|
Name |
Accession |
Description |
Interval |
E-value |
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
73-717 |
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: 1385.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 73 PGVLRNLETRYELNEIYTYTGNILIAVNPFQRLPHIYETDMMEQYKGIALGELSPHVFAIGDAAYRAMINEGKNNSILVS 152
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPHLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 153 GESGAGKTETTKMLMRYLAFLGGRSGVEGRTVEQQVLESNPVLEAFGNAKTLRNNNSSRFGKFVEIQFDKNGRISGAAIR 232
Cdd:cd01384 81 GESGAGKTETTKMLMQYLAYMGGRAVTEGRSVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAGRISGAAIR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 233 TYLLERSRVCQISDPERNYHCFYLLCA-APPEDIKKYKLENPHKFHYLNQSSCYKLDGVDDASEYLETRRAMDVVGISNE 311
Cdd:cd01384 161 TYLLERSRVVQVSDPERNYHCFYQLCAgAPPEDREKYKLKDPKQFHYLNQSKCFELDGVDDAEEYRATRRAMDVVGISEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 312 EQEAIFRVVAAILHLGNIDFGKGEEIDSSVIKDKDSRSHLNMAAELLMCNAQSLEDALIRRVMVTPEEIITRTLDPDNAI 391
Cdd:cd01384 241 EQDAIFRVVAAILHLGNIEFSKGEEDDSSVPKDEKSEFHLKAAAELLMCDEKALEDALCKRVIVTPDGIITKPLDPDAAT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 392 ASRDTLAKTIYSHLFDWIVNKINTSIGQDPRSKSIIGVLDIYGFESFKCNSFEQFCINFTNEKLQQHFNQHVFKMEQEEY 471
Cdd:cd01384 321 LSRDALAKTIYSRLFDWLVDKINRSIGQDPNSKRLIGVLDIYGFESFKTNSFEQFCINLANEKLQQHFNQHVFKMEQEEY 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 472 TKEEIAWSYIEFIDNQDVLELIEKKPGGIISLLDEACMFPKSTHETFSQKLFQTFKEHERFAKPKLSRTDFTISHYAGEV 551
Cdd:cd01384 401 TKEEIDWSYIEFVDNQDVLDLIEKKPGGIIALLDEACMFPRSTHETFAQKLYQTLKDHKRFSKPKLSRTDFTIDHYAGDV 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 552 TYQSNHFIDKNKDYIVAEHQALFTASNCKFVAGLFHAL-HEDSSRSSKFSSIGSRFKQQLHSLMESLNGTEPHYIRCIKP 630
Cdd:cd01384 481 TYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLFPPLpREGTSSSSKFSSIGSRFKQQLQELMETLNTTEPHYIRCIKP 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 631 NNVLKPGIFENFNVIHQLRCGGVLEAIRISCAGYPTRLAFYDFLDRFGLLAPEVLEGNYDDKVACQMILDKKSLTDYQIG 710
Cdd:cd01384 561 NNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGLLAPEVLKGSDDEKAACKKILEKAGLKGYQIG 640
|
....*..
gi 30685403 711 KTKIFLR 717
Cdd:cd01384 641 KTKVFLR 647
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
60-728 |
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: 1022.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 60 GVDDMTKLSYLHEPGVLRNLETRYELNEIYTYTGNILIAVNPFQRLPhIYETDMMEQYKGIALGELSPHVFAIGDAAYRA 139
Cdd:smart00242 7 GVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLP-IYTDEVIKKYRGKSRGELPPHVFAIADNAYRN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 140 MINEGKNNSILVSGESGAGKTETTKMLMRYLAFLGGrSGVEGRTVEQQVLESNPVLEAFGNAKTLRNNNSSRFGKFVEIQ 219
Cdd:smart00242 86 MLNDKENQSIIISGESGAGKTENTKKIMQYLASVSG-SNTEVGSVEDQILESNPILEAFGNAKTLRNNNSSRFGKFIEIH 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 220 FDKNGRISGAAIRTYLLERSRVCQISDPERNYHCFYLLCA-APPEDIKKYKLENPHKFHYLNQSSCYKLDGVDDASEYLE 298
Cdd:smart00242 165 FDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAgASEELKKELGLKSPEDYRYLNQGGCLTVDGIDDAEEFKE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 299 TRRAMDVVGISNEEQEAIFRVVAAILHLGNIDFG-KGEEIDSSVIKDKDsrsHLNMAAELLMCNAQSLEDALIRRVMVTP 377
Cdd:smart00242 245 TLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEeGRNDNAASTVKDKE---ELSNAAELLGVDPEELEKALTKRKIKTG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 378 EEIITRTLDPDNAIASRDTLAKTIYSHLFDWIVNKINTSIGQDPRSKSIIGVLDIYGFESFKCNSFEQFCINFTNEKLQQ 457
Cdd:smart00242 322 GEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGSTYFIGVLDIYGFEIFEVNSFEQLCINYANEKLQQ 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 458 HFNQHVFKMEQEEYTKEEIAWSYIEFIDNQDVLELIEKKPGGIISLLDEACMFPKSTHETFSQKLFQTFKEHERFAKP-K 536
Cdd:smart00242 402 FFNQHVFKLEQEEYEREGIDWTFIDFFDNQDCIDLIEKKPPGILSLLDEECRFPKGTDQTFLEKLNQHHKKHPHFSKPkK 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 537 LSRTDFTISHYAGEVTYQSNHFIDKNKDYIVAEHQALFTASNCKFVAGLFHALHEDSSRSSKFSSIGSRFKQQLHSLMES 616
Cdd:smart00242 482 KGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSGVSNAGSKKRFQTVGSQFKEQLNELMDT 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 617 LNGTEPHYIRCIKPNNVLKPGIFENFNVIHQLRCGGVLEAIRISCAGYPTRLAFYDFLDRFGLLAPEVLE-GNYDDKVAC 695
Cdd:smart00242 562 LNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRLPFDEFLQRYRVLLPDTWPpWGGDAKKAC 641
|
650 660 670
....*....|....*....|....*....|....*
gi 30685403 696 QMILDKKSL--TDYQIGKTKIFLRAGQMAELDARR 728
Cdd:smart00242 642 EALLQSLGLdeDEYQLGKTKVFLRPGQLAELEELR 676
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
8-1122 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 907.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 8 VGSHVWVEDPHLAWIDGEVTRIDGI-NVHVKTKKGKTVVTNVYFPKDTEA------PSGGVDDMTKLSYLHEPGVLRNLE 80
Cdd:COG5022 8 VGSGCWIPDEEKGWIWAEIIKEAFNkGKVTEEGKKEDGESVSVKKKVLGNdriklpKFDGVDDLTELSYLNEPAVLHNLE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 81 TRYELNEIYTYTGNILIAVNPFQRLPhIYETDMMEQYKGIALGELSPHVFAIGDAAYRAMINEGKNNSILVSGESGAGKT 160
Cdd:COG5022 88 KRYNNGQIYTYSGLVLIAVNPYRDLG-IYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 161 ETTKMLMRYLAFLGGRSGVEGRTVEQQVLESNPVLEAFGNAKTLRNNNSSRFGKFVEIQFDKNGRISGAAIRTYLLERSR 240
Cdd:COG5022 167 ENAKRIMQYLASVTSSSTVEISSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETYLLEKSR 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 241 VCQISDPERNYHCFYLLCAAPPEDIKKYKL-ENPHKFHYLNQSSCYKLDGVDDASEYLETRRAMDVVGISNEEQEAIFRV 319
Cdd:COG5022 247 VVHQNKNERNYHIFYQLLAGDPEELKKLLLlQNPKDYIYLSQGGCDKIDGIDDAKEFKITLDALKTIGIDEEEQDQIFKI 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 320 VAAILHLGNIDFGKGEEiDSSVIKDKDsrsHLNMAAELLMCNAQSLEDALIRRVMVTPEEIITRTLDPDNAIASRDTLAK 399
Cdd:COG5022 327 LAAILHIGNIEFKEDRN-GAAIFSDNS---VLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALAIRDSLAK 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 400 TIYSHLFDWIVNKINTSIGQDPRSKSIIGVLDIYGFESFKCNSFEQFCINFTNEKLQQHFNQHVFKMEQEEYTKEEIAWS 479
Cdd:COG5022 403 ALYSNLFDWIVDRINKSLDHSAAASNFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKEGIEWS 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 480 YIEFIDNQDVLELIEKK-PGGIISLLDEACMFPKSTHETFSQKLFQTFKEH--ERFAKPKLSRTDFTISHYAGEVTYQSN 556
Cdd:COG5022 483 FIDYFDNQPCIDLIEKKnPLGILSLLDEECVMPHATDESFTSKLAQRLNKNsnPKFKKSRFRDNKFVVKHYAGDVEYDVE 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 557 HFIDKNKDYIVAEHQALFTASNCKFVAGLFHALhEDSSRSSKFSSIGSRFKQQLHSLMESLNGTEPHYIRCIKPNNVLKP 636
Cdd:COG5022 563 GFLDKNKDPLNDDLLELLKASTNEFVSTLFDDE-ENIESKGRFPTLGSRFKESLNSLMSTLNSTQPHYIRCIKPNEEKSP 641
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 637 GIFENFNVIHQLRCGGVLEAIRISCAGYPTRLAFYDFLDRFGLLAPE-VLEGNY----DDKVACQMILD--KKSLTDYQI 709
Cdd:COG5022 642 WTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSkSWTGEYtwkeDTKNAVKSILEelVIDSSKYQI 721
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 710 GKTKIFLRAGQMAELDARRAEVLGNAARVIQRQFRTCMARKNYRSIRNAAIVLQSFLRGEIARAVHKKLRIEAAALRVQK 789
Cdd:COG5022 722 GNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKKIQVIQHGFRLRRLVDYELKWRLFIKLQP 801
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 790 NFRRYVDRKSFVTTRSSTIVLQTGL-RAMIARSEFRLRRQRKAAIVLQAHWRGRQAFSYYTRLQKAAIVTQCAWRCRLAR 868
Cdd:COG5022 802 LLSLLGSRKEYRSYLACIIKLQKTIkREKKLRETEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAE 881
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 869 RELRMLKMAARDTGALKDAKNKLEQRVEELSLRLHLEKRLRTdleEAKVQEVAKLQEALHTMRLQLKETTAMVVKEQEAA 948
Cdd:COG5022 882 RQLQELKIDVKSISSLKLVNLELESEIIELKKSLSSDLIENL---EFKTELIARLKKLLNNIDLEEGPSIEYVKLPELNK 958
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 949 RVaiEEASSVNKEPVVVEDTekIDSLSNEIDRLKGLLS-SETHKADEAQHAYQSALVQNEElcKKLEEAGRKIDQLQDSV 1027
Cdd:COG5022 959 LH--EVESKLKETSEEYEDL--LKKSTILVREGNKANSeLKNFKKELAELSKQYGALQEST--KQLKELPVEVAELQSAS 1032
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 1028 QRF-------------QEKVFSLESENKVLRQQTLTIS---PTTRALALRPKTTIIQRTPEKD-TFSNGE--TTQLQEPE 1088
Cdd:COG5022 1033 KIIssestelsilkplQKLKGLLLLENNQLQARYKALKlrrENSLLDDKQLYQLESTENLLKTiNVKDLEvtNRNLVKPA 1112
|
1130 1140 1150
....*....|....*....|....*....|....*...
gi 30685403 1089 TEDR----PQKSLNQKQQENqelllKSISEDIGFSEGK 1122
Cdd:COG5022 1113 NVLQfivaQMIKLNLLQEIS-----KFLSQLVNTLEPV 1145
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
73-717 |
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: 899.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 73 PGVLRNLETRYELNEIYTYTGNILIAVNPFQRLPhIYETDMMEQYKGIALG-ELSPHVFAIGDAAYRAMINEGKNNSILV 151
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLP-LYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 152 SGESGAGKTETTKMLMRYLAFLGG----RSGVEGRTVEQQVLESNPVLEAFGNAKTLRNNNSSRFGKFVEIQFDKNGRIS 227
Cdd:cd00124 80 SGESGAGKTETTKLVLKYLAALSGsgssKSSSSASSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPTGRLV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 228 GAAIRTYLLERSRVCQISDPERNYHCFYLLCA-----APPEDIKKYKLENPHKFHYLNQSSCYKLDGVDDASEYLETRRA 302
Cdd:cd00124 160 GASIETYLLEKSRVVSQAPGERNFHIFYQLLAglsdgAREELKLELLLSYYYLNDYLNSSGCDRIDGVDDAEEFQELLDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 303 MDVVGISNEEQEAIFRVVAAILHLGNIDFGKGEEIDSSVIKDKDSrSHLNMAAELLMCNAQSLEDALIRRVMVTPEEIIT 382
Cdd:cd00124 240 LDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDEDSSAEVADD-ESLKAAAKLLGVDAEDLEEALTTRTIKVGGETIT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 383 RTLDPDNAIASRDTLAKTIYSHLFDWIVNKINTSIGQDPR--SKSIIGVLDIYGFESFKCNSFEQFCINFTNEKLQQHFN 460
Cdd:cd00124 319 KPLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAaeSTSFIGILDIFGFENFEVNSFEQLCINYANEKLQQFFN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 461 QHVFKMEQEEYTKEEIAWSYIEFIDNQDVLELIEKKPGGIISLLDEACMFPKSTHETFSQKLFQTFKEHERF-AKPKLSR 539
Cdd:cd00124 399 QHVFKLEQEEYEEEGIDWSFIDFPDNQDCLDLIEGKPLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFfSKKRKAK 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 540 TDFTISHYAGEVTYQSNHFIDKNKDYIVAEHQALFTAsnckfvaglfhalhedssrsskfssiGSRFKQQLHSLMESLNG 619
Cdd:cd00124 479 LEFGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRS--------------------------GSQFRSQLDALMDTLNS 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 620 TEPHYIRCIKPNNVLKPGIFENFNVIHQLRCGGVLEAIRISCAGYPTRLAFYDFLDRFGLLAP---EVLEGNYDDKVACQ 696
Cdd:cd00124 533 TQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYRILAPgatEKASDSKKAAVLAL 612
|
650 660
....*....|....*....|.
gi 30685403 697 MILDKKSLTDYQIGKTKIFLR 717
Cdd:cd00124 613 LLLLKLDSSGYQLGKTKVFLR 633
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
61-717 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 879.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 61 VDDMTKLSYLHEPGVLRNLETRYELNEIYTYTGNILIAVNPFQRLPhIYETDMMEQYKGIALGELSPHVFAIGDAAYRAM 140
Cdd:pfam00063 1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLP-IYSEDMIKAYRGKRRGELPPHIFAIADEAYRSM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 141 INEGKNNSILVSGESGAGKTETTKMLMRYLAFLGGR-SGVEGRTVEQQVLESNPVLEAFGNAKTLRNNNSSRFGKFVEIQ 219
Cdd:pfam00063 80 LQDKENQSILISGESGAGKTENTKKIMQYLASVSGSgSAGNVGRLEEQILQSNPILEAFGNAKTVRNNNSSRFGKYIEIQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 220 FDKNGRISGAAIRTYLLERSRVCQISDPERNYHCFYLLCA-APPEDIKKYKLENPHKFHYLNQSSCYKLDGVDDASEYLE 298
Cdd:pfam00063 160 FDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAgASAQLKKELRLTNPKDYHYLSQSGCYTIDGIDDSEEFKI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 299 TRRAMDVVGISNEEQEAIFRVVAAILHLGNIDFGKGEEIDSSVIKDKDSrshLNMAAELLMCNAQSLEDALIRRVMVTPE 378
Cdd:pfam00063 240 TDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTEN---LQKAASLLGIDSTELEKALCKRRIKTGR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 379 EIITRTLDPDNAIASRDTLAKTIYSHLFDWIVNKINTSIGQDPRSK-SIIGVLDIYGFESFKCNSFEQFCINFTNEKLQQ 457
Cdd:pfam00063 317 ETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTIEKaSFIGVLDIYGFEIFEKNSFEQLCINYVNEKLQQ 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 458 HFNQHVFKMEQEEYTKEEIAWSYIEFIDNQDVLELIEKKPGGIISLLDEACMFPKSTHETFSQKLFQTFKEHERFAKPKL 537
Cdd:pfam00063 397 FFNHHMFKLEQEEYVREGIEWTFIDFGDNQPCIDLIEKKPLGILSLLDEECLFPKATDQTFLDKLYSTFSKHPHFQKPRL 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 538 -SRTDFTISHYAGEVTYQSNHFIDKNKDYIVAEHQALFTASNCKFVAGLFHALHEDSSRSSKFSS--------------I 602
Cdd:pfam00063 477 qGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESAAANESGkstpkrtkkkrfitV 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 603 GSRFKQQLHSLMESLNGTEPHYIRCIKPNNVLKPGIFENFNVIHQLRCGGVLEAIRISCAGYPTRLAFYDFLDRFGLLAP 682
Cdd:pfam00063 557 GSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQEFVQRYRILAP 636
|
650 660 670
....*....|....*....|....*....|....*...
gi 30685403 683 EVL-EGNYDDKVACQMILDKKSLT--DYQIGKTKIFLR 717
Cdd:pfam00063 637 KTWpKWKGDAKKGCEAILQSLNLDkeEYQFGKTKIFFR 674
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
73-717 |
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: 844.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 73 PGVLRNLETRY-ELNEIYTYTGNILIAVNPFQRLPhIYETDMMEQYKGIALGELSPHVFAIGDAAYRAMINEGKNNSILV 151
Cdd:cd01380 1 PAVLHNLKVRFcQRNAIYTYCGIVLVAINPYEDLP-IYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 152 SGESGAGKTETTKMLMRYLAFLGGRSGVEgRTVEQQVLESNPVLEAFGNAKTLRNNNSSRFGKFVEIQFDKNGRISGAAI 231
Cdd:cd01380 80 SGESGAGKTVSAKYAMRYFATVGGSSSGE-TQVEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYRIIGANM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 232 RTYLLERSRVCQISDPERNYHCFYLLCAAPPEDIKKY-KLENPHKFHYLNQSSCYKLDGVDDASEYLETRRAMDVVGISN 310
Cdd:cd01380 159 RTYLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKElHLGSAEDFFYTNQGGSPVIDGVDDAAEFEETRKALTLLGISE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 311 EEQEAIFRVVAAILHLGNIDFgKGEEIDSSVIKDKDSrsHLNMAAELLMCNAQSLEDALIRRVMVTPEEIITRTLDPDNA 390
Cdd:cd01380 239 EEQMEIFRILAAILHLGNVEI-KATRNDSASISPDDE--HLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPLTLQQA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 391 IASRDTLAKTIYSHLFDWIVNKINTSIG--QDPRSKSIIGVLDIYGFESFKCNSFEQFCINFTNEKLQQHFNQHVFKMEQ 468
Cdd:cd01380 316 IVARDALAKHIYAQLFDWIVDRINKALAspVKEKQHSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHVFKLEQ 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 469 EEYTKEEIAWSYIEFIDNQDVLELIEKKPgGIISLLDEACMFPKSTHETFSQKLFQTFKEHER--FAKPKLSRTDFTISH 546
Cdd:cd01380 396 EEYVKEEIEWSFIDFYDNQPCIDLIEGKL-GILDLLDEECRLPKGSDENWAQKLYNQHLKKPNkhFKKPRFSNTAFIVKH 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 547 YAGEVTYQSNHFIDKNKDYIVAEHQALFTASNckfvaglFHalhedssrsskFSSIGSRFKQQLHSLMESLNGTEPHYIR 626
Cdd:cd01380 475 FADDVEYQVEGFLEKNRDTVSEEHLNVLKASK-------NR-----------KKTVGSQFRDSLILLMETLNSTTPHYVR 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 627 CIKPNNVLKPGIFENFNVIHQLRCGGVLEAIRISCAGYPTRLAFYDFLDRFGLLAPEVLEGNYDDKVACQMILDKKsLTD 706
Cdd:cd01380 537 CIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLPSKEWLRDDKKKTCENILENL-ILD 615
|
650
....*....|....
gi 30685403 707 ---YQIGKTKIFLR 717
Cdd:cd01380 616 pdkYQFGKTKIFFR 629
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
73-717 |
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: 796.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 73 PGVLRNLETRYELNEIYTYTGNILIAVNPFQRLPhIYETDMMEQYKGIALgeLSPHVFAIGDAAYRAMINEGKNNSILVS 152
Cdd:cd01383 1 PSVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVP-LYGNEFITAYRQKLL--DSPHVYAVADTAYREMMRDEINQSIIIS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 153 GESGAGKTETTKMLMRYLAFLGGrsGVEGrtVEQQVLESNPVLEAFGNAKTLRNNNSSRFGKFVEIQFDKNGRISGAAIR 232
Cdd:cd01383 78 GESGAGKTETAKIAMQYLAALGG--GSSG--IENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKICGAKIQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 233 TYLLERSRVCQISDPERNYHCFYLLCA-APPEDIKKYKLENPHKFHYLNQSSCYKLDGVDDASEYLETRRAMDVVGISNE 311
Cdd:cd01383 154 TYLLEKSRVVQLANGERSYHIFYQLCAgASPALREKLNLKSASEYKYLNQSNCLTIDGVDDAKKFHELKEALDTVGISKE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 312 EQEAIFRVVAAILHLGNIDFgkgEEIDS---SVIKDKDSrshLNMAAELLMCNAQSLEDALIRRVMVTPEEIITRTLDPD 388
Cdd:cd01383 234 DQEHIFQMLAAVLWLGNISF---QVIDNenhVEVVADEA---VSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKLTLQ 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 389 NAIASRDTLAKTIYSHLFDWIVNKINTS--IGQDPRSKSIiGVLDIYGFESFKCNSFEQFCINFTNEKLQQHFNQHVFKM 466
Cdd:cd01383 308 QAIDARDALAKAIYASLFDWLVEQINKSleVGKRRTGRSI-SILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLFKL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 467 EQEEYTKEEIAWSYIEFIDNQDVLELIEKKPGGIISLLDEACMFPKSTHETFSQKLFQTFKEHERFAKPKlsRTDFTISH 546
Cdd:cd01383 387 EQEEYELDGIDWTKVDFEDNQECLDLIEKKPLGLISLLDEESNFPKATDLTFANKLKQHLKSNSCFKGER--GGAFTIRH 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 547 YAGEVTYQSNHFIDKNKDYIVAEHQALFTASNCKFVAgLFHALHEDSSRSSKFSS-----------IGSRFKQQLHSLME 615
Cdd:cd01383 465 YAGEVTYDTSGFLEKNRDLLHSDLIQLLSSCSCQLPQ-LFASKMLDASRKALPLTkasgsdsqkqsVATKFKGQLFKLMQ 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 616 SLNGTEPHYIRCIKPNNVLKPGIFENFNVIHQLRCGGVLEAIRISCAGYPTRLAFYDFLDRFGLLAPEVLEGNYDDKVAC 695
Cdd:cd01383 544 RLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLPEDVSASQDPLSTS 623
|
650 660
....*....|....*....|....
