVEAMEEAKKKSYKELEFLQQRFDEKHQINDKLEKTRNRLQQELDDLMVDLDHQRQIVSNL 1446
Cdd:COG1196 319 EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1447 EKKQKKFDQMLAEEKNISARYGEERDRAEAEAREKETKALSLSRALEEAIDLKDELDRQNKQLRAEMDDLVSSKDDVGKN 1526
Cdd:COG1196 399 AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1527 VHELErskRALEQQVQEMKTQIEELEDELQAIEDGKLRLEVNMQAMKAQFERDLQnRDDSNDEKKKLLFKQVREMEVELE 1606
Cdd:COG1196 479 LAELL---EELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLI-GVEAAYEAALEAALAAALQNIVVE 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1607 EERKQKSQILAAKKK---------LEMDLQDMESQMDSANKGRDEAVKQLKKLQLQFKEVWREVEETRAARDEIFVQSRD 1677
Cdd:COG1196 555 DDEVAAAAIEYLKAAkagratflpLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEA 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1678 NEKKLKSLEAELLQLQEDLAAAERAKRQAQQERDDLADELsngvsgksaLLDEKRALEMRISQLEEELDEEQSNTELIND 1757
Cdd:COG1196 635 ALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAAL---------LEAEAELEELAERLAEEELELEEALLAEEEE 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1758 RYRKLTLQVETITTELSAERSFSQKAENARQQMERQNKELKVKLNEMDSTMRSKYKitIASLEAKISQLEEQME------ 1831
Cdd:COG1196 706 ERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPD--LEELERELERLEREIEalgpvn 783
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1785379719 1832 -------QESKERI--IANKL--VRRAEKRLKEVLLQVEEERRnaDQFKEQLEKANIRMKQL 1882
Cdd:COG1196 784 llaieeyEELEERYdfLSEQRedLEEARETLEEAIEEIDRETR--ERFLETFDAVNENFQEL 843
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
872-1473 |
1.17e-13 |
|
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: 77.08 E-value: 1.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 872 ESELKEMANKYQQLFEEKSILAEQLQAETE-----LFAEAEEMRARLASKKQELEEILHdlearveeeeertlQLQNEKK 946
Cdd:pfam15921 248 EALKSESQNKIELLLQQHQDRIEQLISEHEveitgLTEKASSARSQANSIQSQLEIIQE--------------QARNQNS 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 947 KMHQHIQDLEEQLEEEegaRQKLQLEKVTTESRLKKMEEDILLLEDQNAKLAKERKL-------LDDRIGEFTSTMAEEE 1019
Cdd:pfam15921 314 MYMRQLSDLESTVSQL---RSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQfsqesgnLDDQLQKLLADLHKRE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1020 EKVkSLNKLRNKyeaviadledRLKKEEKGRQ-EMEKMKRKLDGETTDLQDQLLELQQQIEELKQQLARKeeelQAALAR 1098
Cdd:pfam15921 391 KEL-SLEKEQNK----------RLWDRDTGNSiTIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQ----MAAIQG 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1099 VDDEVGQKNNLLKQLRDLQSQLAELHEDLESEKAARAKAEKQRRDLGEELEalktELEDTLDSTAAQ-QELRAKREQEVT 1177
Cdd:pfam15921 456 KNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQ----EKERAIEATNAEiTKLRSRVDLKLQ 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1178 DLKKTIEEDVKVRDAQVT------EMRQRhNQVVEEISEQLE-------QARRFKGNLEKVKQTLESENTDLIKEVKNLQ 1244
Cdd:pfam15921 532 ELQHLKNEGDHLRNVQTEcealklQMAEK-DKVIEILRQQIEnmtqlvgQHGRTAGAMQVEKAQLEKEINDRRLELQEFK 610
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1245 AAKQDSEQRRKKLEQQVSEFQIrtnesEKVKF-----ELAEKLQKLQAELDGVSGALGSTEGKSIKLTKDLSTVQSQLQD 1319
Cdd:pfam15921 611 ILKDKKDAKIRELEARVSDLEL-----EKVKLvnagsERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRN 685
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1320 TQELLqEETRQKLNFSSRVRQLEEEKNNLMENLEEEESAKAQLSRQLQALQQQLLesKKRMEDQGGMVEAMEEAKKKSYK 1399
Cdd:pfam15921 686 KSEEM-ETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAK--RGQIDALQSKIQFLEEAMTNANK 762
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1785379719 1400 ELEFLQQRFDEKHQINDKLEKTRNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKNISARYGEERDR 1473
Cdd:pfam15921 763 EKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVR 836
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
847-1716 |
1.36e-13 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 76.55 E-value: 1.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 847 VTRQDEVMQAKVVELQKVKDTQVKTESELKEMANKYQQLFEEKSILAEQLQAETELFAEAEEMRArlASKKQELEEILHD 926
Cdd:pfam02463 164 GSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLY--LDYLKLNEERIDL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 927 LEARveeeeertLQLQNEKKKMHQHIQDLEEQLEEEEGARQKLQLEKVttesrlKKMEEDILLLEDQNAKLAKERKLLDD 1006
Cdd:pfam02463 242 LQEL--------LRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEK------KLQEEELKLLAKEEEELKSELLKLER 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1007 RIGEFTSTMAEEEEKVKSLNKLRNKYEAVIADLEDRLKKEEKGRQEMEKMKrkldgettdlqdqllelqqqieelKQQLA 1086
Cdd:pfam02463 308 RKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEE------------------------EELEK 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1087 RKEEELQAALARVDDEVGQKNNLLKQLRDLQSQLAELHEDLESEKAARAKAEKQRRDLGEELEALKTELEDTLDSTAAQQ 1166
Cdd:pfam02463 364 LQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQ 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1167 ELRAKREQEVTDLKKTIEEDvKVRDAQVTEMRQRHNQVVEEISEQLEQARRFKGNLEKVKQTLESENTDLIKEVKNLQAA 1246
Cdd:pfam02463 444 GKLTEEKEELEKQELKLLKD-ELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGG 522
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1247 KQDSEQRRKKLEQQVSEFQIRTNESEKVKFELAEKLQKLQAELDGVSGALGSTEGKSIKLTKDLstVQSQLQDTQELLQE 1326
Cdd:pfam02463 523 RIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPK--LKLPLKSIAVLEID 600
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1327 ETRQKLNFSSRVRQLEEEKNNLMENLEEEESAKAQLSRQLQALQQQLLESKKRMEDQGGMVEAMEEAKKKSYKELEFLQQ 1406
Cdd:pfam02463 601 PILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQE 680
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1407 RFDEKHQINDKLEKTRNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKNISARYGEERDRAEAEA----REKE 1482
Cdd:pfam02463 681 LQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEeksrLKKE 760
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1483 TKALSLSRALEEAIDLKDELDRQNKQLRAEMDDLVSSKDDVGKNVHELERSKRALEQQVQEMKTQIEELEDELQAIEDGK 1562
Cdd:pfam02463 761 EKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELAL 840
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1563 LRLEVNMQAMKAQFErdlQNRDDSNDEKKKLLFKQVREMEVELEEERKQKSQILAAKKKLEMDLQDMESQMDSANKGRDE 1642
Cdd:pfam02463 841 ELKEEQKLEKLAEEE---LERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKEN 917
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1785379719 1643 AVKQLKKLQLQFKEVWREVEETRAARDEIFVQSRDNEKKLKSLEAELLQLQEDLAAAERAKRQAQQERDDLADE 1716
Cdd:pfam02463 918 EIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYN 991
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1125-1876 |
1.60e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 76.72 E-value: 1.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1125 EDLESEKAARAKAEKQRRdlGEELEALKtELEDTLDSTAAQQELRAKREQEVTDLKKtIEEDVKVRDAQVTEMRQRHNQV 1204
Cdd:PTZ00121 1112 EEARKAEEAKKKAEDARK--AEEARKAE-DARKAEEARKAEDAKRVEIARKAEDARK-AEEARKAEDAKKAEAARKAEEV 1187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1205 VE-------EISEQLEQARRFKgNLEKVKQTLESENTDLIKEVKNLQAAKQDSEQRRKKLEQQVSEFQIRTNESEKVKFE 1277
Cdd:PTZ00121 1188 RKaeelrkaEDARKAEAARKAE-EERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFA 1266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1278 LAEKLQKLQA--ELDGVSGALGSTEGKSIKLTKDLSTVQSQLQDTQELLQEETRQKlnfssrvrQLEEEKNNLMENLEEE 1355
Cdd:PTZ00121 1267 RRQAAIKAEEarKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKK--------KAEEAKKKADAAKKKA 1338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1356 ESAKAQLSRQLQALQQQLLESKKRMEDQGGMVEAMEEAKKKSykelEFLQQRFDEKHQInDKLEKTRNRLQQELDDLMVD 1435
Cdd:PTZ00121 1339 EEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKA----DAAKKKAEEKKKA-DEAKKKAEEDKKKADELKKA 1413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1436 LDHQRQIVSNLEKKQKKFDQMLAEEKNISARYGEERDRAEAEAR---------EKETKALSLSRALEEAIDlKDELDRQN 1506
Cdd:PTZ00121 1414 AAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKkaeeakkkaEEAKKADEAKKKAEEAKK-ADEAKKKA 1492
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1507 KQLRAEMDDLvSSKDDVGKNVHEL---ERSKRALEQQVQEMKTQIEELE--------DELQAIEDGKLRLEVNMQAMKAQ 1575
Cdd:PTZ00121 1493 EEAKKKADEA-KKAAEAKKKADEAkkaEEAKKADEAKKAEEAKKADEAKkaeekkkaDELKKAEELKKAEEKKKAEEAKK 1571
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1576 FERDLQNRDDSNDEKKKLLFKQVREMEVELEEERKQKSQilAAKKKLEMDLQDMESqmdsanKGRDEAVKQLKKLQLQFK 1655
Cdd:PTZ00121 1572 AEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAE--EAKKAEEAKIKAEEL------KKAEEEKKKVEQLKKKEA 1643
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1656 EVWREVEETRAARDEIFVQSRDNEKKlkslEAELLQLQEDLAAAERAKRQAQQERDDLADELSNGVSGKSALLDEKR-AL 1734
Cdd:PTZ00121 1644 EEKKKAEELKKAEEENKIKAAEEAKK----AEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKkAE 1719
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1735 EMRISQLEEELDEEQSNTELINDRYRKLTLQVEtitTELSAERSFSQKAENARQQMERQNKELKVK--LNEMDSTMRSKY 1812
Cdd:PTZ00121 1720 ELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKD---EEEKKKIAHLKKEEEKKAEEIRKEKEAVIEeeLDEEDEKRRMEV 1796
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1785379719 1813 KITIASLEakiSQLEEQMEQESKERIIANKLVRRAEKRLKEVLLQVEEERRNADQFKEQLEKAN 1876
Cdd:PTZ00121 1797 DKKIKDIF---DNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKN 1857
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
905-1550 |
2.63e-13 |
|
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: 75.44 E-value: 2.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 905 EAEEMRARLASKKQEL---EEILHDLEARVEEEEERTLQLQNEKKKMHQHIQDLEEQLEEEEGARQKLQLEKVTTESRLK 981
Cdd:TIGR04523 34 EEKQLEKKLKTIKNELknkEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 982 KMEEDILLLEDQNAKLAKERKLLDDRIGEFTSTMAEEEEKVKSLNKLRNKYEAVIADLEDRLKKEEKGRQEMEKMKRKLD 1061
Cdd:TIGR04523 114 NDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIK 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1062 GETTDLQDQLLELQQQIEELKqQLARKEEELQAALARVDDEVGQKNnllKQLRDLQSQLAELHEDLESEKAARAKAEKQR 1141
Cdd:TIGR04523 194 NKLLKLELLLSNLKKKIQKNK-SLESQISELKKQNNQLKDNIEKKQ---QEINEKTTEISNTQTQLNQLKDEQNKIKKQL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1142 RDLGEELEALKTELEDTLDS-TAAQQELRAKREQEVTDLKKTIEEDVKVRDAQVTEMRQR---HNQVVEEISEQLEQARR 1217
Cdd:TIGR04523 270 SEKQKELEQNNKKIKELEKQlNQLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQisqNNKIISQLNEQISQLKK 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1218 FKGNLEKVKQTLESENTDLIKEVKNLQAAKQDSEQRRKKLEQQVSEFQIRTNESEKVKFELAEKLQKLQAELDGVSgalg 1297
Cdd:TIGR04523 350 ELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLE---- 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1298 stegKSIKLTKdlSTVQSQLQDTQELLQEETRQKLNFSSRVRQLEEEKNNLMENLEEEESAKaqlsrqlqalqQQLLESK 1377
Cdd:TIGR04523 426 ----KEIERLK--ETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIK-----------QNLEQKQ 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1378 KRMEDQGGMVEAMEEAKKKSYKELEFLQQRFDEKHQINDKLEKTRNRLQQELDDLMVDL--DHQRQIVSNLEKKQKKFDQ 1455
Cdd:TIGR04523 489 KELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELnkDDFELKKENLEKEIDEKNK 568
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1456 MLAEEKNISARYGEERDRAEAEAREKETKALSLSRALEEAIDLKDELDRQNKQLRAEMDDLVSSKDDvgknvheLERSKR 1535
Cdd:TIGR04523 569 EIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKN-------IKSKKN 641
|
650
....*....|....*
gi 1785379719 1536 ALEQQVQEMKTQIEE 1550
Cdd:TIGR04523 642 KLKQEVKQIKETIKE 656
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
828-1526 |
5.65e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 74.79 E-value: 5.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 828 KLRHWQWWRLFTKVKPLLQVTRQDEVMQAKVVELQKVKDTQVKTESELKEMANKYQQLFEEKSILAEQLQAEtELFAEAE 907
Cdd:PTZ00121 1247 EERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKAD-EAKKKAE 1325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 908 EMRARLASKKQELEEILHDLEARVEEEEERTLQLQNEKKKMHQHIQDLEEQLEEEEGARQKLQlEKVTTESRLKKMEEDI 987
Cdd:PTZ00121 1326 EAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAE-EKKKADEAKKKAEEDK 1404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 988 LLLEDQNAKLAKERKllddriGEFTSTMAEEEEKVKSLNKlrnkyEAVIADLEDRLKKEEKGRQEMEKMKRKLDgettdl 1067
Cdd:PTZ00121 1405 KKADELKKAAAAKKK------ADEAKKKAEEKKKADEAKK-----KAEEAKKADEAKKKAEEAKKAEEAKKKAE------ 1467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1068 qdqlLELQQQIEELKQQLARKEEELQaalaRVDDEVGQKNNLLKQLRDLQSQLAELHEDLESEKAARAKAEKQRRdlgEE 1147
Cdd:PTZ00121 1468 ----EAKKADEAKKKAEEAKKADEAK----KKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAK---KA 1536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1148 LEALKTELEDTLDSTAAQQELRAKREQEVTDLKKTIEEDVKVRDAQVTEMRQRHNQVVEEI-----------SEQLEQAR 1216
Cdd:PTZ00121 1537 DEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVmklyeeekkmkAEEAKKAE 1616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1217 RFKGNLEKVKQTLESENTDLIKEVKNLQAAKQDSEQRRKKLEQQVSEFQIRTNESEKVKfeLAEKLQKLQAELDGVSGAL 1296
Cdd:PTZ00121 1617 EAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKK--KAEEAKKAEEDEKKAAEAL 1694
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1297 GSTEGKSIKLTKDLSTVQSQLQDTQELLQEETRQKLNFSSRVRQLEEEKNNLMEnleeeesAKAQLSRQLQALQQQLLES 1376
Cdd:PTZ00121 1695 KKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEE-------AKKDEEEKKKIAHLKKEEE 1767
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1377 KKRMEDQGGMVEAMEEAKKKsykelEFLQQRFDEKHQINDKLEKTRNRLQQELDDLMVDLDHQRQIVSNLeKKQKKFDQM 1456
Cdd:PTZ00121 1768 KKAEEIRKEKEAVIEEELDE-----EDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAI-KEVADSKNM 1841
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1457 LAEEKNISARYGEERDRAEAEAREKETKALSLSRALEEAIDLKDELDRQNKQLRAEMDDLVSSKDDVGKN 1526
Cdd:PTZ00121 1842 QLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDKDDIEREIPNNNMAGKN 1911
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
849-1555 |
8.75e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 73.94 E-value: 8.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 849 RQDEVmqAKVVELQKVKDTQVKTESELKEMANKYQQLFEEKSILAEQLQAETELFAEAEEMRARLASKKQELEEILHdle 928
Cdd:PRK03918 133 RQGEI--DAILESDESREKVVRQILGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLR--- 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 929 aRVEEEEERTLQLQNEKKKMHQHIQDLEEQLEEEEgarqKLQLEKVTTESRLKKMEEDILLLEDQNAKLAKERKLLddri 1008
Cdd:PRK03918 208 -EINEISSELPELREELEKLEKEVKELEELKEEIE----ELEKELESLEGSKRKLEEKIRELEERIEELKKEIEEL---- 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1009 geftstmaeeEEKVKSLNKLRNK---YEAVIADLEDRLKKEEKGRQEMEKMKRKLDGettdlQDQLLELQQQIEELKQQL 1085
Cdd:PRK03918 279 ----------EEKVKELKELKEKaeeYIKLSEFYEEYLDELREIEKRLSRLEEEING-----IEERIKELEEKEERLEEL 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1086 ARKEEELQAALARVDDEVgqknNLLKQLRDLQSQLAELHEDLESEKAARAKAEKqrrdlgEELEALKTELEDTLDSTAAQ 1165
Cdd:PRK03918 344 KKKLKELEKRLEELEERH----ELYEEAKAKKEELERLKKRLTGLTPEKLEKEL------EELEKAKEEIEEEISKITAR 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1166 qelRAKREQEVTDLKKTIEEDVKVRD------AQVTEmrqrhnqvvEEISEQLEQARRFKGNLEKVKQTLESENTDLIKE 1239
Cdd:PRK03918 414 ---IGELKKEIKELKKAIEELKKAKGkcpvcgRELTE---------EHRKELLEEYTAELKRIEKELKEIEEKERKLRKE 481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1240 VKNLQaaKQDSEQRRKKLEQQVSEfQIRTNESEKVKFELaEKLQKLQAELDGVsgalgstEGKSIKLTKDLSTVQSQLQD 1319
Cdd:PRK03918 482 LRELE--KVLKKESELIKLKELAE-QLKELEEKLKKYNL-EELEKKAEEYEKL-------KEKLIKLKGEIKSLKKELEK 550
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1320 TQELLQEetrqKLNFSSRVRQLEEEKnnlmenleeeesakaqlsrqlqalqqqlLESKKRMEDQGgmVEAMEEAKKKsYK 1399
Cdd:PRK03918 551 LEELKKK----LAELEKKLDELEEEL----------------------------AELLKELEELG--FESVEELEER-LK 595
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1400 ELEFLQQRFDEKHQINDKLEKTRNRLQQELDDLmvdldhqRQIVSNLEKKQKKFDQMLAEEKNISARYGEErdraeaEAR 1479
Cdd:PRK03918 596 ELEPFYNEYLELKDAEKELEREEKELKKLEEEL-------DKAFEELAETEKRLEELRKELEELEKKYSEE------EYE 662
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1785379719 1480 EKETKALSLSRALEEAIDLKDELDRQNKQLRAEMDDLVSSKDDVGKNVHELERSKRALEqQVQEMKTQIEELEDEL 1555
Cdd:PRK03918 663 ELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALE-RVEELREKVKKYKALL 737
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
870-1428 |
1.30e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 73.17 E-value: 1.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 870 KTESELKEMANKYQQLFEEKSILAEQLQAETELFAEAEEMRARLASKKQELEEilhdLEARVEEEEERTLQLQNEKKKMH 949
Cdd:PRK03918 204 EVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRK----LEEKIRELEERIEELKKEIEELE 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 950 QHIQDLEEQLeeeegarqklqlEKVTTESRLKKMEEDILlleDQNAKLAKERKLLDDRIGEFTSTMAEEEEKVKSLNKLR 1029
Cdd:PRK03918 280 EKVKELKELK------------EKAEEYIKLSEFYEEYL---DELREIEKRLSRLEEEINGIEERIKELEEKEERLEELK 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1030 NKYEAV---IADLEDRLKKEEKGRQEMEKMKRKLDGETTDLQDQLLELQQQIEELKQQLARKEEELQAALARVDDEVGQK 1106
Cdd:PRK03918 345 KKLKELekrLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKEL 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1107 NNLLKQLRDLQS-------QLAELHED--LESEKAARAKAEKQRRDLGEELEALKTELEDTLDSTAAQQELRakREQEVT 1177
Cdd:PRK03918 425 KKAIEELKKAKGkcpvcgrELTEEHRKelLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELI--KLKELA 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1178 DLKKTIEEDVKVRDAQVTEmrqrhnQVVEEISEQLEQARRFKGNLEKVKQTLESENtDLIKEVKNLQAAKQDSEQRRKKL 1257
Cdd:PRK03918 503 EQLKELEEKLKKYNLEELE------KKAEEYEKLKEKLIKLKGEIKSLKKELEKLE-ELKKKLAELEKKLDELEEELAEL 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1258 EQQVSEFQIRTNESEKVKFELAEKLQKLQAELDGVSGALGSTEGKSIKLTKDLSTVQSQLQDTQELLqEETRQKLNfSSR 1337
Cdd:PRK03918 576 LKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRL-EELRKELE-ELE 653
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1338 VRQLEEEKNNLMENLEEEESAKAQLSRQLQALQQQLLESKKRMEDqggmVEAMEEAKKKSYKELEFLQQRFDEKHQINDK 1417
Cdd:PRK03918 654 KKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEK----LKEELEEREKAKKELEKLEKALERVEELREK 729
|
570
....*....|.
gi 1785379719 1418 LEKTRNRLQQE 1428
Cdd:PRK03918 730 VKKYKALLKER 740
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1172-1885 |
1.64e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 73.25 E-value: 1.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1172 REQEVTDLKKTIEEDVKV-RDAQVTEMRQRHNQVVEEISEQLEQARRFKGNLEKVKQTLESENTDL--IKEVKNLQAAKQ 1248
Cdd:PTZ00121 1043 KEKDIIDEDIDGNHEGKAeAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETgkAEEARKAEEAKK 1122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1249 DSEQRRKKLEQQVSEFQIRTNESEKVKFELAEKLQKLQAELDGVSGALGSTEGKSIKLTKDLSTVQ--SQLQDTQELLQE 1326
Cdd:PTZ00121 1123 KAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRkaEELRKAEDARKA 1202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1327 ETRQKlnfSSRVRQLEEEKNNlmenleeeesakaqlsrqlqalqqqllESKKRMEDqggmVEAMEEAKKKSYKEleflqq 1406
Cdd:PTZ00121 1203 EAARK---AEEERKAEEARKA---------------------------EDAKKAEA----VKKAEEAKKDAEEA------ 1242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1407 rfdekhqinDKLEKTRNRLQ-QELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKNIS--ARYGEERDRAEAEAR--EK 1481
Cdd:PTZ00121 1243 ---------KKAEEERNNEEiRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAdeAKKAEEKKKADEAKKkaEE 1313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1482 ETKALSLSRALEEAIDLKDELDRQNKQLRAEMDDLVSSKDDVGKNVHELERSKRALEQQVQEMKTQIEELE---DELQAI 1558
Cdd:PTZ00121 1314 AKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKkkaEEKKKA 1393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1559 EDGKLRLEVNMQamKAQFERDLQNRDDSNDEKKKLLFKQVREMEVELEEERKQKSQilAAKKKLEMDLQDMESQMDSANK 1638
Cdd:PTZ00121 1394 DEAKKKAEEDKK--KADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKAD--EAKKKAEEAKKAEEAKKKAEEA 1469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1639 GRDEAVKQLKKLQLQFKEVWREVEETRAARDEIFVQSRDNEKKLKSLEAELLQLQEDLAAAERAK-----RQAQQERDdl 1713
Cdd:PTZ00121 1470 KKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKkadeaKKAEEKKK-- 1547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1714 ADELSNGVSGKSA-----LLDEKRALEMRISQLEEELDEEQSNTELINDRYRKLTLQVETITTELSAERSFSQKAENARQ 1788
Cdd:PTZ00121 1548 ADELKKAEELKKAeekkkAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKK 1627
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1789 QMERQNKELKVKLNEMDSTMRSK--------YKITIASLEAKISQ----LEEQMEQESKERIIANKLVRRAE--KRLKEV 1854
Cdd:PTZ00121 1628 AEEEKKKVEQLKKKEAEEKKKAEelkkaeeeNKIKAAEEAKKAEEdkkkAEEAKKAEEDEKKAAEALKKEAEeaKKAEEL 1707
|
730 740 750
....*....|....*....|....*....|.
gi 1785379719 1855 LLQVEEERRNADQFKEQLEKANIRMKQLKRQ 1885
Cdd:PTZ00121 1708 KKKEAEEKKKAEELKKAEEENKIKAEEAKKE 1738
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
860-1534 |
3.24e-12 |
|
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: 72.06 E-value: 3.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 860 ELQKVKDTQVKTESELKEMANKYQqlfEEKSILAEQLQAETELFAEAEEMRARLASKKQELEEILHD----------LEA 929
Cdd:pfam05483 86 EAEKIKKWKVSIEAELKQKENKLQ---ENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKEnnatrhlcnlLKE 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 930 RVEEEEERTLQLQNEKKKMHQHIQDLEEQLEEEEGARQKLQLEkvTTESRLK---KMEEDILLLEDQNAKLAKERKLLDD 1006
Cdd:pfam05483 163 TCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQ--AENARLEmhfKLKEDHEKIQHLEEEYKKEINDKEK 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1007 RIGEFTSTMAEEEEKVKSLNKLRNKYEAVIADLEDRLKKEEKGRQEMEKMKRKLDGETTDLQDQLLELQQQIEELkqqla 1086
Cdd:pfam05483 241 QVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKAL----- 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1087 rkEEELQAALARVDDEVGQKNNLLKQLR-----------DLQSQLAELHEDLESEKAARAKAEKQRRDLGEELEALKTEL 1155
Cdd:pfam05483 316 --EEDLQIATKTICQLTEEKEAQMEELNkakaahsfvvtEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSEL 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1156 EDtldstaaQQELRAKREQEVTDLKKTIEEDVKVRD--AQVTEMRQRHNQVVEEISEQLEQARRFKGNLEKVKQTLESEN 1233
Cdd:pfam05483 394 EE-------MTKFKNNKEVELEELKKILAEDEKLLDekKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSE 466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1234 TDLIKEVKNLQAAKQDSEQRRKKLEQQVSEFQIRTNESEKVKFELAEKLQKLQAELDGVSgalgSTEGKSIKLTKDLSTV 1313
Cdd:pfam05483 467 EHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCK----KQEERMLKQIENLEEK 542
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1314 QSQLQDTQELLQEETRQKLN-FSSRVRQLEEEKNNLMENLEEEESAKAQLSRQLQALQQQLLESKKRMEDQGGMVEAMEE 1392
Cdd:pfam05483 543 EMNLRDELESVREEFIQKGDeVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKK 622
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1393 AKKKSYKELEFLQQRFD----EKHQINDKLEKTRNRLQQELDD-------LMVDLDHQRQIVSNLEKKQKKFDQ------ 1455
Cdd:pfam05483 623 KGSAENKQLNAYEIKVNklelELASAKQKFEEIIDNYQKEIEDkkiseekLLEEVEKAKAIADEAVKLQKEIDKrcqhki 702
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1456 -----MLAEEKNISARYGEERDRAEAEAREKETKALSLSRALE-EAIDLKDELDRQNKQLRAEMDDLVSSKDDVGKNVHE 1529
Cdd:pfam05483 703 aemvaLMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEiELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAI 782
|
....*
gi 1785379719 1530 LERSK 1534
Cdd:pfam05483 783 LKDKK 787
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
892-1229 |
4.59e-12 |
|
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: 71.63 E-value: 4.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 892 LAEQLQAETELFAEAEEMRARLASKKQELEEILHDLEARVEEEEERTLQLQNEKKKMHQHIQDLEEQLEEEEGARQKLQL 971
Cdd:TIGR02168 682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEA 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 972 EKVTTESRLKKMEEDILLLEDQNAKLAKERKLLDDRIGEFTSTMAEEEEKVKSLNKLRNKYEAVIADLEDRLKKEEKGRQ 1051
Cdd:TIGR02168 762 EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLE 841
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1052 EMEKMKRK-------LDGETTDLQDQLLELQQQIEELKQQLARKEEELQAALARVDDEVGQKNNLLKQLRDLQSQLAELH 1124
Cdd:TIGR02168 842 DLEEQIEElsediesLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELR 921
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1125 EDLESEKAARAKAEKQRRDLGEEL-EALKTELEDTLDSTAAQQELRAKREQEVTDLKKTIE-------------EDVKVR 1190
Cdd:TIGR02168 922 EKLAQLELRLEGLEVRIDNLQERLsEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKelgpvnlaaieeyEELKER 1001
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1785379719 1191 -------DAQVTEMRQRHNQVVEEISEQLEQarRFKGNLEKVKQTL 1229
Cdd:TIGR02168 1002 ydfltaqKEDLTEAKETLEEAIEEIDREARE--RFKDTFDQVNENF 1045
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
998-1532 |
6.20e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 71.22 E-value: 6.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 998 AKERKLLDDRIGEFTSTMAEEEEKVKSLNKLRNKYEAVIADLEDRLKKEEKGRQEMEKMK---RKLDGETTDLQDQLLEL 1074
Cdd:PRK02224 198 EKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEaeiEDLRETIAETEREREEL 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1075 QQQIEELKQQLARKEEELQAALARVDDEVGQKNNLLKQLRDLQSQLAELHEDLE----SEKAARAKAEKQRRD------- 1143
Cdd:PRK02224 278 AEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEecrvAAQAHNEEAESLREDaddleer 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1144 ---LGEELEALKTELEDTLDSTAAQQELRAKREQEVTDLKKTIE------EDVKVRDAQVTEMRQRHNQVVEEISEQLEQ 1214
Cdd:PRK02224 358 aeeLREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGdapvdlGNAEDFLEELREERDELREREAELEATLRT 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1215 ARrfkGNLEKVKQTLES----ENTDLIKEVKNLQAAkQDSEQRRKKLEQQVSEFQIRTNESEKvKFELAEKLQKLQAELD 1290
Cdd:PRK02224 438 AR---ERVEEAEALLEAgkcpECGQPVEGSPHVETI-EEDRERVEELEAELEDLEEEVEEVEE-RLERAEDLVEAEDRIE 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1291 gvsgalgstegksiKLTKDLSTVQSQLQDTQELLQEETRQKLNFSSRVRQLEEEKNNLMENLEEEESAKAQLSRQLQALQ 1370
Cdd:PRK02224 513 --------------RLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELN 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1371 QQLLESKKRMEDQGGMVEAMEEAKKKSyKELEFLQQRFDEKHQIND----KLEKTRNR---LQQELDDLMVDLDHQR--Q 1441
Cdd:PRK02224 579 SKLAELKERIESLERIRTLLAAIADAE-DEIERLREKREALAELNDerreRLAEKRERkreLEAEFDEARIEEAREDkeR 657
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1442 IVSNLEKKQKKFDQMLAEEKNISARYGE-ERDRAEAEAREKETKALSLSR-ALEEAIDLKDELDRQNKQLRAEMDDlvss 1519
Cdd:PRK02224 658 AEEYLEQVEEKLDELREERDDLQAEIGAvENELEELEELRERREALENRVeALEALYDEAEELESMYGDLRAELRQ---- 733
|
570
....*....|...