gi 30685403 696 QMILDKKSLTD--YQIGKTKIFLR 717
Cdd:cd01383 624 VAILQQFNILPemYQVGYTKLFFR 647
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
73-717 |
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: 772.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 73 PGVLRNLETRYELNEIYTYTGNILIAVNPFQRLPhIYETDMMEQYKGIALGELSPHVFAIGDAAYRAMINEGKNNSILVS 152
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLP-IYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 153 GESGAGKTETTKMLMRYLAFLGGRSGVEGR------TVEQQVLESNPVLEAFGNAKTLRNNNSSRFGKFVEIQFDKNGRI 226
Cdd:cd01377 80 GESGAGKTENTKKVIQYLASVAASSKKKKEsgkkkgTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTGKI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 227 SGAAIRTYLLERSRVCQISDPERNYHCFY-LLCAAPPEDIKKYKLENPHKFHYLNQSSCYKLDGVDDASEYLETRRAMDV 305
Cdd:cd01377 160 AGADIETYLLEKSRVVRQAKGERNYHIFYqLLSGADPELKEKLLLTGDPSYYFFLSQGELTIDGVDDAEEFKLTDEAFDI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 306 VGISNEEQEAIFRVVAAILHLGNIDFGKGEEIDSSVIKDKDSrshLNMAAELLMCNAQSLEDALIR-RVMVtPEEIITRT 384
Cdd:cd01377 240 LGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEE---ADKAAHLLGVNSSDLLKALLKpRIKV-GREWVTKG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 385 LDPDNAIASRDTLAKTIYSHLFDWIVNKINTSIGQDPRSKSIIGVLDIYGFESFKCNSFEQFCINFTNEKLQQHFNQHVF 464
Cdd:cd01377 316 QNKEQVVFSVGALAKALYERLFLWLVKRINKTLDTKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMF 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 465 KMEQEEYTKEEIAWSYIEF-IDNQDVLELIEKKPGGIISLLDEACMFPKSTHETFSQKLFQTFKEHERFA---KPKLSRT 540
Cdd:cd01377 396 VLEQEEYKKEGIEWTFIDFgLDLQPTIDLIEKPNMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKNFkkpKPKKSEA 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 541 DFTISHYAGEVTYQSNHFIDKNKDYI---VAehqALFTASNCKFVAGLFHALHEDSSRSSKFSS-------IGSRFKQQL 610
Cdd:cd01377 476 HFILKHYAGDVEYNIDGWLEKNKDPLnenVV---ALLKKSSDPLVASLFKDYEESGGGGGKKKKkggsfrtVSQLHKEQL 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 611 HSLMESLNGTEPHYIRCIKPNNVLKPGIFENFNVIHQLRCGGVLEAIRISCAGYPTRLAFYDFLDRFGLLAPE-VLEGNY 689
Cdd:cd01377 553 NKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNaIPKGFD 632
|
650 660 670
....*....|....*....|....*....|
gi 30685403 690 DDKVACQMILDKKSL--TDYQIGKTKIFLR 717
Cdd:cd01377 633 DGKAACEKILKALQLdpELYRIGNTKVFFK 662
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
74-717 |
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: 747.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 74 GVLRNLETRYELNEIYTYTGNILIAVNPFQRLPhIYETDMMEQYKGIALGELSPHVFAIGDAAYRAMINEGKNNSILVSG 153
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELP-IYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 154 ESGAGKTETTKMLMRYLAFLGGRSgvegRTVEQQVLESNPVLEAFGNAKTLRNNNSSRFGKFVEIQFDKNGRISGAAIRT 233
Cdd:cd14883 81 ESGAGKTETTKLILQYLCAVTNNH----SWVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGHIKGAIIQD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 234 YLLERSRVCQISDPERNYHCFYLLCA---APPEDIKKYKLENPHKFHYLNQSSCYKLDGVDDASEYLETRRAMDVVGISN 310
Cdd:cd14883 157 YLLEQSRITFQAPGERNYHVFYQLLAgakHSKELKEKLKLGEPEDYHYLNQSGCIRIDNINDKKDFDHLRLAMNVLGIPE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 311 EEQEAIFRVVAAILHLGNIDFGK--GEEIDSSVikdkDSRSHLNMAAELLMCNAQSLEDALIRRVMVTPEEIITRTLDPD 388
Cdd:cd14883 237 EMQEGIFSVLSAILHLGNLTFEDidGETGALTV----EDKEILKIVAKLLGVDPDKLKKALTIRQINVRGNVTEIPLKVQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 389 NAIASRDTLAKTIYSHLFDWIVNKINTSIGQDPRSKSIIGVLDIYGFESFKCNSFEQFCINFTNEKLQQHFNQHVFKMEQ 468
Cdd:cd14883 313 EARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNSRFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHYVFKLEQ 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 469 EEYTKEEIAWSYIEFIDNQDVLELIEKKPGGIISLLDEACMFPKSTHETFSQKLFQTFKEHERFAKP--KLSRTDFTISH 546
Cdd:cd14883 393 EEYEKEGINWSHIVFTDNQECLDLIEKPPLGILKLLDEECRFPKGTDLTYLEKLHAAHEKHPYYEKPdrRRWKTEFGVKH 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 547 YAGEVTYQSNHFIDKNKDYIVAEHQALFTASNCKFVAGLFHALHEDSSRSSKFSS---------------IGSRFKQQLH 611
Cdd:cd14883 473 YAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFTYPDLLALTGLSISLggdttsrgtskgkptVGDTFKHQLQ 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 612 SLMESLNGTEPHYIRCIKPNNVLKPGIFENFNVIHQLRCGGVLEAIRISCAGYPTRLAFYDFLDRFGLLAPEVLEGnyDD 691
Cdd:cd14883 553 SLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCLDPRARSA--DH 630
|
650 660 670
....*....|....*....|....*....|.
gi 30685403 692 KVACQMILDKKSL-----TDYQIGKTKIFLR 717
Cdd:cd14883 631 KETCGAVRALMGLgglpeDEWQVGKTKVFLR 661
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
74-717 |
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: 745.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 74 GVLRNLETRYELNEIYTYTGNILIAVNPFQRLPhIYETDMMEQYKGIALGELSPHVFAIGDAAYRAMINEGKNNSILVSG 153
Cdd:cd01381 2 GILRNLLIRYREKLIYTYTGSILVAVNPYQILP-IYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 154 ESGAGKTETTKMLMRYLAFLGGRSgvegRTVEQQVLESNPVLEAFGNAKTLRNNNSSRFGKFVEIQFDKNGRISGAAIRT 233
Cdd:cd01381 81 ESGAGKTESTKLILQYLAAISGQH----SWIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIEGAKIEQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 234 YLLERSRVCQISDPERNYHCFY-LLCAAPPEDIKKYKLENPHKFHYLNQSSCYKLDGVDDASEYLETRRAMDVVGISNEE 312
Cdd:cd01381 157 YLLEKSRIVSQAPDERNYHIFYcMLAGLSAEEKKKLELGDASDYYYLTQGNCLTCEGRDDAAEFADIRSAMKVLMFTDEE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 313 QEAIFRVVAAILHLGNIDFGKGEE--IDSSVIKDKdsrSHLNMAAELLMCNAQSLEDALIRRVMVTPEEIITRTLDPDNA 390
Cdd:cd01381 237 IWDIFKLLAAILHLGNIKFEATVVdnLDASEVRDP---PNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSPLSAEQA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 391 IASRDTLAKTIYSHLFDWIVNKINTSIGQdPRSKSI----IGVLDIYGFESFKCNSFEQFCINFTNEKLQQHFNQHVFKM 466
Cdd:cd01381 314 LDVRDAFVKGIYGRLFIWIVNKINSAIYK-PRGTDSsrtsIGVLDIFGFENFEVNSFEQLCINFANENLQQFFVRHIFKL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 467 EQEEYTKEEIAWSYIEFIDNQDVLELIEKKPGGIISLLDEACMFPKSTHETFSQKLFQTFKEHERFAKPKlSR--TDFTI 544
Cdd:cd01381 393 EQEEYDKEGINWQHIEFVDNQDVLDLIALKPMNIMSLIDEESKFPKGTDQTMLEKLHSTHGNNKNYLKPK-SDlnTSFGI 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 545 SHYAGEVTYQSNHFIDKNKDYIVAEHQALFTASNCKFVAGLF-HALHEDSSRSSKFSSIGSRFKQQLHSLMESLNGTEPH 623
Cdd:cd01381 472 NHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFnEDISMGSETRKKSPTLSSQFRKSLDQLMKTLSACQPF 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 624 YIRCIKPNNVLKPGIFENFNVIHQLRCGGVLEAIRISCAGYPTRLAFYDFLDRFGLLAPEVL-EGNYDDKVACQMILDKK 702
Cdd:cd01381 552 FVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVLVPGIPpAHKTDCRAATRKICCAV 631
|
650
....*....|....*..
gi 30685403 703 SLT--DYQIGKTKIFLR 717
Cdd:cd01381 632 LGGdaDYQLGKTKIFLK 648
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
75-717 |
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: 740.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 75 VLRNLETRYELNEIYTYTGNILIAVNPFQRLPhIYETDMMEQYKGIALGELSPHVFAIGDAAYRAMINEGKNNSILVSGE 154
Cdd:cd01378 3 INENLKKRFENDEIYTYIGHVLISVNPFKDLG-IYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 155 SGAGKTETTKMLMRYLAFLGGRSGVEGRTVEQQVLESNPVLEAFGNAKTLRNNNSSRFGKFVEIQFDKNGRISGAAIRTY 234
Cdd:cd01378 82 SGAGKTEASKRIMQYIAAVSGGSESEVERVKDMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEPVGGHITNY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 235 LLERSRVCQISDPERNYHCFY-LLCAAPPEDIKKYKLENPHKFHYLNQSSCYKLDGVDDASEYLETRRAMDVVGISNEEQ 313
Cdd:cd01378 162 LLEKSRVVGQIKGERNFHIFYqLLKGASQEYLQELGLQRPEQYYYYSKSGCFDVDGIDDAADFKEVLNAMKVIGFTEEEQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 314 EAIFRVVAAILHLGNIDFGKGEEiDSSVIKDKdsrSHLNMAAELLMCNAQSLEDALIRRVMVT---PEEIITRTLDPDNA 390
Cdd:cd01378 242 DSIFRILAAILHLGNIQFAEDEE-GNAAISDT---SVLDFVAYLLGVDPDQLEKALTHRTIETgggGRSVYEVPLNVEQA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 391 IASRDTLAKTIYSHLFDWIVNKINTSI-GQDPRSKSIIGVLDIYGFESFKCNSFEQFCINFTNEKLQQHFNQHVFKMEQE 469
Cdd:cd01378 318 AYARDALAKAIYSRLFDWIVERINKSLaAKSGGKKKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFIELTLKAEQE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 470 EYTKEEIAWSYIEFIDNQDVLELIEKKPGGIISLLDEACMFP-KSTHETFSQKLFQTFKEHERFAKPK----LSRTDFTI 544
Cdd:cd01378 398 EYVREGIEWTPIKYFNNKIICDLIEEKPPGIFAILDDACLTAgDATDQTFLQKLNQLFSNHPHFECPSghfeLRRGEFRI 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 545 SHYAGEVTYQSNHFIDKNKDYIVAEHQALFTASNCKFVAGLFhalHEDSSRSSKFSSI--GSRFKQQLHSLMESLNGTEP 622
Cdd:cd01378 478 KHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLF---PEGVDLDSKKRPPtaGTKFKNSANALVETLMKKQP 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 623 HYIRCIKPNNVLKPGIFENFNVIHQLRCGGVLEAIRISCAGYPTRLAFYDFLDRFGLLAPEVL-EGNYDDKVACQMILDK 701
Cdd:cd01378 555 SYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYKLLSPKTWpAWDGTWQGGVESILKD 634
|
650
....*....|....*...
gi 30685403 702 KSL--TDYQIGKTKIFLR 717
Cdd:cd01378 635 LNIppEEYQMGKTKIFIR 652
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
76-717 |
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: 693.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 76 LRNLETRYELNEIYTYTGNILIAVNPFQRLPHIYETDMMEQYKGIALGELSPHVFAIGDAAYRAMINEGKNNSILVSGES 155
Cdd:cd01382 4 LNNIRVRYSKDKIYTYVANILIAVNPYFDIPKLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVSGES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 156 GAGKTETTKMLMRYLAFLGGRSGvegRTVEQQVLESNPVLEAFGNAKTLRNNNSSRFGKFVEIQFDKNGRISGAAIRTYL 235
Cdd:cd01382 84 GAGKTESTKYILRYLTESWGSGA---GPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVGGFVSHYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 236 LERSRVCQISDPERNYHCFYLLCAAPPEDIKKYKLENPHkfhylnqsscykldgVDDASEYLETRRAMDVVGISNEEQEA 315
Cdd:cd01382 161 LEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLLKDPL---------------LDDVGDFIRMDKAMKKIGLSDEEKLD 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 316 IFRVVAAILHLGNIDF-GKGEEIDSSVIKDKDSRSHLNMAAELLMCNAQSLEDALIRRVMVTPEE-----IITRTLDPDN 389
Cdd:cd01382 226 IFRVVAAVLHLGNIEFeENGSDSGGGCNVKPKSEQSLEYAAELLGLDQDELRVSLTTRVMQTTRGgakgtVIKVPLKVEE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 390 AIASRDTLAKTIYSHLFDWIVNKINTSIGQDpRSKSIIGVLDIYGFESFKCNSFEQFCINFTNEKLQQHFNQHVFKMEQE 469
Cdd:cd01382 306 ANNARDALAKAIYSKLFDHIVNRINQCIPFE-TSSYFIGVLDIAGFEYFEVNSFEQFCINYCNEKLQQFFNERILKEEQE 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 470 EYTKEEIAWSYIEFIDNQDVLELIEKKPGGIISLLDEACMFPKSTHETFSQKLFQTFKEHERFAKPKLSR-------TD- 541
Cdd:cd01382 385 LYEKEGLGVKEVEYVDNQDCIDLIEAKLVGILDLLDEESKLPKPSDQHFTSAVHQKHKNHFRLSIPRKSKlkihrnlRDd 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 542 --FTISHYAGEVTYQSNHFIDKNKDYIVAEHQALFTASNCKFVAGLFHALHEDSSRSSKFS------SIGSRFKQQLHSL 613
Cdd:cd01382 465 egFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFESSTNNNKDSKQKAgklsfiSVGNKFKTQLNLL 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 614 MESLNGTEPHYIRCIKPNNVLKPGIFENFNVIHQLRCGGVLEAIRISCAGYPTRLAFYDFLDRFGLLAPEVLEGnYDDKV 693
Cdd:cd01382 545 MDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRTSFHDLYNMYKKYLPPKLAR-LDPRL 623
|
650 660
....*....|....*....|....*...
gi 30685403 694 ACQMILdkKSL----TDYQIGKTKIFLR 717
Cdd:cd01382 624 FCKALF--KALglneNDFKFGLTKVFFR 649
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
73-717 |
0e+00 |
|
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: 675.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 73 PGVLRNLETRYELNEIYTYTGNILIAVNPFQRLPHIYETDMMEQYKGIAlGELSPHVFAIGDAAYRAMINEGKNNSILVS 152
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPGLYSDEMLLKFIQPS-ISKSPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 153 GESGAGKTETTKMLMRYLAFLGGRSGVEGRTVEQQVLESNPVLEAFGNAKTLRNNNSSRFGKFVEIQFDKN--------- 223
Cdd:cd14888 80 GESGAGKTESTKYVMKFLACAGSEDIKKRSLVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFSKLkskrmsgdr 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 224 GRISGAAIRTYLLERSRVCQISDPERNYHCFYLLCAA----------PPEDIKKYKLEN-------------PH-KFHYL 279
Cdd:cd14888 160 GRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAareakntglsYEENDEKLAKGAdakpisidmssfePHlKFRYL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 280 NQSSCYKLDGVDDASEYLETRRAMDVVGISNEEQEAIFRVVAAILHLGNIDFGKGEEIDSSVIKDKDSRSHLNMAAELLM 359
Cdd:cd14888 240 TKSSCHELPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFENNEACSEGAVVSASCTDDLEKVASLLG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 360 CNAQSLEDALIRRVMVTPEEIITRTLDPDNAIASRDTLAKTIYSHLFDWIVNKINTSIGQDPRSKSII-GVLDIYGFESF 438
Cdd:cd14888 320 VDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGYSKDNSLLFcGVLDIFGFECF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 439 KCNSFEQFCINFTNEKLQQHFNQHVFKMEQEEYTKEEIAWSYIEFIDNQDVLELIEKKPGGIISLLDEACMFPKSTHETF 518
Cdd:cd14888 400 QLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFPDNQDCVDLLQEKPLGIFCMLDEECFVPGGKDQGL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 519 SQKLFQTFKEHERFAKPKLSRTDFTISHYAGEVTYQSNHFIDKNKDYIVAEHQALFTASNCKFVAGLFHALHEDSSRSSK 598
Cdd:cd14888 480 CNKLCQKHKGHKRFDVVKTDPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKNPFISNLFSAYLRRGTDGNT 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 599 F----SSIGSRFKQQLHSLMESLNGTEPHYIRCIKPNNVLKPGIFENFNVIHQLRCGGVLEAIRISCAGYPTRLAFYDFL 674
Cdd:cd14888 560 KkkkfVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQLKYGGVLQAVQVSRAGYPVRLSHAEFY 639
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 30685403 675 DRFGLLAPEVLegnyddkvacqmildKKSLTDYQIGKTKIFLR 717
Cdd:cd14888 640 NDYRILLNGEG---------------KKQLSIWAVGKTLCFFK 667
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
73-717 |
0e+00 |
|
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or C-terminal to their motor domain and a tail with a MyTH4 domain followed by a SH3 domain in some instances. The monomeric Acanthamoebas were the first identified members of this group and have been joined by Stramenopiles. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276839 Cd Length: 644 Bit Score: 661.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 73 PGVLRNLETRYELNEIYTYTGNILIAVNPFQRLPhIYETDMMEQYKGIALGELSPHVFAIGDAAYRAMINEGKNNSILVS 152
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLP-LYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 153 GESGAGKTETTKMLMRYLAFLGGRSGvegrTVEQQVLESNPVLEAFGNAKTLRNNNSSRFGKFVEIQFDKNGRISGAAIR 232
Cdd:cd14872 80 GESGAGKTEATKQCLSFFAEVAGSTN----GVEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRICGASTE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 233 TYLLERSRVCQISDPERNYHCFYLLCAAPPEDiKKYKLENPHKFHYLNQSSCYKLDGVDDASEYLETRRAMDVVGISNEE 312
Cdd:cd14872 156 NYLLEKSRVVYQIKGERNFHIFYQLLASPDPA-SRGGWGSSAAYGYLSLSGCIEVEGVDDVADFEEVVLAMEQLGFDDAD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 313 QEAIFRVVAAILHLGNIDFGKGEEIDSSVIKDKDSRSHLNMAAELLMCNAQSLEDALIRRVMVTPEEIITRT-LDPDNAI 391
Cdd:cd14872 235 INNVMSLIAAILKLGNIEFASGGGKSLVSGSTVANRDVLKEVATLLGVDAATLEEALTSRLMEIKGCDPTRIpLTPAQAT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 392 ASRDTLAKTIYSHLFDWIVNKINTSIGQDPRSKS-IIGVLDIYGFESFKCNSFEQFCINFTNEKLQQHFNQHVFKMEQEE 470
Cdd:cd14872 315 DACDALAKAAYSRLFDWLVKKINESMRPQKGAKTtFIGVLDIFGFEIFEKNSFEQLCINFTNEKLQQHFNQYTFKLEEAL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 471 YTKEEIAWSYIEFIDNQDVLELIEKKPGGIISLLDEACMFPKSTHETFSQKLFQTF--KEHERFAKPKLSRTDFTISHYA 548
Cdd:cd14872 395 YQSEGVKFEHIDFIDNQPVLDLIEKKQPGLMLALDDQVKIPKGSDATFMIAANQTHaaKSTFVYAEVRTSRTEFIVKHYA 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 549 GEVTYQSNHFIDKNKDYIVAEHQALFTASNCKFVAGLFHALHEDssRSSKFSSIGSRFKQQLHSLMESLNGTEPHYIRCI 628
Cdd:cd14872 475 GDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLFPPSEGD--QKTSKVTLGGQFRKQLSALMTALNATEPHYIRCV 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 629 KPNNVLKPGIFENFNVIHQLRCGGVLEAIRISCAGYPTRLAFYDFLDRFGLLAPEVLEGN-YDDKVACQMILD--KKSLT 705
Cdd:cd14872 553 KPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKRYRFLVKTIAKRVgPDDRQRCDLLLKslKQDFS 632
|
650
....*....|..
gi 30685403 706 DYQIGKTKIFLR 717
Cdd:cd14872 633 KVQVGKTRVLYR 644
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
73-717 |
0e+00 |
|
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: 652.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 73 PGVLRNLETRYELNEIYTYTGNILIAVNPFQRLPHIYETDMMEQYKGIALGELSPHVFAIGDAAYRAMINEGKNNSILVS 152
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPELYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 153 GESGAGKTETTKMLMRYLAFLGGrsGVEGRTVEQqVLESNPVLEAFGNAKTLRNNNSSRFGKFVEIQFDKNGRISGAAIR 232
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIAG--GLNDSTIKK-IIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKNGTLVGAKCR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 233 TYLLERSRVCQISDPERNYHCFYLLCAAPpEDIKKYKLENPHKFHYLNQSSCYKLDGVDDASEYLETRRAMDVVGISNEE 312
Cdd:cd14903 158 TYLLEKTRVISHERPERNYHIFYQLLASP-DVEERLFLDSANECAYTGANKTIKIEGMSDRKHFARTKEALSLIGVSEEK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 313 QEAIFRVVAAILHLGNIDF-GKGEEIDSSVIKDKDSrsHLNMAAELLMCNAQSLEDALIRRVMVTPEEIITRTLDPDNAI 391
Cdd:cd14903 237 QEVLFEVLAGILHLGQLQIqSKPNDDEKSAIAPGDQ--GAVYATKLLGLSPEALEKALCSRTMRAAGDVYTVPLKKDQAE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 392 ASRDTLAKTIYSHLFDWIVNKINTSIGQDPRSKSIIGVLDIYGFESFKCNSFEQFCINFTNEKLQQHFNQHVFKMEQEEY 471
Cdd:cd14903 315 DCRDALAKAIYSNVFDWLVATINASLGNDAKMANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFTQDVFKTVQIEY 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 472 TKEEIAWSYIEFIDNQDVLELIEKKPgGIISLLDEACMFPKSTHETFSQKLFQTFKEHERFAK-PKLSRTDFTISHYAGE 550
Cdd:cd14903 395 EEEGIRWAHIDFADNQDVLAVIEDRL-GIISLLNDEVMRPKGNEESFVSKLSSIHKDEQDVIEfPRTSRTQFTIKHYAGP 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 551 VTYQSNHFIDKNKDYIVAEHQALFTASNCKFVAGLF--HALHEDSSRSSKFSS-------------IGSRFKQQLHSLME 615
Cdd:cd14903 474 VTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFkeKVESPAAASTSLARGarrrrggalttttVGTQFKDSLNELMT 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 616 SLNGTEPHYIRCIKPNNVLKPGIFENFNVIHQLRCGGVLEAIRISCAGYPTRLAFYDFLDRFGLLAPEvlEGNYDDKVA- 694
Cdd:cd14903 554 TIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWLFLPE--GRNTDVPVAe 631
|
650 660
....*....|....*....|....*..
gi 30685403 695 -CQMILDK---KSLTDYQIGKTKIFLR 717
Cdd:cd14903 632 rCEALMKKlklESPEQYQMGLTRIYFQ 658
|
|
| MyosinXI_CBD |
cd15475 |
cargo binding domain of myosin XI; Class XI myosins are a plant specific group, homologous to ... |
1099-1486 |
0e+00 |
|
cargo binding domain of myosin XI; Class XI myosins are a plant specific group, homologous to class V myosins. C-terminal domain of Arabidopsis myosin XI has been shown to be homologous to the cargo-binding domain of yeast myosin V myo2p, which targets myosin to vacuole- and mitochondria, as well as secretory vesicle.