gi 1785379719 1520 kddvgKNVHELER 1532
Cdd:PRK02224 734 -----RNVETLER 741
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
850-1151 |
6.27e-12 |
|
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: 71.24 E-value: 6.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 850 QDEVMQAKVVELQKVKDTQvktESELKEMANKYQQLFEEKSILAEQLQAETELFAEAEEMRARLASKKQELEEILHDLEA 929
Cdd:TIGR02168 706 ELEELEEELEQLRKELEEL---SRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEA 782
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 930 RVEEEEERTLQLQNEKKKMHQHIQDLEEQLEEEEGARQKLQLEKVTTESRLKKMEEDILLLEDQNAKLAKERKLLDDRIG 1009
Cdd:TIGR02168 783 EIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIE 862
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1010 EFTSTMAEEEEKVKSLNKLRNKYEAVIADLEDRLKKEEKGRQEMEKMKRKLDGETTDLQDQLLELQQQIEELKQQLARKE 1089
Cdd:TIGR02168 863 ELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQ 942
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1785379719 1090 E--------ELQAALARVDDEVGQKNNLLKQLRDLQSQLAELH-------EDLESEKAARAKAEKQRRDLGEELEAL 1151
Cdd:TIGR02168 943 ErlseeyslTLEEAEALENKIEDDEEEARRRLKRLENKIKELGpvnlaaiEEYEELKERYDFLTAQKEDLTEAKETL 1019
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1416-1926 |
7.29e-12 |
|
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: 70.82 E-value: 7.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1416 DKLEKTRNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKNISARYGEERDRAEAEAREKETKALSLSRALEEA 1495
Cdd:TIGR04523 176 NLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1496 IDLKDELDRQNKQLRAEMDDLVSSK---DDVGKNVHELERSKRALEQQVQ-----EMKTQIEELEDELQAIEDGKLRLEV 1567
Cdd:TIGR04523 256 NQLKDEQNKIKKQLSEKQKELEQNNkkiKELEKQLNQLKSEISDLNNQKEqdwnkELKSELKNQEKKLEEIQNQISQNNK 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1568 NMQAMK---AQFERDLQNRDDSNDEKKKllfkQVREMEVELEEERKQKSQILAAKKKLEMDLQDMESQMDSANKGRDEAV 1644
Cdd:TIGR04523 336 IISQLNeqiSQLKKELTNSESENSEKQR----ELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKD 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1645 KQLKKLQLQFKEVWREVEETRAAR-------DEIFVQSRDNEKKLKSLEAELLQLQEDLAAAERAKRQAQQERDDLADEL 1717
Cdd:TIGR04523 412 EQIKKLQQEKELLEKEIERLKETIiknnseiKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKEL 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1718 SNGVSGKSALLDEKRALEMrisqleeeldeeqsntelindryrkltlQVETITTELSAERSFSQKAENARQQMERQNKEL 1797
Cdd:TIGR04523 492 KSKEKELKKLNEEKKELEE----------------------------KVKDLTKKISSLKEKIEKLESEKKEKESKISDL 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1798 KVKLNEMDSTM-RSKYKITIASLEAKISQLEEqmeqeskeriiANKLVRRAEKRLKEVLLQVEEERRNadqFKEQLEKAN 1876
Cdd:TIGR04523 544 EDELNKDDFELkKENLEKEIDEKNKEIEELKQ-----------TQKSLKKKQEEKQELIDQKEKEKKD---LIKEIEEKE 609
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1877 IRMKQLKRQLEEAEEEASRANSNRRRLQRELEDVTESAESMNREVTTLRS 1926
Cdd:TIGR04523 610 KKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRN 659
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1036-1594 |
1.29e-11 |
|
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: 70.25 E-value: 1.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1036 IADLEDRLKKEEKGRQEMEKMKR-KLDGETTDLQDQLLELQQQIEELKQQLARKEEELQAALARV----DDEVGQKNNLL 1110
Cdd:pfam12128 267 YKSDETLIASRQEERQETSAELNqLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHgaflDADIETAAADQ 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1111 KQLRDLQSQLAELHEDLE--SEKAARAKAEKQRRDLGEELEaLKTELEDTLDSTAAQQELRakreqevtDLKKTIEEDVk 1188
Cdd:pfam12128 347 EQLPSWQSELENLEERLKalTGKHQDVTAKYNRRRSKIKEQ-NNRDIAGIKDKLAKIREAR--------DRQLAVAEDD- 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1189 vRDAQVTEMRQRHNQVVEEISEQleqARRFKGNLEKVK------QTLESENTDLIKEVKNLQAAKQDSEQRRKKLEQQVS 1262
Cdd:pfam12128 417 -LQALESELREQLEAGKLEFNEE---EYRLKSRLGELKlrlnqaTATPELLLQLENFDERIERAREEQEAANAEVERLQS 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1263 EFQI----RTNESEKVKF------ELAEKLQKLQAELDGVSGAL-----GSTEGKSIKLTKDLSTVQSQLQDTQ-ELLQE 1326
Cdd:pfam12128 493 ELRQarkrRDQASEALRQasrrleERQSALDELELQLFPQAGTLlhflrKEAPDWEQSIGKVISPELLHRTDLDpEVWDG 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1327 ETRQKLNFSS---RVRQLEEEKNNLMENLEEEESAKAQLSRQLQALQQQLLESK-KRMEDQGGMVEAMEEAKKKSYKELE 1402
Cdd:pfam12128 573 SVGGELNLYGvklDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQlVQANGELEKASREETFARTALKNAR 652
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1403 FLQQR-FDEKHQINDKLEKTRNRLQQELDDLMVDLDHQRQIvsnLEKKQKKFDQMLAEEKNISARYGEERDRAEAEAREK 1481
Cdd:pfam12128 653 LDLRRlFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQ---LDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDA 729
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1482 ETKALSLSRALEEAidlkdELDRQNKQLRAEMDDLVSSKDDVGKNVHELERSKRALEQQV-------------------- 1541
Cdd:pfam12128 730 QLALLKAAIAARRS-----GAKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIeriavrrqevlryfdwyqet 804
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 1785379719 1542 -----QEMKTQIEELEDELQAIEDGKLRLEVNMQAMKAQFERDLQNRDDSNDEKKKLL 1594
Cdd:pfam12128 805 wlqrrPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENL 862
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
873-1883 |
1.98e-11 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 69.69 E-value: 1.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 873 SELKEMANKYQQLFEEksilaeqlqaeTELFAEAEEMRARLASKKQELEEilHDLEarveeeeertLQLQNEKKKMHQHI 952
Cdd:TIGR00606 166 SEGKALKQKFDEIFSA-----------TRYIKALETLRQVRQTQGQKVQE--HQME----------LKYLKQYKEKACEI 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 953 QDLEEQLEEEEGARQKLQLEKvttESRLKKMEEDILLLEDQNAKLAKerklLDDRIGEFTSTMAEEEEKVKSLNKLRnky 1032
Cdd:TIGR00606 223 RDQITSKEAQLESSREIVKSY---ENELDPLKNRLKEIEHNLSKIMK----LDNEIKALKSRKKQMEKDNSELELKM--- 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1033 EAVIADLEDRLKKEEKGRQEMEKMKRKLDGETTDLQDQLLELQQQIEELKQQLARKEEELQAALARVDDEVgQKNNLLKQ 1112
Cdd:TIGR00606 293 EKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHI-RARDSLIQ 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1113 LRDLQSQLAELHEDLESEKAARAKAEKQRRDLGEELEALKTELEDTLDSTAAQQELRAKREQEVTDLKKTIEEDVKVRDA 1192
Cdd:TIGR00606 372 SLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEK 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1193 QVTEMRQRHNQV------VEEISEQLEQARRFKGNLEKVKQTLESENtdLIKEVKNLQAAKQDSEQRRKKLEQQVSEFQI 1266
Cdd:TIGR00606 452 KQEELKFVIKELqqlegsSDRILELDQELRKAERELSKAEKNSLTET--LKKEVKSLQNEKADLDRKLRKLDQEMEQLNH 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1267 RTNESEKVKFELAEKLQKLQA-------ELDGVSGALGSTEGKSI------KLTKDLSTVQSQLQDTQELLQEETRQKLN 1333
Cdd:TIGR00606 530 HTTTRTQMEMLTKDKMDKDEQirkiksrHSDELTSLLGYFPNKKQledwlhSKSKEINQTRDRLAKLNKELASLEQNKNH 609
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1334 FSSRVRQLEEEKNNLMENLEEEESAKAQLSRQLQALQQQLLESKKRmedqggmveAMEEAKKKSYKelEFLQQRFDEKHQ 1413
Cdd:TIGR00606 610 INNELESKEEQLSSYEDKLFDVCGSQDEESDLERLKEEIEKSSKQR---------AMLAGATAVYS--QFITQLTDENQS 678
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1414 ---INDKLEKTRNRLQQELDDLMVDL----DHQRQIVSNLEKKQKKFDQMLAeeknISARYGEERDRAEAEAREKETKAL 1486
Cdd:TIGR00606 679 ccpVCQRVFQTEAELQEFISDLQSKLrlapDKLKSTESELKKKEKRRDEMLG----LAPGRQSIIDLKEKEIPELRNKLQ 754
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1487 SLSRALEEaidLKDELDRQNKQLRAEMDDLVSSKdDVGKNVHELERskraLEQQVQEMKTQIEELEDELQAIEDGKLRLE 1566
Cdd:TIGR00606 755 KVNRDIQR---LKNDIEEQETLLGTIMPEEESAK-VCLTDVTIMER----FQMELKDVERKIAQQAAKLQGSDLDRTVQQ 826
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1567 VNmqamkaQFERDLQNRDDSNDEKKKLLFKqvremeveleEERKQKSQILAAKKKLEmDLQDMESQMDSANKGRDEAVKQ 1646
Cdd:TIGR00606 827 VN------QEKQEKQHELDTVVSKIELNRK----------LIQDQQEQIQHLKSKTN-ELKSEKLQIGTNLQRRQQFEEQ 889
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1647 LKKLQLQFKEVWREVEEtraARDEIFVQSrdnekklKSLEAELLQLQEDLAAAERAKRQAQQERDDLADELSNGVSGKSA 1726
Cdd:TIGR00606 890 LVELSTEVQSLIREIKD---AKEQDSPLE-------TFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKD 959
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1727 LL--------DEKRALEMRISQLEEELDEEQSNTELINDRYRKLTLQVET--ITTELSAERSFSQKAENARQQMERQNKE 1796
Cdd:TIGR00606 960 IEnkiqdgkdDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTqkIQERWLQDNLTLRKRENELKEVEEELKQ 1039
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1797 LKVKLNEMDST-MRSKYKI------TIASLEAKISQLEEQMEQESK--ERIIANKLVRRAEKRLKEVLLQV---EEERRN 1864
Cdd:TIGR00606 1040 HLKEMGQMQVLqMKQEHQKleenidLIKRNHVLALGRQKGYEKEIKhfKKELREPQFRDAEEKYREMMIVMrttELVNKD 1119
|
1050
....*....|....*....
gi 1785379719 1865 ADQFKEQLEKANIRMKQLK 1883
Cdd:TIGR00606 1120 LDIYYKTLDQAIMKFHSMK 1138
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1279-1930 |
2.93e-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: 69.05 E-value: 2.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1279 AEKLQKLQAELDGVSGALGSTEGKSIKLTKDLSTVQSQLQDTQELLQEETRQKLNFSSRVRQLEEeknnlmenleeeesa 1358
Cdd:pfam01576 11 EEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEE--------------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1359 kaqlsrqlqalqqQLLESKKRMEDQGGMVEAMEEAKKKSYKELEFLQQRFDEKHQINDKLEKTRNRLQQELDDLMVDLDH 1438
Cdd:pfam01576 76 -------------ILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1439 QRQIVSNLEKKQKKFDQMLAEeknISARYGEErdraeaearEKETKALSLSRALEEAI--DLKDELDRQNKQlRAEMDdl 1516
Cdd:pfam01576 143 LEDQNSKLSKERKLLEERISE---FTSNLAEE---------EEKAKSLSKLKNKHEAMisDLEERLKKEEKG-RQELE-- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1517 vsskddvgKNVHELERSKRALEQQVQEMKTQIEEL-------EDELQAIEDgklRLEvNMQAMKAQFERDLQNRDDSNDE 1589
Cdd:pfam01576 208 --------KAKRKLEGESTDLQEQIAELQAQIAELraqlakkEEELQAALA---RLE-EETAQKNNALKKIRELEAQISE 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1590 KKKLLFKQVREMEVELEEERKQKSQILAAKKKLEMDLQDMESQMDSANKgRDEAVKQLKKLQlqfkevwreVEETRAARD 1669
Cdd:pfam01576 276 LQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSK-REQEVTELKKAL---------EEETRSHEA 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1670 EIFVQSRDNEKKLKSLEAELLQLQEDLAAAERAKRQAQQERDDLADELSNGVSGKSALLDEKRALEMRISQLEEELDEEQ 1749
Cdd:pfam01576 346 QLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESE 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1750 SNTELINDRYRKLTLQVETITTELSAERSFSQKAENARQQMERQNKELKVKLNEmDSTMRSKYKITIASLEAKISQLEEQ 1829
Cdd:pfam01576 426 RQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQE-ETRQKLNLSTRLRQLEDERNSLQEQ 504
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1830 MEQESKERIIANKLVRRAEKRLKEVLLQVEEERRNADQFKEQLEKANIRMKQLKRQLEEAEEEASRANSNRRRLQRELED 1909
Cdd:pfam01576 505 LEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDD 584
|
650 660
....*....|....*....|.
gi 1785379719 1910 VTESAESMNREVTTLRSRLRR 1930
Cdd:pfam01576 585 LLVDLDHQRQLVSNLEKKQKK 605
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
838-1719 |
7.89e-11 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 67.76 E-value: 7.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 838 FTKVKPLLQVTRQD--EVMQAKVVELQKVKDTQVKTESELKEMANKYQQLFEEKSIlAEQLQAETELFAEAEEMRARLAS 915
Cdd:TIGR00606 184 YIKALETLRQVRQTqgQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREI-VKSYENELDPLKNRLKEIEHNLS 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 916 KKQELEEILHDLEArveeeeeRTLQLQNEKKKMHQhiqdleEQLEEEEGARQKLQLEKVTTESRLKKMEEDILLLEDQNA 995
Cdd:TIGR00606 263 KIMKLDNEIKALKS-------RKKQMEKDNSELEL------KMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 996 KLAKERKLLDDRIGEFTSTMAEEEEKVKSLNKLRNKYEAVIADLEDRLK------------------KEEKGRQEME-KM 1056
Cdd:TIGR00606 330 KLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLEldgfergpfserqiknfhTLVIERQEDEaKT 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1057 KRKLDGETTDLQDQLLELQQQIEELKQQLARKEEELQAALARVDDEVGQKNNLLKQLRDLQSQLAELHEDLESEKAARAK 1136
Cdd:TIGR00606 410 AAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSK 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1137 AEKQR--RDLGEELEALKTELEDTLDSTAAQQELRAKREQEVTDLKKT--IEEDVKVRDAQVTEMRQRHNQVVEEISEQL 1212
Cdd:TIGR00606 490 AEKNSltETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMemLTKDKMDKDEQIRKIKSRHSDELTSLLGYF 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1213 EQARRFKGNLEKVKQTLESENTDLIKEVKNLQAAKQDSEQRR---KKLEQQVSEFQIRTNESEKVKfELAEKLQKLQAEL 1289
Cdd:TIGR00606 570 PNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINnelESKEEQLSSYEDKLFDVCGSQ-DEESDLERLKEEI 648
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1290 DGVSGALGSTEGKSIKLTKDLSTVQSQLQDTQELLQEETRQKLNFSSRVRQLEEEKNNLMENLEEEESakaqlsrqlqal 1369
Cdd:TIGR00606 649 EKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTES------------ 716
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1370 qqQLLESKKRMEDQGGMVEAMEEAKKKSYKELEFLQQRF--------DEKHQI--NDKLEKTRNRLQQELDDLMVDLDHQ 1439
Cdd:TIGR00606 717 --ELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLqkvnrdiqRLKNDIeeQETLLGTIMPEEESAKVCLTDVTIM 794
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1440 RQIVSNLEKKQKKFDQMLAEEKNISARYGEERDRAEAEarEKETKALSLSRALEEAIDLKDELDRQNKQLRAEMDDLVSS 1519
Cdd:TIGR00606 795 ERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQ--EKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSE 872
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1520 KDDVGKNVHElersKRALEQQVQEMKTQIEELedeLQAIEDGKLRLEVNMQAMKAQFERDLQNRDDSNDEKKKLLFKQVR 1599
Cdd:TIGR00606 873 KLQIGTNLQR----RQQFEEQLVELSTEVQSL---IREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVND 945
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1600 EMEVELEEERKQKSQILAAKKKLEMDLQDMESQMDSANKGRDEAVKQLKKLQLQFKEVWREVE----ETRAARDEIFVQS 1675
Cdd:TIGR00606 946 IKEKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDtqkiQERWLQDNLTLRK 1025
|
890 900 910 920
....*....|....*....|....*....|....*....|....
gi 1785379719 1676 RDNEkkLKSLEAELLQLQEDLaaAERAKRQAQQERDDLADELSN 1719
Cdd:TIGR00606 1026 RENE--LKEVEEELKQHLKEM--GQMQVLQMKQEHQKLEENIDL 1065
|
|
| Myosin_N |
pfam02736 |
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ... |
31-76 |
8.39e-11 |
|
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: 58.60 E-value: 8.39e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1785379719 31 TAKRQVWVPSEKHGFEAASIKEERGEEVIVELaENGKRVPVAKDDI 76
Cdd:pfam02736 1 DAKKLVWVPDPKEGFVKGEIKEEEGDKVTVET-EDGKTVTVKKDDV 45
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1082-1289 |
2.48e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 64.79 E-value: 2.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1082 KQQLARKEEELQAALARVDDEVGQKNNLLKQLRDLQSQLAELHEDLESEKAARAKAEKQRRDLGEELEALKTELEdtlds 1161
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE----- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1162 taAQQELRAKREQEVTDLKKTIEEDVKVRD---AQVTEMRQRHNQVVEEISEQLEQARRFKGNLEKVKQTLESENTDL-- 1236
Cdd:COG4942 101 --AQKEELAELLRALYRLGRQPPLALLLSPedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELea 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1785379719 1237 -----IKEVKNLQAAKQDSEQRRKKLEQQVSEFQIRTNESEKVKFELAEKLQKLQAEL 1289
Cdd:COG4942 179 llaelEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1196-1874 |
2.56e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 65.86 E-value: 2.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1196 EMRQRHNQVVEEISeQLEQARRFKGNLEKVKQTLESEntdlIKEVKNLQAAKQDSEQRRKKLEQQVSEFQIRTNESEKVK 1275
Cdd:PRK03918 142 ESDESREKVVRQIL-GLDDYENAYKNLGEVIKEIKRR----IERLEKFIKRTENIEELIKEKEKELEEVLREINEISSEL 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1276 FELAEKLQKLQAELDgvsgalgstegksikltkdlstvqsQLQDTQELLQEETRQKLNFSSRVRQLEEEKNNLMENLEee 1355
Cdd:PRK03918 217 PELREELEKLEKEVK-------------------------ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIE-- 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1356 esakaqlsrqlqalqqqllESKKRMEDQGGMVEAMEEAKKKSyKELEFLQQRFDEKHQINDKLEKTRNRLQQELDDLmvd 1435
Cdd:PRK03918 270 -------------------ELKKEIEELEEKVKELKELKEKA-EEYIKLSEFYEEYLDELREIEKRLSRLEEEINGI--- 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1436 ldhQRQIvSNLEKKQKKFDQMLAEEKNISARYGEERDRAEAeareketkalslsraLEEAIDLKDELDRQNKQLRAEmdd 1515
Cdd:PRK03918 327 ---EERI-KELEEKEERLEELKKKLKELEKRLEELEERHEL---------------YEEAKAKKEELERLKKRLTGL--- 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1516 lvsSKDDVGKNVHELERSKRALEQQVQEMKTQIEELEDELQAIEDGKLRLEvnmqamKAQFERDLQNRDDSNDEKKKLLF 1595
Cdd:PRK03918 385 ---TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELK------KAKGKCPVCGRELTEEHRKELLE 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1596 K---QVREMEVELEEERKQKSQILAAKKKLEMDLQDME--SQMDSANKGRDEAVKQLKKLQLQ-FKEVWREVEETRAARD 1669
Cdd:PRK03918 456 EytaELKRIEKELKEIEEKERKLRKELRELEKVLKKESelIKLKELAEQLKELEEKLKKYNLEeLEKKAEEYEKLKEKLI 535
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1670 EIFVQSRDNEKKLKSLEAellqLQEDLAAAERAKRQAQQERDDLADELSNgVSGKSALLDEKRALEMrisqleeeldeeq 1749
Cdd:PRK03918 536 KLKGEIKSLKKELEKLEE----LKKKLAELEKKLDELEEELAELLKELEE-LGFESVEELEERLKEL------------- 597
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1750 sntELINDRYRKLtlqvetittelsaersfsqkaENARQQMERQNKELKVKLNEMDST--MRSKYKITIASLEAKISQL- 1826
Cdd:PRK03918 598 ---EPFYNEYLEL---------------------KDAEKELEREEKELKKLEEELDKAfeELAETEKRLEELRKELEELe 653
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 1785379719 1827 ----EEQMEQESKERIIANKLVRRAEKRLKEVLLQVEEERRNADQFKEQLEK 1874
Cdd:PRK03918 654 kkysEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEE 705
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1083-1717 |
2.72e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 65.71 E-value: 2.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1083 QQLARKEEELQAALARVDDEVGQ-KNNLLKQ-LRDLQSQLAELHEDLESEKAARAKAEKQRRDL--------GEELEALK 1152
Cdd:COG4913 265 AAARERLAELEYLRAALRLWFAQrRLELLEAeLEELRAELARLEAELERLEARLDALREELDELeaqirgngGDRLEQLE 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1153 TELEDTLDSTAAQQELRAKREQEVTDLKKTIEEDvkvrDAQVTEMRQRHNQVVEEISEQLEQARRFKGNLEKVKQTLESE 1232
Cdd:COG4913 345 REIERLERELEERERRRARLEALLAALGLPLPAS----AEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRE 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1233 NTDLIKEVKNLQAAK----QDSEQRRKKLEQQVSefqirtNESEKVKFeLAEKLQKLQAELD---GVSGALGstegkSIK 1305
Cdd:COG4913 421 LRELEAEIASLERRKsnipARLLALRDALAEALG------LDEAELPF-VGELIEVRPEEERwrgAIERVLG-----GFA 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1306 LT-----KDLSTVQSQLQDTQellqeeTRQKLNFsSRVRQLEEEKNNLMEnleeeesakaqlsrqlqalqqqlleskkrm 1380
Cdd:COG4913 489 LTllvppEHYAAALRWVNRLH------LRGRLVY-ERVRTGLPDPERPRL------------------------------ 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1381 eDQGGMVEAMEEAKKKSYKELEF-LQQRFD---------------------------EKHQINDKLEKTRN--------- 1423
Cdd:COG4913 532 -DPDSLAGKLDFKPHPFRAWLEAeLGRRFDyvcvdspeelrrhpraitragqvkgngTRHEKDDRRRIRSRyvlgfdnra 610
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1424 ---RLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKNISARYGEERDRAEAEAREKETKALsLSRALEEAIDLKd 1500
Cdd:COG4913 611 klaALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAE-LERLDASSDDLA- 688
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1501 ELDRQNKQLRAEMDDLVSSKDdvgknvhELERSKRALEQQVQEMKTQIEELEDELQAIEDGKlrlevnMQAMKAQFERDL 1580
Cdd:COG4913 689 ALEEQLEELEAELEELEEELD-------ELKGEIGRLEKELEQAEEELDELQDRLEAAEDLA------RLELRALLEERF 755
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1581 QNRDDSNDEKKKllfkqvremeveleeerkqksqilaakkklemdLQDMESQMDSANKGRDEAVKQLKKLQLQFKEVWR- 1659
Cdd:COG4913 756 AAALGDAVEREL---------------------------------RENLEERIDALRARLNRAEEELERAMRAFNREWPa 802
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 1785379719 1660 EVEETRAARDEIfvqsRDNEKKLKSLEAE-LLQLQEDLaaAERAKRQAQQERDDLADEL 1717
Cdd:COG4913 803 ETADLDADLESL----PEYLALLDRLEEDgLPEYEERF--KELLNENSIEFVADLLSKL 855
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1199-1920 |
2.75e-10 |
|
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: 65.76 E-value: 2.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1199 QRHNQVVEEISEQLEQARRFKgNLEKVKQTLESENTDLIKEVKNLQAAKQDSEQRRKKLEqqvsEFQIRTNESEKVKFEL 1278
Cdd:pfam02463 153 ERRLEIEEEAAGSRLKRKKKE-ALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALE----YYQLKEKLELEEEYLL 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1279 AEKLQKLQAELDGVSGALGSTEGKSIKLTKDLSTVQSQLQDTQELLQEETRQKLNFssrvrqLEEEKNNLMENLEEEESA 1358
Cdd:pfam02463 228 YLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKL------QEEELKLLAKEEEELKSE 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1359 KAQLSRQLQALQQQLLESKKRMEDQGGMVEAMEEAKKKSYKELEFLQQRFDEKHQINDKLEKTRNRLQQELDDLMVDLDH 1438
Cdd:pfam02463 302 LLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1439 QRQIVSNLEKKQKKFDQMLAEEKNISARYGEERDRAEAEAREKETKALSLSRALEEAIDLKDEldrqNKQLRAEMDDLVS 1518
Cdd:pfam02463 382 ESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQG----KLTEEKEELEKQE 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1519 SKDDVGKNVHELERSKRALEQQVQEMKTQIEELEDELQAIEDGKLRLEVNMQAMK-AQFERDLQNRDDSNDEKKKLLFKQ 1597
Cdd:pfam02463 458 LKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLlALIKDGVGGRIISAHGRLGDLGVA 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1598 VREMEVELEEERKQKSQILAAKKKLEMDLQDMESQMDSaNKGRDEAVKQLKKLQLQFKEVWREVEETRAARDEIFVQSRD 1677
Cdd:pfam02463 538 VENYKVAISTAVIVEVSATADEVEERQKLVRALTELPL-GARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEAD 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1678 NEKKLKSLEAELLQLQEDLAAAERAKRQAQQERDD--LADELSNGVSGKSALLDEKRALEMRISQLEEELDEEQSNTELI 1755
Cdd:pfam02463 617 EDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGvsLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILR 696
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1756 NDRYRKLTLQVETITTELSAERSFSQKAENARQQMERQNKELKVKLNEMDSTMRSKYKITIASLEAKISQLE-EQMEQES 1834
Cdd:pfam02463 697 RQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSElSLKEKEL 776
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1835 KERIIANKLVRRAEKRLKEVLLQVEEERRNADQFKEQLEKANIRMkqlKRQLEEAEEEASRANSNRRRLQRELEDVTESA 1914
Cdd:pfam02463 777 AEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQ---LLIEQEEKIKEEELEELALELKEEQKLEKLAE 853
|
....*.
gi 1785379719 1915 ESMNRE 1920
Cdd:pfam02463 854 EELERL 859
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1375-1929 |
3.63e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 65.47 E-value: 3.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1375 ESKKRMEDQGGMVEAMEEAKKKSYKELEFLQQRFDEkhqINDKLEKTRNRLQqELDDLMVDLDHQRQIVSNLEKKQKKFD 1454
Cdd:PRK03918 176 RRIERLEKFIKRTENIEELIKEKEKELEEVLREINE---ISSELPELREELE-KLEKEVKELEELKEEIEELEKELESLE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1455 QmlaEEKNISARYGEERDRAEaEAREKETKALSLSRALEEAIDLKDELDRqnkqLRAEMDDLVSSKDDVGKNVHELERSK 1534
Cdd:PRK03918 252 G---SKRKLEEKIRELEERIE-ELKKEIEELEEKVKELKELKEKAEEYIK----LSEFYEEYLDELREIEKRLSRLEEEI 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1535 RALEQQVQE---MKTQIEELEDELQAIEDGKLRLEVNMQAmkaqFERDLQNRDDSNDEKKKLLFKQVREMEVELEEERKQ 1611
Cdd:PRK03918 324 NGIEERIKEleeKEERLEELKKKLKELEKRLEELEERHEL----YEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKA 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1612 KSQILAAKKKLEmdlqDMESQMDSANKGRDEAVKQLKKLQLQFKEVWREVEEtraardeifvqsRDNEKKLKSLEAELLQ 1691
Cdd:PRK03918 400 KEEIEEEISKIT----ARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTE------------EHRKELLEEYTAELKR 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1692 LQEDLAAAERAKRQAQQERDDLADELSNG--VSGKSALLDEKRALEMRISQ-LEEELDEEQSNTELINDRYRKLTLQVET 1768
Cdd:PRK03918 464 IEKELKEIEEKERKLRKELRELEKVLKKEseLIKLKELAEQLKELEEKLKKyNLEELEKKAEEYEKLKEKLIKLKGEIKS 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1769 ITTELSAERSFsqkaENARQQMERQNKELKVKLNEMDSTMRSKYKITIASLEAKISQLEEQMEQESKeriianklVRRAE 1848
Cdd:PRK03918 544 LKKELEKLEEL----KKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLE--------LKDAE 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1849 KRLKEVLLQVEEERRNADQFKEQLEKANIRMKQLKRQLEEAEEEAS-----RANSNRRRLQRELEDVTESAESMNREVTT 1923
Cdd:PRK03918 612 KELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSeeeyeELREEYLELSRELAGLRAELEELEKRREE 691
|
....*.
gi 1785379719 1924 LRSRLR 1929
Cdd:PRK03918 692 IKKTLE 697
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
872-1339 |
4.48e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 65.06 E-value: 4.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 872 ESELKEMANKYQQLFEEKSILAEQLQAETELFAEAEEMRARLASKKQELEEILHDLEA----------RVEEEEERTLQL 941
Cdd:PRK02224 212 ESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAEterereelaeEVRDLRERLEEL 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 942 QNEKKKMHQHIQDLEEQLEEEEGARQKLQLEKVTTESRL--------------KKMEEDILLLEDQNAKLAKERKLLDDR 1007
Cdd:PRK02224 292 EEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLeecrvaaqahneeaESLREDADDLEERAEELREEAAELESE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1008 IGEFTSTMAEEEEKVKSLNKLRNKYEAVIADLEDRLKKEEKGRQEMEKMKRKLDGETTDLQDQLLELQQQIeelkqqlaR 1087
Cdd:PRK02224 372 LEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERV--------E 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1088 KEEELQAA---------------LARVDDEVGQKNNLLKQLRDLQSQLAELHEDLESEKAArAKAEKQRRDLGEELEALK 1152
Cdd:PRK02224 444 EAEALLEAgkcpecgqpvegsphVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDL-VEAEDRIERLEERREDLE 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1153 TELEDTLDSTAAQQELRAKREQEVTDLkktieedvkvrDAQVTEMRQRHNQVVEEISEQLEQARRFKGNLEKVKQTLESE 1232
Cdd:PRK02224 523 ELIAERRETIEEKRERAEELRERAAEL-----------EAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESL 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1233 NT---------DLIKEVKNLQAAKQD----SEQRRKKL---------------EQQVSEFQIRTNESEKVKFELAEKLQK 1284
Cdd:PRK02224 592 ERirtllaaiaDAEDEIERLREKREAlaelNDERRERLaekrerkreleaefdEARIEEAREDKERAEEYLEQVEEKLDE 671
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1785379719 1285 LQAELDGVSGALGSTEGkSIKLTKDLSTVQSQLQDTQELLQ---EETRQKLNFSSRVR 1339
Cdd:PRK02224 672 LREERDDLQAEIGAVEN-ELEELEELRERREALENRVEALEalyDEAEELESMYGDLR 728
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1392-1974 |
4.73e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 65.16 E-value: 4.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1392 EAKKKSYKELEFLQQRFDEKHQINDKLEKTRNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEE--KNISARYGE 1469
Cdd:PTZ00121 1070 EGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDarKAEEARKAE 1149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1470 ERDRAEAEAREKETKALSLSRALEEAIDL----KDELDRQNKQLRAEMDDLVSSKDDVGKNVHELERSKRALEQQVQEMK 1545
Cdd:PTZ00121 1150 DAKRVEIARKAEDARKAEEARKAEDAKKAeaarKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAV 1229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1546 TQIEEL---EDELQAIEDGKLRLEVNM--QAMKAQFERDLQNRDDSNDEKKKLLFKQVREMEVELEEERKQKSQILAAKK 1620
Cdd:PTZ00121 1230 KKAEEAkkdAEEAKKAEEERNNEEIRKfeEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKK 1309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1621 KLEMdlqdmESQMDSANKGRDEAVKQLKKLQLQFKEVWREVEetrAARDEIFVQSRDNEKKLKSLEAELLQLQEDLAAAE 1700
Cdd:PTZ00121 1310 KAEE-----AKKADEAKKKAEEAKKKADAAKKKAEEAKKAAE---AAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKAD 1381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1701 RAKRQAQQERDdlADELSngvsgKSALLDEKRALEMRISQLEEELDEEQSNTELINDRYRKLTLQVETI--TTELSAERS 1778
Cdd:PTZ00121 1382 AAKKKAEEKKK--ADEAK-----KKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAkkADEAKKKAE 1454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1779 FSQKAENARQQMERQNK--ELKVKLNEMDSTMRSKYKITIA---SLEAKISQLEEQMEQESKERIIANKL--VRRAEKRL 1851
Cdd:PTZ00121 1455 EAKKAEEAKKKAEEAKKadEAKKKAEEAKKADEAKKKAEEAkkkADEAKKAAEAKKKADEAKKAEEAKKAdeAKKAEEAK 1534
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1852 KEVLLQVEEERRNADQFK--EQLEKANIRMKqlkrqleeaEEEASRANSNRRRLQRELEDVTESAESMNREVTTLRSRLR 1929
Cdd:PTZ00121 1535 KADEAKKAEEKKKADELKkaEELKKAEEKKK---------AEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEK 1605
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 1785379719 1930 RAPIQFTTRTIRQVYQLEAVSDEEPESHSGEPSANHQQQQPPQAE 1974
Cdd:PTZ00121 1606 KMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAE 1650
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
852-1432 |
1.17e-09 |
|
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: 63.93 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 852 EVMQAKVVELQKV-------KDTQVKTESELKEMANKYQQLFEEKSILAEQLQAETELFAEAEEMRARLASKKQELEEIL 924
Cdd:TIGR02169 364 EELEDLRAELEEVdkefaetRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEK 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 925 HDLEARVEEEEERTLQLQNEKKKMHQHIQDLEEQLEEEEGARQKLQLEKVTTESRLKKMEEDILLLEDQnaklakeRKLL 1004
Cdd:TIGR02169 444 EDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAV-------EEVL 516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1005 DDRIGEFTSTMAE----EEEKVKSL-----NKLRN---KYEAVIADLEDRLKKEEKGR---------------------- 1050
Cdd:TIGR02169 517 KASIQGVHGTVAQlgsvGERYATAIevaagNRLNNvvvEDDAVAKEAIELLKRRKAGRatflplnkmrderrdlsilsed 596
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1051 ------------------------------QEMEKMKR--------KLDGETTDLQDQLLELQQQIEELKQQLARKEEEL 1092
Cdd:TIGR02169 597 gvigfavdlvefdpkyepafkyvfgdtlvvEDIEAARRlmgkyrmvTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAEL 676
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1093 QAALARVDDEVGQKNNLLKQLRDLQSQLAELHEDLESEKAARAKAEKQRRDLGEELEALKTELEDTLDSTAAQQELRAKR 1172
Cdd:TIGR02169 677 QRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENV 756
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1173 EQEVTDLKKTI---EEDVKVRDAQVTEMRQRHN-QVVEEISEQLEQARRFKGNLEKVKQTLESENTDLIKEVKNLQAAKQ 1248
Cdd:TIGR02169 757 KSELKELEARIeelEEDLHKLEEALNDLEARLShSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQ 836
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1249 DSEQRRKKLEQQVSEFQIRTNESEKVKFELAEKLQKLQAELDGVSGALGSTEGKSIKLTKDLSTVQSQLQDtqellQEET 1328
Cdd:TIGR02169 837 ELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEE-----LEAQ 911
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1329 RQKLNfsSRVRQLEEEKNNLMENLEEEESAKAQLSRQLQALQQQLLESKKRMEDQGGMvEAMEEAKKKSYKELEFLQQRF 1408
Cdd:TIGR02169 912 IEKKR--KRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEI-RALEPVNMLAIQEYEEVLKRL 988
|
650 660
....*....|....*....|....
gi 1785379719 1409 DEKHQINDKLEKTRNRLQQELDDL 1432
Cdd:TIGR02169 989 DELKEKRAKLEEERKAILERIEEY 1012
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1119-1735 |
1.51e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 63.14 E-value: 1.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1119 QLAELHEDLESEKAARAKAEKQRRDLGEELEALKTELEDtldstaaqqelraKREQEVTDLKKTIEEDVKVRDAQvtemr 1198
Cdd:PRK02224 160 QLGKLEEYRERASDARLGVERVLSDQRGSLDQLKAQIEE-------------KEEKDLHERLNGLESELAELDEE----- 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1199 qrhnqvVEEISEQLEQARRFKGNLEKV----KQTLEsENTDLIKEVKNLQAAKQDSEQRRKKLEQQVSEFQIRTNesekv 1274
Cdd:PRK02224 222 ------IERYEEQREQARETRDEADEVleehEERRE-ELETLEAEIEDLRETIAETEREREELAEEVRDLRERLE----- 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1275 kfELAEKLQKLQAELDGVSGALGSTEGKSIKLTKDLSTVQSQLQDTQELLQEETRQKLNFSSRVRQLEEEKNNLMENLEE 1354
Cdd:PRK02224 290 --ELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAE 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1355 EESAkaqlsrqlqalqqqLLESKKRMEDQGGMVEAMEEAKKKSYKELEFLQQRFDEKHQINDKLEKTRNRLQQELDDLMV 1434
Cdd:PRK02224 368 LESE--------------LEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEA 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1435 DLdhqrqivSNLEKKQKKFDQMLAEEK-----------NISARYGEERDRAEAEAREKETKALSLSrALEEAIDLKDELd 1503
Cdd:PRK02224 434 TL-------RTARERVEEAEALLEAGKcpecgqpvegsPHVETIEEDRERVEELEAELEDLEEEVE-EVEERLERAEDL- 504
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1504 rqnKQLRAEMDDLVSSKDDVGKNVHELERSKRALEQQVQEMKTQIEELEDELQAIEDGKLRLEVNMQAMK---AQFERDL 1580
Cdd:PRK02224 505 ---VEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAReevAELNSKL 581
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1581 QNRDDSNDEKKKLlfkqvremeveleeerkqkSQILAAKKKLEMDLQDMESQMDSANKGRDEAVKQLKKLQLQFKEVWRE 1660
Cdd:PRK02224 582 AELKERIESLERI-------------------RTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAE 642
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1661 VEETRA----ARDEIFVQSRDN-EKKLKSLEAELLQLQEDLAAAERAKRQAQQERDDLaDELSNGVSGKSALLDEKRALE 1735
Cdd:PRK02224 643 FDEARIeearEDKERAEEYLEQvEEKLDELREERDDLQAEIGAVENELEELEELRERR-EALENRVEALEALYDEAEELE 721
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1082-1874 |
1.71e-09 |
|
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: 63.12 E-value: 1.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1082 KQQLARKEEELQAALARVDDEVGQKNNLLKQLRDLQSQLAELHEDLESEKaarakaeKQRRDLGEELEALKTELEDtlds 1161
Cdd:TIGR04523 46 KNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNK-------DKINKLNSDLSKINSEIKN---- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1162 taaQQELRAKREQEVTDLKKTIEEDVKVRDAQVTEMRQRHNQVvEEISEQLEQARRFKGNLEKVKQTLESENTDLIKEVK 1241
Cdd:TIGR04523 115 ---DKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKEL-EKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNID 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1242 NLQAAKQDSE----------QRRKKLEQQVSEFQIRTNESEKVKFELAEKLQKLQAELDGVSGALGSTEGKSIKLTKDLS 1311
Cdd:TIGR04523 191 KIKNKLLKLElllsnlkkkiQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLS 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1312 TVQSQLQDTQELLQEETRQKLNFSSRVRQLEEEKnnlmenleeeesakaqlsrqlqalqqqlleskkrmeDQGGMVEAME 1391
Cdd:TIGR04523 271 EKQKELEQNNKKIKELEKQLNQLKSEISDLNNQK------------------------------------EQDWNKELKS 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1392 EAKKKSyKELEFLQQRFDEKHQINDKLEKTRNRLQQELddlmvdldhqrqivSNLEKKQKKFDQMLAEEKNisarygeer 1471
Cdd:TIGR04523 315 ELKNQE-KKLEEIQNQISQNNKIISQLNEQISQLKKEL--------------TNSESENSEKQRELEEKQN--------- 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1472 dRAEAEAREKETKALSLSRALEEAIDLKDELDRQnKQLRAEMDdlvsskddvgKNVHELERSKRALEQQVQEMKTQIEEL 1551
Cdd:TIGR04523 371 -EIEKLKKENQSYKQEIKNLESQINDLESKIQNQ-EKLNQQKD----------EQIKKLQQEKELLEKEIERLKETIIKN 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1552 EDELQAIEDGKLRLEVNMQAMKAQFERDLQNRDDSNDEKKKLLFKQVREMEVELEEErKQKSQILAAKKKLEMDLQDMES 1631
Cdd:TIGR04523 439 NSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKE-KELKKLNEEKKELEEKVKDLTK 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1632 QMDSANKGRDEAVKQLKKLQLQFKEVWREVEEtraarDEIFVQSRDNEKKLKSLEAELLQLQEDLAAAERAKRQAQQERD 1711
Cdd:TIGR04523 518 KISSLKEKIEKLESEKKEKESKISDLEDELNK-----DDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELID 592
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1712 DLADElsngvsgKSALLDEKRALEMRISQleeeldeEQSNTELINDRYRKLTLQVETIttelsaeRSFSQKAENARQQME 1791
Cdd:TIGR04523 593 QKEKE-------KKDLIKEIEEKEKKISS-------LEKELEKAKKENEKLSSIIKNI-------KSKKNKLKQEVKQIK 651
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1792 RQNKELKVKLNEMDSTMR-SKYKITiasleaKISQLEEQMEQESKERI---IANKLVRRAEKRLKEVLLQVEEERRNADQ 1867
Cdd:TIGR04523 652 ETIKEIRNKWPEIIKKIKeSKTKID------DIIELMKDWLKELSLHYkkyITRMIRIKDLPKLEEKYKEIEKELKKLDE 725
|
....*..
gi 1785379719 1868 FKEQLEK 1874
Cdd:TIGR04523 726 FSKELEN 732
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1402-1928 |
2.34e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 62.75 E-value: 2.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1402 EFLQQRFDEKHQINDKLEKTRnrlqQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKNISARYGEERDRAEAEArek 1481
Cdd:PRK02224 230 EQARETRDEADEVLEEHEERR----EELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEA--- 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1482 etkalSLSRALEEAI-DLKDELDRQNKQLRAEMDDLVSSKDDVGKNVHELERSKRALEQQVQEMKTQIEELEDELQ---- 1556
Cdd:PRK02224 303 -----GLDDADAEAVeARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEeare 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1557 AIEDGKLRLEvnmqamkaqferDLQNRDDSNDEkkkllfkqvremeveleeerkqksqilaAKKKLEMDLQDMESQMDSA 1636
Cdd:PRK02224 378 AVEDRREEIE------------ELEEEIEELRE----------------------------RFGDAPVDLGNAEDFLEEL 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1637 NKGRDEAVKQLKKLQLQFKEVWREVEETRAARDE--------------IFVQSRDNEKKLKSLEAELLQLQEDLAAAEra 1702
Cdd:PRK02224 418 REERDELREREAELEATLRTARERVEEAEALLEAgkcpecgqpvegspHVETIEEDRERVEELEAELEDLEEEVEEVE-- 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1703 krqaqqERDDLADELSNGVSGKSALLDEKRALEMRISQLEEELDEEQSNTELINDRyrkltlqVETITTELSAERSFSQK 1782
Cdd:PRK02224 496 ------ERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRER-------AAELEAEAEEKREAAAE 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1783 AENARQQMERQNKELKVKLNEMDSTMRSKYKitIASLEAKISQLEEQMEqeskeriianklvRRAEKRlkEVLLQVEEER 1862
Cdd:PRK02224 563 AEEEAEEAREEVAELNSKLAELKERIESLER--IRTLLAAIADAEDEIE-------------RLREKR--EALAELNDER 625
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1785379719 1863 RnadqfkEQLEKANIRMKQLKRQLEEAEEEASRAnsNRRRLQRELEDVTESAESMNREVTTLRSRL 1928
Cdd:PRK02224 626 R------ERLAEKRERKRELEAEFDEARIEEARE--DKERAEEYLEQVEEKLDELREERDDLQAEI 683
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1106-1943 |
2.58e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 62.63 E-value: 2.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1106 KNNLLKQLRDLQSQLAELHEdleSEKAARaKAEKQRRDLgEELEALKTELEDTLDSTAAQQELRAKREQEvtdlkkTIEE 1185
Cdd:COG4913 220 EPDTFEAADALVEHFDDLER---AHEALE-DAREQIELL-EPIRELAERYAAARERLAELEYLRAALRLW------FAQR 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1186 DVKVRDAQVTEMRQRHNQVVEEISEQLEQARRFKGNLEKVKQTLESENTDLI----KEVKNLQAAKQDSEQRRKKLEQQV 1261
Cdd:COG4913 289 RLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLeqleREIERLERELEERERRRARLEALL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1262 SEFQIRTNESEKvkfELAEKLQKLQAELDGVSGALGSTEGKSIKLTKDLSTVQSQLQDTQELLQEETRQKLNFSSRVRQl 1341
Cdd:COG4913 369 AALGLPLPASAE---EFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLA- 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1342 eeeknnlmenleeeesakaqlsrqlqalqqqlleskkrmedqggMVEAMEEAKKKSYKEL----EFLQQRFDEkhqindk 1417
Cdd:COG4913 445 --------------------------------------------LRDALAEALGLDEAELpfvgELIEVRPEE------- 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1418 lEKTRNRLQQELD----DLMVDLDHQRQIVSNLEkkQKKFDQMLaeeknisaRYGEERDRAEAEAREKETKAlSLSRale 1493
Cdd:COG4913 474 -ERWRGAIERVLGgfalTLLVPPEHYAAALRWVN--RLHLRGRL--------VYERVRTGLPDPERPRLDPD-SLAG--- 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1494 eaidlkdELDRQNKQLRAEMDDLVSSKDDVGK--NVHELERSKRALEQQVQemktqieeledelqaiedgklrlevnMQA 1571
Cdd:COG4913 539 -------KLDFKPHPFRAWLEAELGRRFDYVCvdSPEELRRHPRAITRAGQ--------------------------VKG 585
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1572 MKAQFERDLQNRDDS-------NDEKKKLLfkqvremeveleeeRKQKSQILAAKKKLEMDLQDMESQMDSANKgRDEAV 1644
Cdd:COG4913 586 NGTRHEKDDRRRIRSryvlgfdNRAKLAAL--------------EAELAELEEELAEAEERLEALEAELDALQE-RREAL 650
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1645 KQLKKLQLQFKEVW---REVEETRAARDEIfvqsRDNEKKLKSLEAELLQLQEDLAAAERAKRQAQQERDDLADELSngv 1721
Cdd:COG4913 651 QRLAEYSWDEIDVAsaeREIAELEAELERL----DASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELE--- 723
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1722 sgksALLDEKRALEMRISQLEEELDEEQsnTELINDRYRkltlqvetittELSAERSFSQKAENARQQMERQNKELKVKL 1801
Cdd:COG4913 724 ----QAEEELDELQDRLEAAEDLARLEL--RALLEERFA-----------AALGDAVERELRENLEERIDALRARLNRAE 786
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1802 NEMDSTMR---SKYKITIASLEAKISQLEEQMEQesKERIIANKLVRRaEKRLKEVLLQVEEERRN--ADQFKEQLEKAN 1876
Cdd:COG4913 787 EELERAMRafnREWPAETADLDADLESLPEYLAL--LDRLEEDGLPEY-EERFKELLNENSIEFVAdlLSKLRRAIREIK 863
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1877 IRMKQLKRQLEEAE---------EEASRANSNRRRLQRELEDVTESAESMNRE--------VTTLRSRLRRAPIQFTTRT 1939
Cdd:COG4913 864 ERIDPLNDSLKRIPfgpgrylrlEARPRPDPEVREFRQELRAVTSGASLFDEElsearfaaLKRLIERLRSEEEESDRRW 943
|
....
gi 1785379719 1940 IRQV 1943
Cdd:COG4913 944 RARV 947
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
861-1325 |
2.71e-09 |
|
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: 62.35 E-value: 2.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 861 LQKVKDTQVKTESELKEMANKYQQLFEEKSILAEQLQAETELFAEAEEMRARLASKKQELEEILHDLEARVEEEEERTLQ 940
Cdd:TIGR04523 206 LKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 941 LQNEKKKMHQHIQDLEEQLEEEEGARQKLQLE-----KVTTESRLKKMEEDILLLEDQNAKLAKERKLLDDRIGEFTSTM 1015
Cdd:TIGR04523 286 LEKQLNQLKSEISDLNNQKEQDWNKELKSELKnqekkLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQREL 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1016 AEEEEKVKSLNKLRNKYEAVIADLEDRLKKEEKGRQEMEKMKRKLDgettdlqdqllelqqqieelkQQLARKEEELQAA 1095
Cdd:TIGR04523 366 EEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKD---------------------EQIKKLQQEKELL 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1096 LARVDDEVGQKNNLLKQLRDLQSQLAELHEDLESEKAARAKAEKQRRDLGEELEALKTELEDTldstaaQQELRAKREQ- 1174
Cdd:TIGR04523 425 EKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQK------QKELKSKEKEl 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1175 -EVTDLKKTIEEDVKVRDAQVTEMRQRHNQVVEEISEQLEQARRFKGNLEKVKQTLESENtdLIKEVKNLQAAKQDSEQR 1253
Cdd:TIGR04523 499 kKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKEN--LEKEIDEKNKEIEELKQT 576
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1785379719 1254 RKKLEQQVSEFQIRTNESEKVKFELAEKLQKLQAELDGVSGALGSTEGKSIKLTKDLSTVQSQLQDTQELLQ 1325
Cdd:TIGR04523 577 QKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVK 648
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
850-1245 |
3.43e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 61.98 E-value: 3.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 850 QDEVMQAKVVELQKVKDTQVKTEsELKEMANKYQQLFEEKSILAEQLQAETELFAEAEEMRARLASKKQELEEILHDLEA 929
Cdd:PRK02224 327 RDRLEECRVAAQAHNEEAESLRE-DADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPV 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 930 RVEEEEERTLQLQNEKKKMHQHIQDLEEQLEEEEGARQKLQ--------------LEKVTTESRLKKMEEDILLLEDQNA 995
Cdd:PRK02224 406 DLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEalleagkcpecgqpVEGSPHVETIEEDRERVEELEAELE 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 996 KLAKERKLLDDRIgEFTSTMAEEEEKVKSLNKLRNKYEAVIADLEDRLKKEEKGRQEMEKMKRKLDGETTDLQDQLLELQ 1075
Cdd:PRK02224 486 DLEEEVEEVEERL-ERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAE 564
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1076 QQIEELKQQLARKEEELQAALARVDDevgqknnlLKQLRDLQSQLAELHEDLES---EKAARAKAEKQRRDLGEELEALK 1152
Cdd:PRK02224 565 EEAEEAREEVAELNSKLAELKERIES--------LERIRTLLAAIADAEDEIERlreKREALAELNDERRERLAEKRERK 636
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1153 TELEDTLDStAAQQELRAKREQEVTDLKKtIEEDVKVRDAQVTEMRQRHNQVVEEIsEQLEQARRFKGNLEKVKQTLESe 1232
Cdd:PRK02224 637 RELEAEFDE-ARIEEAREDKERAEEYLEQ-VEEKLDELREERDDLQAEIGAVENEL-EELEELRERREALENRVEALEA- 712
|
410
....*....|...