Pssm-ID: 271259 Cd Length: 326 Bit Score: 648.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 1099 QKQQENQELLLKSISEDIGFSEGKPVAACLIYKCLIHWRSFEVERTSIFNRIIETIASAIEMQENSDVLCYWLSNSATLL 1178
Cdd:cd15475 1 ERQQENVDALIKCVSENLGFSEGKPVAAFTIYKCLLHWKSFEAEKTSVFDRIIQTIGSAIEDQDNNDHLAYWLSNTSTLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 1179 MFLQRTLkagatgsittprrrgmpsslfgrvsqsfrgspqsagfpfmtgraigggldelrqveakyPALLFKQQLTAFLE 1258
Cdd:cd15475 81 FLLQRSL-----------------------------------------------------------PALLFKQQLTAYVE 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 1259 KIYGMIRDKMKKEISPLLASCIQVPRTPRSGLVKGRSQNtqnNVVAPKPMIAHWQNIVTCLNGHLRTMRANYVPSLLISK 1338
Cdd:cd15475 102 KIYGIIRDNLKKELSPLLSLCIQAPRTSRGSSSKSSSSA---NSLGQQSPSSHWQSIIKSLNSLLSTLKENHVPPFLVQK 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 1339 VFGQIFSFINVQLFNSLLLRRECCSFSNGEYVKTGLAELEKWCHDATEEFVGSAWDELKHIRQAVGFLVIHQKPKKSLKE 1418
Cdd:cd15475 179 IFTQVFSFINVQLFNSLLLRRECCSFSNGEYVKAGLAELELWCSQATEEYAGSSWDELKHIRQAVGFLVIHQKSRKSYDE 258
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30685403 1419 ITTELCPVLSIQQLYRISTMYWDDKYGTHSVSTEVIATMRAEVSDVSKSAISNSFLLDDDSSIPFSLD 1486
Cdd:cd15475 259 ITNDLCPVLSVQQLYRICTMYWDDKYGTQSVSPEVISSMRVLMTEDSNNAVSNSFLLDDDSSIPFSVE 326
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
73-716 |
0e+00 |
|
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: 640.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 73 PGVLRNLETRYELNEIYTYTGNILIAVNPFQRLPhIYETDMMEQY------KGIALGELSPHVFAIGDAAYRAMI----N 142
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLP-LYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLfasrG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 143 EGKNNSILVSGESGAGKTETTKMLMRYLAFLG-----GRSGVEGRTVEQQVLESNPVLEAFGNAKTLRNNNSSRFGKFVE 217
Cdd:cd14901 80 QKCDQSILVSGESGAGKTETTKIIMNYLASVSsatthGQNATERENVRDRVLESNPILEAFGNARTNRNNNSSRFGKFIR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 218 IQFDKNGRISGAAIRTYLLERSRVCQISDPERNYHCFYLLC-AAPPEDIKKYKLENPHKFHYLNQSSCY-KLDGVDDASE 295
Cdd:cd14901 160 LGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLrGASSDELHALGLTHVEEYKYLNSSQCYdRRDGVDDSVQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 296 YLETRRAMDVVGISNEEQEAIFRVVAAILHLGNIDFGKGEEIDSSVikdkDSRSHLNMAA--ELLMCNAQSLEDALIRRV 373
Cdd:cd14901 240 YAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFVKKDGEGGTF----SMSSLANVRAacDLLGLDMDVLEKTLCTRE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 374 MVTPEEIITRTLDPDNAIASRDTLAKTIYSHLFDWIVNKINTSIGQDPRS--KSIIGVLDIYGFESFKCNSFEQFCINFT 451
Cdd:cd14901 316 IRAGGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSESTgaSRFIGIVDIFGFEIFATNSLEQLCINFA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 452 NEKLQQHFNQHVFKMEQEEYTKEEIAWSYIEFIDNQDVLELIEKKPGGIISLLDEACMFPKSTHETFSQKLFQTFKEHER 531
Cdd:cd14901 396 NEKLQQLFGKFVFEMEQDEYVAEAIPWTFVEYPNNDACVAMFEARPTGLFSLLDEQCLLPRGNDEKLANKYYDLLAKHAS 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 532 FAKPKLSR--TDFTISHYAGEVTYQSNHFIDKNKDYIVAEHQALFTASNCKFVAglfhalhedssrsskfSSIGSRFKQQ 609
Cdd:cd14901 476 FSVSKLQQgkRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLS----------------STVVAKFKVQ 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 610 LHSLMESLNGTEPHYIRCIKPNNVLKPGIFENFNVIHQLRCGGVLEAIRISCAGYPTRLAFYDFLDRFGLLAPEV--LEG 687
Cdd:cd14901 540 LSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFPHDAFVHTYSCLAPDGasDTW 619
|
650 660 670
....*....|....*....|....*....|....*
gi 30685403 688 NYDDKVACQMILDKKSLTD------YQIGKTKIFL 716
Cdd:cd14901 620 KVNELAERLMSQLQHSELNiehlppFQVGKTKVFL 654
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
75-717 |
0e+00 |
|
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: 637.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 75 VLRNLETRYELNEIYTYTGNILIAVNPFQRLPHIYETDMMEQYKGIALGELSPHVFAIGDAAYRAMINEG----KNNSIL 150
Cdd:cd14890 3 LLHTLRLRYERDEIYTYVGPILISINPYKSIPDLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQSGvldpSNQSII 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 151 VSGESGAGKTETTKMLMRYLA-------------FLGGRSGVEGRT--VEQQVLESNPVLEAFGNAKTLRNNNSSRFGKF 215
Cdd:cd14890 83 ISGESGAGKTEATKIIMQYLAritsgfaqgasgeGEAASEAIEQTLgsLEDRVLSSNPLLESFGNAKTLRNDNSSRFGKF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 216 VEIQFDKNGRISGAAIRTYLLERSRVCQISDPERNYHCFYLLCAAPPEDIKK-YKLENPHKFHYLnQSSCYKLDGVDDAS 294
Cdd:cd14890 163 IEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRErLKLQTPVEYFYL-RGECSSIPSCDDAK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 295 EYLETRRAMDVVGISNEEQEAIFRVVAAILHLGNIDFgKGEEiDSSVIKDKDSRSHLNMAAELLMCNAQSLEDALIRRVM 374
Cdd:cd14890 242 AFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDF-ESEN-DTTVLEDATTLQSLKLAAELLGVNEDALEKALLTRQL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 375 VTPEEIITRTLDPDNAIASRDTLAKTIYSHLFDWIVNKINTSIGQDPRSKSIIGVLDIYGFESFKCNSFEQFCINFTNEK 454
Cdd:cd14890 320 FVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDKWGFIGVLDIYGFEKFEWNTFEQLCINYANEK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 455 LQQHFNQHVFKMEQEEYTKEEIAWSYIEFIDNQDVLELIEKKPG---GIISLLDEACMFPKST---------HETF---- 518
Cdd:cd14890 400 LQRHFNQHMFEVEQVEYSNEGIDWQYITFNDNQACLELIEGKVNgkpGIFITLDDCWRFKGEEankkfvsqlHASFgrks 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 519 -SQKLFQTFKEHERFAKPKL-SRTDFTISHYAGEVTYQSNHFIDKNKDYIVAEHQALFTASNckfvaglfHALHEdssrs 596
Cdd:cd14890 480 gSGGTRRGSSQHPHFVHPKFdADKQFGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSR--------RSIRE----- 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 597 skfSSIGSRFKQQLHSLMESLNGTEPHYIRCIKPNNVLKPGIFENFNVIHQLRCGGVLEAIRISCAGYPTRLAFYDFLDR 676
Cdd:cd14890 547 ---VSVGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGMMEAIQIRQQGFALREEHDSFFYD 623
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 30685403 677 FGLLAPEVLEGNYDDKVACQMIldKKSLTDYQIGKTKIFLR 717
Cdd:cd14890 624 FQVLLPTAENIEQLVAVLSKML--GLGKADWQIGSSKIFLK 662
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
76-717 |
0e+00 |
|
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: 632.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 76 LRNLETRYELNEIYTYTGNILIAVNPFQRLPhIYETDMMEQYKGIALGELSPHVFAIGDAAYRAMINEGKNNSILVSGES 155
Cdd:cd01385 4 LENLRARFKHGKIYTYVGSILIAVNPFKFLP-IYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 156 GAGKTETTKMLMRYLAFLGGRSGveGRTVEQQVLESNPVLEAFGNAKTLRNNNSSRFGKFVEIQFDKNGRISGAAIRTYL 235
Cdd:cd01385 83 GSGKTESTNFLLHHLTALSQKGY--GSGVEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRGAVVEKYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 236 LERSRVCQISDPERNYH-CFYLLCAAPPEDIKKYKLENPHKFHYLNQSSCYKLDGVDDASEYLETRRAMDVVGISNEEQE 314
Cdd:cd01385 161 LEKSRIVSQEKNERNYHvFYYLLAGASEEERKELHLKQPEDYHYLNQSDCYTLEGEDEKYEFERLKQAMEMVGFLPETQR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 315 AIFRVVAAILHLGNIDFG-KGEEIDSSV-IKDKDSrshLNMAAELLMCNAQSLEDALIRRVMVTPEE-IITRTLDPDnAI 391
Cdd:cd01385 241 QIFSVLSAVLHLGNIEYKkKAYHRDESVtVGNPEV---LDIISELLRVKEETLLEALTTKKTVTVGEtLILPYKLPE-AI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 392 ASRDTLAKTIYSHLFDWIVNKINTSiGQDPRSKSI-----IGVLDIYGFESFKCNSFEQFCINFTNEKLQQHFNQHVFKM 466
Cdd:cd01385 317 ATRDAMAKCLYSALFDWIVLRINHA-LLNKKDLEEakglsIGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQHIFKL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 467 EQEEYTKEEIAWSYIEFIDNQDVLELIEKKPGGIISLLDEACMFPKSTHETFSQKLFQTFKEHERFAKPKLSRTDFTISH 546
Cdd:cd01385 396 EQEEYKKEGISWHNIEYTDNTGCLQLISKKPTGLLCLLDEESNFPGATNQTLLAKFKQQHKDNKYYEKPQVMEPAFIIAH 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 547 YAGEVTYQSNHFIDKNKDYIVAEHQALFTASNCKFVAGL--------------------FHALHE--------------- 591
Cdd:cd01385 476 YAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVRELigidpvavfrwavlraffraMAAFREagrrraqrtaghslt 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 592 ----------DSSRSSKFSSIGSRFKQQLHSLMESLNGTEPHYIRCIKPNNVLKPGIFENFNVIHQLRCGGVLEAIRISC 661
Cdd:cd01385 556 lhdrttksllHLHKKKKPPSVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVLRQLRYTGMLETVRIRR 635
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 30685403 662 AGYPTRLAFYDFLDRFGLLAPEVLEGNYDD--KVACQMILDKkslTDYQIGKTKIFLR 717
Cdd:cd01385 636 SGYSVRYTFQEFITQFQVLLPKGLISSKEDikDFLEKLNLDR---DNYQIGKTKVFLK 690
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
75-717 |
0e+00 |
|
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: 611.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 75 VLRNLETRYELNEIYTYTGNILIAVNPFqRLPHIYETDMMEQYKGIALGELSPHVFAIGDAAYRAMINEGKNNSILVSGE 154
Cdd:cd01387 3 VLWNLKTRYERNLIYTYIGSILVSVNPY-KMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 155 SGAGKTETTKMLMRYLAFLGGRSGVegrTVEQQVLESNPVLEAFGNAKTLRNNNSSRFGKFVEIQFdKNGRISGAAIRTY 234
Cdd:cd01387 82 SGSGKTEATKLIMQYLAAVNQRRNN---LVTEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFF-EGGVIVGAITSQY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 235 LLERSRVCQISDPERNYHCFYLLCAAPPEDIK-KYKLENPHKFHYLNQSSCYKLDGVDDASEYLETRRAMDVVGISNEEQ 313
Cdd:cd01387 158 LLEKSRIVTQAKNERNYHVFYELLAGLPAQLRqKYGLQEAEKYFYLNQGGNCEIAGKSDADDFRRLLAAMQVLGFSSEEQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 314 EAIFRVVAAILHLGNIDFGKGEEIDSSVIKDKDSRSHLNMAAELLMCNAQSLEDALIRRVMVTPEEIITRTLDPDNAIAS 393
Cdd:cd01387 238 DSIFRILASVLHLGNVYFHKRQLRHGQEGVSVGSDAEIQWVAHLLQISPEGLQKALTFKVTETRRERIFTPLTIDQALDA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 394 RDTLAKTIYSHLFDWIVNKINtSIGQDPRSKSI-IGVLDIYGFESFKCNSFEQFCINFTNEKLQQHFNQHVFKMEQEEYT 472
Cdd:cd01387 318 RDAIAKALYALLFSWLVTRVN-AIVYSGTQDTLsIAILDIFGFEDLSENSFEQLCINYANENLQYYFNKHVFKLEQEEYI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 473 KEEIAWSYIEFIDNQDVLELIEKKPGGIISLLDEACMFPKSTHETFSQKLFQTFKEHERFAKPKLSRTDFTISHYAGEVT 552
Cdd:cd01387 397 REQIDWTEIAFADNQPVINLISKKPVGILHILDDECNFPQATDHSFLEKCHYHHALNELYSKPRMPLPEFTIKHYAGQVW 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 553 YQSNHFIDKNKDYIVAEHQALFTASNCKFVAGLFHALHEDSSRSSKFSSIGS-------------RFKQQLHSLMESLNG 619
Cdd:cd01387 477 YQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSSHRAQTDKAPPRLGKGRfvtmkprtptvaaRFQDSLLQLLEKMER 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 620 TEPHYIRCIKPNNVLKPGIFENFNVIHQLRCGGVLEAIRISCAGYPTRLAFYDFLDRFGLLAPEVLE--GNYDDKVACQM 697
Cdd:cd01387 557 CNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYRCLVALKLPrpAPGDMCVSLLS 636
|
650 660
....*....|....*....|.
gi 30685403 698 ILDKKSLT-DYQIGKTKIFLR 717
Cdd:cd01387 637 RLCTVTPKdMYRLGATKVFLR 657
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
79-717 |
0e+00 |
|
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: 610.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 79 LETRYELNEIYTYTGNILIAVNPFQRLPHIYET-DMMEQYKGIALGELS-PHVFAIGDAAYRAM----INEGKNNSILVS 152
Cdd:cd14892 7 LRRRYERDAIYTFTADILISINPYKSIPLLYDVpGFDSQRKEEATASSPpPHVFSIAERAYRAMkgvgKGQGTPQSIVVS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 153 GESGAGKTETTKMLMRYLAFLG--GRSGVEGRT-------VEQQVLESNPVLEAFGNAKTLRNNNSSRFGKFVEIQFDKN 223
Cdd:cd14892 87 GESGAGKTEASKYIMKYLATASklAKGASTSKGaanahesIEECVLLSNLILEAFGNAKTIRNDNSSRFGKYIQIHYNSD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 224 GRISGAAIRTYLLERSRVCQISDPERNYHCFYLLCAAPPEDIK-KYKLENPHKFHYLNQSSCYKLDGVDDASEYLETRRA 302
Cdd:cd14892 167 GRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENaALELTPAESFLFLNQGNCVEVDGVDDATEFKQLRDA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 303 MDVVGISNEEQEAIFRVVAAILHLGNIDFGKGEEiDSSVIKDKDSRSHLNMAAELLMCNAQSLEDALIRRVMVT-PEEII 381
Cdd:cd14892 247 MEQLGFDAEFQRPIFEVLAAVLHLGNVRFEENAD-DEDVFAQSADGVNVAKAAGLLGVDAAELMFKLVTQTTSTaRGSVL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 382 TRTLDPDNAIASRDTLAKTIYSHLFDWIVNKINTSIGQ----------DPRSKSIIGVLDIYGFESFKCNSFEQFCINFT 451
Cdd:cd14892 326 EIKLTAREAKNALDALCKYLYGELFDWLISRINACHKQqtsgvtggaaSPTFSPFIGILDIFGFEIMPTNSFEQLCINFT 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 452 NEKLQQHFNQHVFKMEQEEYTKEEIAWSYIEFIDNQDVLELIEKKPGGIISLLDEACMFP-KSTHETFSQKLFQT-FKEH 529
Cdd:cd14892 406 NEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQDNQDCLDLIQKKPLGLLPLLEEQMLLKrKTTDKQLLTIYHQThLDKH 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 530 ERFAKPKLSRTDFTISHYAGEVTYQSNHFIDKNKDyivaehqalftasnckfvaglfhALHEDSSRSSKFssiGSRFKQQ 609
Cdd:cd14892 486 PHYAKPRFECDEFVLRHYAGDVTYDVHGFLAKNND-----------------------NLHDDLRDLLRS---SSKFRTQ 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 610 LHSLMESLNGTEPHYIRCIKPNNVLKPGIFENFNVIHQLRCGGVLEAIRISCAGYPTRLAFYDFLDRFGLLA-------- 681
Cdd:cd14892 540 LAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVRIRREGFPIRRQFEEFYEKFWPLArnkagvaa 619
|
650 660 670
....*....|....*....|....*....|....*..
gi 30685403 682 -PEVLEGNYDDKVACQMILDKKSLTDYQIGKTKIFLR 717
Cdd:cd14892 620 sPDACDATTARKKCEEIVARALERENFQLGRTKVFLR 656
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
75-717 |
0e+00 |
|
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: 589.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 75 VLRNLETRYELNEIYTYTGNILIAVNPFQRLPHIYETDMMEQYKGIALGELSPHVFAIGDAAYRAMINEGKNNSILVSGE 154
Cdd:cd14873 3 IMYNLFQRYKRNQIYTYIGSILASVNPYQPIAGLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILISGE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 155 SGAGKTETTKMLMRYLAFL-----GGRSGVEGRTVEQQVLESNPVLEAFGNAKTLRNNNSSRFGKFVEIQFDKNGRISGA 229
Cdd:cd14873 83 SGAGKTESTKLILKFLSVIsqqslELSLKEKTSCVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNIQGG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 230 AIRTYLLERSRVCQISDPERNYHCFY-LLCAAPPEDIKKYKLENPHKFHYLNQSSCYKLDGVDDASEYLETRRAMDVVGI 308
Cdd:cd14873 163 RIVDYLLEKNRVVRQNPGERNYHIFYaLLAGLEHEEREEFYLSTPENYHYLNQSGCVEDKTISDQESFREVITAMEVMQF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 309 SNEEQEAIFRVVAAILHLGNIDF--GKGEEIdssvikdkDSRSHLNMAAELLMCNAQSLEDALIRRVMVTPEEIITRTLD 386
Cdd:cd14873 243 SKEEVREVSRLLAGILHLGNIEFitAGGAQV--------SFKTALGRSAELLGLDPTQLTDALTQRSMFLRGEEILTPLN 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 387 PDNAIASRDTLAKTIYSHLFDWIVNKINTSIGQDPRSKSiIGVLDIYGFESFKCNSFEQFCINFTNEKLQQHFNQHVFKM 466
Cdd:cd14873 315 VQQAVDSRDSLAMALYARCFEWVIKKINSRIKGKEDFKS-IGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKHIFSL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 467 EQEEYTKEEIAWSYIEFIDNQDVLELIEKKPgGIISLLDEACMFPKSTHETFSQKLFQTFKEHERFAKPKLSRTDFTISH 546
Cdd:cd14873 394 EQLEYSREGLVWEDIDWIDNGECLDLIEKKL-GLLALINEESHFPQATDSTLLEKLHSQHANNHFYVKPRVAVNNFGVKH 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 547 YAGEVTYQSNHFIDKNKDYIVAEHQALFTASNCKFVAGLFHAL----HEDSSRSSKFS---SIGSRFKQQLHSLMESLNG 619
Cdd:cd14873 473 YAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEHVssrnNQDTLKCGSKHrrpTVSSQFKDSLHSLMATLSS 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 620 TEPHYIRCIKPNNVLKPGIFENFNVIHQLRCGGVLEAIRISCAGYPTRLAFYDFLDRFGLLAPEV-LEGNYDDKVACQMI 698
Cdd:cd14873 553 SNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMRNLaLPEDVRGKCTSLLQ 632
|
650
....*....|....*....