gi 1785379719 1233 ntdLIKEVKNLQA 1245
Cdd:PRK02224 713 ---LYDEAEELES 722
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1000-1879 |
4.22e-09 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 61.99 E-value: 4.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1000 ERKLLDDR--IGEFTSTMAEEEEKVKSLNKLrNKYEAVIADLEDRLkkeEKGRQEMEKMKRKLDGETTDLQDQLLELQQQ 1077
Cdd:TIGR01612 889 EKKFNDSKslINEINKSIEEEYQNINTLKKV-DEYIKICENTKESI---EKFHNKQNILKEILNKNIDTIKESNLIEKSY 964
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1078 IEELKQQLARKEEELQAAL--ARVDDEVGQKNNLLKQLRDLQSQLAELHEDL------ESEKAAR---AKAEKQRRDLGE 1146
Cdd:TIGR01612 965 KDKFDNTLIDKINELDKAFkdASLNDYEAKNNELIKYFNDLKANLGKNKENMlyhqfdEKEKATNdieQKIEDANKNIPN 1044
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1147 ELEALKTELEDTLDstaaqqELRAKREQEVTDLKKTIEEDVKVRDAQVTEMRQR--HNQVVEEISEQleqARRFKGNLEK 1224
Cdd:TIGR01612 1045 IEIAIHTSIYNIID------EIEKEIGKNIELLNKEILEEAEINITNFNEIKEKlkHYNFDDFGKEE---NIKYADEINK 1115
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1225 VKQTLESENTDLIKEVKNLQAAKQDSEQRRKKLEQQVSEFQIRTNES---EKVKfELAEKLQKLQAELDgvsgalgstEG 1301
Cdd:TIGR01612 1116 IKDDIKNLDQKIDHHIKALEEIKKKSENYIDEIKAQINDLEDVADKAisnDDPE-EIEKKIENIVTKID---------KK 1185
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1302 KSI--KLTKDLSTVqSQLQDTQELLQEETRQKLNFSSRVRQLEEEKNNlmenleeeesakaqlsrqlqalqqqllESKKR 1379
Cdd:TIGR01612 1186 KNIydEIKKLLNEI-AEIEKDKTSLEEVKGINLSYGKNLGKLFLEKID---------------------------EEKKK 1237
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1380 MEDqggMVEAME-------EAKKKSYKELEFLQQRFDEKHQINdklekTRNRLQQELDDLMVDLDHQRQIVSNLEKKQKK 1452
Cdd:TIGR01612 1238 SEH---MIKAMEayiedldEIKEKSPEIENEMGIEMDIKAEME-----TFNISHDDDKDHHIISKKHDENISDIREKSLK 1309
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1453 FDQMLAEEKNISarygEERDRAEAEAREKETKALSLSRALEEAIDLKDELDRQN-KQLRAEMDDLVSSKDDVGKNVH-EL 1530
Cdd:TIGR01612 1310 IIEDFSEESDIN----DIKKELQKNLLDAQKHNSDINLYLNEIANIYNILKLNKiKKIIDEVKEYTKEIEENNKNIKdEL 1385
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1531 ERSKRaLEQQVQEmKTQIEELEDELQAIEDGKLRLEV--NMQAMKAQFERDLQNRD------DSNDEKKKLLFKQVREME 1602
Cdd:TIGR01612 1386 DKSEK-LIKKIKD-DINLEECKSKIESTLDDKDIDECikKIKELKNHILSEESNIDtyfknaDENNENVLLLFKNIEMAD 1463
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1603 VELEEERKQKSQilAAKKKLEMDLQDMESQMDSANKGRDEA---VKQLKKLQLQFKEVWREVEE------TRAARDEIFV 1673
Cdd:TIGR01612 1464 NKSQHILKIKKD--NATNDHDFNINELKEHIDKSKGCKDEAdknAKAIEKNKELFEQYKKDVTEllnkysALAIKNKFAK 1541
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1674 QSRDNEKKLKSLEAELLQLQEDLAAAERAKRQAQQERDDLADELSNGVSGKSALLDEKRALE------MRISQLEEELDE 1747
Cdd:TIGR01612 1542 TKKDSEIIIKEIKDAHKKFILEAEKSEQKIKEIKKEKFRIEDDAAKNDKSNKAAIDIQLSLEnfenkfLKISDIKKKIND 1621
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1748 EQSNTELINDRYRklTLQVETITTELSAERSFSQKAENARQQMERQNKELKVKLNEMDStMRSKykitIASLEAKISQLE 1827
Cdd:TIGR01612 1622 CLKETESIEKKIS--SFSIDSQDTELKENGDNLNSLQEFLESLKDQKKNIEDKKKELDE-LDSE----IEKIEIDVDQHK 1694
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1785379719 1828 EQME----QESKERIIANKLVRRAEKRLKEVLLQVEEERRNADQFK-----EQLEKANIRM 1879
Cdd:TIGR01612 1695 KNYEigiiEKIKEIAIANKEEIESIKELIEPTIENLISSFNTNDLEgidpnEKLEEYNTEI 1755
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
860-1316 |
6.45e-09 |
|
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: 61.19 E-value: 6.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 860 ELQKVKDTQVKTESELKEMANKYQQLFEEKSILAEQLQAETELFAEAEemrarlaskkqELEEILHDLEARVEEEEERTL 939
Cdd:TIGR04523 174 ELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQIS-----------ELKKQNNQLKDNIEKKQQEIN 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 940 QLQNEKKKMHQHIQDLEEQLEEEEGARQKLQLEKVTTESRLKKMEEDILLLEDQNAKLAKERKllDDRIGEFTSTMAEEE 1019
Cdd:TIGR04523 243 EKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKE--QDWNKELKSELKNQE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1020 EKVKSLNKLRNKYEAVIADLEDRLKKEEKGRQEMEKMKRKLDGETTDLQDQLLELQQQIEELKQQLARKEEELQAALARV 1099
Cdd:TIGR04523 321 KKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKI 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1100 DDEVGQKNNLLKQLRDLQSQLAELHEDLESEKAARAKAEKQRRDLGEELEALKTELEDTLDSTAAQQELRAKREQEVTDL 1179
Cdd:TIGR04523 401 QNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKI 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1180 KKTIEEDVKVRDAQVTEMRQRHNQVVEEISEQLEQARRFKGNLEKVKQtLESENTDLIKEVKNLQAA--KQDSEQRRKKL 1257
Cdd:TIGR04523 481 KQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEK-LESEKKEKESKISDLEDElnKDDFELKKENL 559
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1785379719 1258 EQQVSEFQIR-------TNESEKVKFELAEKLQKLQAELDGVSGALGSTEGKSIKLTKDLSTVQSQ 1316
Cdd:TIGR04523 560 EKEIDEKNKEieelkqtQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKE 625
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1082-1486 |
6.58e-09 |
|
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: 60.99 E-value: 6.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1082 KQQLARKEEELQAALARVDDEVGQkNNLLKQLRD---------------LQSQLAELHEDLESEKAARAKAEKQRRDLGE 1146
Cdd:pfam10174 295 KQELSKKESELLALQTKLETLTNQ-NSDCKQHIEvlkesltakeqraaiLQTEVDALRLRLEEKESFLNKKTKQLQDLTE 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1147 ELEALKTELEDTLDSTAAqqelrakREQEVTDLKKTIE---EDVKVRDAQVTEMRQRHNQVVEEISEQ------LEQARR 1217
Cdd:pfam10174 374 EKSTLAGEIRDLKDMLDV-------KERKINVLQKKIEnlqEQLRDKDKQLAGLKERVKSLQTDSSNTdtalttLEEALS 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1218 FKGN-LEKVKQTLESENTDLIKEVknlqaakQDSEQRRKKLEQQVSEFQIRTNESEKVKFELAEKLQKLQAELDGVSGAL 1296
Cdd:pfam10174 447 EKERiIERLKEQREREDRERLEEL-------ESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKL 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1297 GSTEGKSIKLTKDLSTVQSQLQDTQELlQEETRQKLNFSSRVRQLEEEknnlmENLEEEESAKAQLSRQLQALQQQLLES 1376
Cdd:pfam10174 520 KSLEIAVEQKKEECSKLENQLKKAHNA-EEAVRTNPEINDRIRLLEQE-----VARYKEESGKAQAEVERLLGILREVEN 593
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1377 KKRMEDQggMVEAMEEAKKKSYKELEFLQQRFDEKHQI-------------NDKLEKTRNRLQQELDDLMVDLDHQRQIV 1443
Cdd:pfam10174 594 EKNDKDK--KIAELESLTLRQMKEQNKKVANIKHGQQEmkkkgaqlleearRREDNLADNSQQLQLEELMGALEKTRQEL 671
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1785379719 1444 SNLEKKQKKFDQMLAEEKNISARYGEERDRAEAEAREKETKAL 1486
Cdd:pfam10174 672 DATKARLSSTQQSLAEKDGHLTNLRAERRKQLEEILEMKQEAL 714
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1246-1962 |
2.35e-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: 59.36 E-value: 2.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1246 AKQDSEQRRKKLEQQVSEFQIRTNES----EKVKF-------ELAEKLQKLQAELDgvsgALGSTEGKSIKLTKDLstvQ 1314
Cdd:pfam15921 72 GKEHIERVLEEYSHQVKDLQRRLNESnelhEKQKFylrqsviDLQTKLQEMQMERD----AMADIRRRESQSQEDL---R 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1315 SQLQDTQELLQEETRQKLNFssrvrqLEEEKNNLMENLEEEESAKAQLSRQLQALQQQLLESKKRMEDQGGM----VEAM 1390
Cdd:pfam15921 145 NQLQNTVHELEAAKCLKEDM------LEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSMstmhFRSL 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1391 EEAKKKSYKELE----FLQQRFdekHQINDKLEKTRNRLQQELDDLmvdldhqrqivsnLEKKQKKFDQMLAE-EKNISA 1465
Cdd:pfam15921 219 GSAISKILRELDteisYLKGRI---FPVEDQLEALKSESQNKIELL-------------LQQHQDRIEQLISEhEVEITG 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1466 rygeerdraeaeAREKETKALSLSRALEEAIDLKDELDR-QNKQLRAEMDDLVSSkddVGKNVHELERSKRALEQQVQEM 1544
Cdd:pfam15921 283 ------------LTEKASSARSQANSIQSQLEIIQEQARnQNSMYMRQLSDLEST---VSQLRSELREAKRMYEDKIEEL 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1545 KTQI---------------------EELEDELQAIEDGKLRLEVNMQAMKAQFERdLQNRDDSNDEKKKLLFKQVREMEV 1603
Cdd:pfam15921 348 EKQLvlanseltearterdqfsqesGNLDDQLQKLLADLHKREKELSLEKEQNKR-LWDRDTGNSITIDHLRRELDDRNM 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1604 ELeeerkQKSQILAAKKKLEMDLQdMESQMdSANKGRDEAVKQLKKLQLQF---KEVWREVEETRAARdeifvqsrdnEK 1680
Cdd:pfam15921 427 EV-----QRLEALLKAMKSECQGQ-MERQM-AAIQGKNESLEKVSSLTAQLestKEMLRKVVEELTAK----------KM 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1681 KLKSLEAELLQLQEDLAAAERAKRQAQQERDDLADELSNGVSGKSALLDEKRALEMRISQLEEELDEEQSNTELIndryR 1760
Cdd:pfam15921 490 TLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVI----E 565
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1761 KLTLQVETITTELSAERSFSQKAENARQQMERQNKELKVKLNEMdSTMRSKYKITIASLEAKISQLEEQ---MEQESKER 1837
Cdd:pfam15921 566 ILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEF-KILKDKKDAKIRELEARVSDLELEkvkLVNAGSER 644
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1838 IIAnklVRRAEKRLKEVLLQVEEERRNADQFKEQLE--KANIRMK---------QLKRQLEEAEEEASRANSNRRRLQRE 1906
Cdd:pfam15921 645 LRA---VKDIKQERDQLLNEVKTSRNELNSLSEDYEvlKRNFRNKseemetttnKLKMQLKSAQSELEQTRNTLKSMEGS 721
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*...
gi 1785379719 1907 LEDVTESAESMNREVTTLRSRLR--RAPIQFTTRTIRQVYQLEAVSDEEPESHSGEPS 1962
Cdd:pfam15921 722 DGHAMKVAMGMQKQITAKRGQIDalQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELS 779
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1619-1931 |
3.56e-08 |
|
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: 58.93 E-value: 3.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1619 KKKLEMDLQDMESQMDSANKGRDEAVKQLKKLQ------LQFKEVWREVEETRAArdeifvqsrDNEKKLKSLEAELLQL 1692
Cdd:TIGR02169 172 KEKALEELEEVEENIERLDLIIDEKRQQLERLRrerekaERYQALLKEKREYEGY---------ELLKEKEALERQKEAI 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1693 QEDLAAAERAKRQAQQERDDLADELSngvsgksALLDEKRALEMRISqleeeldeeqsntELINDRYRKLTLQVETITTE 1772
Cdd:TIGR02169 243 ERQLASLEEELEKLTEEISELEKRLE-------EIEQLLEELNKKIK-------------DLGEEEQLRVKEKIGELEAE 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1773 LS-AERSFSQKAENArQQMERQNKELKVKLNEmdstmrskykitiasLEAKISQLEEQMEQESKERIIANKLVRRAEKRL 1851
Cdd:TIGR02169 303 IAsLERSIAEKEREL-EDAEERLAKLEAEIDK---------------LLAEIEELEREIEEERKRRDKLTEEYAELKEEL 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1852 KEVLLQVEEE-------RRNADQFKEQLEKANIRMKQLKRQLEEAEEEASRANSNRRRLQRELEDVTESAESMNREVTTL 1924
Cdd:TIGR02169 367 EDLRAELEEVdkefaetRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDK 446
|
....*..
gi 1785379719 1925 RSRLRRA 1931
Cdd:TIGR02169 447 ALEIKKQ 453
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1615-1921 |
4.94e-08 |
|
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: 58.54 E-value: 4.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1615 ILAAKKKLEMDLQDMESQMDSANKgrdeavkQLKKLQLQFKEVWREVEETRAARDEIFVQSRD-NEKKLKSLEAELLQLQ 1693
Cdd:TIGR02169 228 LLKEKEALERQKEAIERQLASLEE-------ELEKLTEEISELEKRLEEIEQLLEELNKKIKDlGEEEQLRVKEKIGELE 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1694 EDLAAAERAKRQAQQERDDLADELSNGVSGKSALLDEKRALEMRISQLEEELDEEQSNTELINDRYRKLTLQVETITTEL 1773
Cdd:TIGR02169 301 AEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEF 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1774 SAERSFSQKAENARQQMERQNKELKVKLNEMDSTMRsKYKITIASLEAKISQLEEQMEQeskeriianklvrrAEKRLKE 1853
Cdd:TIGR02169 381 AETRDELKDYREKLEKLKREINELKRELDRLQEELQ-RLSEELADLNAAIAGIEAKINE--------------LEEEKED 445
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1785379719 1854 VLLQVEEERRNADQFKEQLEKAnirmkqlKRQLEEAEEEASRANSNRRRLQRELEDVTESAESMNREV 1921
Cdd:TIGR02169 446 KALEIKKQEWKLEQLAADLSKY-------EQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERV 506
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1089-1304 |
6.36e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 57.15 E-value: 6.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1089 EEELQAALARVDDEVGQKNNLLKQLRDLQSQLAELHEDLESEKAARAKAEKQRRDLGEELEALKTELEdtldstAAQQEL 1168
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIE------ERREEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1169 --RAKREQEVTDLKKTIE--------EDVKVRDAQVTEMRQRHNQVVEEISEQLEQARRFKGNLEKVKQTLESENTDLIK 1238
Cdd:COG3883 89 geRARALYRSGGSVSYLDvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1785379719 1239 EVKNLQAAKQDSEQRRKKLEQQVSEFQIRTNESEKVKFELAEKLQKLQAELDGVSGALGSTEGKSI 1304
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAA 234
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1680-1923 |
7.56e-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: 7.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1680 KKLKSLEAELLQLQEDLAAAERAKRQAQQERDDLADELsngvsgksalldekRALEMRISQLEEELDEEQSNTELINDRY 1759
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQL--------------AALERRIAALARRIRALEQELAALEAEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1760 RKLTLQVETITTELSAERSFSQKAENARQQMERQNKeLKVKLNEMDSTMRSKYKITIASLEAKISQLEEQMEQESKERII 1839
Cdd:COG4942 86 AELEKEIAELRAELEAQKEELAELLRALYRLGRQPP-LALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1840 ANKLVRRAEKRLKEVLLQVEEERRNADQFKEQLEKAnirMKQLKRQLEEAEEEASRANSNRRRLQRELEDVTESAESMNR 1919
Cdd:COG4942 165 LRAELEAERAELEALLAELEEERAALEALKAERQKL---LARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
....
gi 1785379719 1920 EVTT 1923
Cdd:COG4942 242 RTPA 245
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1635-1853 |
8.18e-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: 8.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1635 SANKGRDEAVKQLKKLQLQFKEVWREVEETRAARDEIFVQSRDNEKKLKSLEAELLQLQEDLAAAERAKRQAQQERDDLA 1714
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1715 DELSNGVSGKSALLDE----KRALEMRISQLEEELDEEQSNTELINDRYRKLTLQVETITTELSAERSFSQKAENARQQM 1790
Cdd:COG4942 97 AELEAQKEELAELLRAlyrlGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1785379719 1791 ERQNKELKVKLNEMDSTMRSKyKITIASLEAKISQLEEQMEQESKERIIANKLVRRAEKRLKE 1853
Cdd:COG4942 177 EALLAELEEERAALEALKAER-QKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
827-1469 |
8.48e-08 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 57.67 E-value: 8.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 827 LKLRHWQWWRLFTKVKPLLQVTRQDEVMQAKVVELQkvkdTQVKTESELKEMANKYQQlfeeKSILAEQLQAETELFAEA 906
Cdd:TIGR00618 238 TQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELR----AQEAVLEETQERINRARK----AAPLAAHIKAVTQIEQQA 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 907 EEMRARLASKKQELEEILHDLEARVEEEEERTLQLQNEKKKMHQHIQDLEEQLEEEEGARQKLQleKVTTESRLKKMEED 986
Cdd:TIGR00618 310 QRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQ--QHTLTQHIHTLQQQ 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 987 ILLLEDQNAKLAKERKLLDDRIGEFTSTMAEEEE------KVKSLNKLRNKYEAVIADLEDRLKKEEKGRQ-EMEKMKRK 1059
Cdd:TIGR00618 388 KTTLTQKLQSLCKELDILQREQATIDTRTSAFRDlqgqlaHAKKQQELQQRYAELCAAAITCTAQCEKLEKiHLQESAQS 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1060 LDGETTDLQDQLLELQQQIEELKQQLARKEE-----------ELQAALARVD-DEVGQKNNLLKQLRDLQSQLAELHEDL 1127
Cdd:TIGR00618 468 LKEREQQLQTKEQIHLQETRKKAVVLARLLElqeepcplcgsCIHPNPARQDiDNPGPLTRRMQRGEQTYAQLETSEEDV 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1128 ESEKAARakaEKQRRDLGEELEALKTELEDTLDSTAAQQELRAKREQEVTDLKKTIEEDVKVRDAQVTEMRQRHNQVVEE 1207
Cdd:TIGR00618 548 YHQLTSE---RKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPE 624
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1208 ISEQLEQA--RRFKGNLEKVKQTLESENTDLIKE--VKNLQAAKQDSEQRRKKLEQQVSEFQIRTNESEKVKFELAEKLQ 1283
Cdd:TIGR00618 625 QDLQDVRLhlQQCSQELALKLTALHALQLTLTQErvREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQT 704
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1284 KLQAELDGVSGALGSTEGKSIKLTKDLSTVQSQLQDTQELLQEETRQklnfssRVRQLEEEKNNLMENLEEEESAKAQLS 1363
Cdd:TIGR00618 705 LLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQ------ARTVLKARTEAHFNNNEEVTAALQTGA 778
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1364 RQLQALQQQLLESKKRMEDQGGMVEAMEEAKKKSYkelEFLQQRFDEKHQINDKLEKTRNRLqQELDDLMVDLDHQRQiv 1443
Cdd:TIGR00618 779 ELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIP---SDEDILNLQCETLVQEEEQFLSRL-EEKSATLGEITHQLL-- 852
|
650 660
....*....|....*....|....*.
gi 1785379719 1444 sNLEKKQKKFDQMLAEEKNISARYGE 1469
Cdd:TIGR00618 853 -KYEECSKQLAQLTQEQAKIIQLSDK 877
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1083-1292 |
1.26e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.23 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1083 QQLARKEEELQAALARVDdevgqknnLLKQLRDLQSQLAELHEDLESEKAARAK-----AEKQRRDLGEELEALKTELED 1157
Cdd:COG4913 235 DDLERAHEALEDAREQIE--------LLEPIRELAERYAAARERLAELEYLRAAlrlwfAQRRLELLEAELEELRAELAR 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1158 TLDSTAAQQELRAKREQEVTDLKKTIEEDVkvrDAQVTEMRQRHNQVVEEISEQLEQARRFKGNLEKVKQTLESENTDLI 1237
Cdd:COG4913 307 LEAELERLEARLDALREELDELEAQIRGNG---GDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFA 383
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1785379719 1238 KEVKNLQAAKQDSEQRRKKLEQQVSEfqirtneSEKVKFELAEKLQKLQAELDGV 1292
Cdd:COG4913 384 ALRAEAAALLEALEEELEALEEALAE-------AEAALRDLRRELRELEAEIASL 431
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
860-1244 |
1.76e-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: 56.57 E-value: 1.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 860 ELQKVKDTQVKTESELKEMANKYQQLFEEKSILAEQLqaeTELFAEAEEMRARLASKKQELEEILHDLEARVEEEEertl 939
Cdd:TIGR04523 315 ELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKEL---TNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIK---- 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 940 QLQNEKKKMHQHIQDLEEQLEEEegarqklqlekvttESRLKKMEEDILLLEDQNAKLAKERKLLDDRIGEFTSTMAEEE 1019
Cdd:TIGR04523 388 NLESQINDLESKIQNQEKLNQQK--------------DEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKE 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1020 EKVKSLNKLRNKYEAVIADLEDRLKKEEkgrQEMEKMKRKLDGETTDLQDQLLELQQQIEELKqQLARKEEELQAALARV 1099
Cdd:TIGR04523 454 LIIKNLDNTRESLETQLKVLSRSINKIK---QNLEQKQKELKSKEKELKKLNEEKKELEEKVK-DLTKKISSLKEKIEKL 529
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1100 DDEVGQKNNllkQLRDLQSQLAELHEDLESEkaaraKAEKQRRDLGEELEALKTELEDTLDSTAAQQELRAKREQEVTDL 1179
Cdd:TIGR04523 530 ESEKKEKES---KISDLEDELNKDDFELKKE-----NLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDL 601
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1785379719 1180 KKTIEEdvkvrdaqvtemrqrHNQVVEEISEQLEQARRFKGNLEKVKQTLESENTDLIKEVKNLQ 1244
Cdd:TIGR04523 602 IKEIEE---------------KEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIK 651
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1177-1883 |
1.78e-07 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 56.27 E-value: 1.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1177 TDLKKTIEEDVKVRDAQVTEMRQRHNQVVEE---ISEQLEQARRFKGNLEKVKQTLE---SENTDLIKEVKNLQAAKQDS 1250
Cdd:pfam05483 81 SKLYKEAEKIKKWKVSIEAELKQKENKLQENrkiIEAQRKAIQELQFENEKVSLKLEeeiQENKDLIKENNATRHLCNLL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1251 EQRRKKLEQQVSEFQIRTNESEKVKFELAEKLQKLQAELDGVS-GALGSTEGKSIKLTKDLSTVQSQLQDTQELLQEETR 1329
Cdd:pfam05483 161 KETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRvQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEK 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1330 QklnFSSRVRQLEEEKNNLMENLEEEESAKAQLSRQLQALQQQLLESKKRMEDQGGMVEAMEEAKKKSYKELEfLQQRFD 1409
Cdd:pfam05483 241 Q---VSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMS-TQKALE 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1410 EKHQIndkLEKTRNRLQQELDDLMVDLDHQRQ----IVSNLEKKQKKFDQMLAEEKNisaRYGEERDRAEAEAREKETKa 1485
Cdd:pfam05483 317 EDLQI---ATKTICQLTEEKEAQMEELNKAKAahsfVVTEFEATTCSLEELLRTEQQ---RLEKNEDQLKIITMELQKK- 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1486 lslSRALEEAIDLKDELDRQNKQLR---AEMDDLVSSKDDVGKNVHELERSKRALEQQVQEMKTQIEELEDELQAIEDGK 1562
Cdd:pfam05483 390 ---SSELEEMTKFKNNKEVELEELKkilAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSE 466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1563 LRLEVNMQAMKAQFERDLQNRDDSNDEKKKLLFKQVREMEVELE---EERKQKSQILAAKKKLEMDLQDMESQMDSANKG 1639
Cdd:pfam05483 467 EHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDmtlELKKHQEDIINCKKQEERMLKQIENLEEKEMNL 546
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1640 RDEAVKQLKKLQLQFKEVWREVEETRAARDEIFVQSRDNEKKLKSLEAELLQLQEDLAAAERAKRQAQQERDDLADElsn 1719
Cdd:pfam05483 547 RDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKK--- 623
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1720 gvsgKSALLDEKRALEMRISQLEEELDEEQSNTELINDRYRKlTLQVETITTELSAERSFSQK--AENARQQMERQNKEL 1797
Cdd:pfam05483 624 ----GSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQK-EIEDKKISEEKLLEEVEKAKaiADEAVKLQKEIDKRC 698
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1798 KVKLNEMDSTM---RSKYKITIASLEAKISQLEEQMEQESKERIIANKLVRRAEKRLKEVLLQVEEERRNADQFKEQLEK 1874
Cdd:pfam05483 699 QHKIAEMVALMekhKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKE 778
|
....*....
gi 1785379719 1875 ANIRMKQLK 1883
Cdd:pfam05483 779 NTAILKDKK 787
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
846-1260 |
2.09e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.93 E-value: 2.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 846 QVTRQDEVMQAKVVELQKVKDTQVKTESELKEMANKYQQLFEEKSILAEQLQAEtELFAEAEEMRARLASKKQELEEI-- 923
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLL-PLYQELEALEAELAELPERLEELee 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 924 ----LHDLEARVEEEEERTLQLQNEKKK--------MHQHIQDLEEQLEEEEGARQKLQLEKVTTESRLKKMEEDILLLE 991
Cdd:COG4717 154 rleeLRELEEELEELEAELAELQEELEElleqlslaTEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLE 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 992 DQNAKLAKERKLLDDR--------IGEFTSTMAEEEEKVKSLNKLRNKYEAVIADLEDRLKKEEKGRQEMEKMKRKLDGE 1063
Cdd:COG4717 234 NELEAAALEERLKEARlllliaaaLLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPAL 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1064 TTDLQDQLLELQQQIEELKQQLARKEEELQAALARVDDEVGQKNNLLKQLR------DLQSQLAELHEDLESEKAARAKA 1137
Cdd:COG4717 314 EELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQleeleqEIAALLAEAGVEDEEELRAALEQ 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1138 EKQRRDLGEELEALKTELEDTLDstAAQQELRAKREQEVTDLKKTIEEDVKVRDAQVTEMRQRHNQVVEEIsEQLEQARR 1217
Cdd:COG4717 394 AEEYQELKEELEELEEQLEELLG--ELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAEL-EQLEEDGE 470
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1785379719 1218 FkGNLEKVKQTLESENTDLIKEVKNLQAAKQDSEQRRKKLEQQ 1260
Cdd:COG4717 471 L-AELLQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1409-1928 |
2.17e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 56.20 E-value: 2.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1409 DEKHQINDKLEK----TRNRLQQELDDLMVDLDHqrqivsnLEKKQKKFDQMLAEEKNISARYGEERDRAEaearEKETK 1484
Cdd:PRK02224 191 QLKAQIEEKEEKdlheRLNGLESELAELDEEIER-------YEEQREQARETRDEADEVLEEHEERREELE----TLEAE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1485 ALSLSRALEEAIDLKDELDRQNKQLRAEMDDLVSSKDDVGKNVHELERSKRALEQQVQEMKTQIEELEDELQAIEdgklr 1564
Cdd:PRK02224 260 IEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECR----- 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1565 leVNMQAMKAQFERDLQNRDDSNDEKKKLLFKQVR---EMEVELEEERKQKSQILAAKKKLE----------MDLQDMES 1631
Cdd:PRK02224 335 --VAAQAHNEEAESLREDADDLEERAEELREEAAElesELEEAREAVEDRREEIEELEEEIEelrerfgdapVDLGNAED 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1632 QMDSANKGRDEAVKQLKKLQLQFKEVWREVEETRAARDE--------------IFVQSRDNEKKLKSLEAELLQLQEDLA 1697
Cdd:PRK02224 413 FLEELREERDELREREAELEATLRTARERVEEAEALLEAgkcpecgqpvegspHVETIEEDRERVEELEAELEDLEEEVE 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1698 AAErakrqaqqERDDLADELSNGVSGKSALLDEKRALEMRISQLEEELDEEQSNTELINDRyrkltlqVETITTELSAER 1777
Cdd:PRK02224 493 EVE--------ERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRER-------AAELEAEAEEKR 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1778 SFSQKAENARQQMERQNKELKVKLNEMDSTMRSKYKI-----TIASLEAKISQLEEQ------MEQESKERIianklvrr 1846
Cdd:PRK02224 558 EAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIrtllaAIADAEDEIERLREKrealaeLNDERRERL-------- 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1847 AEKRlkevllqvEEERRNADQFKE-QLEKANIRMKQLKRQLEEAEEEASRANSNRRRLQRELEDVTESAESMNrevtTLR 1925
Cdd:PRK02224 630 AEKR--------ERKRELEAEFDEaRIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELE----ELR 697
|
...
gi 1785379719 1926 SRL 1928
Cdd:PRK02224 698 ERR 700
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1090-1512 |
2.82e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.54 E-value: 2.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1090 EELQAALARVDDEVGQKNNLLKQLRDLQSQLAELHEDLES--EKAARAKAEKQRRDLGEELEALKTELEDT---LDSTAA 1164
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEElrEELEKLEKLLQLLPLYQELEALEAELAELperLEELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1165 QQELRAKREQEVTDLKKTIEEDVKVRDAQVTEMRQRHNQVVEEISEQLEQARRFKGNLEKVKQTLESENTDLIKEVKNLQ 1244
Cdd:COG4717 154 RLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLE 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1245 AAKQDsEQRRKKLEQQVSEFQIRTnesekVKFELAEKLQKLQAELDGVSGALGSTEG----KSIKLTKDLSTVQSQLQDT 1320
Cdd:COG4717 234 NELEA-AALEERLKEARLLLLIAA-----ALLALLGLGGSLLSLILTIAGVLFLVLGllalLFLLLAREKASLGKEAEEL 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1321 QELLQEETRQKLNFSSRVRQLEEEKNNLMENLEEEESaKAQLSRQLQALQQQLLESKKRMEDQGGMVEAMEEAKKKSYKE 1400
Cdd:COG4717 308 QALPALEELEEEELEELLAALGLPPDLSPEELLELLD-RIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEE 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1401 LEFLQQRFDEKHQINDKLEKTRNRLQQELDDLMVDLDHQrqivsNLEKKQKKFDQMLAEEKNISARYgeERDRAEAEARE 1480
Cdd:COG4717 387 LRAALEQAEEYQELKEELEELEEQLEELLGELEELLEAL-----DEEELEEELEELEEELEELEEEL--EELREELAELE 459
|
410 420 430
....*....|....*....|....*....|..