gi 30685403 699 LDKKSLTDYQIGKTKIFLR 717
Cdd:cd14873 633 LYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
75-717 |
0e+00 |
|
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: 588.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 75 VLRNLETRYELNEIYTYTGNILIAVNPFQRLPhIYETDMMEQYKGIAL-GELSPHVFAIGDAAYRAMINEGKNNSILVSG 153
Cdd:cd14897 3 IVQTLKSRYNKDKFYTYIGDILVAVNPCKPLP-IFDKKHHEEYSNLSVrSQRPPHLFWIADQAYRRLLETGRNQCILVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 154 ESGAGKTETTKMLMRYLAFLggrSGVEGRTVEQQVLESNPVLEAFGNAKTLRNNNSSRFGKFVEIQFDKNGRISGAAIRT 233
Cdd:cd14897 82 ESGAGKTESTKYMIKHLMKL---SPSDDSDLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQLLGAKIDD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 234 YLLERSRVCQISDPERNYHCFYLLCA-APPEDIKKYKLENPHKFHYLNQSSCYKldGVDDASEYLETRRA--------MD 304
Cdd:cd14897 159 YLLEKSRVVHRGNGEKNFHIFYALFAgMSRDRLLYYFLEDPDCHRILRDDNRNR--PVFNDSEELEYYRQmfhdltniMK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 305 VVGISNEEQEAIFRVVAAILHLGNIDFGKGEEIDSSVIKDKDsrsHLNMAAELLMCNAQSLEDALIRRVMVTPEEIITRT 384
Cdd:cd14897 237 LIGFSEEDISVIFTILAAILHLTNIVFIPDEDTDGVTVADEY---PLHAVAKLLGIDEVELTEALISNVNTIRGERIQSW 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 385 LDPDNAIASRDTLAKTIYSHLFDWIVNKINTSI-----GQDPRSKSIIGVLDIYGFESFKCNSFEQFCINFTNEKLQQHF 459
Cdd:cd14897 314 KSLRQANDSRDALAKDLYSRLFGWIVGQINRNLwpdkdFQIMTRGPSIGILDMSGFENFKINSFDQLCINLSNERLQQYF 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 460 NQHVFKMEQEEYTKEEIAWSYIEFIDNQDVLELIEKKPGGIISLLDEACMFPKSTHETFSQKLFQTFKEHERFAKPKLSR 539
Cdd:cd14897 394 NDYVFPRERSEYEIEGIEWRDIEYHDNDDVLELFFKKPLGILPLLDEESTFPQSTDSSLVQKLNKYCGESPRYVASPGNR 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 540 TDFTISHYAGEVTYQSNHFIDKNKDYIVAEHQALFTASNCKFVAGLFhalhedssrsskfssiGSRFKQQLHSLMESLNG 619
Cdd:cd14897 474 VAFGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLF----------------TSYFKRSLSDLMTKLNS 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 620 TEPHYIRCIKPNNVLKPGIFENFNVIHQLRCGGVLEAIRISCAGYPTRLAFYDFLDRFGLLAPEVLEGNYDDKVACQMIL 699
Cdd:cd14897 538 ADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYEDFVKRYKEICDFSNKVRSDDLGKCQKIL 617
|
650
....*....|....*...
gi 30685403 700 DKKSLTDYQIGKTKIFLR 717
Cdd:cd14897 618 KTAGIKGYQFGKTKVFLK 635
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
75-717 |
0e+00 |
|
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: 586.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 75 VLRNLETRYELNEIYTYTGNILIAVNPFQRLPhIYETDMMEQYKGIALGELSPHVFAIGDAAYRAMINEGKNNSILVSGE 154
Cdd:cd01379 3 IVSQLQKRYSRDQIYTYIGDILIAVNPFQNLG-IYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 155 SGAGKTETTKMLMRYLAFLGGRSGvegRTVEQQVLESNPVLEAFGNAKTLRNNNSSRFGKFVEIQFDKNGRISGAAIRTY 234
Cdd:cd01379 82 SGAGKTESANLLVQQLTVLGKANN---RTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAVTGARISEY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 235 LLERSRVCQISDPERNYHCFYLLCA--APPEDIKKYKLENPHKFHYLNQSSCYKLDGVDDAS---EYLETRRAMDVVGIS 309
Cdd:cd01379 159 LLEKSRVVHQAIGERNFHIFYYIYAglAEDKKLAKYKLPENKPPRYLQNDGLTVQDIVNNSGnreKFEEIEQCFKVIGFT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 310 NEEQEAIFRVVAAILHLGNIDF----GKGEEIDSSVIKDKDSrshLNMAAELLMCNAQSLEDALIRRVMVTPEEIITRTL 385
Cdd:cd01379 239 KEEVDSVYSILAAILHIGDIEFteveSNHQTDKSSRISNPEA---LNNVAKLLGIEADELQEALTSHSVVTRGETIIRNN 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 386 DPDNAIASRDTLAKTIYSHLFDWIVNKINTSIGQDPRSKS---IIGVLDIYGFESFKCNSFEQFCINFTNEKLQQHFNQH 462
Cdd:cd01379 316 TVEEATDARDAMAKALYGRLFSWIVNRINSLLKPDRSASDeplSIGILDIFGFENFQKNSFEQLCINIANEQIQYYFNQH 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 463 VFKMEQEEYTKEEIAWSYIEFIDNQDVLELIEKKPGGIISLLDEACMFPKSTHETFSQKLFQTFKEHErFAKPKLSRTDF 542
Cdd:cd01379 396 IFAWEQQEYLNEGIDVDLIEYEDNRPLLDMFLQKPMGLLALLDEESRFPKATDQTLVEKFHNNIKSKY-YWRPKSNALSF 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 543 TISHYAGEVTYQSNHFIDKNKDYIVAEHQALFTASNCKFVaglfhalhedssrsskFSSIGSRFKqqlHSLMESLN---- 618
Cdd:cd01379 475 GIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLV----------------RQTVATYFR---YSLMDLLSkmvv 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 619 GTePHYIRCIKPNNVLKPGIFENFNVIHQLRCGGVLEAIRISCAGYPTRLAFYDFLDRFGLLApevleGNYDDKV----- 693
Cdd:cd01379 536 GQ-PHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRILFADFLKRYYFLA-----FKWNEEVvanre 609
|
650 660
....*....|....*....|....
gi 30685403 694 ACQMILDKKSLTDYQIGKTKIFLR 717
Cdd:cd01379 610 NCRLILERLKLDNWALGKTKVFLK 633
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
73-717 |
0e+00 |
|
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: 581.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 73 PGVLRNLETRYELNEI--YTYTGNILIAVNPFQRLPhiyETDMMEqYKGIALGELSPHVFAIGDAAYRAMI-NEGK--NN 147
Cdd:cd14891 1 AGILHNLEERSKLDNQrpYTFMANVLIAVNPLRRLP---EPDKSD-YINTPLDPCPPHPYAIAEMAYQQMClGSGRmqNQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 148 SILVSGESGAGKTETTKMLMRYLAF--LGGRSGVE-------------GRTVEQQVLESNPVLEAFGNAKTLRNNNSSRF 212
Cdd:cd14891 77 SIVISGESGAGKTETSKIILRFLTTraVGGKKASGqdieqsskkrklsVTSLDERLMDTNPILESFGNAKTLRNHNSSRF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 213 GKFVEIQFDKNG-RISGAAIRTYLLERSRVCQISDPERNYHCFY-LLCAAPPEDIKKYKLENPHKFHYLNQSSCYKLDGV 290
Cdd:cd14891 157 GKFMKLQFTKDKfKLAGAFIETYLLEKSRLVAQPPGERNFHIFYqLLAGASAELLKELLLLSPEDFIYLNQSGCVSDDNI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 291 DDASEYLETRRAMDVVGISNEEQEAIFRVVAAILHLGNIDFGKGE-EIDSSVIKDKDSRSHLNMAAELLMCNAQSLEDAL 369
Cdd:cd14891 237 DDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEEDtSEGEAEIASESDKEALATAAELLGVDEEALEKVI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 370 IRRVMVTPEEIITRTLDPDNAIASRDTLAKTIYSHLFDWIVNKINTSIGQDPRSKSIIGVLDIYGFESFK-CNSFEQFCI 448
Cdd:cd14891 317 TQREIVTRGETFTIKRNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGHDPDPLPYIGVLDIFGFESFEtKNDFEQLLI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 449 NFTNEKLQQHFNQHVFKMEQEEYTKEEIAWSYIEFIDNQDVLELIEKKPGGIISLLDEACMFPKSTHETFSQKLFQTFKE 528
Cdd:cd14891 397 NYANEALQATFNQQVFIAEQELYKSEGIDVGVITWPDNRECLDLIASKPNGILPLLDNEARNPNPSDAKLNETLHKTHKR 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 529 HERF--AKPKLSRTDFTISHYAGEVTYQSNHFIDKNKDYIVAEHQALFTASNckfvaglfhalhedssrsskfssigsRF 606
Cdd:cd14891 477 HPCFprPHPKDMREMFIVKHYAGTVSYTIGSFIDKNNDIIPEDFEDLLASSA--------------------------KF 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 607 KQQLHSLMESLNGTEPHYIRCIKPNNVLKPGIFENFNVIHQLRCGGVLEAIRISCAGYPTRLAFYDFLDRFG-LLAPEV- 684
Cdd:cd14891 531 SDQMQELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVLKVGLPTRVTYAELVDVYKpVLPPSVt 610
|
650 660 670
....*....|....*....|....*....|....*.
gi 30685403 685 -LEGNYdDKVACQMIL--DKKSLTDYQIGKTKIFLR 717
Cdd:cd14891 611 rLFAEN-DRTLTQAILwaFRVPSDAYRLGRTRVFFR 645
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
73-717 |
0e+00 |
|
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: 574.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 73 PGVLRNLETRYELNEIYTYTGNILIAVNPFQRLPhIYETDMMEQYKGIAL---------GELSPHVFAIGDAAYRAMINE 143
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLP-LYGKEILESYRQEGLlrsqgiespQALGPHVFAIADRSYRQMMSE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 144 G-KNNSILVSGESGAGKTETTKMLMRYLAFLGGRSGV--------EGRTVEQQVLESNPVLEAFGNAKTLRNNNSSRFGK 214
Cdd:cd14908 80 IrASQSILISGESGAGKTESTKIVMLYLTTLGNGEEGapnegeelGKLSIMDRVLQSNPILEAFGNARTLRNDNSSRFGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 215 FVEIQFDKNGRISGAAIRTYLLERSRVCQISDPERNYHCFYLLC-AAPPEDIKKYK--------LENPHKFHYLNQSSCY 285
Cdd:cd14908 160 FIELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLrGGDEEEHEKYEfhdgitggLQLPNEFHYTGQGGAP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 286 KLDGVDDASEYLETRRAMDVVGISNEEQEAIFRVVAAILHLGNIDFGKGEEIDSSVIKDKDSRSHLNMAAELLMCNAQSL 365
Cdd:cd14908 240 DLREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDGAAEIAEEGNEKCLARVAKLLGVDVDKL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 366 EDALIRRVMVTPEEIITRTLDPDNAIASRDTLAKTIYSHLFDWIVNKINTSIGQDPRS--KSIIGVLDIYGFESFKCNSF 443
Cdd:cd14908 320 LRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSINWENDKdiRSSVGVLDIFGFECFAHNSF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 444 EQFCINFTNEKLQQHFNQHVFKMEQEEYTKEEIAWSYIEFIDNQDVLELIEKKPGGIISLLDEACMFP-KSTHETFSQKL 522
Cdd:cd14908 400 EQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFPDNQDCLDTIQAKKKGILTMLDDECRLGiRGSDANYASRL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 523 F--------QTFKEHERFAKPKLSRTD--FTISHYAGEVTYQ-SNHFIDKNKDYIVAEHQALFTAsnckfvaglfhalhe 591
Cdd:cd14908 480 YetylpeknQTHSENTRFEATSIQKTKliFAVRHFAGQVQYTvETTFCEKNKDEIPLTADSLFES--------------- 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 592 dssrsskfssiGSRFKQQLHSLMESLNGTEPHYIRCIKPNNVLKPGIFENFNVIHQLRCGGVLEAIRISCAGYPTRLAFY 671
Cdd:cd14908 545 -----------GQQFKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRYGGVLEAVRVARSGYPVRLPHK 613
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30685403 672 DFLDRFGLLAPEVLE-------GNYDDKVACQMILDK--------------KSL--TDYQIGKTKIFLR 717
Cdd:cd14908 614 DFFKRYRMLLPLIPEvvlswsmERLDPQKLCVKKMCKdlvkgvlspamvsmKNIpeDTMQLGKSKVFMR 682
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
75-717 |
0e+00 |
|
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: 567.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 75 VLRNLETRYELNEIYTYTGNILIAVNPFQRLPHIYETDMMEQYKGIA--------LGELSPHVFAIGDAAYRAMINEGKN 146
Cdd:cd14907 3 LLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDNLFSEEVMQMYKEQIiqngeyfdIKKEPPHIYAIAALAFKQLFENNKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 147 NSILVSGESGAGKTETTKMLMRYLAFLGG----------------RSGVEGRTVEQQVLESNPVLEAFGNAKTLRNNNSS 210
Cdd:cd14907 83 QAIVISGESGAGKTENAKYAMKFLTQLSQqeqnseevltltssirATSKSTKSIEQKILSCNPILEAFGNAKTVRNDNSS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 211 RFGKFVEIQFD-KNGRISGAAIRTYLLERSRVCQISDPERNYHCFY-LLCAAPPEDIKKYKLENPHK---FHYLNQSSCY 285
Cdd:cd14907 163 RFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYhLLYGADQQLLQQLGLKNQLSgdrYDYLKKSNCY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 286 KLDGVDDASEYLETRRAMDVVGISNEEQEAIFRVVAAILHLGNIDFGKGEEIDSS--VIKDKDSrshLNMAAELLMCNAQ 363
Cdd:cd14907 243 EVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDSTLDDNSpcCVKNKET---LQIIAKLLGIDEE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 364 SLEDALIRRVMVTPEEIITRTLDPDNAIASRDTLAKTIYSHLFDWIVNKINTSIGQDPRSK--------SIIGVLDIYGF 435
Cdd:cd14907 320 ELKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTIMPKDEKDqqlfqnkyLSIGLLDIFGF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 436 ESFKCNSFEQFCINFTNEKLQQHFNQHVFKMEQEEYTKE--EIAWSYIEFIDNQDVLELIEKKPGGIISLLDEACMFPKS 513
Cdd:cd14907 400 EVFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEglEDYLNQLSYTDNQDVIDLLDKPPIGIFNLLDDSCKLATG 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 514 THETFSQKLFQTFKEHERFAKP-KLSRTDFTISHYAGEVTYQSNHFIDKNKDYIVAEHQALFTASNCKFVAGLFHALHED 592
Cdd:cd14907 480 TDEKLLNKIKKQHKNNSKLIFPnKINKDTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIFSGEDGS 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 593 SSRSSKFSS--------IGSRFKQQLHSLMESLNGTEPHYIRCIKPNNVLKPGIFENFNVIHQLRCGGVLEAIRISCAGY 664
Cdd:cd14907 560 QQQNQSKQKksqkkdkfLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYLGVLESIRVRKQGY 639
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 30685403 665 PTRLAFYDFLDRFGLLAPEVLegnyddkvacqmildkksltdyqIGKTKIFLR 717
Cdd:cd14907 640 PYRKSYEDFYKQYSLLKKNVL-----------------------FGKTKIFMK 669
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
73-717 |
0e+00 |
|
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: 556.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 73 PGVLRNLETRYELNEIYTYTGNILIAVNPFQRLPHIYETDMMEQYKGIALGELSPHVFAIGDAAYRAMINEGKNNSILVS 152
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDNLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 153 GESGAGKTETTKMLMRYLAFLGGrsGVEGRTVEqQVLESNPVLEAFGNAKTLRNNNSSRFGKFVEIQFDKNGRISGAAIR 232
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVAG--GRKDKTIA-KVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRGKLIGAKCE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 233 TYLLERSRVCQISDPERNYHCFY-LLCAAPPEDIKKYKLENPHKFHYLNQSSC-YKLDGVDDASEYLETRRAMDVVGISN 310
Cdd:cd14904 158 TYLLEKSRVVSIAEGERNYHIFYqLLAGLSSEERKEFGLDPNCQYQYLGDSLAqMQIPGLDDAKLFASTQKSLSLIGLDN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 311 EEQEAIFRVVAAILHLGNIDFGKGEEiDSSVIKDKDSrshLNMAAELLMCNAQSLEDALIRRVMVTPEEIITRTLDPDNA 390
Cdd:cd14904 238 DAQRTLFKILSGVLHLGEVMFDKSDE-NGSRISNGSQ---LSQVAKMLGLPTTRIEEALCNRSVVTRNESVTVPLAPVEA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 391 IASRDTLAKTIYSHLFDWIVNKINTSIGQD-PRSKSIIGVLDIYGFESFKCNSFEQFCINFTNEKLQQHFNQHVFKMEQE 469
Cdd:cd14904 314 EENRDALAKAIYSKLFDWMVVKINAAISTDdDRIKGQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDVFKTVEE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 470 EYTKEEIAWSYIEFIDNQDVLELIEKKPgGIISLLDEACMFPKSTHETFSQKL---FQTFKEHERFAKPKLSRTDFTISH 546
Cdd:cd14904 394 EYIREGLQWDHIEYQDNQGIVEVIDGKM-GIIALMNDHLRQPRGTEEALVNKIrtnHQTKKDNESIDFPKVKRTQFIINH 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 547 YAGEVTYQSNHFIDKNKDYIVAEHQALFTASNCKFVAGLF--------HALHEDSSRSSKFSSIGSRFKQQLHSLMESLN 618
Cdd:cd14904 473 YAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFgsseapseTKEGKSGKGTKAPKSLGSQFKTSLSQLMDNIK 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 619 GTEPHYIRCIKPNNVLKPGIFENFNVIHQLRCGGVLEAIRISCAGYPTRLAFYDFLDRFGLLAPEVLEgNYDDKVACQMI 698
Cdd:cd14904 553 TTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAIMFPPSMH-SKDVRRTCSVF 631
|
650 660
....*....|....*....|..
gi 30685403 699 LD---KKSLTDYQIGKTKIFLR 717
Cdd:cd14904 632 MTaigRKSPLEYQIGKSLIYFK 653
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
75-717 |
1.79e-177 |
|
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: 546.50 E-value: 1.79e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 75 VLRNLETRYELNEIYTYTGNILIAVNPFQRLPhIYETDMMEQYKGIALGELSPHVFAIGDAAYRAMINEGKNNSILVSGE 154
Cdd:cd14911 3 VLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLP-IYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 155 SGAGKTETTKMLMRYLAFLG-----GRSGVEGRTV---------EQQVLESNPVLEAFGNAKTLRNNNSSRFGKFVEIQF 220
Cdd:cd14911 82 SGAGKTENTKKVIQFLAYVAaskpkGSGAVPHPAVnpavligelEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 221 DKNGRISGAAIRTYLLERSRVCQISDPERNYHCFY-LLCAAPPEDIKKYKLENPHKFHYLNQSScYKLDGVDDASEYLET 299
Cdd:cd14911 162 DASGFISGANIETYLLEKSRAIRQAKDERTFHIFYqLLAGATPEQREKFILDDVKSYAFLSNGS-LPVPGVDDYAEFQAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 300 RRAMDVVGISNEEQEAIFRVVAAILHLGNIDFGKGEEIDSSVIKDKDSRSHLnmaAELLMCNAQSLEDALIRRVMVTPEE 379
Cdd:cd14911 241 VKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKI---AHLLGLSVTDMTRAFLTPRIKVGRD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 380 IITRTLDPDNAIASRDTLAKTIYSHLFDWIVNKINTSIGQDPRS-KSIIGVLDIYGFESFKCNSFEQFCINFTNEKLQQH 458
Cdd:cd14911 318 FVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQgASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 459 FNQHVFKMEQEEYTKEEIAWSYIEF-IDNQDVLELIEkKPGGIISLLDEACMFPKSTHETFSQKLFQTFKEHERFAKPKL 537
Cdd:cd14911 398 FNHTMFILEQEEYQREGIEWKFIDFgLDLQPTIDLID-KPGGIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMKTDF 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 538 SRT-DFTISHYAGEVTYQSNHFIDKNKDYIVAEHQALFTASNCKFV---------AGLFHALHEDSSRSSKFS-----SI 602
Cdd:cd14911 477 RGVaDFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVvniwkdaeiVGMAQQALTDTQFGARTRkgmfrTV 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 603 GSRFKQQLHSLMESLNGTEPHYIRCIKPNNVLKPGIFENFNVIHQLRCGGVLEAIRISCAGYPTRLAFYDFLDRFGLLAP 682
Cdd:cd14911 557 SHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTP 636
|
650 660 670
....*....|....*....|....*....|....*...