gi 1785379719 1481 KETKALSLSRALEEAIDLKDELDRQNKQLRAE 1512
Cdd:COG4717 460 AELEQLEEDGELAELLQELEELKAELRELAEE 491
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
873-1463 |
4.18e-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: 55.03 E-value: 4.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 873 SELKEMANKYQQLFEEKSILAEQLQAETELFAEAEEMRARLASKKQELEEILHDLEARVEEEEERTLQLQNEKKKMHQHI 952
Cdd:TIGR04523 89 DKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQK 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 953 QDLEEQLEEEEGARQKLQLEKVTTESRLKKMEEDILLLEdqnaKLAKERKLLDDRIGEFTSTMAEEEEKVKSLNKLRNKY 1032
Cdd:TIGR04523 169 EELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLK----KKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEK 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1033 EAVIADLEDRLKKEekgRQEMEKMKRKLDGETtdlqdqllelqQQIEELKQQLARKEEELQAALARVDDEVGQKNNLLkq 1112
Cdd:TIGR04523 245 TTEISNTQTQLNQL---KDEQNKIKKQLSEKQ-----------KELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDW-- 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1113 LRDLQSQLAELHEDLESEKAARAKAEKQRRDLGEELEALKTELED-TLDSTAAQQELRAKrEQEVTDLKKTIEEDVKvrd 1191
Cdd:TIGR04523 309 NKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNsESENSEKQRELEEK-QNEIEKLKKENQSYKQ--- 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1192 aQVTEMRQRHNQVVEEISEQLEQARRFKGNLEKvkqtLESENTDLIKEVKNLQAAKQDSEQRRKKLEQQVSEFQIRTNES 1271
Cdd:TIGR04523 385 -EIKNLESQINDLESKIQNQEKLNQQKDEQIKK----LQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNL 459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1272 EKVKFELAEKLQKLQAELDGVSGALGSTEGKSIKLTKDLSTVQSQLQDTQELLQEETRQKLNFSSRVRQLEEEKnnlmen 1351
Cdd:TIGR04523 460 DNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEK------ 533
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1352 leeeesakaqlsrQLQALQQQLLESKKRMEDQGGMVEAMEEAKKKSYKELEFLQQRFDEKHQINDKLEKTRNRLQQELDD 1431
Cdd:TIGR04523 534 -------------KEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKD 600
|
570 580 590
....*....|....*....|....*....|....*.
gi 1785379719 1432 LMVDLDHQRQIVSNLEKK----QKKFDQMLAEEKNI 1463
Cdd:TIGR04523 601 LIKEIEEKEKKISSLEKElekaKKENEKLSSIIKNI 636
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1474-1702 |
4.71e-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: 54.38 E-value: 4.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1474 AEAEAREKETKALSLSRALEEAIDLKDELDRQNKQLRAEMDDLVSSKDDVGKNVHELERSKRALEQQVQEMKTQIEELED 1553
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1554 ELQAIEDGKLRLEVNMQAMKAQ-FERDLQNRDDSNDEKKKL-LFKQVREMEVELEEERKQKSQILAAKKklemdlQDMES 1631
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRQpPLALLLSPEDFLDAVRRLqYLKYLAPARREQAEELRADLAELAALR------AELEA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1785379719 1632 QMDSANKGRDEAVKQLKKLQLQFKEVWREVEETRAARDEIFVQSRDNEKKLKSLEAELLQLQEDLAAAERA 1702
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1011-1232 |
6.12e-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: 54.00 E-value: 6.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1011 FTSTMAEEEEKVKSLNKLRNKYEAVIADLEDRLKKEEKGRQEMEKMKRKLDGETTDLQDQLLELQQQIEELKQQLARKEE 1090
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1091 ELQAALARVDDevgQKNNLLKQLRDLQ--SQLAELHEDLESEKAARA--------KAEKQRRDLGEELEALKTELEDTLD 1160
Cdd:COG4942 91 EIAELRAELEA---QKEELAELLRALYrlGRQPPLALLLSPEDFLDAvrrlqylkYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1785379719 1161 STAAQQELRAKREQEVTDLKKTIEEDVKVRDAQVTEMRQRHNQVVEEISEQLEQARRFKGNLEKVKQTLESE 1232
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1485-1718 |
6.51e-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: 54.00 E-value: 6.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1485 ALSLSRALEEAIDLKDELDRQNKQLRAEMDDLVSSKDDVGKNVHELERSKRALEQQVQEMKTQIEELEDELQAIEDGKLR 1564
Cdd:COG4942 8 ALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1565 LEVNMQAMKAQferdLQNRDDSNDEKKKLLFKQVREMEVELEEERKQKSQILAAKKKLEMDLQDMESQMDSANKGRDEAV 1644
Cdd:COG4942 88 LEKEIAELRAE----LEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1785379719 1645 KQLKKLQLQFKEVWREVEETRAARDEIFVQSRDNEKKLKSLEAELLQLQEDLAAAERAKRQAQQERDDLADELS 1718
Cdd:COG4942 164 ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
992-1217 |
6.68e-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: 54.00 E-value: 6.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 992 DQNAKLAKERKLLDDRIGEFTSTMAEEEEKVKSLNKLRNKYEAVIADLEDRLKKEEKGRQEMEKMKRKLDGETTDLQDQL 1071
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1072 LELQQQIEELKQQLARKEEELQAALARVDDEVGQKNNLLKQLRDLQSQLAELHEDLESEKAARAKAEKQRRDLGEELEAL 1151
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1785379719 1152 KTELEDTLdstAAQQELRAKREQEVTDLKKTIEEDvKVRDAQVTEMRQRHNQVVEEISEQLEQARR 1217
Cdd:COG4942 180 LAELEEER---AALEALKAERQKLLARLEKELAEL-AAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
979-1187 |
6.98e-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: 52.62 E-value: 6.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 979 RLKKMEEDILLLEDQNAKLAKERKLLDDRIGEFTSTMAEEEEKVKSLNKLRNKYEAVIADLEDRLKKEEKgrqemekmkr 1058
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE---------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1059 kldgettdlqdqllelqqqieelKQQLARKEEELQAALARVDdevgqknNLLKQLRDLQSQLAELHEDLESEKAARAKAE 1138
Cdd:COG1579 81 -----------------------QLGNVRNNKEYEALQKEIE-------SLKRRISDLEDEILELMERIEELEEELAELE 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1139 KQRRDLGEELEALKTELEDTLDSTAAQ-QELRAKREQevtdLKKTIEEDV 1187
Cdd:COG1579 131 AELAELEAELEEKKAELDEELAELEAElEELEAEREE----LAAKIPPEL 176
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1389-1593 |
1.03e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 53.23 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1389 AMEEAKKKSYKELEFLQQRFDEKHQINDKLEKTRNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLA----EEKNIS 1464
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAelekEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1465 ARYGEERDR-------AEAEAREKETKALSLSRALEEAIDLKDELDRQNKQLRAEMDDLVSSKDDVGKNVHELERSKRAL 1537
Cdd:COG4942 97 AELEAQKEElaellraLYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1785379719 1538 EQQVQEMKTQIEELEDELQAIEDGKLRLEVNMQAMKAQFERDLQNRDDSNDEKKKL 1593
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1429-1944 |
1.20e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.91 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1429 LDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKNISARYGEERDRAEAEAREketkalsLSRALEEAIDLKDELDRQNKQ 1508
Cdd:PRK03918 157 LDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLRE-------INEISSELPELREELEKLEKE 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1509 LRaEMDDLVSSKDDVGKNVHELERSKRALEQQVQEMKTQIEELEDELQAIEDGKLRLEvNMQAMKAQFERDLQNRDDSND 1588
Cdd:PRK03918 230 VK-ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK-ELKEKAEEYIKLSEFYEEYLD 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1589 EKKKLlfkqvremeveLEEERKQKSQILAAKKKLEmDLQDMESQMDSANKGRDEAVKQLKKLQ---LQFKEVWREVEETR 1665
Cdd:PRK03918 308 ELREI-----------EKRLSRLEEEINGIEERIK-ELEEKEERLEELKKKLKELEKRLEELEerhELYEEAKAKKEELE 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1666 AARDEIFVQSRDN-EKKLKSLEAELLQLQEDLAAAERAKRQAQQERDDLADELSNGVSGKS------ALLDEKRALEMrI 1738
Cdd:PRK03918 376 RLKKRLTGLTPEKlEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGkcpvcgRELTEEHRKEL-L 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1739 SQLEEELDEEQSNTELINDRYRKLTLQVETITTELSAERSFSQKAENARQQMERQNKELKVKLNEM--DSTMRSKYKITI 1816
Cdd:PRK03918 455 EEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELekKAEEYEKLKEKL 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1817 ASLEAKISQLEEQMEQES---KERIIANKLVRRAEKRLKEVLLQVEEERRnadqfkEQLEKANIRMKQLKR------QLE 1887
Cdd:PRK03918 535 IKLKGEIKSLKKELEKLEelkKKLAELEKKLDELEEELAELLKELEELGF------ESVEELEERLKELEPfyneylELK 608
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1785379719 1888 EAEEEASRANSNRRRLQRELEDVTESAESMNREVTTLRSRLRRAPIQFTTRTIRQVY 1944
Cdd:PRK03918 609 DAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELR 665
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1645-1957 |
1.95e-06 |
|
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: 53.14 E-value: 1.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1645 KQLKKLQLQfkevwreveeTRAARDEIFVQSRDNEKKLKSLEAELLQLQEDLAAAERAKRQAQQERDDLADELSNGVSGK 1724
Cdd:TIGR02168 200 RQLKSLERQ----------AEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1725 SALLDEKRALEMRIsqleeeldeeqsntELINDRYRKLTLQVETITTELsaersfsQKAENARQQMERQNKELKVKLNEM 1804
Cdd:TIGR02168 270 EELRLEVSELEEEI--------------EELQKELYALANEISRLEQQK-------QILRERLANLERQLEELEAQLEEL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1805 DStMRSKYKITIASLEAKISQLEEQMEQESKERIIANKLVRRAEKRLKEVllqveeerrnadqfKEQLEKANIRMKQLKR 1884
Cdd:TIGR02168 329 ES-KLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEEL--------------EEQLETLRSKVAQLEL 393
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1785379719 1885 QLEeaeeeasRANSNRRRLQRELEDVTESAESMNREVTTLRSRLRRAPIQFTTRTIRQVYQLEAVSDEEPESH 1957
Cdd:TIGR02168 394 QIA-------SLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERL 459
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1469-1696 |
2.24e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 51.45 E-value: 2.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1469 EERDRAEAEAREKETKALSLSRALEEAIDLKDELDRQNKQLRAEMDDLVSSKDDVGKNVHELERSKRALEQQVQEMKTQI 1548
Cdd:COG1340 15 EKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREEL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1549 EELEDELQAIEDGKLRLEvNMQAMKAQFERDLQNRDDSNDEKKKLL--FKQVREMEVELEEERKQKSQILAAKKKLEmdl 1626
Cdd:COG1340 95 DELRKELAELNKAGGSID-KLRKEIERLEWRQQTEVLSPEEEKELVekIKELEKELEKAKKALEKNEKLKELRAELK--- 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1627 qDMESQMDSANKGRDEAVKQLKKLQLQFKEVWREVEETRAARDEIFVQSRDNEKKLKSLEAELLQLQEDL 1696
Cdd:COG1340 171 -ELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKEL 239
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1758-1953 |
2.46e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.63 E-value: 2.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1758 RYRKLTLQVETITTELSAERSFSQKAENARQQMERQNKELKVKLNEMDSTMRSKyKITIASLEAKISQLEEQMEQESKER 1837
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEA-QAEEYELLAELARLEQDIARLEERR 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1838 IIANKLVRRAEKRLKEVLLQVEEERRNADQFKEQLEKANIRMKQLKRQLEEAEEEASRANSNRRRLQRELEDVTESAESM 1917
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
|
170 180 190
....*....|....*....|....*....|....*.
gi 1785379719 1918 NREVTTLRSRLRRAPIQFTTRTIRQVYQLEAVSDEE 1953
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELE 427
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1662-1934 |
2.66e-06 |
|
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: 52.76 E-value: 2.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1662 EETRAARDEIfVQSRDNEKKLKSLEAELLQ----LQEDLAAAERAKRQAQQERDDLADELSNGvsgKSALLDEKRALEMR 1737
Cdd:TIGR02169 170 RKKEKALEEL-EEVEENIERLDLIIDEKRQqlerLRREREKAERYQALLKEKREYEGYELLKE---KEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1738 ISQLEEELDEEQSNTELINDRYRKLTLQVETITTELSAERSfsqkaenarqqmERQNkELKVKLNEMdstmrskyKITIA 1817
Cdd:TIGR02169 246 LASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGE------------EEQL-RVKEKIGEL--------EAEIA 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1818 SLEAKISQLEEQMEQESKERIIANKLVRRAEKRLKEVLLQVEEERRNADQFKEQLEKANIRMKQLKRQLEEAEEEASRAN 1897
Cdd:TIGR02169 305 SLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETR 384
|
250 260 270
....*....|....*....|....*....|....*..
gi 1785379719 1898 SNRRRLQRELEDVTESAESMNREVTTLRSRLRRAPIQ 1934
Cdd:TIGR02169 385 DELKDYREKLEKLKREINELKRELDRLQEELQRLSEE 421
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
947-1708 |
3.40e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 52.28 E-value: 3.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 947 KMHQHIQDLEEQLEEEEGARQKLQLEKVTTESRLKKMEEDILLLEDQNAKLAKERKLLDDRIGEFTSTMAEEEEKVKSLN 1026
Cdd:TIGR00618 174 PLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQE 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1027 KlRNKYEAVIADLEDRLKKEEKGRQEMEKMKRKLDgeTTDLQDQLLELQQQIEELKQQLARKEEELQAALARVDDEVGQK 1106
Cdd:TIGR00618 254 E-QLKKQQLLKQLRARIEELRAQEAVLEETQERIN--RARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKR 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1107 NNLLKQLRDLQSQLAELHEDLESEKAARAKAEKQRRDLGEELEAlkTELEDTLDSTAAQQELRAKREQEVTDLKKTIEED 1186
Cdd:TIGR00618 331 AAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQ--HTLTQHIHTLQQQKTTLTQKLQSLCKELDILQRE 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1187 VKVRDAQVTEMR-QRHNQVVEEISEQLEQARrfkgnLEKVKQTLESENTDLIKEVKNLQAAKQdSEQRRKKLEQQVSEFQ 1265
Cdd:TIGR00618 409 QATIDTRTSAFRdLQGQLAHAKKQQELQQRY-----AELCAAAITCTAQCEKLEKIHLQESAQ-SLKEREQQLQTKEQIH 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1266 IRTNESEKVKFELAEKLQKLQAELDGVSGALGSTEGKSIKLTKDLSTVQSQLQDTQELLQEETRQKLNFSSRVRQLEEEK 1345
Cdd:TIGR00618 483 LQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLK 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1346 NNLMENLEEEEsakaqlsrqlqalqqqlleskkrmedqggmveAMEEAKKKSYKELEFLQQRFDEKHQINDKLEKTRNRL 1425
Cdd:TIGR00618 563 EQMQEIQQSFS--------------------------------ILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDML 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1426 QQELDDLMVDLDHQrQIVSNLEKKQKKFDQMLAEEKNISARYGEERdraeaeAREKETKALSLSRALEEaidlkdeldRQ 1505
Cdd:TIGR00618 611 ACEQHALLRKLQPE-QDLQDVRLHLQQCSQELALKLTALHALQLTL------TQERVREHALSIRVLPK---------EL 674
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1506 NKQLRAEMDDLVSSKDDVGKNVHELERSKRALeqqvQEMKTQIEELEDELQAIEdgklrlevnmQAMKAQfERDLQNRDD 1585
Cdd:TIGR00618 675 LASRQLALQKMQSEKEQLTYWKEMLAQCQTLL----RELETHIEEYDREFNEIE----------NASSSL-GSDLAARED 739
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1586 SNDEKKKLLFKQVREMEVELEEERKQKSQILAAKKKLEMDLQDMESQMDSANKGRDEAVKQLKKLQLQFKEVWREVEETR 1665
Cdd:TIGR00618 740 ALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDIL 819
|
730 740 750 760
....*....|....*....|....*....|....*....|....
gi 1785379719 1666 AARDEIFVQSRDNEK-KLKSLEAELLQLQEDLAAAERAKRQAQQ 1708
Cdd:TIGR00618 820 NLQCETLVQEEEQFLsRLEEKSATLGEITHQLLKYEECSKQLAQ 863
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1680-1931 |
3.44e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.25 E-value: 3.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1680 KKLKSLEAELLQLQEDLAAAERAKRQAQQERddLADELSNGVSGKSALLDEKRALEMRISQLEEELDEEQSNTELINDRY 1759
Cdd:COG1196 213 ERYRELKEELKELEAELLLLKLRELEAELEE--LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1760 RKLTLQVETITTELSAERsfsQKAENARQQMERQNKElkvklnemdstmrskykitIASLEAKISQLEEQMEQESKERII 1839
Cdd:COG1196 291 YELLAELARLEQDIARLE---ERRRELEERLEELEEE-------------------LAELEEELEELEEELEELEEELEE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1840 ANKLVRRAEKRLKevllQVEEERRNAdqfKEQLEKANIRMKQLKRQLEEAEEEASRANSNRRRLQRELEDVTESAESMNR 1919
Cdd:COG1196 349 AEEELEEAEAELA----EAEEALLEA---EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421
|
250
....*....|..
gi 1785379719 1920 EVTTLRSRLRRA 1931
Cdd:COG1196 422 ELEELEEALAEL 433
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1147-1804 |
3.68e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 52.35 E-value: 3.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1147 ELEALKTELEDTLDSTAAQQELRAKREQEVTDLKKTIEEDV-KVRDAQVTEMRQRHNQVVEEIS---EQLEQARRFKGNL 1222
Cdd:PRK02224 160 QLGKLEEYRERASDARLGVERVLSDQRGSLDQLKAQIEEKEeKDLHERLNGLESELAELDEEIEryeEQREQARETRDEA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1223 EKV----KQTLEsENTDLIKEVKNLQAAKQDSEQRRKKLEQQVSEFQIRTNEsekvkfeLAEKLQKLQAELDGVSGALGS 1298
Cdd:PRK02224 240 DEVleehEERRE-ELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEE-------LEEERDDLLAEAGLDDADAEA 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1299 TEGKSIKLTKDLSTVQSQLQDTQELLQEETRQKLNFSSRVRQLEEEKNNLMENLEEEESAkaqlsrqlqalqqqLLESKK 1378
Cdd:PRK02224 312 VEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESE--------------LEEARE 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1379 RMEDQGGMVEAMEEAKKKSYKELEFLQQRFDEKHQINDKLEKTRNRLQQELDDLMVDLdhqrqivSNLEKKQKKFDQMLA 1458
Cdd:PRK02224 378 AVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATL-------RTARERVEEAEALLE 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1459 EEKNISARYGEERDRAEAEAREKETKALSLSRALEeaiDLKDELDRQNKQL-RAEmdDLVSSKDDVGKnvheLERSKRAL 1537
Cdd:PRK02224 451 AGKCPECGQPVEGSPHVETIEEDRERVEELEAELE---DLEEEVEEVEERLeRAE--DLVEAEDRIER----LEERREDL 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1538 EQQVQEMKTQIEELEDELQAIEDGKLRLEVNMQAMKAQFERDLQNRDDSNDEKKKLlfkqvremeveleeerkqksqila 1617
Cdd:PRK02224 522 EELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAEL------------------------ 577
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1618 akkklEMDLQDMESQMDSANKGRDeavkqlkkLQLQFKEVWREVEETRAARDEIFVQSRDNEKKLKSLEAELLQLQEDLA 1697
Cdd:PRK02224 578 -----NSKLAELKERIESLERIRT--------LLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFD 644
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1698 AAERAKRQAQQERddlADELSNGVSGKSALLDEKR-ALEMRISQLEeeldEEQSNTELINDRYRKLTLQVETITTELSAE 1776
Cdd:PRK02224 645 EARIEEAREDKER---AEEYLEQVEEKLDELREERdDLQAEIGAVE----NELEELEELRERREALENRVEALEALYDEA 717
|
650 660
....*....|....*....|....*....
gi 1785379719 1777 RSFSQKAENARQQMERQNKE-LKVKLNEM 1804
Cdd:PRK02224 718 EELESMYGDLRAELRQRNVEtLERMLNET 746
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1630-1849 |
4.03e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 51.37 E-value: 4.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1630 ESQMDSANKGRDEAVKQLKKLQLQFKEVWREVEETRAARDEIfvqsrdnEKKLKSLEAELLQLQEDLAAAERAKRQAQQE 1709
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNEL-------QAELEALQAEIDKLQAEIAEAEAEIEERREE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1710 RDDLADEL---SNGVSGKSALLDEKRALEMrisqleeelDEEQSNTELINDRYRKLTLQVETITTELSAERSfsqKAENA 1786
Cdd:COG3883 88 LGERARALyrsGGSVSYLDVLLGSESFSDF---------LDRLSALSKIADADADLLEELKADKAELEAKKA---ELEAK 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1785379719 1787 RQQMERQNKELKVKLNEMDSTmRSKYKITIASLEAKISQLEEQMEQESKERIIANKLVRRAEK 1849
Cdd:COG3883 156 LAELEALKAELEAAKAELEAQ-QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAA 217
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1082-1286 |
4.98e-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: 4.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1082 KQQLARKEEELQAALAR--VDDEVGQKNNLLKQLRDLQSQLAELhedleseKAARAKAEKQRRDLGEELEALKTELEDTL 1159
Cdd:COG3206 188 RKELEEAEAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAEA-------RAELAEAEARLAALRAQLGSGPDALPELL 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1160 DSTAAQQELRAKREQEvtdlkktieedvkvrdAQVTEMRQR----HNQVVeEISEQLEQARR-FKGNLEKVKQTLESENT 1234
Cdd:COG3206 261 QSPVIQQLRAQLAELE----------------AELAELSARytpnHPDVI-ALRAQIAALRAqLQQEAQRILASLEAELE 323
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1785379719 1235 DLIKEVKNLQAAKQDSEQRRKKLEQQVSEFQIRTNESEKVKFELAEKLQKLQ 1286
Cdd:COG3206 324 ALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLE 375
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1500-1931 |
7.28e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.92 E-value: 7.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1500 DELDRQNKQLRAEMDDLvsskddvgknvHELERSKRALEQQVQEMKTQIEELEDELQAIEDGKLRLEVnmqamkAQFERD 1579
Cdd:COG4717 74 KELEEELKEAEEKEEEY-----------AELQEELEELEEELEELEAELEELREELEKLEKLLQLLPL------YQELEA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1580 LQNRDDSNDEKKKLLFKQVREMEVELEEERKQKSQILAAKKKLEMDLQD----MESQMDSANKGRDEAVKQLKKLQLQFK 1655
Cdd:COG4717 137 LEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQlslaTEEELQDLAEELEELQQRLAELEEELE 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1656 EVWREVEETRAARDEIFVQSRDNEKKLKSLEAELLQLQEDLAAAERAKRQAQQERDD-----LADELSNGVSGKSALLDE 1730
Cdd:COG4717 217 EAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILtiagvLFLVLGLLALLFLLLARE 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1731 KRALEMRISQLEEELDEEQSNTELINDRYRKLTLQVETITTELSAERSFSQKAENARQQMERQNKELKVK--LNEMDSTM 1808
Cdd:COG4717 297 KASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEelEQEIAALL 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1809 RSKYKITIASLEAKISQLEEQMEQESKeriianklVRRAEKRLKEVLLQVEEERRNADqfKEQLEKaniRMKQLKRQLEE 1888
Cdd:COG4717 377 AEAGVEDEEELRAALEQAEEYQELKEE--------LEELEEQLEELLGELEELLEALD--EEELEE---ELEELEEELEE 443
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1785379719 1889 AEEEASRANSNRRRLQRELEDVTESAE--SMNREVTTLRSRLRRA 1931
Cdd:COG4717 444 LEEELEELREELAELEAELEQLEEDGElaELLQELEELKAELREL 488
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1110-1290 |
7.54e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 49.15 E-value: 7.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1110 LKQLRDLQ---SQLAELHEDLESEKAARAKAEKQRRDLGEELEALKTELEDTldstaaqQELRAKREQEVTDLKKTIEED 1186
Cdd:COG1579 6 LRALLDLQeldSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDL-------EKEIKRLELEIEEVEARIKKY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1187 vKVRDAQVTEMRQrhnqvVEEISEQLEQarrfkgnLEKVKQTLESENTDLIKEVKNLQAAKQDSEQRRKKLEQQV----S 1262
Cdd:COG1579 79 -EEQLGNVRNNKE-----YEALQKEIES-------LKRRISDLEDEILELMERIEELEEELAELEAELAELEAELeekkA 145
|
170 180
....*....|....*....|....*...
gi 1785379719 1263 EFQIRTNESEKVKFELAEKLQKLQAELD 1290
Cdd:COG1579 146 ELDEELAELEAELEELEAEREELAAKIP 173
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1091-1263 |
8.49e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 49.15 E-value: 8.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1091 ELQAALARVDDEVGQKNNLLKQLRDLQSQLAELHEDLESEKAARAKAEKQRRDLGEELEALKT---ELEDTLDSTAAQQE 1167
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEArikKYEEQLGNVRNNKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1168 LRAkREQEVTDLKKTIEEdvkvrdaqvteMRQRHNQVVEEISEQLEQARRFKGNLEKVKQTLESENTDLIKEVKNLQAAK 1247
Cdd:COG1579 91 YEA-LQKEIESLKRRISD-----------LEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAEL 158
|
170
....*....|....*.
gi 1785379719 1248 QDSEQRRKKLEQQVSE 1263
Cdd:COG1579 159 EELEAEREELAAKIPP 174
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
845-1217 |
1.32e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 845 LQVTRQDEVMQAKVVELQKVKDTQVKTESELKEMANKYQQLFEEKSILAEQLQAETELFAEAEEMRARLASKKQEL---- 920
Cdd:COG4717 111 LEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLslat 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 921 EEILHDLEARVEEEEERTLQLQNEKKKMHQHIQDLEEQLEEEEGARQKLQLEKVTTESRLKKMEEDIL------------ 988
Cdd:COG4717 191 EEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALlallglggslls 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 989 --------------LLEDQNAKLAKERKLLDDRIGEFTSTMAEEEEKVKSLNKLRNKYE-------AVIADLEDRLKKEE 1047
Cdd:COG4717 271 liltiagvlflvlgLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGlppdlspEELLELLDRIEELQ 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1048 KGRQEMEKMKRKLDGETTDLQDQLLELQQQIEELKQ-----QLARKEEELQAALARVDDEVGQKNNLLKQLRDlQSQLAE 1122
Cdd:COG4717 351 ELLREAEELEEELQLEELEQEIAALLAEAGVEDEEElraalEQAEEYQELKEELEELEEQLEELLGELEELLE-ALDEEE 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1123 LHEDLESEKAARAKAEKQRRDLGEELEALKTELEDTLDSTAAqQELRAKREQEVTDLKKTIEEDVKVRDAQvtemrqrhn 1202
Cdd:COG4717 430 LEEELEELEEELEELEEELEELREELAELEAELEQLEEDGEL-AELLQELEELKAELRELAEEWAALKLAL--------- 499
|
410
....*....|....*
gi 1785379719 1203 QVVEEISEQLEQARR 1217
Cdd:COG4717 500 ELLEEAREEYREERL 514
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1400-1575 |
1.61e-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: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1400 ELEFLQQRFDEKHQINDKLEKTRNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAE-EKNISARYGEERDRAEAEA 1478
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEaEAEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1479 REKET------------------KALSLSRALEEAIDLKDELDRQNKQLRAEMDDLVSSKDDVGKNVHELERSKRALEQQ 1540
Cdd:COG3883 97 RSGGSvsyldvllgsesfsdfldRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
170 180 190
....*....|....*....|....*....|....*
gi 1785379719 1541 VQEMKTQIEELEDELQAIEDGKLRLEVNMQAMKAQ 1575
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAA 211
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1277-1489 |
1.67e-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: 49.38 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1277 ELAEKLQKLQAELDGVSGALGSTEGKSIKLTKDLSTVQSQLQDTQELLQEETRQKLNFSSRVRQLEEEKNNLMENLEEEE 1356
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1357 SAKAQLSRQLQALQQQL-----------LESKKRMEDQGGMVEAMEEAKKKSYKELEFLQQRFDEKHQINDKLEKTRNRL 1425
Cdd:COG4942 104 EELAELLRALYRLGRQPplalllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAEL 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1785379719 1426 QQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKNISARYGEERDRAEAEAREKETKALSLS 1489
Cdd:COG4942 184 EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1019-1267 |
1.70e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.91 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1019 EEKVKSLNKLRNKYEAVIADLEDRLKKEEKGRQEMEKMKRKLdgettdlqdQLLELQQQIEELKQQLARKEEELQAALAR 1098
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREAL---------QRLAEYSWDEIDVASAEREIAELEAELER 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1099 VDDEVGQKNNLLKQLRDLQSQLAELHEDLESEKAARAKAEKQRRDLGEELEALKTELEDTLDSTAAQQELRAKREQEVTD 1178
Cdd:COG4913 680 LDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAAL 759
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1179 LKKTIEEDVKVRDAQVTEMRQRHNQVVEEISEQLEQA-RRFKGNLEKVKQTLESeNTDLIKEVKNLQAakQDSEQRRKKL 1257
Cdd:COG4913 760 GDAVERELRENLEERIDALRARLNRAEEELERAMRAFnREWPAETADLDADLES-LPEYLALLDRLEE--DGLPEYEERF 836
|
250
....*....|
gi 1785379719 1258 EQQVSEFQIR 1267
Cdd:COG4913 837 KELLNENSIE 846
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
657-681 |
1.82e-05 |
|
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.
Pssm-ID: 276814 [Multi-domain] Cd Length: 170 Bit Score: 46.95 E-value: 1.82e-05
10 20
....*....|....*....|....*
gi 1785379719 657 YKESLSKLMSTLRNTNPNFVRCIIP 681
Cdd:cd01363 146 INESLNTLMNVLRATRPHFVRCISP 170
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1427-1915 |
2.24e-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: 49.84 E-value: 2.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1427 QELDDLMVDLDHQRQIVSN---LEKKQKKFDQMLAEEKNISARYGEERDRAEAEAREKETKALSLSRALEEAIDLKDELd 1503
Cdd:pfam12128 221 QQVEHWIRDIQAIAGIMKIrpeFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQW- 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1504 rqnKQLRAEMD-DLVSSKDDVGKNVHELER-------------SKRALEQ-QVQEMKTQIEELEDELQAIEDGKLRLEVN 1568
Cdd:pfam12128 300 ---KEKRDELNgELSAADAAVAKDRSELEAledqhgafldadiETAAADQeQLPSWQSELENLEERLKALTGKHQDVTAK 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1569 MQAMKAQfeRDLQNRDDSNDEKKKLlfkqvremEVELEEERKQKSQILAAKKKLEMDLQD-MESQMDSANKGRDEAVKQL 1647
Cdd:pfam12128 377 YNRRRSK--IKEQNNRDIAGIKDKL--------AKIREARDRQLAVAEDDLQALESELREqLEAGKLEFNEEEYRLKSRL 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1648 KKLQLQ-------------------------------FKEVWR---EVEETRAARDEIFVQSRDNEKKLKSLEAELLQLQ 1693
Cdd:pfam12128 447 GELKLRlnqatatpelllqlenfderierareeqeaaNAEVERlqsELRQARKRRDQASEALRQASRRLEERQSALDELE 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1694 EDLAAA-----ERAKRQAQQERDDLADELS-------------NGVSGKSAL------LDEKR-----------ALEMRI 1738
Cdd:pfam12128 527 LQLFPQagtllHFLRKEAPDWEQSIGKVISpellhrtdldpevWDGSVGGELnlygvkLDLKRidvpewaaseeELRERL 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1739 SQLEEELDEEQSNTELINDRYRKLTLQVETITTELSAERSFSQKAENARQQMERQNKELKVKLNEMDSTMRSKYKITIAS 1818
Cdd:pfam12128 607 DKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNS 686
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1819 LEAKISQLEEQMeQESKERIIANKLVRRAEKrlKEVLLQVEEERRNA-DQFKEQLEKANI----RMKQLKRQLEEAEEEA 1893
Cdd:pfam12128 687 LEAQLKQLDKKH-QAWLEEQKEQKREARTEK--QAYWQVVEGALDAQlALLKAAIAARRSgakaELKALETWYKRDLASL 763
|
570 580
....*....|....*....|..
gi 1785379719 1894 SRANSNRRRLQRELEDVTESAE 1915
Cdd:pfam12128 764 GVDPDVIAKLKREIRTLERKIE 785
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
802-1430 |
2.25e-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: 49.73 E-value: 2.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 802 ARRAFYKKQQQMSALKVVQRNCAAyLKLRHWQwwRLFTKVKPLLQVTRQDEVM-QAKVVELQKvkdTQVKTESELKEMAN 880
Cdd:pfam15921 290 ARSQANSIQSQLEIIQEQARNQNS-MYMRQLS--DLESTVSQLRSELREAKRMyEDKIEELEK---QLVLANSELTEART 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 881 KYQQLFEEKSILAEQLQaetelfaeaeemrarlaskkqeleEILHDLEARveeeeERTLQLQNEKKKmhqhiqdleeqle 960
Cdd:pfam15921 364 ERDQFSQESGNLDDQLQ------------------------KLLADLHKR-----EKELSLEKEQNK------------- 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 961 eeegarqKLQLEKVTTESRLKKMEEDillLEDQNAKLAKERKLLDDRIGEFTSTMAEEEEKVKSLNKLRNKYEAVIADLE 1040
Cdd:pfam15921 402 -------RLWDRDTGNSITIDHLRRE---LDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLE 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1041 drlkkeekgrqEMEKMKRKLDGETTDLQDQLLELQQQIEELKQQLARKEEELQAA---LARVDDEVGQKNNLLKQLRDLQ 1117
Cdd:pfam15921 472 -----------STKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATnaeITKLRSRVDLKLQELQHLKNEG 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1118 SQLAELHEDLESEKAARAKAEKQRRDLGEELEALKTELEDTLDSTAAQQELRAKREQEVTDLKKTIEEDVKVRDAQVTEM 1197
Cdd:pfam15921 541 DHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKI 620
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1198 RQRHNQVVEeisEQLEQARRFKGNLEKVK--QTLESENTDLIKEVKN----LQAAKQDSEQRRKKLEQQVSEFQIRTNes 1271
Cdd:pfam15921 621 RELEARVSD---LELEKVKLVNAGSERLRavKDIKQERDQLLNEVKTsrneLNSLSEDYEVLKRNFRNKSEEMETTTN-- 695
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1272 ekvkfELAEKLQKLQAELDGVSGALGSTEGK-------SIKLTKDLSTVQSQLQDTQELLQEETRQKLNFSSRVRQLEEE 1344
Cdd:pfam15921 696 -----KLKMQLKSAQSELEQTRNTLKSMEGSdghamkvAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEE 770
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1345 KnnlmENLEEEESAKAQLSRQLQALQQQLLESKKRMEDQGGMVEAMEEAKKKSYKELEFLQQRFDEkhqindklEKTRNR 1424
Cdd:pfam15921 771 K----NKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQ--------ESVRLK 838
|
....*.
gi 1785379719 1425 LQQELD 1430
Cdd:pfam15921 839 LQHTLD 844
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
940-1165 |
2.30e-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: 2.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 940 QLQNEKKKMHQHIQDLEEqleeeegARQKLQLEKVTTESRLKKMEEDILLLEDQNAKLAKERKLLDDRIGEFTstmAEEE 1019
Cdd:COG4942 24 EAEAELEQLQQEIAELEK-------ELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE---KEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1020 EKVKSLNKLRNKYEAVIADLEDRLKKEE-------KGRQEMEKMKRKLDGETTDLQDQLLELQQQIEELKQQLARKEEEL 1092
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLGRQPPlalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1785379719 1093 QAALARVDDEVGQKNNLLKQLRDLQSQLAELHEDLESEKAARAKAEKQRRDLGEELEALKTELEDTLDSTAAQ 1165
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
979-1567 |
2.72e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.53 E-value: 2.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 979 RLKKMEEDILLLEDQNAKL-----AKERKLLDDRIGEFTSTMAEEEEKVKSLNKLRNKYEAVIADLEDRLkkEEKGRQEM 1053
Cdd:COG4913 263 RYAAARERLAELEYLRAALrlwfaQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQI--RGNGGDRL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1054 EKMKRKLDGETtdlqdqllelqQQIEELKQQLARKEEELQAALARVDDEVGQKNNLLKQLRDLQSQLAELHEDLEsekAA 1133
Cdd:COG4913 341 EQLEREIERLE-----------RELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALE---EA 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1134 RAKAEKQRRDLGEELEALKTELEdtldstaaqqELRAKR---EQEVTDLKKTIEEDVKVRDAQVtemrqrhnQVVEEISE 1210
Cdd:COG4913 407 LAEAEAALRDLRRELRELEAEIA----------SLERRKsniPARLLALRDALAEALGLDEAEL--------PFVGELIE 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1211 QLEQARRFKGNLEKVkqtLESENTDLIKEVKNLQAAKQDSEQRRKKLEQQVSEFQIRTNESEKVKFE---LAEKLQ---- 1283
Cdd:COG4913 469 VRPEEERWRGAIERV---LGGFALTLLVPPEHYAAALRWVNRLHLRGRLVYERVRTGLPDPERPRLDpdsLAGKLDfkph 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1284 KLQAELDGVSGALG-----------STEGKSIK---LTKDLSTVQsQLQDTQELLQE-----ETRQKLN-FSSRVRQLEE 1343
Cdd:COG4913 546 PFRAWLEAELGRRFdyvcvdspeelRRHPRAITragQVKGNGTRH-EKDDRRRIRSRyvlgfDNRAKLAaLEAELAELEE 624
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1344 EKNNLMENLEEEESAKAQLSRQLQALQQQLLES---------KKRMEDQGGMVEAMEEAK---KKSYKELEFLQQRFDEK 1411
Cdd:COG4913 625 ELAEAEERLEALEAELDALQERREALQRLAEYSwdeidvasaEREIAELEAELERLDASSddlAALEEQLEELEAELEEL 704
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1412 HQINDKLEKTRNRLQQELDDLMVDLDHQRQIVSNLEKKQKK-----FDQMLAE------EKNISARYGEERDRAEAEARE 1480
Cdd:COG4913 705 EEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLelralLEERFAAalgdavERELRENLEERIDALRARLNR 784
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1481 KETK---------------ALSLSRALEEAIDLKDELDRQNK----QLRAEMDDLVSSkddvgKNVHELERSKRALEQQV 1541
Cdd:COG4913 785 AEEEleramrafnrewpaeTADLDADLESLPEYLALLDRLEEdglpEYEERFKELLNE-----NSIEFVADLLSKLRRAI 859
|
650 660
....*....|....*....|....*....
gi 1785379719 1542 QEMKTQIEELEDELQAIE---DGKLRLEV 1567
Cdd:COG4913 860 REIKERIDPLNDSLKRIPfgpGRYLRLEA 888
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1416-1596 |
2.74e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 49.24 E-value: 2.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1416 DKLEKTRNR-LQQELDDLMVDLDH-QRQIVS--------------NLEKKQKKFDQMLAEEKNISARYGEERDRAEAEAR 1479
Cdd:PHA02562 169 DKLNKDKIReLNQQIQTLDMKIDHiQQQIKTynknieeqrkkngeNIARKQNKYDELVEEAKTIKAEIEELTDELLNLVM 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1480 EKETKALSLSRALEEAIDLKDELDRQNK---------------QLRAEMDDLVSSKDDVGKNV-HELERSKRALEQ---- 1539
Cdd:PHA02562 249 DIEDPSAALNKLNTAAAKIKSKIEQFQKvikmyekggvcptctQQISEGPDRITKIKDKLKELqHSLEKLDTAIDEleei 328
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1785379719 1540 ---------QVQEMKTQIEELEDELQAIEDGKLRLEVNMQAMKAQFERDLQNRDDSNDEKKKLLFK 1596
Cdd:PHA02562 329 mdefneqskKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKT 394
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1390-1930 |
3.27e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 49.13 E-value: 3.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1390 MEEAKKKSYKELEFLQQRFDEKHQINDKLEKTRNRLQQELDDLMVDLDHQRQIVSNL---EKKQKKFDQMLAE-EKNISA 1465
Cdd:PRK01156 188 LEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELsslEDMKNRYESEIKTaESDLSM 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1466 RYGEERDRAEAEAREKETKALSLSRALEEAID-LKDELDRQN-KQLRAEMDDLVSSKDDVGKNVHELERSKRALEQQVQE 1543
Cdd:PRK01156 268 ELEKNNYYKELEERHMKIINDPVYKNRNYINDyFKYKNDIENkKQILSNIDAEINKYHAIIKKLSVLQKDYNDYIKKKSR 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1544 MKtQIEELEDELQAIEDGKLRLEVNMQAMKAQFERDLQNRDDSNDEKKKLLFKQVRemeveleeerkQKSQILAAKKKLE 1623
Cdd:PRK01156 348 YD-DLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEI-----------DPDAIKKELNEIN 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1624 MDLQDMESQMDSANKGRDEAVKQLKKLQLQFKEVWRE----VEETRAARDEIFVQSRDNEKKLKSLEAELLQLQEDLAAA 1699
Cdd:PRK01156 416 VKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQsvcpVCGTTLGEEKSNHIINHYNEKKSRLEEKIREIEIEVKDI 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1700 ERAKRQAQQERDDLADELSNGVSGKSALLDEKRALEMRISQLEEELDEEQSNTELINDRYRKLTL----QVETITTELSA 1775
Cdd:PRK01156 496 DEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSLKLedldSKRTSWLNALA 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1776 ERSfSQKAENARQQMERQNKelkvKLNEMDSTMRsKYKITIASLEAKISQLEEQMEQESKeriiankLVRRAEKRLKEVL 1855
Cdd:PRK01156 576 VIS-LIDIETNRSRSNEIKK----QLNDLESRLQ-EIEIGFPDDKSYIDKSIREIENEAN-------NLNNKYNEIQENK 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1856 LQVEEERRNADQFKEQLEK----------ANIRMKQLKRQLEEAEEEASRANSNRRRLQRELEDVTESAESMNREVTTLR 1925
Cdd:PRK01156 643 ILIEKLRGKIDNYKKQIAEidsiipdlkeITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDIN 722
|
....*
gi 1785379719 1926 SRLRR 1930
Cdd:PRK01156 723 ETLES 727
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1081-1301 |
4.03e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.29 E-value: 4.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1081 LKQQLARKEEELQAALARVDDEVGQKNNLLKQLRDLQSQLAELHEDLesekAARAKAEKQRRDLGEELEALK--TELEDT 1158
Cdd:COG3883 42 LQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL----GERARALYRSGGSVSYLDVLLgsESFSDF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1159 LDSTAAQQELRAKREQEVTDLKKTIEEdvkVRDAQvtemrqrhnqvvEEISEQLEQARRFKGNLEKVKQTLESENTDLIK 1238
Cdd:COG3883 118 LDRLSALSKIADADADLLEELKADKAE---LEAKK------------AELEAKLAELEALKAELEAAKAELEAQQAEQEA 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1785379719 1239 EVKNLQAAKQDSEQRRKKLEQQVSEFQIRTNESEKVKFELAEKLQKLQAELDGVSGALGSTEG 1301
Cdd:COG3883 183 LLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAS 245
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1117-1337 |
4.43e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.90 E-value: 4.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1117 QSQLAELHEDLESEKAARAKAEKQRRDLGEELEALKTELEDTLDSTAAQQELRAKREQEVTDLKKTIEEDVkvrdaqvte 1196
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERR--------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1197 mrqrhnqvvEEISEQLEQARRFKGNLEKVKQTLESEN-TDLIKEVKNLQA-AKQDSE------QRRKKLEQQVSEFQIRT 1268
Cdd:COG3883 86 ---------EELGERARALYRSGGSVSYLDVLLGSESfSDFLDRLSALSKiADADADlleelkADKAELEAKKAELEAKL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1785379719 1269 NESEKVKFELAEKLQKLQAELDGVSGALGSTEGKSIKLTKDLSTVQSQLQDTQELLQEETRQKLNFSSR 1337
Cdd:COG3883 157 AELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAA 225
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
764-1125 |
4.61e-05 |
|
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: 48.51 E-value: 4.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 764 GQSKIFFRAGVLAHLEEERDLKITDIIVFFQAAARgylARRAFYKKQQQMSALKVVQRNCAAYLKLRHWQWWRLFTKVKP 843
Cdd:TIGR02168 668 TNSSILERRREIEELEEKIEELEEKIAELEKALAE---LRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 844 LLQ-VTRQDEVMQAKVVELQKVKDTQVKTESELKEMANKYQQLFEEKSILAEQLQAETELFAEAEEMRARLASKKQELEE 922
Cdd:TIGR02168 745 LEErIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 923 ILHDLEARVEEEEERTLQLQNEKKKMHQHIQDLEEQLEEEEGARQKLQLEKVTTESRLKKMEEDILLLEDQNAKLAKERK 1002
Cdd:TIGR02168 825 RLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELR 904
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1003 LLDDRIGEFTSTMAEEEEKVKSLNKLRNKYEAVIADLEDRLKkeEKGRQEMEKMKRKldgettdlqdqLLELQQQIEELK 1082
Cdd:TIGR02168 905 ELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLS--EEYSLTLEEAEAL-----------ENKIEDDEEEAR 971
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1083 QQLARKEEELQ-------AALARVDDEVGQKNNLLKQLRDLQSQLAELHE 1125
Cdd:TIGR02168 972 RRLKRLENKIKelgpvnlAAIEEYEELKERYDFLTAQKEDLTEAKETLEE 1021
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1036-1222 |
4.82e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.84 E-value: 4.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1036 IADLEDRLKKEEKGRQEMEKMKRKLDGETTDLQDQLLELQQQIEELKQQLARKEEELQAALARVDDEVGQKNNLLKQlRD 1115
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNN-KE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1116 LQSQLAELhedlESEKAARAKAEKQRRDLGEELEALKTELEDTldstaaqQELRAKREQEVTDLKKTIEEDVKVRDAQVT 1195
Cdd:COG1579 91 YEALQKEI----ESLKRRISDLEDEILELMERIEELEEELAEL-------EAELAELEAELEEKKAELDEELAELEAELE 159
|
170 180 190
....*....|....*....|....*....|.
gi 1785379719 1196 EMRQRHNQVVEEISEQL----EQARRFKGNL 1222
Cdd:COG1579 160 ELEAEREELAAKIPPELlalyERIRKRKNGL 190
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
896-1188 |
6.15e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 48.36 E-value: 6.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 896 LQAETELFAEAEEMRARLASKKQELEEILHDLEARVEEEEERTLQLQNEKKKMHQHIQDLEEQLEEEEGARQKLQLEKVT 975
Cdd:PLN02939 102 MQRDEAIAAIDNEQQTNSKDGEQLSDFQLEDLVGMIQNAEKNILLLNQARLQALEDLEKILTEKEALQGKINILEMRLSE 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 976 TESRLKKMEE---DILLLEDQNAKLAKERKLLDDRIGEFTSTMAEEEEKVKSLN-KLRNKYEAV------IADLEDRLKK 1045
Cdd:PLN02939 182 TDARIKLAAQekiHVEILEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEENmLLKDDIQFLkaelieVAETEERVFK 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1046 EEKGRQEMEKMKRKLDgetTDLQDQLLELQQQIEELKQQLARKEEELQAALARVDDEVGQKNNLLKQLRDLQSQLAELHE 1125
Cdd:PLN02939 262 LEKERSLLDASLRELE---SKFIVAQEDVSKLSPLQYDCWWEKVENLQDLLDRATNQVEKAALVLDQNQDLRDKVDKLEA 338
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1785379719 1126 DLESEKAARAKAEKQRRdLGEELEALKTELEDTLDSTAAQQELRAKREQEVTD-LKKTIEEDVK 1188
Cdd:PLN02939 339 SLKEANVSKFSSYKVEL-LQQKLKLLEERLQASDHEIHSYIQLYQESIKEFQDtLSKLKEESKK 401
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1674-1908 |
8.36e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.70 E-value: 8.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1674 QSRDNEKKLKSLEAELLQLQEDLAAAERAKRQAQQERD--DLADELSNGVSGKSALLDEKRALEMRISQleeeldeeqsn 1751
Cdd:COG3206 169 RREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEARAELAE----------- 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1752 telINDRYRKLTLQVETITTELSAersfsQKAENARQQMERQNKELKVKLNEMDSTMRSKYkITIASLEAKISQLEEQME 1831
Cdd:COG3206 238 ---AEARLAALRAQLGSGPDALPE-----LLQSPVIQQLRAQLAELEAELAELSARYTPNH-PDVIALRAQIAALRAQLQ 308
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1785379719 1832 QESKERIIAnklvrrAEKRLKEVLLQVEEERRNADQFKEQLEKANirmkQLKRQLeeaeeeasransnrRRLQRELE 1908
Cdd:COG3206 309 QEAQRILAS------LEAELEALQAREASLQAQLAQLEARLAELP----ELEAEL--------------RRLEREVE 361
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
967-1309 |
1.06e-04 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 47.54 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 967 QKLQLEKVTTESRLKKMEEDILLledqnaklaKERKLLDDRIGEFTSTMAEEEEKVKSLnKLRNKYEAVIADLEDRLKK- 1045
Cdd:PLN03229 372 QQIKIAINENMDELGKMDTEELL---------KHRMLKFRKIGGFQEGVPVDPERKVNM-KKREAVKTPVRELEGEVEKl 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1046 ---------------EEKGRQEMEKMKRKLDGETTDLQDQLLELQQQIEEL-----------------KQQLARKEEELQ 1093
Cdd:PLN03229 442 keqilkakessskpsELALNEMIEKLKKEIDLEYTEAVIAMGLQERLENLReefskansqdqlmhpvlMEKIEKLKDEFN 521
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1094 AALARVDDEVGQKNNLlKQLRDLQ-----SQLAELHEDLESEKAARAKAEKQRRDLGEELEALKTELEDTLDSTAAqqEL 1168
Cdd:PLN03229 522 KRLSRAPNYLSLKYKL-DMLNEFSrakalSEKKSKAEKLKAEINKKFKEVMDRPEIKEKMEALKAEVASSGASSGD--EL 598
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1169 RAKREQEVTDLKKTIEEDV----KVRDAQVTEMRQRHNQVVEEISEQleqarRFKGNLEKVKQTLESENTDLIK--EVKN 1242
Cdd:PLN03229 599 DDDLKEKVEKMKKEIELELagvlKSMGLEVIGVTKKNKDTAEQTPPP-----NLQEKIESLNEEINKKIERVIRssDLKS 673
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1785379719 1243 ------LQAAK------QDSEQRRKKLEQQVSEfQIRTNESEKvkfELAEKLQKLQAELdgvSGALGSTEGKSIKLTKD 1309
Cdd:PLN03229 674 kiellkLEVAKasktpdVTEKEKIEALEQQIKQ-KIAEALNSS---ELKEKFEELEAEL---AAARETAAESNGSLKND 745
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
866-1063 |
1.08e-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: 46.68 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 866 DTQVKTESELKEMANKYQQLFEEKSILAEQLQAETELFAEAEEMRARLASKKQELEEILHDLEARVEEEEERTLQLQNEK 945
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 946 KKMHQHIQDLEEQLEEE---------------EGARQKLQLEKVTTESRLKKMEEdillLEDQNAKLAKERKLLDDRIGE 1010
Cdd:COG4942 100 EAQKEELAELLRALYRLgrqpplalllspedfLDAVRRLQYLKYLAPARREQAEE----LRADLAELAALRAELEAERAE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1785379719 1011 FTSTMAEEEEKVKSLNKLRNKYEAVIADLEDRLKKEEKGRQEMEKMKRKLDGE 1063
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1495-1738 |
1.31e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.36 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1495 AIDLKDELDRQNKQLRAEMDDLVSSKDDVGKNVHELERSKRALEQQVQEMKTQIEELEDELQAIEDgklRLEVNMQAMKA 1574
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEA---EIEERREELGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1575 QFeRDLQNRDDSNDekkkllfkqvremeveleeerkQKSQILAAKkklemDLQDMESQMDsankgrdeAVKQLKKLQLQf 1654
Cdd:COG3883 91 RA-RALYRSGGSVS----------------------YLDVLLGSE-----SFSDFLDRLS--------ALSKIADADAD- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1655 kevwrEVEETRAARDEIFVQSRDNEKKLKSLEAELLQLQEDLAAAERAKRQAQQERDDLADELSNGVSGKSALLDEKRAL 1734
Cdd:COG3883 134 -----LLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAA 208
|
....
gi 1785379719 1735 EMRI 1738
Cdd:COG3883 209 EAAA 212
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
884-1260 |
1.88e-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: 46.43 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 884 QLFEEKSILAEQLQAETELFAEAEEMRARLASKKQELEEILHDLEARVEEEEERTLQLQNEKKKMHQHIQDLEEQLEEEE 963
Cdd:pfam07888 35 RLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 964 GARQKLQLEKVTTESRLKKMEEDILLLEDQNAKLAKERKLLDDRIGEFTSTMAEEEEKVKSLNklrnkyeaviADLEDRL 1043
Cdd:pfam07888 115 EEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQ----------AKLQQTE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1044 KKEEKGRQEMEKMKRKLDGETTDLqdqllelqqqieelkQQLARKEEELQAALARVDDEVGQKNNLLKQLRDLQSQLAE- 1122
Cdd:pfam07888 185 EELRSLSKEFQELRNSLAQRDTQV---------------LQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNAs 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1123 ------LHEDLESEKAARAKAEKQRRDLGEELEALKTELEdtlDSTAAQQELRAKREQEVTDLKKTIEEDVKVRDAQVTE 1196
Cdd:pfam07888 250 erkvegLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLA---DASLALREGRARWAQERETLQQSAEADKDRIEKLSAE 326
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1785379719 1197 MRQRHNQVVEEISE----QLEQARRFKGNLEKVKQT------LESENTDLIKEVKNLQAAKQDSEQRRKKLEQQ 1260
Cdd:pfam07888 327 LQRLEERLQEERMEreklEVELGREKDCNRVQLSESrrelqeLKASLRVAQKEKEQLQAEKQELLEYIRQLEQR 400
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1116-1343 |
1.94e-04 |
|
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: 46.76 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1116 LQSQLAELHEDLESEKAARAKAEKQRRDLGEELEALKTELEDTLDS-----------TAAQQELRAKREQEVTDLKKTIE 1184
Cdd:pfam12128 602 LRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTAlknarldlrrlFDEKQSEKDKKNKALAERKDSAN 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1185 EDVKVRDAQVTEMRQRHNQVVEEISEQLEQARRFK------------GNLEKVKQTLESENTDLIKEVKNLQ-------A 1245
Cdd:pfam12128 682 ERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKqaywqvvegaldAQLALLKAAIAARRSGAKAELKALEtwykrdlA 761
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1246 AKQDSEQRRKKLEQQVSEF-----QIRTNESEKVKFE------LAEKLQKLQAELDGVSGALGSTEGKSIKLTKDLSTVQ 1314
Cdd:pfam12128 762 SLGVDPDVIAKLKREIRTLerkieRIAVRRQEVLRYFdwyqetWLQRRPRLATQLSNIERAISELQQQLARLIADTKLRR 841
|
250 260 270
....*....|....*....|....*....|....*.