gi 30685403 683 EVL-EGNYDDKVACQMILDKKSLTD--YQIGKTKIFLR 717
Cdd:cd14911 637 NVIpKGFMDGKKACEKMIQALELDSnlYRVGQSKIFFR 674
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
75-681 |
2.28e-171 |
|
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: 528.34 E-value: 2.28e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 75 VLRNLETRYELNEIYTYTGNILIAVNPFQRLPHIYETDMMEQY-------------KGIAlgELSPHVFAIGDAAYRAMI 141
Cdd:cd14900 3 ILSALETRFYAQKIYTNTGAILLAVNPFQKLPGLYSSDTMAKYllsfearssstrnKGSD--PMPPHIYQVAGEAYKAMM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 142 N----EGKNNSILVSGESGAGKTETTKMLMRYLAFLGG-------RSGVEGRTVEQQVLESNPVLEAFGNAKTLRNNNSS 210
Cdd:cd14900 81 LglngVMSDQSILVSGESGSGKTESTKFLMEYLAQAGDnnlaasvSMGKSTSGIAAKVLQTNILLESFGNARTLRNDNSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 211 RFGKFVEIQFDKNGRISGAAIRTYLLERSRVCQISDPERNYHCFY--LLCAAPPEdikkyklenpHKFHYLNQsscykld 288
Cdd:cd14900 161 RFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYemAIGASEAA----------RKRDMYRR------- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 289 gvddaseyleTRRAMDVVGISNEEQEAIFRVVAAILHLGNIDFgKGEEIDSSVIKDKD-----SRSHLNMAAELLMCNAQ 363
Cdd:cd14900 224 ----------VMDAMDIIGFTPHERAGIFDLLAALLHIGNLTF-EHDENSDRLGQLKSdlapsSIWSRDAAATLLSVDAT 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 364 SLEDALIRRVMVTPEEIITRTLDPDNAIASRDTLAKTIYSHLFDWIVNKINTSIGQDPRSKS-----IIGVLDIYGFESF 438
Cdd:cd14900 293 KLEKALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLKMDDSSKShgglhFIGILDIFGFEVF 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 439 KCNSFEQFCINFTNEKLQQHFNQHVFKMEQEEYTKEEIAWSYIEFIDNQDVLELIEKKPGGIISLLDEACMFPKSTHETF 518
Cdd:cd14900 373 PKNSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFCDNQDCVNLISQRPTGILSLIDEECVMPKGSDTTL 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 519 SQKLFQTFKEHERFAKPKLSRTD--FTISHYAGEVTYQSNHFIDKNKDYIVAEHQALFTAsnckfvaglfhalhedssrs 596
Cdd:cd14900 453 ASKLYRACGSHPRFSASRIQRARglFTIVHYAGHVEYSTDGFLEKNKDVLHQEAVDLFVY-------------------- 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 597 skfssiGSRFKQQLHSLMESLNGTEPHYIRCIKPNNVLKPGIFENFNVIHQLRCGGVLEAIRISCAGYPTRLAFYDFLDR 676
Cdd:cd14900 513 ------GLQFKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVMEAVRVARAGFPIRLLHDEFVAR 586
|
....*
gi 30685403 677 FGLLA 681
Cdd:cd14900 587 YFSLA 591
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
75-717 |
1.80e-170 |
|
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: 527.17 E-value: 1.80e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 75 VLRNLETRYELNEIYTYTGNILIAVNPFQRLpHIYETDMMEQYKGIALGELSPHVFAIGDAAYRAMINEG----KNNSIL 150
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYL-HIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLGRLargpKNQCIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 151 VSGESGAGKTETTKMLMRYLAFLggrsgVEGRT-VEQQVLESNPVLEAFGNAKTLRNNNSSRFGKFVEIQFdKNGRISGA 229
Cdd:cd14889 82 ISGESGAGKTESTKLLLRQIMEL-----CRGNSqLEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRF-RNGHVKGA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 230 AIRTYLLERSRVCQISDPERNYHCFYLLCAA-PPEDIKKYKLENPHKFHYLNQSSCYKLDGVDDASEYLETRRAMDVVGI 308
Cdd:cd14889 156 KINEYLLEKSRVVHQDGGEENFHIFYYMFAGiSAEDRENYGLLDPGKYRYLNNGAGCKREVQYWKKKYDEVCNAMDMVGF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 309 SNEEQEAIFRVVAAILHLGNIDFgkgEEIDSSVIK-DKDSRSHLNMAAELLMCNAQSLEDALIRRVMVTPEEIITRTLDP 387
Cdd:cd14889 236 TEQEEVDMFTILAGILSLGNITF---EMDDDEALKvENDSNGWLKAAAGQFGVSEEDLLKTLTCTVTFTRGEQIQRHHTK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 388 DNAIASRDTLAKTIYSHLFDWIVNKINTSIGqdPRSKSI-----IGVLDIYGFESFKCNSFEQFCINFTNEKLQQHFNQH 462
Cdd:cd14889 313 QQAEDARDSIAKVAYGRVFGWIVSKINQLLA--PKDDSSvelreIGILDIFGFENFAVNRFEQACINLANEQLQYFFNHH 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 463 VFKMEQEEYTKEEIAWSYIEFIDNQDVLELIEKKPGGIISLLDEACMFPKSTHETFSQKLFQTFKEHERFAKPKLSRTDF 542
Cdd:cd14889 391 IFLMEQKEYKKEGIDWKEITYKDNKPILDLFLNKPIGILSLLDEQSHFPQATDESFVDKLNIHFKGNSYYGKSRSKSPKF 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 543 TISHYAGEVTYQSNHFIDKNKDYIVAEHQALFTASNCKFVAGLFHA----------------LHEDSSRSSKFSSIGSRF 606
Cdd:cd14889 471 TVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFTAtrsrtgtlmpraklpqAGSDNFNSTRKQSVGAQF 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 607 KQQLHSLMESLNGTEPHYIRCIKPNNVLKPGIFENFNVIHQLRCGGVLEAIRISCAGYPTRLAFYDFLDRFGLLapeVLE 686
Cdd:cd14889 551 KHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFSWRPSFAEFAERYKIL---LCE 627
|
650 660 670
....*....|....*....|....*....|..
gi 30685403 687 GNYD-DKVACQMILDKKSLTDYQIGKTKIFLR 717
Cdd:cd14889 628 PALPgTKQSCLRILKATKLVGWKCGKTRLFFK 659
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
73-717 |
2.70e-166 |
|
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: 515.48 E-value: 2.70e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 73 PGVLRNLETRYELNEIYTYTGNILIAVNPFQRLPhIYETDMMEQYKGIALGELSPHVFAIGDAAYRAMINEGKNNSILVS 152
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLP-LFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 153 GESGAGKTETTKMLMRYLAFLGGRSGvegRTVEQQVLESNPVLEAFGNAKTLRNNNSSRFGKFVEIQFdKNGRISGAAIR 232
Cdd:cd14896 80 GHSGSGKTEAAKKIVQFLSSLYQDQT---EDRLRQPEDVLPILESFGHAKTILNANASRFGQVLRLHL-QHGVIVGASVS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 233 TYLLERSRVCQISDPERNYHCFY-LLCAAPPEDIKKYKLENPHKFHYLNQSSCYKLDGVDDASEYLETRRAMDVVGISNE 311
Cdd:cd14896 156 HYLLETSRVVFQAQAERSFHVFYeLLAGLDPEEREQLSLQGPETYYYLNQGGACRLQGKEDAQDFEGLLKALQGLGLCAE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 312 EQEAIFRVVAAILHLGNIDFGKGEEiDSSVIKDKDSRSHLNMAAELLMCNAQSLEDALIRRVMVTPEEIITRTLDPDNAI 391
Cdd:cd14896 236 ELTAIWAVLAAILQLGNICFSSSER-ESQEVAAVSSWAEIHTAARLLQVPPERLEGAVTHRVTETPYGRVSRPLPVEGAI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 392 ASRDTLAKTIYSHLFDWIVNKINTSIG--QDPRSKSIIGVLDIYGFESFKCNSFEQFCINFTNEKLQQHFNQHVFKMEQE 469
Cdd:cd14896 315 DARDALAKTLYSRLFTWLLKRINAWLAppGEAESDATIGVVDAYGFEALRVNGLEQLCINLASERLQLFSSQTLLAQEEE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 470 EYTKEEIAWSYIEFIDNQDVLELIEKKPGGIISLLDEACMFPKSTHETFSQKLFQTFKEHERFAKPKLSRTDFTISHYAG 549
Cdd:cd14896 395 ECQRELLPWVPIPQPPRESCLDLLVDQPHSLLSILDDQTWLSQATDHTFLQKCHYHHGDHPSYAKPQLPLPVFTVRHYAG 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 550 EVTYQSNHFIDKNKDYIVAEHQALFTASNCKFVAGLFHALHEDSSRSSKFSSIGSRFKQQLHSLMESLNGTEPHYIRCIK 629
Cdd:cd14896 475 TVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQEAEPQYGLGQGKPTLASRFQQSLGDLTARLGRSHVYFIHCLN 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 630 PNNVLKPGIFENFNVIHQLRCGGVLEAIRISCAGYPTRLAFYDFLDRFGLLAPEVLEGnYDDKVACQMILDK---KSLTD 706
Cdd:cd14896 555 PNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGALGSERQEA-LSDRERCGAILSQvlgAESPL 633
|
650
....*....|.
gi 30685403 707 YQIGKTKIFLR 717
Cdd:cd14896 634 YHLGATKVLLK 644
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
73-682 |
1.41e-165 |
|
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: 516.37 E-value: 1.41e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 73 PGVLRNLETRYELNEIYTYTGNILIAVNPFQRLPHIYETDMMEQYK--------GIALGELSPHVFAIGDAAYRAMI-NE 143
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPDLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLkPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 144 GKNNSILVSGESGAGKTETTKMLMRYLAFLG------GRSGVEGRTVEQQVLESNPVLEAFGNAKTLRNNNSSRFGKFVE 217
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLTSVGrdqsstEQEGSDAVEIGKRILQTNPILESFGNAQTIRNDNSSRFGKFIK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 218 IQFDKNGRISGAAIRTYLLERSRVCQISDPERNYHCFYLLCAAPPEDIKK-YKLENPHKFHYLNQSSCY----KLDGVDD 292
Cdd:cd14902 161 IQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDlLGLQKGGKYELLNSYGPSfarkRAVADKY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 293 ASEYLETRRAMDVVGISNEEQEAIFRVVAAILHLGNIDFGKGEEIDSSVIKDKDSRSHLNMAAELLMCNAQSLEDALIRR 372
Cdd:cd14902 241 AQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAENGQEDATAVTAASRFHLAKCAELMGVDVDKLETLLSSR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 373 VMVTPEEIITRTLDPDNAIASRDTLAKTIYSHLFDWIVNKINTSIGQDPRSKSI---------IGVLDIYGFESFKCNSF 443
Cdd:cd14902 321 EIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINYFDSAVSIsdedeelatIGILDIFGFESLNRNGF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 444 EQFCINFTNEKLQQHFNQHVFKMEQEEYTKEEIAWSYIEFIDNQDVLELIEKKPGGIISLLDEACMFPKSTHETFSQKLF 523
Cdd:cd14902 401 EQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYPSNAACLALFDDKSNGLFSLLDQECLMPKGSNQALSTKFY 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 524 QTFkeherfakpkLSRTDFTISHYAGEVTYQSNHFIDKNKDYIVAEHQALFTASNCKFVAGLFHALHEDSSRSSK----- 598
Cdd:cd14902 481 RYH----------GGLGQFVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVVVAIGADENRDSPGADNgaagr 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 599 -------FSSIGSRFKQQLHSLMESLNGTEPHYIRCIKPNNVLKPGIFENFNVIHQLRCGGVLEAIRISCAGYPTRLAFY 671
Cdd:cd14902 551 rrysmlrAPSVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLEAVRIARHGYSVRLAHA 630
|
650
....*....|.
gi 30685403 672 DFLDRFGLLAP 682
Cdd:cd14902 631 SFIELFSGFKC 641
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
61-796 |
7.24e-165 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 518.05 E-value: 7.24e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 61 VDDMTKLSYLHEPGVLRNLETRYELNEIYTYTGNILIAVNPFQRLPHIYEtDMMEQYKGIA-LGELSPHVFAIGDAAYRA 139
Cdd:PTZ00014 98 YGDIGLLPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTN-DWIRRYRDAKdSDKLPPHVFTTARRALEN 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 140 MINEGKNNSILVSGESGAGKTETTKMLMRYlaFLGGRSGVEGRTVEQQVLESNPVLEAFGNAKTLRNNNSSRFGKFVEIQ 219
Cdd:PTZ00014 177 LHGVKKSQTIIVSGESGAGKTEATKQIMRY--FASSKSGNMDLKIQNAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQ 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 220 FDKNGRISGAAIRTYLLERSRVCQISDPERNYHCFY-LLCAAPPEDIKKYKLENPHKFHYLNqSSCYKLDGVDDASEYLE 298
Cdd:PTZ00014 255 LGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYqLLKGANDEMKEKYKLKSLEEYKYIN-PKCLDVPGIDDVKDFEE 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 299 TRRAMDVVGISNEEQEAIFRVVAAILHLGNIDFGKGEE---IDSSVIKDKDSRShLNMAAELLMCNAQSLEDALIRRVMV 375
Cdd:PTZ00014 334 VMESFDSMGLSESQIEDIFSILSGVLLLGNVEIEGKEEgglTDAAAISDESLEV-FNEACELLFLDYESLKKELTVKVTY 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 376 TPEEIITRTLDPDNAIASRDTLAKTIYSHLFDWIVNKINTSIGQDPRSKSIIGVLDIYGFESFKCNSFEQFCINFTNEKL 455
Cdd:PTZ00014 413 AGNQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGFKVFIGMLDIFGFEVFKNNSLEQLFINITNEML 492
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 456 QQHFNQHVFKMEQEEYTKEEIAWSYIEFIDNQDVLELIEKKPGGIISLLDEACMFPKSTHETFSQKLFQTFKEHERFAKP 535
Cdd:PTZ00014 493 QKNFVDIVFERESKLYKDEGISTEELEYTSNESVIDLLCGKGKSVLSILEDQCLAPGGTDEKFVSSCNTNLKNNPKYKPA 572
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 536 KLS-RTDFTISHYAGEVTYQSNHFIDKNKDYIVAEHQALFTASNCKFVAGLFHALHEDSSRSSKFSSIGSRFKQQLHSLM 614
Cdd:PTZ00014 573 KVDsNKNFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLFEGVEVEKGKLAKGQLIGSQFLNQLDSLM 652
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 615 ESLNGTEPHYIRCIKPNNVLKPGIFENFNVIHQLRCGGVLEAIRISCAGYPTRLAFYDFLDRFGLLAPEVLE-GNYDDKV 693
Cdd:PTZ00014 653 SLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKYLDLAVSNdSSLDPKE 732
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 694 ACQMILDKKSLTD--YQIGKTKIFLRAGQMAELdarraevlgnaaRVIQRQfrtcmarkNYRSIRNaaivLQSFLRGEIA 771
Cdd:PTZ00014 733 KAEKLLERSGLPKdsYAIGKTMVFLKKDAAKEL------------TQIQRE--------KLAAWEP----LVSVLEALIL 788
|
730 740
....*....|....*....|....*..
gi 30685403 772 RAVHKKLRIEAA--ALRVQKNFRRYVD 796
Cdd:PTZ00014 789 KIKKKRKVRKNIksLVRIQAHLRRHLV 815
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
73-717 |
7.39e-165 |
|
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: 512.46 E-value: 7.39e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 73 PGVLRNLETRYELNEIYTYTGNILIAVNPFQRLPhIYETDMMEQYKGIALGELSPHVFAIGDAAYRAMINEGKNNSILVS 152
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYP-VYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 153 GESGAGKTETTKMLMRYLAFLGG-----RSGVEGRTVEQQVLESNPVLEAFGNAKTLRNNNSSRFGKFVEIQFDKNGRIS 227
Cdd:cd14909 80 GESGAGKTENTKKVIAYFATVGAskktdEAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 228 GAAIRTYLLERSRVCQISDPERNYHCFYLLCAAPPEDIKKYKL--ENPHKFHYLNQSSCyKLDGVDDASEYLETRRAMDV 305
Cdd:cd14909 160 GADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLlsDNIYDYYIVSQGKV-TVPNVDDGEEFSLTDQAFDI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 306 VGISNEEQEAIFRVVAAILHLGNIDF---GKGEEIDSSVIKDKDSrshlnmAAELLMCNAQSLEDALIRRVMVTPEEIIT 382
Cdd:cd14909 239 LGFTKQEKEDVYRITAAVMHMGGMKFkqrGREEQAEQDGEEEGGR------VSKLFGCDTAELYKNLLKPRIKVGNEFVT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 383 RTLDPDNAIASRDTLAKTIYSHLFDWIVNKINTSIGQDPRSKSIIGVLDIYGFESFKCNSFEQFCINFTNEKLQQHFNQH 462
Cdd:cd14909 313 QGRNVQQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHH 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 463 VFKMEQEEYTKEEIAWSYIEF-IDNQDVLELIEkKPGGIISLLDEACMFPKSTHETFSQKLFQT-FKEHERFAKPKLSR- 539
Cdd:cd14909 393 MFVLEQEEYKREGIDWAFIDFgMDLLACIDLIE-KPMGILSILEEESMFPKATDQTFSEKLTNThLGKSAPFQKPKPPKp 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 540 ----TDFTISHYAGEVTYQSNHFIDKNKDYIVAEHQALFTASNCKFVAGLFhALHEDSSRSSKF------------SSIG 603
Cdd:cd14909 472 gqqaAHFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIF-ADHAGQSGGGEQakggrgkkgggfATVS 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 604 SRFKQQLHSLMESLNGTEPHYIRCIKPNNVLKPGIFENFNVIHQLRCGGVLEAIRISCAGYPTRLAFYDFLDRFGLLAPE 683
Cdd:cd14909 551 SAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNPA 630
|
650 660 670
....*....|....*....|....*....|....*.
gi 30685403 684 VLEGNYDDKVACQMILDKKSLTD--YQIGKTKIFLR 717
Cdd:cd14909 631 GIQGEEDPKKAAEIILESIALDPdqYRLGHTKVFFR 666
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
73-717 |
1.57e-164 |
|
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: 513.35 E-value: 1.57e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 73 PGVLRNLETRYELNEIYTYTGNILIAVNPFQRLPHIYETDmmeQYKGIALG--ELSPHVFAIGDAAYRAM-------INE 143
Cdd:cd14895 1 PAFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIPGLYDLH---KYREEMPGwtALPPHVFSIAEGAYRSLrrrlhepGAS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 144 GKNNSILVSGESGAGKTETTKMLMRYLA-----FLGGRSGVEGRTVE-QQVLESNPVLEAFGNAKTLRNNNSSRFGKFVE 217
Cdd:cd14895 78 KKNQTILVSGESGAGKTETTKFIMNYLAesskhTTATSSSKRRRAISgSELLSANPILESFGNARTLRNDNSSRFGKFVR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 218 IQF-----DKNGRISGAAIRTYLLERSRVCQISDPERNYHCFYLLCAAPPEDIKK---YKLENPHKFHYLNQSSCY-KLD 288
Cdd:cd14895 158 MFFeghelDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLelqLELLSAQEFQYISGGQCYqRND 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 289 GVDDASEYLETRRAMDVVGISNEEQEAIFRVVAAILHLGNIDF-----GKGEE----------IDSSVIKDKDSRSHLNM 353
Cdd:cd14895 238 GVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFvasseDEGEEdngaasapcrLASASPSSLTVQQHLDI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 354 AAELLMCNAQSLEDALIRRVMVTPEEIITRTLDPDNAIASRDTLAKTIYSHLFDWIVNKINTSIGQ----DPRSKSI--- 426
Cdd:cd14895 318 VSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASPQrqfaLNPNKAAnkd 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 427 ----IGVLDIYGFESFKCNSFEQFCINFTNEKLQQHFNQHVFKMEQEEYTKEEIAWSYIEFIDNQDVLELIEKKPGGIIS 502
Cdd:cd14895 398 ttpcIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDNSVCLEMLEQRPSGIFS 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 503 LLDEACMFPKSTHETFSQKLFQTFKEHERFAKpklSRTD-----FTISHYAGEVTYQSNHFIDKNKDYIVAEHQALFTAS 577
Cdd:cd14895 478 LLDEECVVPKGSDAGFARKLYQRLQEHSNFSA---SRTDqadvaFQIHHYAGAVRYQAEGFCEKNKDQPNAELFSVLGKT 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 578 NCKFVAGLFH---ALHEDSSRSSKFSS-----------IGSRFKQQLHSLMESLNGTEPHYIRCIKPNNVLKPGIFENFN 643
Cdd:cd14895 555 SDAHLRELFEffkASESAELSLGQPKLrrrssvlssvgIGSQFKQQLASLLDVVQQTQTHYIRCIKPNDESASDQFDMAK 634
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30685403 644 VIHQLRCGGVLEAIRISCAGYPTRLAFYDFLDRFGLLapeVLEGNYDDKVACQMILDKKSLtDYQIGKTKIFLR 717
Cdd:cd14895 635 VSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLL---VAAKNASDATASALIETLKVD-HAELGKTRVFLR 704
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
73-717 |
1.97e-164 |
|
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: 511.44 E-value: 1.97e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 73 PGVLRNLETRYELNEIYTYTGNILIAVNPFQRLPhIYETDMMEQYKGIALGELSPHVFAIGDAAYRAMINEGKNNSILVS 152
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLP-VYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 153 GESGAGKTETTKMLMRYLAFLG--GRSGVEGRTVEQQVLESNPVLEAFGNAKTLRNNNSSRFGKFVEIQFDKNGRISGAA 230
Cdd:cd14929 80 GESGAGKTVNTKHIIQYFATIAamIESKKKLGALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSAD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 231 IRTYLLERSRVCQISDPERNYHCFYLLCAAPPEdIKKYKL--ENPHKFHYlnqSSC--YKLDGVDDASEYLETRRAMDVV 306
Cdd:cd14929 160 IDIYLLEKSRVIFQQPGERNYHIFYQILSGKKE-LRDLLLvsANPSDFHF---CSCgaVAVESLDDAEELLATEQAMDIL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 307 GISNEEQEAIFRVVAAILHLGNIDFGKG---EEIDSsvikdkDSRSHLNMAAELLMCNAQSLEDALIRRVMVTPEEIITR 383
Cdd:cd14929 236 GFLPDEKYGCYKLTGAIMHFGNMKFKQKpreEQLEA------DGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 384 TLDPDNAIASRDTLAKTIYSHLFDWIVNKINTSIGQDPRSKSIIGVLDIYGFESFKCNSFEQFCINFTNEKLQQHFNQHV 463
Cdd:cd14929 310 SQNIEQVTYAVGALSKSIYERMFKWLVARINRVLDAKLSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHM 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 464 FKMEQEEYTKEEIAWSYIEF-IDNQDVLELIEkKPGGIISLLDEACMFPKSTHETFSQKLFQT-FKEHERFAKPKLSR-- 539
Cdd:cd14929 390 FVLEQEEYRKEGIDWVSIDFgLDLQACIDLIE-KPMGIFSILEEECMFPKATDLTFKTKLFDNhFGKSVHFQKPKPDKkk 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 540 --TDFTISHYAGEVTYQSNHFIDKNKDYIVAEHQALFTASNCKFVAGLFH-------ALH---EDSSRSSKFSSIGSRFK 607
Cdd:cd14929 469 feAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFEnyistdsAIQfgeKKRKKGASFQTVASLHK 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 608 QQLHSLMESLNGTEPHYIRCIKPNNVLKPGIFENFNVIHQLRCGGVLEAIRISCAGYPTRLAFYDFLDRFGLLAPEVLEG 687
Cdd:cd14929 549 ENLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNPRTFPK 628
|
650 660 670
....*....|....*....|....*....|....