gi 1785379719 1315 SQL-------QDTQELLQEETRQKLNFSSRVRQLEE 1343
Cdd:pfam12128 842 AKLemerkasEKQQVRLSENLRGLRCEMSKLATLKE 877
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1473-1837 |
2.18e-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: 46.04 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1473 RAEAEAREKETKALSLSRALEEAIDLKDELDRQNKQLRAEMDDLVSSKDDVGKNVHELERSKRALEQQVQEMKTQIEELE 1552
Cdd:pfam07888 56 QREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1553 DELQAIEDGKLRLEVNMQAMKAQFERDLQNRDDSNDEKKKLLFKQVremeveleeerkqksQILAAKKKLEMDLQDMESQ 1632
Cdd:pfam07888 136 EDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQ---------------QTEEELRSLSKEFQELRNS 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1633 MDSankgRDEAVKQLK----KLQLQFKEVWREVEETRAARDEIfvqsRDNEKKLKSLEAELLQLQEDLA--AAERAKRQA 1706
Cdd:pfam07888 201 LAQ----RDTQVLQLQdtitTLTQKLTTAHRKEAENEALLEEL----RSLQERLNASERKVEGLGEELSsmAAQRDRTQA 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1707 QQERDDL-ADELSNGVSGKSALLDEKRAlemrisQLEEELDEEQSNTELINDRYRKLTLQVETITTELSAERSFSQKAE- 1784
Cdd:pfam07888 273 ELHQARLqAAQLTLQLADASLALREGRA------RWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEv 346
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1785379719 1785 ---NARQQMERQNKELKVKLNEMDSTMRSKYKITIASLEAK------ISQLEEQMEQESKER 1837
Cdd:pfam07888 347 elgREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKqelleyIRQLEQRLETVADAK 408
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
840-1278 |
2.28e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.67 E-value: 2.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 840 KVKPLLQVTRQDEVMQAKVVELQKVKDTQVKTESELKEMANKYQQLFEEKSILAEQLQAETELFAEAEEMRarlasKKQE 919
Cdd:PTZ00121 1556 ELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELK-----KAEE 1630
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 920 leeilhdlearveeeeertlqlqnEKKKMHQhiqdleeqleeeegaRQKLQLEKVTTESRLKKMEEDILLLEDQNAKLAK 999
Cdd:PTZ00121 1631 ------------------------EKKKVEQ---------------LKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAE 1671
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1000 ERKLLDDRIGEftstmAEEEEKVKslnklrnkyeaviadlEDRLKKEEKGRQEMEKMKRKlDGETTDLQDQLLELQQQIE 1079
Cdd:PTZ00121 1672 EDKKKAEEAKK-----AEEDEKKA----------------AEALKKEAEEAKKAEELKKK-EAEEKKKAEELKKAEEENK 1729
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1080 ELKQQLARKEEELQAALARVDDEVGQKNnllkQLRDLQSQLAELHEDLESEKAARAKAEKQRRDLGEELEALKTeLEDTL 1159
Cdd:PTZ00121 1730 IKAEEAKKEAEEDKKKAEEAKKDEEEKK----KIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKK-IKDIF 1804
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1160 DSTAAQQELRAKREQEVTDLKKTieedvkvRDAQVTEMRQRHNQVVEEiSEQLEQARRFKGNLEKVKQTLES----ENTD 1235
Cdd:PTZ00121 1805 DNFANIIEGGKEGNLVINDSKEM-------EDSAIKEVADSKNMQLEE-ADAFEKHKFNKNNENGEDGNKEAdfnkEKDL 1876
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1785379719 1236 LIKEVKNLQAAKQDSEQRRKKLEQQVSEFQIRTNESEKVKFEL 1278
Cdd:PTZ00121 1877 KEDDEEEIEEADEIEKIDKDDIEREIPNNNMAGKNNDIIDDKL 1919
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1292-1512 |
2.48e-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: 45.53 E-value: 2.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1292 VSGALGSTEGKSIKLTKDLSTVQSQLQDTQELLQEETRQKLNFSSRVRQLEEEKNNLMENLEEEESAKAQLSRQLQALQQ 1371
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1372 QLLESKKRMEDQ----GGMVEAMEEAKKKSYKELEFLQQRFDEKHQINDKLEKTRNRLQQELDDLMVDLDHQRQIVSNLE 1447
Cdd:COG4942 91 EIAELRAELEAQkeelAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1785379719 1448 KKQKKFDQMLAEEKNISARYGEERDRAEAEAREKETKALSLSRALEEAIDLKDELDRQNKQLRAE 1512
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1115-1919 |
3.50e-04 |
|
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: 45.81 E-value: 3.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1115 DLQSQLAELHEDLESEKAARAKAEKQRRDLGE---ELEALKTELEDTLDSTAAQQELRAKREQEVTDLKKTIEEDVKVRD 1191
Cdd:TIGR00606 221 EIRDQITSKEAQLESSREIVKSYENELDPLKNrlkEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTD 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1192 AQVTEMRQRHNQVVEEISEQLEQARRFKGNLEKVKQTLESENTDLIKEV--KNLQAAKQDSEQRRKKLEQQVSEFQIRTN 1269
Cdd:TIGR00606 301 EQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQgrLQLQADRHQEHIRARDSLIQSLATRLELD 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1270 ESEKVKFELAEKLQKLQAELDGVsgalgstEGKSIKLTKDLSTVQSQLQDTQELLqEETRQKLNFSSRVRQLEEEKNnlm 1349
Cdd:TIGR00606 381 GFERGPFSERQIKNFHTLVIERQ-------EDEAKTAAQLCADLQSKERLKQEQA-DEIRDEKKGLGRTIELKKEIL--- 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1350 enleeeeSAKAQLSRQLQALQQQLLESKKRMEDqggmveaMEEAKKKSYKELEFLqqrfdEKHQINDKLEKTRNRLQQEL 1429
Cdd:TIGR00606 450 -------EKKQEELKFVIKELQQLEGSSDRILE-------LDQELRKAERELSKA-----EKNSLTETLKKEVKSLQNEK 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1430 DDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKNISARYGEERDRAEAEAREketkALSLSRALEEAIDLKDELDRQNKQL 1509
Cdd:TIGR00606 511 ADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDE----LTSLLGYFPNKKQLEDWLHSKSKEI 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1510 RAEMDDLVsskdDVGKNVHELERSKRALEQQVQEMKTQIEELEDELQAIeDGKLRLEVNMQAMKAQFERdlQNRDDSNDE 1589
Cdd:TIGR00606 587 NQTRDRLA----KLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDV-CGSQDEESDLERLKEEIEK--SSKQRAMLA 659
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1590 KKKLLFKQVREMEVELEEERKQKSQ-ILAAKKKLEMDLQDMESQMDSANKGRDEAVKQLKKLQLQFKEVWREVEETRAAR 1668
Cdd:TIGR00606 660 GATAVYSQFITQLTDENQSCCPVCQrVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSII 739
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1669 DEIFVQSRDNEKKLKSLEAELLQLQEDLAAAERAKRQAQQErDDLADELSNGVSGKSALLDEKRALEMRISQleeeldee 1748
Cdd:TIGR00606 740 DLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPE-EESAKVCLTDVTIMERFQMELKDVERKIAQ-------- 810
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1749 qsntelindryrkltlqvetittelsaersfsQKAENARQQMERQNKELKVKLNEMDSTMRskykitiasleaKISQLEE 1828
Cdd:TIGR00606 811 --------------------------------QAAKLQGSDLDRTVQQVNQEKQEKQHELD------------TVVSKIE 846
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1829 QMEQESKERIIANKLVRRAEKRLKEVLLQVEEERRNADQFKEQLEKANIRMKQLKRQLEEAEEEASRANSNRRRLQRELE 1908
Cdd:TIGR00606 847 LNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKE 926
|
810
....*....|.
gi 1785379719 1909 DVTESAESMNR 1919
Cdd:TIGR00606 927 ELISSKETSNK 937
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1104-1886 |
4.27e-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: 45.34 E-value: 4.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1104 GQKNNLLKQLRDLQSQLAELHEDLESEKAARAKAEKQRRDLGEELEALKTELEDTLDSTAAQQELRAKREQEVTDLKKTI 1183
Cdd:TIGR00618 152 GEFAQFLKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHL 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1184 EEDVKvrdaqvtEMRQRHNQVVEEISEQLEQARRFKgnLEKVKQTLESENTDLIKEVKNLQAAKQDSEQRRKKLEQQVSE 1263
Cdd:TIGR00618 232 REALQ-------QTQQSHAYLTQKREAQEEQLKKQQ--LLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAV 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1264 FQIRtNESEKVKFELAEKLQKLQAELDGVSGALgSTEGKSIKLTKDLSTVQSQ------LQDTQELLQEETRQKLNFSSR 1337
Cdd:TIGR00618 303 TQIE-QQAQRIHTELQSKMRSRAKLLMKRAAHV-KQQSSIEEQRRLLQTLHSQeihirdAHEVATSIREISCQQHTLTQH 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1338 VRQLEEEKNNLMENLEeeeSAKAQLSRQLQALQQQLLESKKRMEDQGGMVEAmEEAKKKSYKELEFLQQRFDEKHQIndk 1417
Cdd:TIGR00618 381 IHTLQQQKTTLTQKLQ---SLCKELDILQREQATIDTRTSAFRDLQGQLAHA-KKQQELQQRYAELCAAAITCTAQC--- 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1418 lEKTRNRLQQELddlmvdldhqrqivsnlEKKQKKFDQMLAEEKNISARygeerdraeaearEKETKALSLSRALEEAiD 1497
Cdd:TIGR00618 454 -EKLEKIHLQES-----------------AQSLKEREQQLQTKEQIHLQ-------------ETRKKAVVLARLLELQ-E 501
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1498 LKDELDRQNKQLRAEMDDLvsskDDVGKNVHELERskraLEQQVQEMKTQIEELEDELQAIEDGKLRLEVNMQAMKAQFE 1577
Cdd:TIGR00618 502 EPCPLCGSCIHPNPARQDI----DNPGPLTRRMQR----GEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFS 573
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1578 RDLQNRDDSNDEKKKLLfKQVREMEVELEEERKQKSQILAAKKKLEMDLQDmesqmdSANKGRDEAVKQLKKLQLQFKEV 1657
Cdd:TIGR00618 574 ILTQCDNRSKEDIPNLQ-NITVRLQDLTEKLSEAEDMLACEQHALLRKLQP------EQDLQDVRLHLQQCSQELALKLT 646
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1658 WREVEETRAARDEIfvqsRDNEKKLKSLEAELLQL-QEDLAAAERAKRQAQQERDDLADELSNGVSGKSALLDEKRALEM 1736
Cdd:TIGR00618 647 ALHALQLTLTQERV----REHALSIRVLPKELLASrQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNE 722
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1737 RISQLEEELDEEQSNTELINDRYRKLTLQVETITTELSAERSFSQKAENARQQMERQNKELKVKLNEMDSTMrskykiti 1816
Cdd:TIGR00618 723 IENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLR-------- 794
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1817 ASLEAKISQLEEQMEQESKERiianklvrraekrLKEVLLQVEEERRNADQFKEQLEKANIRMKQLKRQL 1886
Cdd:TIGR00618 795 EEDTHLLKTLEAEIGQEIPSD-------------EDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQL 851
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
999-1344 |
5.39e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 5.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 999 KERKLLDDRIGEFTSTMAEEEEKVKSLNKLRNKYEAVIADLEDRLKKEEKGRQEMEKMKRKLDgettdlqdqLLELQQQI 1078
Cdd:COG4717 64 RKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ---------LLPLYQEL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1079 EELKQQLARKEEELQAALARVDdevgQKNNLLKQLRDLQSQLAELHEDLESEKA-ARAKAEKQRRDLGEELEALKTELED 1157
Cdd:COG4717 135 EALEAELAELPERLEELEERLE----ELRELEEELEELEAELAELQEELEELLEqLSLATEEELQDLAEELEELQQRLAE 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1158 TLDSTAAQQELRAKREQEVTDLKKTIEEDVKVRDAQ-------------------------------------------V 1194
Cdd:COG4717 211 LEEELEEAQEELEELEEELEQLENELEAAALEERLKearlllliaaallallglggsllsliltiagvlflvlgllallF 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1195 TEMRQRHNQVVEEISEQLEQARRFKGNLEKVKQTLE----------SENTDLIKEVKNLQAAKQDSEQRRKKLEQQVSEF 1264
Cdd:COG4717 291 LLLAREKASLGKEAEELQALPALEELEEEELEELLAalglppdlspEELLELLDRIEELQELLREAEELEEELQLEELEQ 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1265 QIR--------TNESE-KVKFELAEKLQKLQAELDGVSGALGSTEGKSIKL--TKDLSTVQSQLQDTQELLQEETRQKLN 1333
Cdd:COG4717 371 EIAallaeagvEDEEElRAALEQAEEYQELKEELEELEEQLEELLGELEELleALDEEELEEELEELEEELEELEEELEE 450
|
410
....*....|.
gi 1785379719 1334 FSSRVRQLEEE 1344
Cdd:COG4717 451 LREELAELEAE 461
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1773-1884 |
6.22e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.77 E-value: 6.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1773 LSAERSFSQKAENARQQMERQNKELKVKLNEMDSTMRSKYKITIASLEAKISQLEEQMEQesKERIIANKL--VRRAEKR 1850
Cdd:PRK12704 34 KEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQ--KEENLDRKLelLEKREEE 111
|
90 100 110
....*....|....*....|....*....|....
gi 1785379719 1851 LKEVLLQVEEERRNADQFKEQLEKanIRMKQLKR 1884
Cdd:PRK12704 112 LEKKEKELEQKQQELEKKEEELEE--LIEEQLQE 143
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
879-1265 |
7.49e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 44.94 E-value: 7.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 879 ANKYQQLFEEKSILAEQLQAETELFAEAEEMRARLASKKQELEEILHDLEARVEEEEERtLQL------QNEKKKMHQH- 951
Cdd:COG3096 277 ANERRELSERALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDH-LNLvqtalrQQEKIERYQEd 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 952 IQDLEEQLEEEEGARQKLQLEKVTTESRLKKMEEDILLLEDQNA---------------------KLAKERKLLD----- 1005
Cdd:COG3096 356 LEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLAdyqqaldvqqtraiqyqqavqALEKARALCGlpdlt 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1006 -DRIGEFTSTMAEEEEKVKSlnklrnkyeaVIADLEDRLKKEEKGRQEMEK---MKRKLDGETTDLQDQLLElqqqieel 1081
Cdd:COG3096 436 pENAEDYLAAFRAKEQQATE----------EVLELEQKLSVADAARRQFEKayeLVCKIAGEVERSQAWQTA-------- 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1082 kQQLARKEEELQAALARVDdevgqknnllkqlrDLQSQLAELHEDLESEKAARAKAEK----------QRRDLGEELEAL 1151
Cdd:COG3096 498 -RELLRRYRSQQALAQRLQ--------------QLRAQLAELEQRLRQQQNAERLLEEfcqrigqqldAAEELEELLAEL 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1152 KTELEDTLDSTAAQQELRAKREQEVTDLKKTIEEDVKV----RDAQvtemrQRHNQVVEEISEQLEQARrfkGNLEKVKQ 1227
Cdd:COG3096 563 EAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARapawLAAQ-----DALERLREQSGEALADSQ---EVTAAMQQ 634
|
410 420 430
....*....|....*....|....*....|....*...
gi 1785379719 1228 TLESEntdlikevKNLQAAKQDSEQRRKKLEQQVSEFQ 1265
Cdd:COG3096 635 LLERE--------REATVERDELAARKQALESQIERLS 664
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
902-1137 |
8.13e-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: 43.98 E-value: 8.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 902 LFAEAEEMRARLASKKQELEEILHDLEArveeEEERTLQLQNEKKKMHQHIQDLEEQLEEEEGARQKLQLEKVTTESRLK 981
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAE----LEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 982 KMEEDIlllEDQNAKLAKERKLLDDRIGEFTSTMAEEEEKV-------KSLNKLRNKYEAVIADLEDRLKKEEKGRQEME 1054
Cdd:COG4942 87 ELEKEI---AELRAELEAQKEELAELLRALYRLGRQPPLALllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1055 KMKRKLDGETTdlqdQLLELQQQIEELKQQLARKEEELQAALARVDDEVGQKNNLLKQLRDLQSQLAELHEDLESEKAAR 1134
Cdd:COG4942 164 ALRAELEAERA----ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
...
gi 1785379719 1135 AKA 1137
Cdd:COG4942 240 AER 242
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
1487-1584 |
8.15e-04 |
|
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.
Pssm-ID: 463295 [Multi-domain] Cd Length: 151 Bit Score: 41.92 E-value: 8.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1487 SLSRALEEAIDLKDELDRQNKQLRAEMDDLVSSKDDVGKNVHELERSKRALEQQVQEMKTQIEELEDELQAIEDGKLRLE 1566
Cdd:pfam11559 42 ELLQQRDRDLEFRESLNETIRTLEAEIERLQSKIERLKTQLEDLERELALLQAKERQLEKKLKTLEQKLKNEKEELQRLK 121
|
90
....*....|....*...
gi 1785379719 1567 VNMQAMKAQFERDLQNRD 1584
Cdd:pfam11559 122 NALQQIKTQFAHEVKKRD 139
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
967-1344 |
8.17e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 8.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 967 QKLQLEKVTTESRLKKMEEDILLLEDQNAKLAKERKLLDDrIGEFTSTMAEEEEKVKSLNKLRNKYEAVIADLEDRLKKE 1046
Cdd:COG4717 91 AELQEELEELEEELEELEAELEELREELEKLEKLLQLLPL-YQELEALEAELAELPERLEELEERLEELRELEEELEELE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1047 EKGRQEMEKMKRKLDGETTDLQDQLLELQQQIEELKQQLARKEEELQAALARVDDEVGQKNNLLKQLRDLQ--SQLAELH 1124
Cdd:COG4717 170 AELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAAleERLKEAR 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1125 EDLESEKAARAKAEKQRRDLGEELEAL--------------------KTELEDTLDSTAAQQELRAKREQEVTDLKKTIE 1184
Cdd:COG4717 250 LLLLIAAALLALLGLGGSLLSLILTIAgvlflvlgllallflllareKASLGKEAEELQALPALEELEEEELEELLAALG 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1185 EDVKVRDAQVTEMRQRHNQVVEEISE--QLEQARRFKGNLEKVKQTLESENTDLIKEVknLQAAKQDSEQRRKKLEQQVS 1262
Cdd:COG4717 330 LPPDLSPEELLELLDRIEELQELLREaeELEEELQLEELEQEIAALLAEAGVEDEEEL--RAALEQAEEYQELKEELEEL 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1263 EFQIRTNESEKVKFELAEKLQKLQAELDGVSGALGSTEGKSIKLTKDLSTVQSQLQD--TQELLQEETRQKLNFSSRVRQ 1340
Cdd:COG4717 408 EEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQleEDGELAELLQELEELKAELRE 487
|
....
gi 1785379719 1341 LEEE 1344
Cdd:COG4717 488 LAEE 491
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1112-1321 |
9.26e-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: 44.12 E-value: 9.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1112 QLRDLQSQLAELHEDLESEKAARAKAEKQRRdlgeELEALKTELEDTLDSTAAQQELRAKREQEVTDLKKTIEEDVKVRD 1191
Cdd:pfam07888 74 QRRELESRVAELKEELRQSREKHEELEEKYK----ELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1192 AQVTEMRQRHNQVVEEISEQLEQARRFKGNLEKVKQTLESENTDLikevknlQAAKQDSEQRRKKLEQQVSEFQIRTNES 1271
Cdd:pfam07888 150 TELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEF-------QELRNSLAQRDTQVLQLQDTITTLTQKL 222
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1272 EKVKFELAEkLQKLQAELDGVSGALGSTEGKSIKLTKDLSTVQSQLQDTQ 1321
Cdd:pfam07888 223 TTAHRKEAE-NEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQ 271
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1632-1957 |
1.15e-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: 43.96 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1632 QMDSANKGRDEAVKQLKKLQLQFKEVWREVEETRAARD-EIFVQSR---DNEKKLKSLEAELLQLQEDlaaaERAKRQAQ 1707
Cdd:pfam17380 289 QQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQaEMDRQAAiyaEQERMAMERERELERIRQE----ERKRELER 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1708 QERDDLADELSNGVSGKSALLDEKRALEmRISQLEEELDEEQSNTElinDRYRKLTLQVETITtELSAERSFSQKAENAR 1787
Cdd:pfam17380 365 IRQEEIAMEISRMRELERLQMERQQKNE-RVRQELEAARKVKILEE---ERQRKIQQQKVEME-QIRAEQEEARQREVRR 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1788 QQMERQNKELKVKLNEMDstmRSKYKITIASLEAKISQLEEQMEQESKERIIANKLVRRA-EKRLKEVLLQ-VEEERRNA 1865
Cdd:pfam17380 440 LEEERAREMERVRLEEQE---RQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKIlEKELEERKQAmIEEERKRK 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1866 DQFKEQLEKANIRMKQLKRQLEEAEEEASRANSNRRRLQRELEDVTESA---ESMNREVTTLR----SRLRRAPIQFTTR 1938
Cdd:pfam17380 517 LLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERsrlEAMEREREMMRqiveSEKARAEYEATTP 596
|
330 340
....*....|....*....|...
gi 1785379719 1939 --TIRQVYQLEAVSDEEP--ESH 1957
Cdd:pfam17380 597 itTIKPIYRPRISEYQPPdvESH 619
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1124-1482 |
1.30e-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: 43.96 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1124 HEDLESEKAARAKAEKQRRDLGEELEALKTELEDTLDSTAAQQELRAKREQEvtdLKKTIEEDVKVRDAQVTEmrqrhnq 1203
Cdd:pfam17380 298 QERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERE---LERIRQEERKRELERIRQ------- 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1204 vvEEISEQLEQARRfkgnLEKVKQTLESENTDLIKEVKNLQAAKQDSEQRRKKLEQQVSEFqirtnesEKVKFElaeklq 1283
Cdd:pfam17380 368 --EEIAMEISRMRE----LERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEM-------EQIRAE------ 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1284 klqaeldgvsgalgstegksikltkdlstvqsqlqdtqellQEETRQKlnfssRVRQLEEEKNNLMENLEEEESAKAQLS 1363
Cdd:pfam17380 429 -----------------------------------------QEEARQR-----EVRRLEEERAREMERVRLEEQERQQQV 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1364 RQLQALQQQLLESKKRMEDQGGMVEAMEEAKKKsykeleFLQQRFDEKHQINDKLEKTRNRLQQELDDLMVDL--DHQRQ 1441
Cdd:pfam17380 463 ERLRQQEEERKRKKLELEKEKRDRKRAEEQRRK------ILEKELEERKQAMIEEERKRKLLEKEMEERQKAIyeEERRR 536
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1785379719 1442 IVSNLEKKQKKFDQMLAEEKNISaRYGEERDRAEAEAREKE 1482
Cdd:pfam17380 537 EAEEERRKQQEMEERRRIQEQMR-KATEERSRLEAMERERE 576
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1387-1937 |
1.31e-03 |
|
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: 43.88 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1387 VEAMEEAKKKSYKELEFLQQRFDEKHQINDKLEKTRNRLQQELDDLMVDLDHQRQIVSNlEKKQKKFDQMLAEEKNISAR 1466
Cdd:TIGR00606 257 IEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVR-EKERELVDCQRELEKLNKER 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1467 YGEERDRAEAEAREKEtkaLSLSRALEEAIDLKDELDRQNKQLRAEMDDLVSSKDDVG--KNVHELERskralEQQVQEM 1544
Cdd:TIGR00606 336 RLLNQEKTELLVEQGR---LQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERqiKNFHTLVI-----ERQEDEA 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1545 KTqIEELEDELQAIEDGKLRLEVNMQAMKAQFERDLQNrddsndEKKKLLFKQVREMEVELEEERKQKSqilaAKKKLEM 1624
Cdd:TIGR00606 408 KT-AAQLCADLQSKERLKQEQADEIRDEKKGLGRTIEL------KKEILEKKQEELKFVIKELQQLEGS----SDRILEL 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1625 DLQDMESQMDSANKGRDEAVKQLKKLQLQFKEVWREVEETRAARDEIFVQSRDNEKKLKSLEaelLQLQEDLAAAERAKR 1704
Cdd:TIGR00606 477 DQELRKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQME---MLTKDKMDKDEQIRK 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1705 QAQQERDDLADELSNGVSGK------SALLDEKRALEMRISQLEEELDEEQSNTELINDRYRKLTLQVETITT---ELSA 1775
Cdd:TIGR00606 554 IKSRHSDELTSLLGYFPNKKqledwlHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDklfDVCG 633
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1776 ERSFSQKAENARQQMERQNKELKVklnemdstmrskykitIASLEAKISQLEEQMEQESKERIIANKLVRRAEKRLKEVL 1855
Cdd:TIGR00606 634 SQDEESDLERLKEEIEKSSKQRAM----------------LAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFI 697
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1856 LQVEEERRNADQFKEQLEKaniRMKQLKRQLEEAEEEASRANSNRRRLQRELEDVTESAESMNREVTTLRSRLRRAPIQF 1935
Cdd:TIGR00606 698 SDLQSKLRLAPDKLKSTES---ELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLL 774
|
..
gi 1785379719 1936 TT 1937
Cdd:TIGR00606 775 GT 776
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1388-1921 |
1.60e-03 |
|
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: 43.56 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1388 EAMEEAKKKSYKELEFLQQRFDEKHQINDKLEKTRNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKNISARY 1467
Cdd:pfam05483 88 EKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRHLCNLLKETCARS 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1468 GEERDRAEAEAREKETKALSLSRALEEAIDLKDELDRQNKQLRAEMDdlVSSKDDVGKNVHELERSKRAL---EQQVQEM 1544
Cdd:pfam05483 168 AEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMH--FKLKEDHEKIQHLEEEYKKEIndkEKQVSLL 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1545 KTQIEELEDELQaieDGKLRLEVNMQAMKaqferDLQNRDDSNDEKKKLLFKQVREMEVELEEERKQKSQILAAKKKLEM 1624
Cdd:pfam05483 246 LIQITEKENKMK---DLTFLLEESRDKAN-----QLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEE 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1625 DLQ-----------DMESQMDSANKGR-----------------DEAVK----QLKKLQLQFKEVWREVEETRAARDEIF 1672
Cdd:pfam05483 318 DLQiatkticqlteEKEAQMEELNKAKaahsfvvtefeattcslEELLRteqqRLEKNEDQLKIITMELQKKSSELEEMT 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1673 VQSRDNEKKLKSLEAELLQLQ---------EDLAAAERAKRQA--------QQERDDLADELSNGVSGKSALLDEKRALE 1735
Cdd:pfam05483 398 KFKNNKEVELEELKKILAEDEklldekkqfEKIAEELKGKEQElifllqarEKEIHDLEIQLTAIKTSEEHYLKEVEDLK 477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1736 MRISQLEEELDEEQSNTELINDRYRKLTLQVETITTELSAERsfsQKAENARQQMERQNK------ELKVKLNEMDSTMR 1809
Cdd:pfam05483 478 TELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQ---EDIINCKKQEERMLKqienleEKEMNLRDELESVR 554
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1810 SKYKITIASLEAKISQLEEQMEQESKERIIANKLVRRAEKRLKEVLLQVEEERRNADQFKE--------------QLEKA 1875
Cdd:pfam05483 555 EEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQenkalkkkgsaenkQLNAY 634
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 1785379719 1876 NIRMKQLKRQLEEAEEEASRANSNrrrLQRELEDVTESAESMNREV 1921
Cdd:pfam05483 635 EIKVNKLELELASAKQKFEEIIDN---YQKEIEDKKISEEKLLEEV 677
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1402-1930 |
1.63e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 43.66 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1402 EFLQQRFDEKHQINDKLEKTRNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLaEEKNISARYGEERDR-----AEA 1476
Cdd:pfam10174 112 ELTEENFRRLQSEHERQAKELFLLRKTLEEMELRIETQKQTLGARDESIKKLLEML-QSKGLPKKSGEEDWErtrriAEA 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1477 EAREKETKALsLSRALEEAIDLKDELDRQNK--QLRAEMDDLVSSKDDVGKNVHELERSKRALEQQVQE----------- 1543
Cdd:pfam10174 191 EMQLGHLEVL-LDQKEKENIHLREELHRRNQlqPDPAKTKALQTVIEMKDTKISSLERNIRDLEDEVQMlktngllhted 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1544 -----------------MKTQIEELEDELQAIE------------------DGKLRLEVNMQAMKAQFERD--LQNRDDS 1586
Cdd:pfam10174 270 reeeikqmevykshskfMKNKIDQLKQELSKKEsellalqtkletltnqnsDCKQHIEVLKESLTAKEQRAaiLQTEVDA 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1587 ----NDEKKKLLFKQVremeveleeerKQKSQILAAKKKLEMDLQDMESQMDSANKGRDEAVKQLKKLQLQFKEVWREVE 1662
Cdd:pfam10174 350 lrlrLEEKESFLNKKT-----------KQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLA 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1663 ETRAARDEIFVQSRDNEKKLKSLEaELLQLQEDLAAA-----ERAKRQAQQERDDLADELSNGVSGKSALLDEKRALEMR 1737
Cdd:pfam10174 419 GLKERVKSLQTDSSNTDTALTTLE-EALSEKERIIERlkeqrEREDRERLEELESLKKENKDLKEKVSALQPELTEKESS 497
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1738 ISQLEEELDEEQSNTELINDRYRKLTLQVETITTELSAERSFSQKAENARQQmERQNKELKVKLNEMDSTMrSKYKITIA 1817
Cdd:pfam10174 498 LIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEA-VRTNPEINDRIRLLEQEV-ARYKEESG 575
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1818 SLEAKISQL-----EEQMEQESKERIIANkLVRRAEKRLKEV--------LLQVEEERRNADQFKEQL-EKANIRMKQLK 1883
Cdd:pfam10174 576 KAQAEVERLlgilrEVENEKNDKDKKIAE-LESLTLRQMKEQnkkvanikHGQQEMKKKGAQLLEEARrREDNLADNSQQ 654
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 1785379719 1884 RQLEEAEEEASRANSNRRRLQRELEDVTESAESMNREVTTLRSRLRR 1930
Cdd:pfam10174 655 LQLEELMGALEKTRQELDATKARLSSTQQSLAEKDGHLTNLRAERRK 701
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1082-1257 |
1.75e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.23 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1082 KQQLARKEEELQAALARVDDEVGQKNNLLKQLRDLQSQLAELHEDLESEKAARAKAEKQRRDLGEELEALKTELEDTLDS 1161
Cdd:PRK12704 32 KIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1162 TAAQQELRAKREQEVTDLKKTIEedvkvrdaqvtEMRQRHNQVVEEISE-QLEQARRFKgnLEKVKQTLESENTDLIKEV 1240
Cdd:PRK12704 112 LEKKEKELEQKQQELEKKEEELE-----------ELIEEQLQELERISGlTAEEAKEIL--LEKVEEEARHEAAVLIKEI 178
|
170
....*....|....*..
gi 1785379719 1241 KNLqaAKQDSEQRRKKL 1257
Cdd:PRK12704 179 EEE--AKEEADKKAKEI 193
|
|
| Gp58 |
pfam07902 |
gp58-like protein; Sequences found in this family are derived from a number of bacteriophage ... |
1104-1341 |
1.81e-03 |
|
gp58-like protein; Sequences found in this family are derived from a number of bacteriophage and prophage proteins. They are similar to gp58, a minor structural protein of Lactococcus delbrueckii bacteriophage LL-H.
Pssm-ID: 369586 [Multi-domain] Cd Length: 594 Bit Score: 43.41 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1104 GQKNNLLKQLRDLQSQLAELHEDLESEKAARAKAEKQRRDLGEELEALKTELEDTLDSTAAQqelrakreqevtdLKKTI 1183
Cdd:pfam07902 71 GESTGLFKSLEEMLSQLKELNLELTDTKNSNLWSKIKLNNNGMLREYHNDTIKTEIVESAEG-------------IATRI 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1184 EEDVKVRDAQVTEMRQRHNQVVEEISEQLeqARRFKGNLEKVKQTLESENTDLIKEVKNLQ---AAKQDSEQRR------ 1254
Cdd:pfam07902 138 SEDTDKKLALINETISGIRREYQDADRQL--SSSYQAGIEGLKATMASDKIGLQAEIQASAqglSQRYDNEIRKlsakit 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1255 -----------KKLEQQVSEFqirTNESEKVKFELAEKLQKL----QAELDGVSGALGSTEGKSIKLTKDLSTVQSQLQD 1319
Cdd:pfam07902 216 ttssgtteayeSKLDDLRAEF---TRSNQGMRTELESKISGLqstqQSTAYQISQEISNREGAVSRVQQDLDSYQRRLQD 292
|
250 260 270
....*....|....*....|....*....|...
gi 1785379719 1320 TQEL----------LQEETR-QKLNFSSRVRQL 1341
Cdd:pfam07902 293 AEKNyssltqtvkgLQSTVSdPNSKLESRITQL 325
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
969-1224 |
1.82e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 42.93 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 969 LQLEKVTTESRLKKMEEDillledQNAKLAKERKLlDDRIGEFTstmaEEEEKVKSLNKLRNKYEAVIADLEDRLKKEEK 1048
Cdd:pfam02029 93 IADEKESVAERKENNEEE------ENSSWEKEEKR-DSRLGRYK----EEETEIREKEYQENKWSTEVRQAEEEGEEEED 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1049 GRQEMEKMKRKLDGETTDLQDQLLELQQQIEELKQQLARK----EEELQAALARVDDEVGQKNNLLKQLRDLQSQLAELH 1124
Cdd:pfam02029 162 KSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKrghpEVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAE 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1125 EDLESEKaaraKAEKQRRDLGE----ELEALKTEledtldstaaQQElrakREQEVTDLKKTIEEDVKVRDAqvtEMRQR 1200
Cdd:pfam02029 242 VFLEAEQ----KLEELRRRRQEkeseEFEKLRQK----------QQE----AELELEELKKKREERRKLLEE---EEQRR 300
|
250 260
....*....|....*....|....
gi 1785379719 1201 HNQVVEEISEQLEQARRFKGNLEK 1224
Cdd:pfam02029 301 KQEEAERKLREEEEKRRMKEEIER 324
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1131-1344 |
2.09e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.84 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1131 KAARAKAEKQRRDLGEELEALKTEledtldstaaqQELRAKreQEVTDLKKTIEEDVKVRDaqvtemrqrhnqvvEEISE 1210
Cdd:PRK12704 34 KEAEEEAKRILEEAKKEAEAIKKE-----------ALLEAK--EEIHKLRNEFEKELRERR--------------NELQK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1211 QLEQARRFKGNLEKVKQTLESENTDLIKEVKNLQAAKQDSEQRRKKLEqqvsefqirtnesekvkfelaEKLQKLQAELD 1290
Cdd:PRK12704 87 LEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELE---------------------ELIEEQLQELE 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1785379719 1291 GVSGaLGSTEGKSIKLTKdlstvqsqlqdtqelLQEETRQKLnfSSRVRQLEEE 1344
Cdd:PRK12704 146 RISG-LTAEEAKEILLEK---------------VEEEARHEA--AVLIKEIEEE 181
|
|
| PRK05431 |
PRK05431 |
seryl-tRNA synthetase; Provisional |
1490-1560 |
2.13e-03 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 235461 [Multi-domain] Cd Length: 425 Bit Score: 42.75 E-value: 2.13e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1785379719 1490 RALEEAIDLKDELDRQNKQLRAEMDDLVSSKDDVGKNVHELERSK---RALEQQVQEMKTQIEELEDELQAIED 1560
Cdd:PRK05431 21 RGFPLDVDELLELDEERRELQTELEELQAERNALSKEIGQAKRKGedaEALIAEVKELKEEIKALEAELDELEA 94
|
|
| COG4487 |
COG4487 |
Uncharacterized conserved protein, contains DUF2130 domain [Function unknown]; |
864-1059 |
2.27e-03 |
|
Uncharacterized conserved protein, contains DUF2130 domain [Function unknown];
Pssm-ID: 443580 [Multi-domain] Cd Length: 425 Bit Score: 42.63 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 864 VKDTQVKTESELKEMANKYQQlfEEKSILAEQLQAETELFAEAEEMRARLASKKQELEEILHDLEARVEEEEERTL-QLQ 942
Cdd:COG4487 24 VKQRRAEFEKELAERLADAAK--REAALELAEAKAKAQLQEQVAEKDAEIAELRARLEAEERKKALAVAEEKEKELaALQ 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 943 NEKKKMHQHIQDLEeqleeeegaRQKLQLEKVTTEsrlkkmeediLLLEDQNAKLAKERKLLDDRIGEFTSTMAEEEEKV 1022
Cdd:COG4487 102 EALAEKDAKLAELQ---------AKELELLKKERE----------LEDAKREAELTVEKERDEELDELKEKLKKEEEEKQ 162
|
170 180 190
....*....|....*....|....*....|....*...
gi 1785379719 1023 KSLNKLRN-KYEAVIADLEDrlkkeekgrqEMEKMKRK 1059
Cdd:COG4487 163 LAEKSLKVaEYEKQLKDMQE----------QIEELKRK 190
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
914-1136 |
2.42e-03 |
|
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: 42.44 E-value: 2.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 914 ASKKQELEEILHDLEARVEEEEERTLQLQNEKKKMHQHIQDLEEQLEEEEGARQKLQLEKVTTESRLKKMEEDIlllEDQ 993
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI---AEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 994 NAKLAKERKLLDDRIGE--------------FTSTMAEEEEKVKSLNKLRNKYEAVIADLEDRLKKEEKGRQEMEKMKRK 1059
Cdd:COG4942 96 RAELEAQKEELAELLRAlyrlgrqpplalllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1785379719 1060 LDGETTDLQDQLLELQQQIEELKQQLARKEEELQAALARVDDEVGQKNNLLKQLRDLQSQLAELHEDLESEKAARAK 1136
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1149-1516 |
2.63e-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: 42.57 E-value: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1149 EALKTELEDTLDSTAAQQELRAKREQEVTDLKKTIEEDVKVRDAQVTEMRQRhnqvVEEISEQLEQARRFKGNLEKVKQT 1228
Cdd:pfam07888 30 ELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESR----VAELKEELRQSREKHEELEEKYKE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1229 LESENTDLIKEVKNLQAAKQDSEQRRKKLEQQVSEFQIRTNESEKVKFELAEKLQKLQAELDGVSGALGSTEGKSIKLTK 1308
Cdd:pfam07888 106 LSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1309 DLSTVQSQLQDTQELLQEETRQKLNFSSRVRQLEEEKNNLMENLEEEESAKAQLSRQLQALQQqlleSKKRMEDQGGMVE 1388
Cdd:pfam07888 186 ELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNA----SERKVEGLGEELS 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1389 AMEEAKKKSYKELEflQQRFdEKHQINDKLEKT-------RNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEK 1461
Cdd:pfam07888 262 SMAAQRDRTQAELH--QARL-QAAQLTLQLADAslalregRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEER 338
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1785379719 1462 NisarygeERDRAEAE-AREKETKALSLSRALEEAIDLKDEL---DRQNKQLRAEMDDL 1516
Cdd:pfam07888 339 M-------EREKLEVElGREKDCNRVQLSESRRELQELKASLrvaQKEKEQLQAEKQEL 390
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
846-1031 |
3.00e-03 |
|
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: 42.06 E-value: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 846 QVTRQDEVMQAKVVELQKVKDTQVKTESELKEMANKYQQLFEE----KSILAEQLQA--------ETELFAEAEEMrARL 913
Cdd:COG4942 56 QLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEleaqKEELAELLRAlyrlgrqpPLALLLSPEDF-LDA 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 914 ASKKQELEEILHDLEARVEEEEERTLQLQNEKKKMHQHIQDLEEQLEEEEGARQKLQLEKVTTESRLKKMEEDILLLEDQ 993
Cdd:COG4942 135 VRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAE 214
|
170 180 190
....*....|....*....|....*....|....*...
gi 1785379719 994 NAKLAKERKLLDDRIGEFTSTMAEEEEKVKSLNKLRNK 1031
Cdd:COG4942 215 LAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
928-1326 |
3.42e-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: 42.42 E-value: 3.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 928 EARVEEEEERTLQLQNEKKKMhqhiqdleeqleEEEGARQKLQLEKVTTESRLKKMEEdilllEDQNAKLAKERKLLDDR 1007
Cdd:pfam05557 1 RAELIESKARLSQLQNEKKQM------------ELEHKRARIELEKKASALKRQLDRE-----SDRNQELQKRIRLLEKR 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1008 IGEFTSTMAEEEEkvksLNKLRNKYEAVIADLedrLKKEEKGRQEMEKMKRKLDGETtdlqdqlLELQQQIEELKQQLAR 1087
Cdd:pfam05557 64 EAEAEEALREQAE----LNRLKKKYLEALNKK---LNEKESQLADAREVISCLKNEL-------SELRRQIQRAELELQS 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1088 KEEELQAALARVDDEVGQKNNLLKQLRDLQSQLAELHEDLESEKAARAKAEKQRRDlGEELEALKTELEDTLDSTAAQQE 1167
Cdd:pfam05557 130 TNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQD-SEIVKNSKSELARIPELEKELER 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1168 LRAKREQ-------------EVTDLKKTIEEDVKVRDAQVT-EMRQRHNQVVEEISEQLEQ-----------ARRFKGNL 1222
Cdd:pfam05557 209 LREHNKHlnenienklllkeEVEDLKRKLEREEKYREEAATlELEKEKLEQELQSWVKLAQdtglnlrspedLSRRIEQL 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1223 EKVKQTLESENTDLIKEVKNLQAAKQDSEQRRKKLEQQVSEFQIRTNESEKVKFELAEKLQKLQAELDGVSGALGS---- 1298
Cdd:pfam05557 289 QQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAILESydke 368
|
410 420 430
....*....|....*....|....*....|
gi 1785379719 1299 --TEGKSIKLTKDLSTVQSQLQDTQELLQE 1326
Cdd:pfam05557 369 ltMSNYSPQLLERIEEAEDMTQKMQAHNEE 398
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1482-1716 |
3.67e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 3.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1482 ETKALSLSRALEEAIDLKDELDRQNKQLRAEMDDLVSSKDDVGKNVHELERSKRALEQQVQEMKTQIEELEDELqaiedg 1561
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL------ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1562 klrlevnmqamkAQFERDLQNRDDSNDEKKKLL--------FKQVREMEVELEEERKQKSQILAAKKKLEMDLQDMESQM 1633
Cdd:COG3883 89 ------------GERARALYRSGGSVSYLDVLLgsesfsdfLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1634 DSANKGRDEAVKQLKKLQLQFKEVWREVEETRAARDEIFVQSRDNEKKLKSLEAELLQLQEDLAAAERAKRQAQQERDDL 1713
Cdd:COG3883 157 AELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
...
gi 1785379719 1714 ADE 1716
Cdd:COG3883 237 AAA 239
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1044-1309 |
3.87e-03 |
|
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: 41.72 E-value: 3.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1044 KKEEKGRQEMEKMKRkLDGETTDLQDQLLELQQQIEELKQQLARKEEELQAALArvddevgQKNNLLKQLRDLQSQLAEL 1123
Cdd:pfam15905 63 KKSQKNLKESKDQKE-LEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVR-------EKTSLSASVASLEKQLLEL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1124 HE--DLESEKAARAKAEKQRRDLGEELEALKTELEDTLDSTAAQQELRAKREQEV-TDLKKTIEEDVKVRDAQVTEMRQR 1200
Cdd:pfam15905 135 TRvnELLKAKFSEDGTQKKMSSLSMELMKLRNKLEAKMKEVMAKQEGMEGKLQVTqKNLEHSKGKVAQLEEKLVSTEKEK 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1201 HNQ---------VVEEISEQLEQARRFKGNLEKVKQTLESENTDLIKEVKNLQAAKQDSEqrrKKLEQQVSEFQIRTNES 1271
Cdd:pfam15905 215 IEEkseteklleYITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELS---KQIKDLNEKCKLLESEK 291
|
250 260 270
....*....|....*....|....*....|....*...
gi 1785379719 1272 EKVKFELAEKLQKLQAELDGVSGALGSTEGKSIKLTKD 1309
Cdd:pfam15905 292 EELLREYEEKEQTLNAELEELKEKLTLEEQEHQKLQQK 329
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1006-1943 |
3.89e-03 |
|
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: 42.34 E-value: 3.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1006 DRIGEFTSTMAEEEEKVKSLNKLRNKYEAVIADLEDRLKKEEKGRQEMEKMKRKLDGETtdlqDQLLELQQQIEELKQQL 1085
Cdd:TIGR00606 189 ETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENEL----DPLKNRLKEIEHNLSKI 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1086 ARKEEELQAALARVDDEVGQKNNL-LKQLRDLQSQLAELHEDLESEKAARAKAEKQRRDLGEELEAL----------KTE 1154
Cdd:TIGR00606 265 MKLDNEIKALKSRKKQMEKDNSELeLKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLnkerrllnqeKTE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1155 LEDTLDSTAAQ----QELRAKREQEVTDLKKTIEEDVKVRDAQV-TEMRQRHNQVVEEISEQLEQARRFKGNLEKvKQTL 1229
Cdd:TIGR00606 345 LLVEQGRLQLQadrhQEHIRARDSLIQSLATRLELDGFERGPFSeRQIKNFHTLVIERQEDEAKTAAQLCADLQS-KERL 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1230 ESENTDLIKEVKN-----LQAAKQDSEQRRKKLEQQVSEFQIRTNESEKVkFELAEKLQKLQAELDGVSGAlGSTEGKsI 1304
Cdd:TIGR00606 424 KQEQADEIRDEKKglgrtIELKKEILEKKQEELKFVIKELQQLEGSSDRI-LELDQELRKAERELSKAEKN-SLTETL-K 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1305 KLTKDLSTVQSQLQDTQELLQEETRQKLNFSSRVRQLE---EEKNNLMENLEEEESAKAQLSRQLQALQQQLLESKKRME 1381
Cdd:TIGR00606 501 KEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEmltKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLH 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1382 DQGGMVEAMEEAKKKSYKELEFLQQRfdeKHQINDKLEKTRNRLQQELD---------DLMVDLDHQRQIVsnleKKQKK 1452
Cdd:TIGR00606 581 SKSKEINQTRDRLAKLNKELASLEQN---KNHINNELESKEEQLSSYEDklfdvcgsqDEESDLERLKEEI----EKSSK 653
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1453 FDQMLAEEKNISARYGEERD--------------RAEAEARE----KETKALSLSRALEEAIDLKDELDRQNKQLRAEMD 1514
Cdd:TIGR00606 654 QRAMLAGATAVYSQFITQLTdenqsccpvcqrvfQTEAELQEfisdLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAP 733
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1515 DLVSSKDDVGKNVHELERSKRALEQQVQEMKTQIEELEDELQAIeDGKLRLEVNMQAMKAQFERDLQNRDDSNDEKKKLL 1594
Cdd:TIGR00606 734 GRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTI-MPEEESAKVCLTDVTIMERFQMELKDVERKIAQQA 812
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1595 FKQVREMEVELEEERKQKsqilaaKKKLEMDLQDMESQMDSANKGRDEAVKQLKKLQLQFKEVWRE---VEETRAARDEI 1671
Cdd:TIGR00606 813 AKLQGSDLDRTVQQVNQE------KQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEklqIGTNLQRRQQF 886
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1672 FVQSRDNEKKLKSLEAELLQLQEDLAAAERAKRQAQQERDDLadeLSNGVSGKSALLDEKRALEMRISQLEEELDEEQSN 1751
Cdd:TIGR00606 887 EEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEEL---ISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENK 963
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1752 TELINDRYRKltlQVETITTELSAErsfsqkAENARQQMERQNKELKVKLNEMDSTMRS----KYKITIASLEAKISQLE 1827
Cdd:TIGR00606 964 IQDGKDDYLK---QKETELNTVNAQ------LEECEKHQEKINEDMRLMRQDIDTQKIQerwlQDNLTLRKRENELKEVE 1034
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1828 EQMEQESKEriianklvrRAEKRLKEVLLQVEEERRNADQFKEQLEKANIRMKQLKRQLEEAEEEASRAN-SNRRRLQRE 1906
Cdd:TIGR00606 1035 EELKQHLKE---------MGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQfRDAEEKYRE 1105
|
970 980 990
....*....|....*....|....*....|....*..
gi 1785379719 1907 LEDVTESAESMNREVTTLRSRLRRAPIQFTTRTIRQV 1943
Cdd:TIGR00606 1106 MMIVMRTTELVNKDLDIYYKTLDQAIMKFHSMKMEEI 1142
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1400-1561 |
4.48e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.06 E-value: 4.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1400 ELEFLQQRFDEKHQINDKLEKTRNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAE----EKNISARYGEERDRAE 1475
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEvearIKKYEEQLGNVRNNKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1476 AEAREKETKALSLSRAL--EEAIDLKDELDRQNKQLRAEMDDLVSSKDdvgknvhELERSKRALEQQVQEMKTQIEELED 1553
Cdd:COG1579 91 YEALQKEIESLKRRISDleDEILELMERIEELEEELAELEAELAELEA-------ELEEKKAELDEELAELEAELEELEA 163
|
....*...
gi 1785379719 1554 ELQAIEDG 1561
Cdd:COG1579 164 EREELAAK 171
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
911-1055 |
4.60e-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: 4.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 911 ARLASKKQELEEILHDLEARVEEEEERTLQLQNEKKKMHQHIQDLEEQLEEEEG--ARQKLQLEKVTTESRLKKMEEDIL 988
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEAriKKYEEQLGNVRNNKEYEALQKEIE 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1785379719 989 LLEDQNAKLAKERKLLDDRIGEFTSTMAEEEEKVKS----LNKLRNKYEAVIADLEDRLKKEEKGRQEMEK 1055
Cdd:COG1579 100 SLKRRISDLEDEILELMERIEELEEELAELEAELAEleaeLEEKKAELDEELAELEAELEELEAEREELAA 170
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
851-1095 |
4.68e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 4.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 851 DEVMQAKVVELQKVKDTQVKTESELKEMANKYQQLFEEKSILAEQLqaetelfaeaEEMRARLASKKQELEEILHDLEAR 930
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAEL----------EALQAEIDKLQAEIAEAEAEIEER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 931 VEEEEERTLQLQNEkkkmhqhiQDLEEQLEEEEGAR------QKLQLEKVTTESRLKKMEEdillLEDQNAKLAKERKLL 1004
Cdd:COG3883 85 REELGERARALYRS--------GGSVSYLDVLLGSEsfsdflDRLSALSKIADADADLLEE----LKADKAELEAKKAEL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1005 DDRIGEFTSTMAEEEEKVKSLNKLRNKYEAVIADLEDRLKKEEKGRQEMEKMKRKLDGETTDLQDQLLELQQQIEELKQQ 1084
Cdd:COG3883 153 EAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
250
....*....|.
gi 1785379719 1085 LARKEEELQAA 1095
Cdd:COG3883 233 AAAAAAAAAAA 243
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1469-1913 |
4.87e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 4.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1469 EERDRAEAEAREKETKALSLSRALEEAIDLKDELDRQNKQLRAEMDDLvsskdDVGKNVHELERSKRALEQQVQEMKTQI 1548
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL-----EKLLQLLPLYQELEALEAELAELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1549 EELEDELQAIEDGKLRLE-VNMQAMKAQFERDLQNRDDSNDEKKKLlfkqvREMEVELEEERKQKSQILAAKKKLEMDLQ 1627
Cdd:COG4717 149 EELEERLEELRELEEELEeLEAELAELQEELEELLEQLSLATEEEL-----QDLAEELEELQQRLAELEEELEEAQEELE 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1628 DMESQMDSANKG--RDEAVKQLKKLQLQFK-------------------EVWREVEETRAARDEIFVQSRDNEKKLKSLE 1686
Cdd:COG4717 224 ELEEELEQLENEleAAALEERLKEARLLLLiaaallallglggsllsliLTIAGVLFLVLGLLALLFLLLAREKASLGKE 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1687 AELLQLQEDLAAAERAKRQAQQERDDLADELSNgvsgKSALLDEKRALEMRISQLEEELDEEQSNTELINDRYRKLTLQV 1766
Cdd:COG4717 304 AEELQALPALEELEEEELEELLAALGLPPDLSP----EELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEA 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1767 EtitteLSAERSFSQKAENARQQMERQNK--ELKVKLNEMDSTMRSKY-KITIASLEAKISQLEEQMEQESKERiianKL 1843
Cdd:COG4717 380 G-----VEDEEELRAALEQAEEYQELKEEleELEEQLEELLGELEELLeALDEEELEEELEELEEELEELEEEL----EE 450
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1844 VRRAEKRLKEVLLQVEEERRnadqfkeqLEKANIRMKQLKRQLEEAEEEASRANSNRRRLQRELEDVTES 1913
Cdd:COG4717 451 LREELAELEAELEQLEEDGE--------LAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1457-1558 |
5.04e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.69 E-value: 5.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1457 LAEEKNISARYGEERDRAEAEAREKETKALSLSRALEEAIDLKDELDRQNKQLRAE------------------MDDLVS 1518
Cdd:PRK12704 28 IAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNElqklekrllqkeenldrkLELLEK 107
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1785379719 1519 SKDDVGKNVHELERSKRALEQQVQEMKTQIEELEDELQAI 1558
Cdd:PRK12704 108 REEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERI 147
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1083-1251 |
5.32e-03 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 41.67 E-value: 5.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1083 QQLARKEEELQA-ALARVDDEVGQKNNLLKQLRDLQSQLAELH-------EDLESEKAARAKAEKQRRDLGEELEALKTE 1154
Cdd:pfam09731 297 DQLSKKLAELKKrEEKHIERALEKQKEELDKLAEELSARLEEVraadeaqLRLEFEREREEIRESYEEKLRTELERQAEA 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1155 LEDTLDSTAAQQELRAKREQEvTDLKKTIEEDVKVRDAQVTEMRQRHN---QVVEEISEQLEQARRFK---GNLEKVKQT 1228
Cdd:pfam09731 377 HEEHLKDVLVEQEIELQREFL-QDIKEKVEEERAGRLLKLNELLANLKgleKATSSHSEVEDENRKAQqlwLAVEALRST 455
|
170 180
....*....|....*....|....*...
gi 1785379719 1229 LESENTD-----LIKEVKNLQAAKQDSE 1251
Cdd:pfam09731 456 LEDGSADsrprpLVRELKALKELASDDE 483
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1471-1698 |
5.38e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.84 E-value: 5.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1471 RDRAEAEAREKETKALSLSRALEEAID-LKDELDRQNKQLRAEMDDLVSSKDDVGKnvhELERSKRALEQQVQEMKTQIE 1549
Cdd:PRK05771 34 EDLKEELSNERLRKLRSLLTKLSEALDkLRSYLPKLNPLREEKKKVSVKSLEELIK---DVEEELEKIEKEIKELEEEIS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1550 ELEDELQAIEDGKLRLEVnmqaMKAqFERDLQNRDDS----------NDEKKKLLFKQVREMEVELEEERKQKSQILAAK 1619
Cdd:PRK05771 111 ELENEIKELEQEIERLEP----WGN-FDLDLSLLLGFkyvsvfvgtvPEDKLEELKLESDVENVEYISTDKGYVYVVVVV 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1785379719 1620 KKlemdlqdmesqmdsanKGRDEAVKQLKKlqLQFKEVwrEVEETRAARDEIfvqsRDNEKKLKSLEAELLQLQEDLAA 1698
Cdd:PRK05771 186 LK----------------ELSDEVEEELKK--LGFERL--ELEEEGTPSELI----REIKEELEEIEKERESLLEELKE 240
|
|
| CagA_N |
pfam18971 |
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ... |
1479-1732 |
5.63e-03 |
|
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial virulence determinant and critical for gastric carcinogenesis. X-ray crystallographic analysis of the N-terminal CagA fragment (residues 1-876) revealed that the region has a structure comprised of three discrete domains. Domain I constitutes a mobile CagA N terminus, while Domain II tethers CagA to the plasma membrane by interacting with membrane phosphatidylserine. Domain III interacts intramolecularly with the intrinsically disordered C-terminal region, and this interaction potentiates the pathogenic scaffold/hub function of CagA.
Pssm-ID: 408741 [Multi-domain] Cd Length: 876 Bit Score: 41.68 E-value: 5.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1479 REKETKALSLSRALEEAIDLKDELDRQNKQLRAE---MDDLVSSKDDVGkNVHELERSKRALEQQVQEMKTQIEELEDEL 1555
Cdd:pfam18971 559 RNLENKLTAKGLSLQEANKLIKDFLSSNKELAGKalnFNKAVAEAKSTG-NYDEVKKAQKDLEKSLRKREHLEKEVEKKL 637
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1556 QAIEDGKLRLEVNMQAMKAQFERDLQNRDDSNDEKKKLLFKQVREMEveleeerkqKSQILAAKKKLEMDLQDMESQMDS 1635
Cdd:pfam18971 638 ESKSGNKNKMEAKAQANSQKDEIFALINKEANRDARAIAYTQNLKGI---------KRELSDKLEKISKDLKDFSKSFDE 708
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1636 ANKGRD----EAVKQLKKLQLQFKEV-----W-REVEETRAARDEIFVQSRDNEKKLKSLEAELLQLQEDLAaaerakrq 1705
Cdd:pfam18971 709 FKNGKNkdfsKAEETLKALKGSVKDLginpeWiSKVENLNAALNEFKNGKNKDFSKVTQAKSDLENSVKDVI-------- 780
|
250 260
....*....|....*....|....*..
gi 1785379719 1706 AQQERDDLADELSNGVSGKSALLDEKR 1732
Cdd:pfam18971 781 INQKVTDKVDNLNQAVSVAKAMGDFSR 807
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1082-1284 |
5.75e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 41.22 E-value: 5.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1082 KQQLARKEEELQ-------AALARVDDEVGQKNNLLKQLRDLQSQLAELHEDLESEKAARAKAEK----QRRDLGEELEA 1150
Cdd:PRK11637 53 QQDIAAKEKSVRqqqqqraSLLAQLKKQEEAISQASRKLRETQNTLNQLNKQIDELNASIAKLEQqqaaQERLLAAQLDA 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1151 L-----KTELEDTLDSTAAQQE---------LRAKREQEVTDLKKTIEEdvkvRDAQVTEMRQRHNQVVEEISEQLEQAR 1216
Cdd:PRK11637 133 AfrqgeHTGLQLILSGEESQRGerilayfgyLNQARQETIAELKQTREE----LAAQKAELEEKQSQQKTLLYEQQAQQQ 208
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1785379719 1217 RFKGNLEKVKQTLESENTDLIKEVKNLQAAKQDSEQRRKKLEQQVSEFQIRTN----ESEKVKFELAEKLQK 1284
Cdd:PRK11637 209 KLEQARNERKKTLTGLESSLQKDQQQLSELRANESRLRDSIARAEREAKARAErearEAARVRDKQKQAKRK 280
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
992-1181 |
5.81e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.54 E-value: 5.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 992 DQNAKLAKERK----LLDDRIGEFTSTMAEEEEkvkSLNKLRNKYEAVIADLEdRLKKEEKgrqemekMKRKlDGETTDL 1067
Cdd:PHA02562 223 DELVEEAKTIKaeieELTDELLNLVMDIEDPSA---ALNKLNTAAAKIKSKIE-QFQKVIK-------MYEK-GGVCPTC 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1068 QDQLLELQQQIEELKQQLARKEEELQAALARVDDEVGQKNNLLKQ---LRDLQSQLAELHEDLESE-------KAARAKA 1137
Cdd:PHA02562 291 TQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQskkLLELKNKISTNKQSLITLvdkakkvKAAIEEL 370
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1785379719 1138 EKQRRDLGEELEALKTELEDtLDSTAAQQELRAKREQEVTDLKK 1181
Cdd:PHA02562 371 QAEFVDNAEELAKLQDELDK-IVKTKSELVKEKYHRGIVTDLLK 413
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
952-1159 |
7.85e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 7.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 952 IQDLEEqleeeegarqklqlekvttesRLKKMEEDILLLEDQNAKLAKERKLLDDRIGEFT--STMAEEEEKVKSLnklr 1029
Cdd:COG4913 612 LAALEA---------------------ELAELEEELAEAEERLEALEAELDALQERREALQrlAEYSWDEIDVASA---- 666
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1030 nkyEAVIADLEDRLKKEEKGRQEMEKMKRKLDG---ETTDLQDQLLELQQQIEELKQQLARKEEELQAALARVDDEVGQK 1106
Cdd:COG4913 667 ---EREIAELEAELERLDASSDDLAALEEQLEEleaELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLA 743
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1785379719 1107 NNLLKQlrDLQSQLAELHEDlESEKAARAKAEKQRRDLGEELEALKTELEDTL 1159
Cdd:COG4913 744 RLELRA--LLEERFAAALGD-AVERELRENLEERIDALRARLNRAEEELERAM 793
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1111-1286 |
9.12e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 40.33 E-value: 9.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1111 KQLRDLQSQLAELHEDLESEKAARAkaekqrrDLGEELEALKTELEDTLDSTAAQQELRAKREQEVTDLKKTIEEDVKVR 1190
Cdd:PRK09039 53 SALDRLNSQIAELADLLSLERQGNQ-------DLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQEL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379719 1191 DAQVTEMRQRHNQvVEEISEQLEQARRfkgnlekvkqtlesentdlikEVKNLQAAKQDSEQRRKKLEQQVSEFQIRTNE 1270
Cdd:PRK09039 126 DSEKQVSARALAQ-VELLNQQIAALRR---------------------QLAALEAALDASEKRDRESQAKIADLGRRLNV 183
|
170
....*....|....*.
gi 1785379719 1271 SekvkfeLAEKLQKLQ 1286
Cdd:PRK09039 184 A------LAQRVQELN 193
|
|
| |