gi 30685403 688 N--YDDKVACQMILDKKSL--TDYQIGKTKIFLR 717
Cdd:cd14929 629 SkfVSSRKAAEELLGSLEIdhTQYRFGITKVFFK 662
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
75-717 |
6.48e-164 |
|
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: 510.32 E-value: 6.48e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 75 VLRNLETRYELNEIYTYTGNILIAVNPFQRLPhIYETDMMEQYKGIALGELSPHVFAIGDAAYRAMINEGKNNSILVSGE 154
Cdd:cd14920 3 VLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 155 SGAGKTETTKMLMRYLAFL-----GGRSGVEGRTVEQQVLESNPVLEAFGNAKTLRNNNSSRFGKFVEIQFDKNGRISGA 229
Cdd:cd14920 82 SGAGKTENTKKVIQYLAHVasshkGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 230 AIRTYLLERSRVCQISDPERNYHCFY-LLCAAPPEDIKKYKLENPHKFHYLNQSSCyKLDGVDDASEYLETRRAMDVVGI 308
Cdd:cd14920 162 NIETYLLEKSRAVRQAKDERTFHIFYqLLSGAGEHLKSDLLLEGFNNYRFLSNGYI-PIPGQQDKDNFQETMEAMHIMGF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 309 SNEEQEAIFRVVAAILHLGNIDFGKGEEIDSSVIKDkdsrshlNMAAELLmCNAQSLEDALIRRVMVTP-----EEIITR 383
Cdd:cd14920 241 SHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPE-------NTVAQKL-CHLLGMNVMEFTRAILTPrikvgRDYVQK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 384 TLDPDNAIASRDTLAKTIYSHLFDWIVNKINTSIGQDPRS-KSIIGVLDIYGFESFKCNSFEQFCINFTNEKLQQHFNQH 462
Cdd:cd14920 313 AQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQgASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHT 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 463 VFKMEQEEYTKEEIAWSYIEF-IDNQDVLELIEK--KPGGIISLLDEACMFPKSTHETFSQKLFQTFKEHERFAKPKLSR 539
Cdd:cd14920 393 MFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLK 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 540 --TDFTISHYAGEVTYQSNHFIDKNKDYIVAEHQALFTASNCKFVAGLFH------ALHEDSSRSSKF------------ 599
Cdd:cd14920 473 dkADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKdvdrivGLDQVTGMTETAfgsayktkkgmf 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 600 SSIGSRFKQQLHSLMESLNGTEPHYIRCIKPNNVLKPGIFENFNVIHQLRCGGVLEAIRISCAGYPTRLAFYDFLDRFGL 679
Cdd:cd14920 553 RTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 632
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 30685403 680 LAPEVL-EGNYDDKVACQMILDKKSLTD--YQIGKTKIFLR 717
Cdd:cd14920 633 LTPNAIpKGFMDGKQACERMIRALELDPnlYRIGQSKIFFR 673
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
73-717 |
1.92e-163 |
|
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: 508.82 E-value: 1.92e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 73 PGVLRNLETRYELNEIYTYTGNILIAVNPFQRLPhIYETDMMEQYKGIALGELSPHVFAIGDAAYRAMINEGKNNSILVS 152
Cdd:cd14913 1 PAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLP-VYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 153 GESGAGKTETTKMLMRYLAFLGGRSGVEGR-------TVEQQVLESNPVLEAFGNAKTLRNNNSSRFGKFVEIQFDKNGR 225
Cdd:cd14913 80 GESGAGKTVNTKRVIQYFATIAATGDLAKKkdskmkgTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 226 ISGAAIRTYLLERSRVCQISDPERNYHCFY-LLCAAPPEDIKKYKLE-NPHKFHYLNQSSCyKLDGVDDASEYLETRRAM 303
Cdd:cd14913 160 LASADIETYLLEKSRVTFQLKAERSYHIFYqILSNKKPELIELLLITtNPYDYPFISQGEI-LVASIDDAEELLATDSAI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 304 DVVGISNEEQEAIFRVVAAILHLGNIDFGKGE-----EIDSSVIKDKdsrshlnmAAELLMCNAQSLEDALIRRVMVTPE 378
Cdd:cd14913 239 DILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQreeqaEPDGTEVADK--------TAYLMGLNSSDLLKALCFPRVKVGN 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 379 EIITRTLDPDNAIASRDTLAKTIYSHLFDWIVNKINTSIGQDPRSKSIIGVLDIYGFESFKCNSFEQFCINFTNEKLQQH 458
Cdd:cd14913 311 EYVTKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQF 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 459 FNQHVFKMEQEEYTKEEIAWSYIEF-IDNQDVLELIEkKPGGIISLLDEACMFPKSTHETFSQKLF-QTFKEHERFAKPK 536
Cdd:cd14913 391 FNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYdQHLGKSNNFQKPK 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 537 LSR----TDFTISHYAGEVTYQSNHFIDKNKDYIVAEHQALFTASNCKFVAGL---FHALHEDSSRSSKFSSIGSRF--- 606
Cdd:cd14913 470 VVKgraeAHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLyatFATADADSGKKKVAKKKGSSFqtv 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 607 ----KQQLHSLMESLNGTEPHYIRCIKPNNVLKPGIFENFNVIHQLRCGGVLEAIRISCAGYPTRLAFYDFLDRFGLLAP 682
Cdd:cd14913 550 salfRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNA 629
|
650 660 670
....*....|....*....|....*....|....*....
gi 30685403 683 E-VLEGNY-DDKVACQMILDKKSL--TDYQIGKTKIFLR 717
Cdd:cd14913 630 SaIPEGQFiDSKKACEKLLASIDIdhTQYKFGHTKVFFK 668
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
75-717 |
2.00e-163 |
|
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: 509.11 E-value: 2.00e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 75 VLRNLETRYELNEIYTYTGNILIAVNPFQRLPhIYETDMMEQYKGIALGELSPHVFAIGDAAYRAMINEGKNNSILVSGE 154
Cdd:cd14927 3 VLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLP-VYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 155 SGAGKTETTKMLMRYLAF---LGGRSGVE--------GRTVEQQVLESNPVLEAFGNAKTLRNNNSSRFGKFVEIQFDKN 223
Cdd:cd14927 82 SGAGKTVNTKRVIQYFAIvaaLGDGPGKKaqflatktGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 224 GRISGAAIRTYLLERSRVCQISDPERNYHCFYLLCAAPPEDIKKYKL--ENPHKFHYLNQSSCyKLDGVDDASEYLETRR 301
Cdd:cd14927 162 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLvsMNPYDYHFCSQGVT-TVDNMDDGEELMATDH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 302 AMDVVGISNEEQEAIFRVVAAILHLGNIDFGKGEEIDSSvikDKDSRSHLNMAAELLMCNAQSLEDALIRRVMVTPEEII 381
Cdd:cd14927 241 AMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQA---EADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 382 TRTLDPDNAIASRDTLAKTIYSHLFDWIVNKINTSIGQDPRSKSIIGVLDIYGFESFKCNSFEQFCINFTNEKLQQHFNQ 461
Cdd:cd14927 318 TKGQSVEQVVYAVGALAKATYDRMFKWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNH 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 462 HVFKMEQEEYTKEEIAWSYIEF-IDNQDVLELIEkKPGGIISLLDEACMFPKSTHETFSQKLFQT-FKEHERFAKPKLSR 539
Cdd:cd14927 398 HMFILEQEEYKREGIEWVFIDFgLDLQACIDLIE-KPLGILSILEEECMFPKASDASFKAKLYDNhLGKSPNFQKPRPDK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 540 -----TDFTISHYAGEVTYQSNHFIDKNKDYIVAEHQALFTASNCKFVAGLFH-------------ALHEDSSRSSKFSS 601
Cdd:cd14927 477 krkyeAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYEnyvgsdstedpksGVKEKRKKAASFQT 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 602 IGSRFKQQLHSLMESLNGTEPHYIRCIKPNNVLKPGIFENFNVIHQLRCGGVLEAIRISCAGYPTRLAFYDFLDRFGLLA 681
Cdd:cd14927 557 VSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYRILN 636
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 30685403 682 PEVL-EGNY-DDKVACQMILDKKSL--TDYQIGKTKIFLR 717
Cdd:cd14927 637 PSAIpDDKFvDSRKATEKLLGSLDIdhTQYQFGHTKVFFK 676
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
75-717 |
5.68e-160 |
|
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: 499.55 E-value: 5.68e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 75 VLRNLETRYELNEIYTYTGNILIAVNPFQRLPhIYETDMMEQYKGIALGELSPHVFAIGDAAYRAMINEGKNNSILVSGE 154
Cdd:cd14934 3 VLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLP-IYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 155 SGAGKTETTKMLMRYLAFLG--GRSGVEGR-TVEQQVLESNPVLEAFGNAKTLRNNNSSRFGKFVEIQFDKNGRISGAAI 231
Cdd:cd14934 82 SGAGKTENTKKVIQYFANIGgtGKQSSDGKgSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKLAGADI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 232 RTYLLERSRVCQISDPERNYHCFY-LLCAAPPEDIKKYKL-ENPHKFHYLNQSsCYKLDGVDDASEYLETRRAMDVVGIS 309
Cdd:cd14934 162 ESYLLEKSRVISQQAAERGYHIFYqILSNKKPELIESLLLvPNPKEYHWVSQG-VTVVDNMDDGEELQITDVAFDVLGFS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 310 NEEQEAIFRVVAAILHLGNIDFGKG-----EEIDSSVIKDKdsrshlnmAAELLMCNAQSLEDALIRRVMVTPEEIITRT 384
Cdd:cd14934 241 AEEKIGVYKLTGGIMHFGNMKFKQKpreeqAEVDTTEVADK--------VAHLMGLNSGELQKGITRPRVKVGNEFVQKG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 385 LDPDNAIASRDTLAKTIYSHLFDWIVNKINTSIGQDPRSKSIIGVLDIYGFESFKCNSFEQFCINFTNEKLQQHFNQHVF 464
Cdd:cd14934 313 QNMEQCNNSIGALGKAVYDKMFKWLVVRINKTLDTKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMF 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 465 KMEQEEYTKEEIAWSYIEF-IDNQDVLELIEkKPGGIISLLDEACMFPKSTHETFSQKLFQT-FKEHERFAKPKLSR--- 539
Cdd:cd14934 393 VLEQEEYKREGIEWVFIDFgLDLQACIDLLE-KPMGIFSILEEQCVFPKATDATFKAALYDNhLGKSSNFLKPKGGKgkg 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 540 --TDFTISHYAGEVTYQSNHFIDKNKDYIVAEHQALFTASNCKFVAGLFHalHEDSSRSSKFSSIGSRF-------KQQL 610
Cdd:cd14934 472 peAHFELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSSLGLLALLFK--EEEAPAGSKKQKRGSSFmtvsnfyREQL 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 611 HSLMESLNGTEPHYIRCIKPNNVLKPGIFENFNVIHQLRCGGVLEAIRISCAGYPTRLAFYDFLDRFGLLAPEVL-EGNY 689
Cdd:cd14934 550 NKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLNPNVIpQGFV 629
|
650 660 670
....*....|....*....|....*....|
gi 30685403 690 DDKVACQMILDKKSL--TDYQIGKTKIFLR 717
Cdd:cd14934 630 DNKKASELLLGSIDLdvNEYKIGHTKVFFR 659
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
73-717 |
8.61e-159 |
|
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: 496.05 E-value: 8.61e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 73 PGVLRNLETRYELNEIYTYTGNILIAVNPFQRLPHiyETD-MMEQYKGIA-LGELSPHVFAIGDAAYRAMINEGKNNSIL 150
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGN--ATDeWIRKYRDAPdLTKLPPHVFYTARRALENLHGVNKSQTII 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 151 VSGESGAGKTETTKMLMRYLAflGGRSGVEGRTVEQQVLESNPVLEAFGNAKTLRNNNSSRFGKFVEIQFDKNGRISGAA 230
Cdd:cd14876 79 VSGESGAGKTEATKQIMRYFA--SAKSGNMDLRIQTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVASEGGIRYGS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 231 IRTYLLERSRVCQISDPERNYHCFY-LLCAAPPEDIKKYKLENPHKFHYLNqSSCYKLDGVDDASEYLETRRAMDVVGIS 309
Cdd:cd14876 157 VVAFLLEKSRIVTQDDNERSYHIFYqLLKGADSEMKSKYHLLGLKEYKFLN-PKCLDVPGIDDVADFEEVLESLKSMGLT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 310 NEEQEAIFRVVAAILHLGNIDFGKGEE--IDSSVIKDKDSRSHLNMAAELLMCNAQSLEDALIRRV-MVTPEEIITRTLD 386
Cdd:cd14876 236 EEQIDTVFSIVSGVLLLGNVKITGKTEqgVDDAAAISNESLEVFKEACSLLFLDPEALKRELTVKVtKAGGQEIEGRWTK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 387 PDNAIaSRDTLAKTIYSHLFDWIVNKINTSIGQDPRSKSIIGVLDIYGFESFKCNSFEQFCINFTNEKLQQHFNQHVFKM 466
Cdd:cd14876 316 DDAEM-LKLSLAKAMYDKLFLWIIRNLNSTIEPPGGFKNFMGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFIDIVFER 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 467 EQEEYTKEEIAWSYIEFIDNQDVLELIEKKPGGIISLLDEACMFPKSTHETFSQKLFQTFKEHERFAKPKL-SRTDFTIS 545
Cdd:cd14876 395 ESKLYKDEGIPTAELEYTSNAEVIDVLCGKGKSVLSILEDQCLAPGGSDEKFVSACVSKLKSNGKFKPAKVdSNINFIVV 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 546 HYAGEVTYQSNHFIDKNKDYIVAEHQALFTASNCKFVAGLFHALHEDSSRSSKFSSIGSRFKQQLHSLMESLNGTEPHYI 625
Cdd:cd14876 475 HTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEGVVVEKGKIAKGSLIGSQFLKQLESLMGLINSTEPHFI 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 626 RCIKPNNVLKPGIFENFNVIHQLRCGGVLEAIRISCAGYPTRLAFYDFLDRFGLLAPEVLEGNYDD-KVACQMILDKKSL 704
Cdd:cd14876 555 RCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEFLYQFKFLDLGIANDKSLDpKVAALKLLESSGL 634
|
650
....*....|....*
gi 30685403 705 T--DYQIGKTKIFLR 717
Cdd:cd14876 635 SedEYAIGKTMVFLK 649
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
75-717 |
2.84e-158 |
|
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: 495.70 E-value: 2.84e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 75 VLRNLETRYELNEIYTYTGNILIAVNPFQRLPhIYETDMMEQYKGIALGELSPHVFAIGDAAYRAMINEGKNNSILVSGE 154
Cdd:cd14932 3 VLHNLKERYYSGLIYTYSGLFCVVINPYKYLP-IYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 155 SGAGKTETTKMLMRYLAFLG---------GRSGVEGRTVEQQVLESNPVLEAFGNAKTLRNNNSSRFGKFVEIQFDKNGR 225
Cdd:cd14932 82 SGAGKTENTKKVIQYLAYVAssfktkkdqSSIALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 226 ISGAAIRTYLLERSRVCQISDPERNYHCFYLLCAAPPEDIK-KYKLENPHKFHYLNQSSCyKLDGVDDASEYLETRRAMD 304
Cdd:cd14932 162 IVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRsELCLEDYSKYRFLSNGNV-TIPGQQDKELFAETMEAFR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 305 VVGISNEEQEAIFRVVAAILHLGNIDFGKGEEIDSSVIKDKDSRSHLnmaAELLMCNAQSLEDALIRRVMVTPEEIITRT 384
Cdd:cd14932 241 IMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKV---CHLLGMNVTDFTRAILSPRIKVGRDYVQKA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 385 LDPDNAIASRDTLAKTIYSHLFDWIVNKINTSIGQDPRS-KSIIGVLDIYGFESFKCNSFEQFCINFTNEKLQQHFNQHV 463
Cdd:cd14932 318 QTQEQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQgASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTM 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 464 FKMEQEEYTKEEIAWSYIEF-IDNQDVLELIEKK--PGGIISLLDEACMFPKSTHETFSQKLFQTFKEHERFAKPKLSR- 539
Cdd:cd14932 398 FILEQEEYQREGIEWSFIDFgLDLQPCIELIEKPngPPGILALLDEECWFPKATDKSFVEKVVQEQGNNPKFQKPKKLKd 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 540 -TDFTISHYAGEVTYQSNHFIDKNKDYIVAEHQALFTASNCKF----------------VAGLFHALHEDSSRSS-KFSS 601
Cdd:cd14932 478 dADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFvselwkdvdrivgldkVAGMGESLHGAFKTRKgMFRT 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 602 IGSRFKQQLHSLMESLNGTEPHYIRCIKPNNVLKPGIFENFNVIHQLRCGGVLEAIRISCAGYPTRLAFYDFLDRFGLLA 681
Cdd:cd14932 558 VGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILT 637
|
650 660 670
....*....|....*....|....*....|....*....
gi 30685403 682 PEVL-EGNYDDKVACQMILDKKSLTD--YQIGKTKIFLR 717
Cdd:cd14932 638 PNAIpKGFMDGKQACVLMVKALELDPnlYRIGQSKVFFR 676
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
75-716 |
3.10e-154 |
|
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: 486.02 E-value: 3.10e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 75 VLRNLETRYELNEIYTYTGNILIAVNPFQRLPHIYETDMMEQYKGI-ALGELSPHVFAIGDAAYRAMINEGKNNSILVSG 153
Cdd:cd14906 3 ILNNLGKRYKSDSIYTYIGNVLISINPYKDISSIYSNLILNEYKDInQNKSPIPHIYAVALRAYQSMVSEKKNQSIIISG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 154 ESGAGKTETTKMLMRYLAFLGGRSGVEGR-------TVEQQVLESNPVLEAFGNAKTLRNNNSSRFGKFVEIQFDK-NGR 225
Cdd:cd14906 83 ESGSGKTEASKTILQYLINTSSSNQQQNNnnnnnnnSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFRSsDGK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 226 ISGAAIRTYLLERSRVCQISDPER-NYHCFY-LLCAAPPEDIKKYKLEN-PHKFHYLNQS----SCYK---------LDG 289
Cdd:cd14906 163 IDGASIETYLLEKSRISHRPDNINlSYHIFYyLVYGASKDERSKWGLNNdPSKYRYLDARddviSSFKsqssnknsnHNN 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 290 VDDASEYLE-TRRAMDVVGISNEEQEAIFRVVAAILHLGNIDFGKGEEIDSSVIKDKDSRSHLNMAAELLMCNAQSLEDA 368
Cdd:cd14906 243 KTESIESFQlLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSDFSKYAYQKDKVTASLESVSKLLGYIESVFKQA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 369 LIRRVMVTPEE--IITRTLDPDNAIASRDTLAKTIYSHLFDWIVNKINTSIGQDPRSKSI-----------IGVLDIYGF 435
Cdd:cd14906 323 LLNRNLKAGGRgsVYCRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRKFNQNTQSNDLaggsnkknnlfIGVLDIFGF 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 436 ESFKCNSFEQFCINFTNEKLQQHFNQHVFKMEQEEYTKEEIAWSYIEFIDNQDVLELIEKKPGGIISLLDEACMFPKSTH 515
Cdd:cd14906 403 ENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNFIDNKECIELIEKKSDGILSLLDDECIMPKGSE 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 516 ETFSQKLFQTFKEHERFAKPKLSRTDFTISHYAGEVTYQSNHFIDKNKDYIVAEHQALFTASNCKFVAGLFH----ALHE 591
Cdd:cd14906 483 QSLLEKYNKQYHNTNQYYQRTLAKGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFLKKSLFQqqitSTTN 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 592 DSSRSSKFSSIGSRFKQQLHSLMESLNGTEPHYIRCIKPNNVLKPGIFENFNVIHQLRCGGVLEAIRISCAGYPTRLAFY 671
Cdd:cd14906 563 TTKKQTQSNTVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLSQLRNVGVLNTIKVRKMGYSYRRDFN 642
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30685403 672 DFLDRFGLLApEVLEGNYDDKVACQMILDKKSLTD----------------------------YQIGKTKIFL 716
Cdd:cd14906 643 QFFSRYKCIV-DMYNRKNNNNPKLASQLILQNIQSklktmgisnnkkknnsnsnsnttndkplFQIGKTKIFI 714
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
75-717 |
5.23e-152 |
|
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: 478.82 E-value: 5.23e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 75 VLRNLETRYELNEIYTYTGNILIAVNPFQRLPhIYETDMMEQYKGIALGELSPHVFAIGDAAYRAMINEGKNNSILVSGE 154
Cdd:cd14919 3 VLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 155 SGAGKTETTKMLMRYLAFLGG--RSGVEGRTVEQQVLESNPVLEAFGNAKTLRNNNSSRFGKFVEIQFDKNGRISGAAIR 232
Cdd:cd14919 82 SGAGKTENTKKVIQYLAHVASshKSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 233 TYLLERSRVCQISDPERNYHCFYLLCAAPPEDIKKYKLENPH-KFHYLNQSSCyKLDGVDDASEYLETRRAMDVVGISNE 311
Cdd:cd14919 162 TYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYnKYRFLSNGHV-TIPGQQDKDMFQETMEAMRIMGIPEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 312 EQEAIFRVVAAILHLGNIDFGKGEEIDSSVIKDKDSRSHLnmaAELLMCNAQSLEDALIRRVMVTPEEIITRTLDPDNAI 391
Cdd:cd14919 241 EQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKV---SHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQAD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 392 ASRDTLAKTIYSHLFDWIVNKINTSIGQDPRS-KSIIGVLDIYGFESFKCNSFEQFCINFTNEKLQQHFNQHVFKMEQEE 470
Cdd:cd14919 318 FAIEALAKATYERMFRWLVLRINKALDKTKRQgASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 471 YTKEEIAWSYIEF-IDNQDVLELIEKK--PGGIISLLDEACMFPKSTHETFSQKLFQTFKEHERFAKPKL--SRTDFTIS 545
Cdd:cd14919 398 YQREGIEWNFIDFgLDLQPCIDLIEKPagPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKQlkDKADFCII 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 546 HYAGEVTYQSNHFIDKNKDYIVAEHQALFTASNCKFVAGLFH------------ALHEDS------SRSSKFSSIGSRFK 607
Cdd:cd14919 478 HYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKdvdriigldqvaGMSETAlpgafkTRKGMFRTVGQLYK 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 608 QQLHSLMESLNGTEPHYIRCIKPNNVLKPGIFENFNVIHQLRCGGVLEAIRISCAGYPTRLAFYDFLDRFGLLAPEVL-E 686
Cdd:cd14919 558 EQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIpK 637
|
650 660 670
....*....|....*....|....*....|...
gi 30685403 687 GNYDDKVACQMILDKKSLTD--YQIGKTKIFLR 717
Cdd:cd14919 638 GFMDGKQACVLMIKALELDSnlYRIGQSKVFFR 670
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
75-717 |
5.40e-152 |
|
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: 478.74 E-value: 5.40e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 75 VLRNLETRYELNEIYTYTGNILIAVNPFQRLPhIYETDMMEQYKGIALGELSPHVFAIGDAAYRAMINEGKNNSILVSGE 154
Cdd:cd14921 3 VLHNLRERYFSGLIYTYSGLFCVVVNPYKHLP-IYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 155 SGAGKTETTKMLMRYLAFLGGR------SGVEGRtVEQQVLESNPVLEAFGNAKTLRNNNSSRFGKFVEIQFDKNGRISG 228
Cdd:cd14921 82 SGAGKTENTKKVIQYLAVVASShkgkkdTSITGE-LEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 229 AAIRTYLLERSRVCQISDPERNYHCFYLLCAAPPEDIKK-YKLENPHKFHYLNQSSCyKLDGVDDASEYLETRRAMDVVG 307
Cdd:cd14921 161 ANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSdLLLEGFNNYTFLSNGFV-PIPAAQDDEMFQETLEAMSIMG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 308 ISNEEQEAIFRVVAAILHLGNIDFGKGEEIDSSVIKDkdsrshlNMAAELLmCNAQSLEDALIRRVMVTP-----EEIIT 382
Cdd:cd14921 240 FSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPD-------NTAAQKV-CHLMGINVTDFTRSILTPrikvgRDVVQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 383 RTLDPDNAIASRDTLAKTIYSHLFDWIVNKINTSIGQDPRS-KSIIGVLDIYGFESFKCNSFEQFCINFTNEKLQQHFNQ 461
Cdd:cd14921 312 KAQTKEQADFAIEALAKATYERLFRWILTRVNKALDKTHRQgASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNH 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 462 HVFKMEQEEYTKEEIAWSYIEF-IDNQDVLELIEK--KPGGIISLLDEACMFPKSTHETFSQKLFQTFKEHERFAKPKL- 537
Cdd:cd14921 392 TMFILEQEEYQREGIEWNFIDFgLDLQPCIELIERpnNPPGVLALLDEECWFPKATDKSFVEKLCTEQGNHPKFQKPKQl 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 538 -SRTDFTISHYAGEVTYQSNHFIDKNKDYIVAEHQALFTASNCKFVAGLFHALHE------------------DSSRSSK 598
Cdd:cd14921 472 kDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRivgldqmakmtesslpsaSKTKKGM 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 599 FSSIGSRFKQQLHSLMESLNGTEPHYIRCIKPNNVLKPGIFENFNVIHQLRCGGVLEAIRISCAGYPTRLAFYDFLDRFG 678
Cdd:cd14921 552 FRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 631
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 30685403 679 LLAPEVL-EGNYDDKVACQMILDKKSLTD--YQIGKTKIFLR 717
Cdd:cd14921 632 ILAANAIpKGFMDGKQACILMIKALELDPnlYRIGQSKIFFR 673
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
73-717 |
9.32e-150 |
|
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: 472.68 E-value: 9.32e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 73 PGVLRNLETRYELNEIYTYTGNILIAVNPFQRLPhIYETDMMEQYKGIALGELSPHVFAIGDAAYRAMINEGKNNSILVS 152
Cdd:cd14918 1 PGVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 153 GESGAGKTETTKMLMRYLAFLG-------GRSGVEGRTVEQQVLESNPVLEAFGNAKTLRNNNSSRFGKFVEIQFDKNGR 225
Cdd:cd14918 80 GESGAGKTVNTKRVIQYFATIAvtgekkkEESGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 226 ISGAAIRTYLLERSRVCQISDPERNYHCFYLLCAAPPEDIKKYKL--ENPHKFHYLNQSSCyKLDGVDDASEYLETRRAM 303
Cdd:cd14918 160 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLitTNPYDYAFVSQGEI-TVPSIDDQEELMATDSAI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 304 DVVGISNEEQEAIFRVVAAILHLGNIDFGKGE-----EIDSSVIKDKdsrshlnmAAELLMCNAQSLEDALIRRVMVTPE 378
Cdd:cd14918 239 DILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQreeqaEPDGTEVADK--------AAYLQSLNSADLLKALCYPRVKVGN 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 379 EIITRTLDPDNAIASRDTLAKTIYSHLFDWIVNKINTSIGQDPRSKSIIGVLDIYGFESFKCNSFEQFCINFTNEKLQQH 458
Cdd:cd14918 311 EYVTKGQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQF 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 459 FNQHVFKMEQEEYTKEEIAWSYIEF-IDNQDVLELIEkKPGGIISLLDEACMFPKSTHETFSQKLF-QTFKEHERFAKPK 536
Cdd:cd14918 391 FNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIE-KPLGIFSILEEECMFPKATDTSFKNKLYdQHLGKSANFQKPK 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 537 L----SRTDFTISHYAGEVTYQSNHFIDKNKDYIVAEHQALFTASNCKFVAGLFH---ALHEDSSRSSKFSSIGSR---- 605
Cdd:cd14918 470 VvkgkAEAHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFStyaSAEADSGAKKGAKKKGSSfqtv 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 606 ---FKQQLHSLMESLNGTEPHYIRCIKPNNVLKPGIFENFNVIHQLRCGGVLEAIRISCAGYPTRLAFYDFLDRFGLL-A 681
Cdd:cd14918 550 salFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLnA 629
|
650 660 670
....*....|....*....|....*....|....*....
gi 30685403 682 PEVLEGNY-DDKVACQMILDKKSL--TDYQIGKTKIFLR 717
Cdd:cd14918 630 SAIPEGQFiDSKKASEKLLASIDIdhTQYKFGHTKVFFK 668
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
73-717 |
1.43e-149 |
|
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: 471.89 E-value: 1.43e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 73 PGVLRNLETRYELNEIYTYTGNILIAVNPFQRLPhIYETDMMEQYKGIALGELSPHVFAIGDAAYRAMINEGKNNSILVS 152
Cdd:cd14917 1 PAVLYNLKERYASWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 153 GESGAGKTETTKMLMRYLAFL---GGRSGVE---GR-TVEQQVLESNPVLEAFGNAKTLRNNNSSRFGKFVEIQFDKNGR 225
Cdd:cd14917 80 GESGAGKTVNTKRVIQYFAVIaaiGDRSKKDqtpGKgTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 226 ISGAAIRTYLLERSRVCQISDPERNYHCFY-LLCAAPPEDIKKYKL-ENPHKFHYLNQSSCyKLDGVDDASEYLETRRAM 303
Cdd:cd14917 160 LASADIETYLLEKSRVIFQLKAERDYHIFYqILSNKKPELLDMLLItNNPYDYAFISQGET-TVASIDDAEELMATDNAF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 304 DVVGISNEEQEAIFRVVAAILHLGNIDFGKGEEIDSSvikDKDSRSHLNMAAELLMCNAQSLEDALIRRVMVTPEEIITR 383
Cdd:cd14917 239 DVLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQA---EPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 384 TLDPDNAIASRDTLAKTIYSHLFDWIVNKINTSIGQDPRSKSIIGVLDIYGFESFKCNSFEQFCINFTNEKLQQHFNQHV 463
Cdd:cd14917 316 GQNVQQVIYATGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHM 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 464 FKMEQEEYTKEEIAWSYIEF-IDNQDVLELIEkKPGGIISLLDEACMFPKSTHETFSQKLFQT-FKEHERFAKPK----L 537
Cdd:cd14917 396 FVLEQEEYKKEGIEWTFIDFgMDLQACIDLIE-KPMGIMSILEEECMFPKATDMTFKAKLFDNhLGKSNNFQKPRnikgK 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 538 SRTDFTISHYAGEVTYQSNHFIDKNKDYIVAEHQALFTASNCKFVAGLF---HALHEDSSRSSKFSSIGSRF-------K 607
Cdd:cd14917 475 PEAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFanyAGADAPIEKGKGKAKKGSSFqtvsalhR 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 608 QQLHSLMESLNGTEPHYIRCIKPNNVLKPGIFENFNVIHQLRCGGVLEAIRISCAGYPTRLAFYDFLDRFGLLAPEVL-E 686
Cdd:cd14917 555 ENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIpE 634
|
650 660 670
....*....|....*....|....*....|....
gi 30685403 687 GNY-DDKVACQMILDKKSL--TDYQIGKTKIFLR 717
Cdd:cd14917 635 GQFiDSRKGAEKLLSSLDIdhNQYKFGHTKVFFK 668
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
73-717 |
1.54e-148 |
|
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: 469.21 E-value: 1.54e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 73 PGVLRNLETRYELNEIYTYTGNILIAVNPFQRLPhIYETDMMEQYKGIALGELSPHVFAIGDAAYRAMINEGKNNSILVS 152
Cdd:cd14915 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 153 GESGAGKTETTKMLMRYLAFLG---------GRSGVEGRTVEQQVLESNPVLEAFGNAKTLRNNNSSRFGKFVEIQFDKN 223
Cdd:cd14915 80 GESGAGKTVNTKRVIQYFATIAvtgekkkeeAASGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGAT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 224 GRISGAAIRTYLLERSRVCQISDPERNYHCFY-LLCAAPPEDIKKYKLE-NPHKFHYLNQSSCyKLDGVDDASEYLETRR 301
Cdd:cd14915 160 GKLASADIETYLLEKSRVTFQLKAERSYHIFYqIMSNKKPELIEMLLITtNPYDFAFVSQGEI-TVPSIDDQEELMATDS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 302 AMDVVGISNEEQEAIFRVVAAILHLGNIDFGKGE-----EIDSSVIKDKdsrshlnmAAELLMCNAQSLEDALIRRVMVT 376
Cdd:cd14915 239 AVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQreeqaEPDGTEVADK--------AAYLTSLNSADLLKALCYPRVKV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 377 PEEIITRTLDPDNAIASRDTLAKTIYSHLFDWIVNKINTSIGQDPRSKSIIGVLDIYGFESFKCNSFEQFCINFTNEKLQ 456
Cdd:cd14915 311 GNEYVTKGQTVQQVYNSVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQ 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 457 QHFNQHVFKMEQEEYTKEEIAWSYIEF-IDNQDVLELIEkKPGGIISLLDEACMFPKSTHETFSQKLF-QTFKEHERFAK 534
Cdd:cd14915 391 QFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYeQHLGKSNNFQK 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 535 PKLSR----TDFTISHYAGEVTYQSNHFIDKNKDYIVAEHQALFTASNCKFVAGLFHALHE-----------DSSRSSKF 599
Cdd:cd14915 470 PKPAKgkaeAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFSGGQTaeaeggggkkgGKKKGSSF 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 600 SSIGSRFKQQLHSLMESLNGTEPHYIRCIKPNNVLKPGIFENFNVIHQLRCGGVLEAIRISCAGYPTRLAFYDFLDRFGL 679
Cdd:cd14915 550 QTVSALFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKV 629
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 30685403 680 L-APEVLEGNY-DDKVACQMILDKKSL--TDYQIGKTKIFLR 717
Cdd:cd14915 630 LnASAIPEGQFiDSKKASEKLLGSIDIdhTQYKFGHTKVFFK 671
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
75-716 |
7.28e-148 |
|
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: 467.02 E-value: 7.28e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 75 VLRNLETRYELNEIYTYTGNILIAVNPFQRLPHIYETDMMEQYKGIALGE-LSPHVFAIGDAAYRAMIN--EGKNNSILV 151
Cdd:cd14880 3 VLRCLQARYTADTFYTNAGCTLVALNPFKPVPQLYSPELMREYHAAPQPQkLKPHIFTVGEQTYRNVKSliEPVNQSIVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 152 SGESGAGKTETTKMLMRYLAFLGG-RSGVEGRT----VEQQVLESNPVLEAFGNAKTLRNNNSSRFGKFVEIQFDKNGRI 226
Cdd:cd14880 83 SGESGAGKTWTSRCLMKFYAVVAAsPTSWESHKiaerIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQLNRAQQM 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 227 SGAAIRTYLLERSRV-CQISDpERNYHCFYLLC-AAPPEDIKKYKLENPHKFHYLNQSScYKLDgvDDASEYleTRRAMD 304
Cdd:cd14880 163 TGAAVQTYLLEKTRVaCQAPS-ERNFHIFYQICkGASADERLQWHLPEGAAFSWLPNPE-RNLE--EDCFEV--TREAML 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 305 VVGISNEEQEAIFRVVAAILHLGNIDFGKGEEIDSSVIKDKDSRSHLNMAAELLMCNAQSLEDAL-IRRVMVTPEEIITR 383
Cdd:cd14880 237 HLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPCQPMDDTKESVRTSALLLKLPEDHLLETLqIRTIRAGKQQQVFK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 384 TLDPDNAIASR-DTLAKTIYSHLFDWIVNKINTSIGQDPRS-KSIIGVLDIYGFESFKCNSFEQFCINFTNEKLQQHFNQ 461
Cdd:cd14880 317 KPCSRAECDTRrDCLAKLIYARLFDWLVSVINSSICADTDSwTTFIGLLDVYGFESFPENSLEQLCINYANEKLQQHFVA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 462 HVFKMEQEEYTKEEIAWSYIEFIDNQDVLELIEKKPGGIISLLDEACMF--PKSTHEtFSQKLFQTFKEHERFAKPKLSR 539
Cdd:cd14880 397 HYLRAQQEEYAVEGLEWSFINYQDNQTCLDLIEGSPISICSLINEECRLnrPSSAAQ-LQTRIESALAGNPCLGHNKLSR 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 540 T-DFTISHYAGEVTYQSNHFIDKNKDYIVAEHQALFTASNCKFVAGLFHALHEDSSRSSKFSS-------IGSRFKQQLH 611
Cdd:cd14880 476 EpSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPANPEEKTQEEPSGQsrapvltVVSKFKASLE 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 612 SLMESLNGTEPHYIRCIKPNNVLKPGIFENFNVIHQLRCGGVLEAIRISCAGYPTRLAFYDFLDRFGLLAPEVLEGNYDD 691
Cdd:cd14880 556 QLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQNFVERYKLLRRLRPHTSSGP 635
|
650 660
....*....|....*....|....*
gi 30685403 692 KVACQMILDKKSLtdyQIGKTKIFL 716
Cdd:cd14880 636 HSPYPAKGLSEPV---HCGRTKVFM 657
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
75-717 |
1.76e-147 |
|
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: 466.85 E-value: 1.76e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 75 VLRNLETRYELNEIYTYTGNILIAVNPFQRLPhIYETDMMEQYKGIALGELSPHVFAIGDAAYRAMINEGKNNSILVSGE 154
Cdd:cd15896 3 VLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 155 SGAGKTETTKMLMRYLAFLG---------GRSGVEGRTVEQQVLESNPVLEAFGNAKTLRNNNSSRFGKFVEIQFDKNGR 225
Cdd:cd15896 82 SGAGKTENTKKVIQYLAHVAsshktkkdqNSLALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 226 ISGAAIRTYLLERSRVCQISDPERNYHCFYLLCAAPPEDIK-KYKLENPHKFHYLNQSSCyKLDGVDDASEYLETRRAMD 304
Cdd:cd15896 162 IVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRsELLLENYNNYRFLSNGNV-TIPGQQDKDLFTETMEAFR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 305 VVGISNEEQEAIFRVVAAILHLGNIDFGKGEEIDSSVIKDKDSRSHLnmaAELLMCNAQSLEDALIRRVMVTPEEIITRT 384
Cdd:cd15896 241 IMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKV---CHLMGMNVTDFTRAILSPRIKVGRDYVQKA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 385 LDPDNAIASRDTLAKTIYSHLFDWIVNKINTSIGQDPRS-KSIIGVLDIYGFESFKCNSFEQFCINFTNEKLQQHFNQHV 463
Cdd:cd15896 318 QTQEQAEFAVEALAKATYERMFRWLVMRINKALDKTKRQgASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTM 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 464 FKMEQEEYTKEEIAWSYIEF-IDNQDVLELIEK--KPGGIISLLDEACMFPKSTHETFSQKLFQTFKEHERFAKPKLSR- 539
Cdd:cd15896 398 FILEQEEYQREGIEWSFIDFgLDLQPCIDLIEKpaSPPGILALLDEECWFPKATDKSFVEKVLQEQGTHPKFFKPKKLKd 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 540 -TDFTISHYAGEVTYQSNHFIDKNKDYIVAEHQALFTASNCKFVAGLFHALHED----------------SSRSSKFSSI 602
Cdd:cd15896 478 eADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVDRIvgldkvsgmsempgafKTRKGMFRTV 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 603 GSRFKQQLHSLMESLNGTEPHYIRCIKPNNVLKPGIFENFNVIHQLRCGGVLEAIRISCAGYPTRLAFYDFLDRFGLLAP 682
Cdd:cd15896 558 GQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTP 637
|
650 660 670
....*....|....*....|....*....|....*...
gi 30685403 683 EVL-EGNYDDKVACQMILDKKSLTD--YQIGKTKIFLR 717
Cdd:cd15896 638 NAIpKGFMDGKQACVLMIKSLELDPnlYRIGQSKVFFR 675
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
73-717 |
4.49e-147 |
|
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: 465.36 E-value: 4.49e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 73 PGVLRNLETRYELNEIYTYTGNILIAVNPFQRLPhIYETDMMEQYKGIALGELSPHVFAIGDAAYRAMINEGKNNSILVS 152
Cdd:cd14910 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 153 GESGAGKTETTKMLMRYLAFL---GGR------SGVEGRTVEQQVLESNPVLEAFGNAKTLRNNNSSRFGKFVEIQFDKN 223
Cdd:cd14910 80 GESGAGKTVNTKRVIQYFATIavtGEKkkeeatSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 224 GRISGAAIRTYLLERSRVCQISDPERNYHCFYLLCAAPPEDIKKYKL--ENPHKFHYLNQSSCyKLDGVDDASEYLETRR 301
Cdd:cd14910 160 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLitTNPYDYAFVSQGEI-TVPSIDDQEELMATDS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 302 AMDVVGISNEEQEAIFRVVAAILHLGNIDFGKGE-----EIDSSVIKDKdsrshlnmAAELLMCNAQSLEDALIRRVMVT 376
Cdd:cd14910 239 AIEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQreeqaEPDGTEVADK--------AAYLQNLNSADLLKALCYPRVKV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 377 PEEIITRTLDPDNAIASRDTLAKTIYSHLFDWIVNKINTSIGQDPRSKSIIGVLDIYGFESFKCNSFEQFCINFTNEKLQ 456
Cdd:cd14910 311 GNEYVTKGQTVQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQ 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 457 QHFNQHVFKMEQEEYTKEEIAWSYIEF-IDNQDVLELIEkKPGGIISLLDEACMFPKSTHETFSQKLF-QTFKEHERFAK 534
Cdd:cd14910 391 QFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYeQHLGKSNNFQK 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 535 PKLSR----TDFTISHYAGEVTYQSNHFIDKNKDYIVAEHQALFTASNCKFVAGLFHALHEDSSRS-----------SKF 599
Cdd:cd14910 470 PKPAKgkveAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGAAAAEAEEgggkkggkkkgSSF 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 600 SSIGSRFKQQLHSLMESLNGTEPHYIRCIKPNNVLKPGIFENFNVIHQLRCGGVLEAIRISCAGYPTRLAFYDFLDRFGL 679
Cdd:cd14910 550 QTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKV 629
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 30685403 680 L-APEVLEGNY-DDKVACQMILDKKSL--TDYQIGKTKIFLR 717
Cdd:cd14910 630 LnASAIPEGQFiDSKKASEKLLGSIDIdhTQYKFGHTKVFFK 671
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
73-717 |
1.11e-146 |
|
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: 464.59 E-value: 1.11e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 73 PGVLRNLETRYELNEIYTYTGNILIAVNPFQRLPhIYETDMMEQYKGIALGELSPHVFAIGDAAYRAMINEGKNNSILVS 152
Cdd:cd14912 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 153 GESGAGKTETTKMLMRYLAFLGGR---------SGVEGRTVEQQVLESNPVLEAFGNAKTLRNNNSSRFGKFVEIQFDKN 223
Cdd:cd14912 80 GESGAGKTVNTKRVIQYFATIAVTgekkkeeitSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 224 GRISGAAIRTYLLERSRVCQISDPERNYHCFYLLCA-APPEDIKKYKLE-NPHKFHYLNQSSCyKLDGVDDASEYLETRR 301
Cdd:cd14912 160 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSnKKPELIEMLLITtNPYDYPFVSQGEI-SVASIDDQEELMATDS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 302 AMDVVGISNEEQEAIFRVVAAILHLGNIDFGKGE-----EIDSSVIKDKdsrshlnmAAELLMCNAQSLEDALIRRVMVT 376
Cdd:cd14912 239 AIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQreeqaEPDGTEVADK--------AAYLQSLNSADLLKALCYPRVKV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 377 PEEIITRTLDPDNAIASRDTLAKTIYSHLFDWIVNKINTSIGQDPRSKSIIGVLDIYGFESFKCNSFEQFCINFTNEKLQ 456
Cdd:cd14912 311 GNEYVTKGQTVEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQ 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 457 QHFNQHVFKMEQEEYTKEEIAWSYIEF-IDNQDVLELIEkKPGGIISLLDEACMFPKSTHETFSQKLF-QTFKEHERFAK 534
Cdd:cd14912 391 QFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYeQHLGKSANFQK 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 535 PKL----SRTDFTISHYAGEVTYQSNHFIDKNKDYIVAEHQALFTASNCKFVAGLFH-------------ALHEDSSRSS 597
Cdd:cd14912 470 PKVvkgkAEAHFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSgaqtaegasagggAKKGGKKKGS 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 598 KFSSIGSRFKQQLHSLMESLNGTEPHYIRCIKPNNVLKPGIFENFNVIHQLRCGGVLEAIRISCAGYPTRLAFYDFLDRF 677
Cdd:cd14912 550 SFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRY 629
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 30685403 678 GLL-APEVLEGNY-DDKVACQMILDKKSL--TDYQIGKTKIFLR 717
Cdd:cd14912 630 KVLnASAIPEGQFiDSKKASEKLLASIDIdhTQYKFGHTKVFFK 673
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
73-717 |
3.88e-146 |
|
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: 462.99 E-value: 3.88e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 73 PGVLRNLETRYELNEIYTYTGNILIAVNPFQRLPhIYETDMMEQYKGIALGELSPHVFAIGDAAYRAMINEGKNNSILVS 152
Cdd:cd14916 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 153 GESGAGKTETTKMLMRY---LAFLGGRSGVEGR-----TVEQQVLESNPVLEAFGNAKTLRNNNSSRFGKFVEIQFDKNG 224
Cdd:cd14916 80 GESGAGKTVNTKRVIQYfasIAAIGDRSKKENPnankgTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 225 RISGAAIRTYLLERSRVCQISDPERNYHCFY-LLCAAPPEDIKKYKL-ENPHKFHYLNQSSCyKLDGVDDASEYLETRRA 302
Cdd:cd14916 160 KLASADIETYLLEKSRVIFQLKAERNYHIFYqILSNKKPELLDMLLVtNNPYDYAFVSQGEV-SVASIDDSEELLATDSA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 303 MDVVGISNEEQEAIFRVVAAILHLGNIDFGKGEEIDSSvikDKDSRSHLNMAAELLMCNAQSLEDALIRRVMVTPEEIIT 382
Cdd:cd14916 239 FDVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQA---EPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 383 RTLDPDNAIASRDTLAKTIYSHLFDWIVNKINTSIGQDPRSKSIIGVLDIYGFESFKCNSFEQFCINFTNEKLQQHFNQH 462
Cdd:cd14916 316 KGQSVQQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHH 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 463 VFKMEQEEYTKEEIAWSYIEF-IDNQDVLELIEkKPGGIISLLDEACMFPKSTHETFSQKLFQT-FKEHERFAKPK---- 536
Cdd:cd14916 396 MFVLEQEEYKKEGIEWEFIDFgMDLQACIDLIE-KPMGIMSILEEECMFPKASDMTFKAKLYDNhLGKSNNFQKPRnvkg 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 537 LSRTDFTISHYAGEVTYQSNHFIDKNKDYIVAEHQALFTASNCKFVAGLFH----ALHEDSSRSSKFSSIGSRF------ 606
Cdd:cd14916 475 KQEAHFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFStyasADTGDSGKGKGGKKKGSSFqtvsal 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 607 -KQQLHSLMESLNGTEPHYIRCIKPNNVLKPGIFENFNVIHQLRCGGVLEAIRISCAGYPTRLAFYDFLDRFGLLAPEVL 685
Cdd:cd14916 555 hRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAI 634
|
650 660 670
....*....|....*....|....*....|....*.
gi 30685403 686 -EGNY-DDKVACQMILDKKSL--TDYQIGKTKIFLR 717
Cdd:cd14916 635 pEGQFiDSRKGAEKLLGSLDIdhNQYKFGHTKVFFK 670
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
73-717 |
3.07e-145 |
|
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: 460.69 E-value: 3.07e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 73 PGVLRNLETRYELNEIYTYTGNILIAVNPFQRLPhIYETDMMEQYKGIALGELSPHVFAIGDAAYRAMINEGKNNSILVS 152
Cdd:cd14923 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 153 GESGAGKTETTKMLMRYLAFLG--GRSGVEGR------TVEQQVLESNPVLEAFGNAKTLRNNNSSRFGKFVEIQFDKNG 224
Cdd:cd14923 80 GESGAGKTVNTKRVIQYFATIAvtGDKKKEQQpgkmqgTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 225 RISGAAIRTYLLERSRVCQISDPERNYHCFY-LLCAAPPEDIKKYKLE-NPHKFHYLNQSSCyKLDGVDDASEYLETRRA 302
Cdd:cd14923 160 KLASADIETYLLEKSRVTFQLSSERSYHIFYqIMSNKKPELIDLLLIStNPFDFPFVSQGEV-TVASIDDSEELLATDNA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 303 MDVVGISNEEQEAIFRVVAAILHLGNIDFGKGE-----EIDSSVIKDKdsrshlnmAAELLMCNAQSLEDALIRRVMVTP 377
Cdd:cd14923 239 IDILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQreeqaEPDGTEVADK--------AGYLMGLNSAEMLKGLCCPRVKVG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 378 EEIITRTLDPDNAIASRDTLAKTIYSHLFDWIVNKINTSIGQDPRSKSIIGVLDIYGFESFKCNSFEQFCINFTNEKLQQ 457
Cdd:cd14923 311 NEYVTKGQNVQQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQ 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 458 HFNQHVFKMEQEEYTKEEIAWSYIEF-IDNQDVLELIEkKPGGIISLLDEACMFPKSTHETFSQKLF-QTFKEHERFAKP 535
Cdd:cd14923 391 FFNHHMFVLEQEEYKKEGIEWEFIDFgMDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYdQHLGKSNNFQKP 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 536 KLSR----TDFTISHYAGEVTYQSNHFIDKNKDYIVAEHQALFTASNCKFVAGLF--HALHE----------DSSRSSKF 599
Cdd:cd14923 470 KPAKgkaeAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFsnYAGAEagdsggskkgGKKKGSSF 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 600 SSIGSRFKQQLHSLMESLNGTEPHYIRCIKPNNVLKPGIFENFNVIHQLRCGGVLEAIRISCAGYPTRLAFYDFLDRFGL 679
Cdd:cd14923 550 QTVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRI 629
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 30685403 680 L-APEVLEGNY-DDKVACQMILDKKSL--TDYQIGKTKIFLR 717
Cdd:cd14923 630 LnASAIPEGQFiDSKNASEKLLNSIDVdrEQYRFGHTKVFFK 671
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
75-717 |
1.21e-141 |
|
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: 450.70 E-value: 1.21e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 75 VLRNLETRYELNEIYTYTGNILIAVNPFQRLPhIYETDMMEQYKGIALGELSPHVFAIGDAAYRAMINEGKNNSILVSGE 154
Cdd:cd14930 3 VLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 155 SGAGKTETTKMLMRYLAFLG----GRS--GVEGRtVEQQVLESNPVLEAFGNAKTLRNNNSSRFGKFVEIQFDKNGRISG 228
Cdd:cd14930 82 SGAGKTENTKKVIQYLAHVAsspkGRKepGVPGE-LERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 229 AAIRTYLLERSRVCQISDPERNYHCFYLLCAAPPEDIKKYKLENPHKfHYLNQSSCYKLDGVDDASEYLETRRAMDVVGI 308
Cdd:cd14930 161 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCS-HYRFLTNGPSSSPGQERELFQETLESLRVLGF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 309 SNEEQEAIFRVVAAILHLGNIDFGKGEEIDSSVIKDkdsrshlNMAAELLmCNAQSLEDALIRRVMVTP-----EEIITR 383
Cdd:cd14930 240 SHEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPD-------NTAAQKL-CRLLGLGVTDFSRALLTPrikvgRDYVQK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 384 TLDPDNAIASRDTLAKTIYSHLFDWIVNKINTSIGQDPRS-KSIIGVLDIYGFESFKCNSFEQFCINFTNEKLQQHFNQH 462
Cdd:cd14930 312 AQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQgASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHT 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 463 VFKMEQEEYTKEEIAWSYIEF-IDNQDVLELIEK--KPGGIISLLDEACMFPKSTHETFSQKLFQTFKEHERFAKPKLSR 539
Cdd:cd14930 392 MFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERpaNPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRHLR 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 540 --TDFTISHYAGEVTYQSNHFIDKNKDYIVAEHQALFTASNCKFVAGLFHALHEDSSRSSKFS----------------S 601
Cdd:cd14930 472 dqADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSlgdgppggrprrgmfrT 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 602 IGSRFKQQLHSLMESLNGTEPHYIRCIKPNNVLKPGIFENFNVIHQLRCGGVLEAIRISCAGYPTRLAFYDFLDRFGLLA 681
Cdd:cd14930 552 VGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILT 631
|
650 660 670
....*....|....*....|....*....|....*....
gi 30685403 682 PEVL-EGNYDDKVACQMILDKKSLTD--YQIGKTKIFLR 717
Cdd:cd14930 632 PNAIpKGFMDGKQACEKMIQALELDPnlYRVGQSKIFFR 670
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
75-717 |
2.91e-138 |
|
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: 440.86 E-value: 2.91e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 75 VLRNLETRYELNEIYTYTGNILIAVNPFQRLPHIYETDMMEQYKG--IALG---ELSPHVFAIGDAAYRAMINEGKNNSI 149
Cdd:cd14886 3 VIDILRDRFAKDKIYTYAGKLLVALNPFKQIRNLYGTEVIGRYRQadTSRGfpsDLPPHSYAVAQSALNGLISDGISQSC 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 150 LVSGESGAGKTETTKMLMRYLAFlGGRSGVEgrTVEQQVLESNPVLEAFGNAKTLRNNNSSRFGKFVEIQFDKNGRISGA 229
Cdd:cd14886 83 IVSGESGAGKTETAKQLMNFFAY-GHSTSST--DVQSLILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGPDGGLKGG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 230 AIRTYLLERSRVCQISDPERNYHCFY-LLCAAPPEDIKKYKLENPHKFHYLNQSSCYKLDGVDDASEYLETRRAMDVVgI 308
Cdd:cd14886 160 KITSYMLELSRIEFQSTNERNYHIFYqCIKGLSPEEKKSLGFKSLESYNFLNASKCYDAPGIDDQKEFAPVRSQLEKL-F 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 309 SNEEQEAIFRVVAAILHLGNIDF---GKGEEIDSSVIKDKDSRSHLnmaAELLMCNAQSLEDALIRRVMVTPEEIITRTL 385
Cdd:cd14886 239 SKNEIDSFYKCISGILLAGNIEFseeGDMGVINAAKISNDEDFGKM---CELLGIESSKAAQAIITKVVVINNETIISPV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 386 DPDNAIASRDTLAKTIYSHLFDWIVNKINTSIGQDPRSKSIIGVLDIYGFESFKCNSFEQFCINFTNEKLQQHFNQHVFK 465
Cdd:cd14886 316 TQAQAEVNIRAVAKDLYGALFELCVDTLNEIIQFDADARPWIGILDIYGFEFFERNTYEQLLINYANERLQQYFINQVFK 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 466 MEQEEYTKEEIAWSYIEFIDNQDVLELIEKKPGGIISLLDEACMFPKSTHETFSQKLFQTFKEhERFAKPKLSRTDFTIS 545
Cdd:cd14886 396 SEIQEYEIEGIDHSMITFTDNSNVLAVFDKPNLSIFSFLEEQCLIQTGSSEKFTSSCKSKIKN-NSFIPGKGSQCNFTIV 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 546 HYAGEVTYQSNHFIDKNKDYIVAEHQALFTASNCKFVAGLFHALHEDsSRSSKFSSIGSRFKQQLHSLMESLNGTEPHYI 625
Cdd:cd14886 475 HTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNKAFSDIPNE-DGNMKGKFLGSTFQLSIDQLMKTLSATKSHFI 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 626 RCIKPNNVLKPGIFENFNVIHQLRCGGVLEAIRISCAGYPTRLAFYDFLDRFGLL---APEVLEGNYDDKVACQMILDKK 702
Cdd:cd14886 554 RCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFFHRNKILishNSSSQNAGEDLVEAVKSILENL 633
|
650
....*....|....*..
gi 30685403 703 SL--TDYQIGKTKIFLR 717
Cdd:cd14886 634 GIpcSDYRIGKTKVFLR 650
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
75-677 |
5.68e-135 |
|
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: 434.52 E-value: 5.68e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 75 VLRNLETRYELNEIYTYTGNILIAVNPFQRLPHIYETDMMEQY----------KGIALGELSPHVFAIGDAAYRAMINEG 144
Cdd:cd14899 3 ILNALRLRYERHAIYTHIGDILISINPFQDLPQLYGDEILRGYaydhnsqfgdRVTSTDPREPHLFAVARAAYIDIVQNG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 145 KNNSILVSGESGAGKTETTKMLMRYLAFLGGRSGVEGR--------------TVEQQVLESNPVLEAFGNAKTLRNNNSS 210
Cdd:cd14899 83 RSQSILISGESGAGKTEATKIIMTYFAVHCGTGNNNLTnsesisppaspsrtTIEEQVLQSNPILEAFGNARTVRNDNSS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 211 RFGKFVEIQF-DKNGRISGAAIRTYLLERSRVCQISDPERNYHCFYLLCAAPPEDIKKYKLE------NPHKFHYLNQSS 283
Cdd:cd14899 163 RFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSADNNCVSKEQKQvlalsgGPQSFRLLNQSL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 284 CYKL-DGVDDASEYLETRRAMDVVGISNEEQEAIFRVVAAILHLGNIDF----GKGEE---IDSSVIKDKDSR--SHLNM 353
Cdd:cd14899 243 CSKRrDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFeqipHKGDDtvfADEARVMSSTTGafDHFTK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 354 AAELLMCNAQSLEDALIRRVMVTPEEIITRTLDPDNAIASRDTLAKTIYSHLFDWIVNKINTSI---GQDP--------- 421
Cdd:cd14899 323 AAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLqrqASAPwgadesdvd 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 422 ---RSKSIIGVLDIYGFESFKCNSFEQFCINFTNEKLQQHFNQHVFKMEQEEYTKEEIAWSYIEFIDNQDVLELIEKKPG 498
Cdd:cd14899 403 deeDATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFPNNRACLELFEHRPI 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 499 GIISLLDEACMFPKSTHETFSQKLFQTF---KEHERF-AKPKLSR-TDFTISHYAGEVTYQSNHFIDKNKDYIVAEHQAL 573
Cdd:cd14899 483 GIFSLTDQECVFPQGTDRALVAKYYLEFekkNSHPHFrSAPLIQRtTQFVVAHYAGCVTYTIDGFLAKNKDSFCESAAQL 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 574 FTASNCKFVAGLFHALHEDSSRSSKFSS------------------IGSRFKQQLHSLMESLNGTEPHYIRCIKPNNVLK 635
Cdd:cd14899 563 LAGSSNPLIQALAAGSNDEDANGDSELDgfggrtrrraksaiaavsVGTQFKIQLNELLSTVRATTPRYVRCIKPNDSHV 642
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 30685403 636 PGIFENFNVIHQLRCGGVLEAIRISCAGYPTRLAFYDFLDRF 677
Cdd:cd14899 643 GSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRY 684
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
79-716 |
4.71e-131 |
|
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: 421.19 E-value: 4.71e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 79 LETRYELNEIYTYTG-NILIAVNPFQRLPHIYETDMME---QYKGIALGE---LSPHVFAIGDAAYRAMINEGKNNSILV 151
Cdd:cd14879 10 LASRFRSDLPYTRLGsSALVAVNPYKYLSSNSDASLGEygsEYYDTTSGSkepLPPHAYDLAARAYLRMRRRSEDQAVVF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 152 SGESGAGKTETTKMLMRYLAFLGGRSGVEGRTVEQqVLESNPVLEAFGNAKTLRNNNSSRFGKFVEIQFDKNGRISGAAI 231
Cdd:cd14879 90 LGETGSGKSESRRLLLRQLLRLSSHSKKGTKLSSQ-ISAAEFVLDSFGNAKTLTNPNASRFGRYTELQFNERGRLIGAKV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 232 RTYLLERSRVCQISDPERNYHCFYLLCA-APPEDIKKYKLENPHKFHYLNQSSCYKLD---GVDDASEYLETRRAMDVVG 307
Cdd:cd14879 169 LDYRLERSRVASVPTGERNFHVFYYLLAgASPEERQHLGLDDPSDYALLASYGCHPLPlgpGSDDAEGFQELKTALKTLG 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 308 ISNEEQEAIFRVVAAILHLGNIDFGK---GEEiDSSVIKDKDSrshLNMAAELLMCNAQSLEDAL------IRRvmvtpe 378
Cdd:cd14879 249 FKRKHVAQICQLLAAILHLGNLEFTYdheGGE-ESAVVKNTDV---LDIVAAFLGVSPEDLETSLtyktklVRK------ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 379 EIITRTLDPDNAIASRDTLAKTIYSHLFDWIVNKINTSI-GQDPRSKSIIGVLDIYGFESF---KCNSFEQFCINFTNEK 454
Cdd:cd14879 319 ELCTVFLDPEGAAAQRDELARTLYSLLFAWVVETINQKLcAPEDDFATFISLLDFPGFQNRsstGGNSLDQFCVNFANER 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 455 LQQHFNQHVFKMEQEEYTKEEIAWSYIEFIDNQDVLELIEKKPGGIISLLDEAC-MFPKSTHETFSQKL---FQT---FK 527
Cdd:cd14879 399 LHNYVLRSFFERKAEELEAEGVSVPATSYFDNSDCVRLLRGKPGGLLGILDDQTrRMPKKTDEQMLEALrkrFGNhssFI 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 528 EHERFAKPKLSRTdFTISHYAGEVTYQSNHFIDKNKDYIvaehqalftasNCKFVAgLFHALHEdssrsskfssigsrFK 607
Cdd:cd14879 479 AVGNFATRSGSAS-FTVNHYAGEVTYSVEGFLERNGDVL-----------SPDFVN-LLRGATQ--------------LN 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 608 QQLHSLMESLNGTEPHYIRCIKPNNVLKPGIFENFNVIHQLRCGGVLEAIRISCAGYPTRLAFYDFLDRFGLLAPEVLEG 687
Cdd:cd14879 532 AALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQIRSLGLPELAARLRVEYVVSLEHAEFCERYKSTLRGSAAE 611
|
650 660
....*....|....*....|....*....
gi 30685403 688 NYDDKVACQMILDkksLTDYQIGKTKIFL 716
Cdd:cd14879 612 RIRQCARANGWWE---GRDYVLGNTKVFL 637
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
75-717 |
4.55e-129 |
|
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: 416.52 E-value: 4.55e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 75 VLRNLETRYE-LNEIYTYTGNILIAVNPFQRLPHIYETdmmEQYKGIALGE---LSPHVFAIGDAAYRAMINEGKNN-SI 149
Cdd:cd14875 3 LLHCIKERFEkLHQQYSLMGEMVLSVNPFRLMPFNSEE---ERKKYLALPDprlLPPHIWQVAHKAFNAIFVQGLGNqSV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 150 LVSGESGAGKTETTKMLMRYLAFLG--GRSGVEGRTVEQQVLE----SNPVLEAFGNAKTLRNNNSSRFGKFVEIQFDK- 222
Cdd:cd14875 80 VISGESGSGKTENAKMLIAYLGQLSymHSSNTSQRSIADKIDEnlkwSNPVMESFGNARTVRNDNSSRFGKYIKLYFDPt 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 223 NGRISGAAIRTYLLERSRVCQISDPERNYHCFY-LLCAAPPEDIKKY-KLENPHKFHYLNQSSCYKLDGVD-----DASE 295
Cdd:cd14875 160 SGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYeMLAGLSPEEKKELgGLKTAQDYKCLNGGNTFVRRGVDgktldDAHE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 296 YLETRRAMDVVGISNEEQEAIFRVVAAILHLGNIDFgKGEEIDSSVIKDKDSrshLNMAAELLMCNAQSLEDALIRRvmv 375
Cdd:cd14875 240 FQNVRHALSMIGVELETQNSIFRVLASILHLMEVEF-ESDQNDKAQIADETP---FLTACRLLQLDPAKLRECFLVK--- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 376 TPEEIITRTLDPDNAIASRDTLAKTIYSHLFDWIVNKINTSIgqDPR----SKSIIGVLDIYGFESFKCNSFEQFCINFT 451
Cdd:cd14875 313 SKTSLVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNASI--TPQgdcsGCKYIGLLDIFGFENFTRNSFEQLCINYA 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 452 NEKLQQHFNQHVFKMEQEEYTKEEIAWSYIEFIDNQDVLELIEKKPGGIISLLDEACMFPKSTHETFSQKLFQTFKEHER 531
Cdd:cd14875 391 NESLQNHYNKYTFINDEEECRREGIQIPKIEFPDNSECVNMFDQKRTGIFSMLDEECNFKGGTTERFTTNLWDQWANKSP 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 532 -FAKPKLSRTD-FTISHYAGEVTYQSNHFIDKNKDYIVAEHQALFTASNCKFVAGLFHAlheDSSRSSKFSSIGSRFKQQ 609
Cdd:cd14875 471 yFVLPKSTIPNqFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTLLST---EKGLARRKQTVAIRFQRQ 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 610 LHSLMESLNGTEPHYIRCIKPNNVLKPGIFENFNVIHQLRCGGVLEAIRISCAGYPTRLAFYDFLDRFGLLAPEVL---- 685
Cdd:cd14875 548 LTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRRPIEQFCRYFYLIMPRSTaslf 627
|
650 660 670
....*....|....*....|....*....|....*....
gi 30685403 686 -EGNYDDkvACQMILD------KKSLTDYQIGKTKIFLR 717
Cdd:cd14875 628 kQEKYSE--AAKDFLAyyqrlyGWAKPNYAVGKTKVFLR 664
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
75-717 |
4.05e-116 |
|
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: 380.70 E-value: 4.05e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 75 VLRNLETRYELNEIYTYTGNILIAVNPFQRLPhIYETDMMEQY---KGIALGELSPHVFAIGDAAYRAMINEGKNNSILV 151
Cdd:cd14878 3 LLYEIQKRFGNNQIYTFIGDILLLVNPYKELP-IYSTMVSQLYlssSGQLCSSLPPHLFSCAERAFHQLFQERRPQCFIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 152 SGESGAGKTETTKMLMRYLAFlggRSGVEGRTVEQQVLESNPVLEAFGNAKTLRNNNSSRFGKFVEIQF-DKNGRISGAA 230
Cdd:cd14878 82 SGERGSGKTEASKQIMKHLTC---RASSSRTTFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFcERKKHLTGAR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 231 IRTYLLERSRVcqISDP--ERNYHCFYLLC-AAPPEDIKKYKLENPHKFHYLNQSSCYKLDGVD---DASEYLETRRAMD 304
Cdd:cd14878 159 IYTYMLEKSRL--VSQPpgQSNFLIFYLLMdGLSAEEKYGLHLNNLCAHRYLNQTMREDVSTAErslNREKLAVLKQALN 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 305 VVGISNEEQEAIFRVVAAILHLGNIDFGKGEEIDSSVIKDkdsRSHLNMAAELLMCNAQSLEDALIRRVMVTPEEIITRT 384
Cdd:cd14878 237 VVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSD---LQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 385 LDPDNAIASRDTLAKTIYSHLFDWIVNKINTSIGQDPRSKSI----IGVLDIYGFESFKCNSFEQFCINFTNEKLQQHFN 460
Cdd:cd14878 314 HTIQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLQSQDEQKSMqtldIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYIN 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 461 QHVFKMEQEEYTKEEIAWSYIEFIDNQD-VLELIEKKPGGIISLLDEACMFPKSTHETFSQKL------------FQTFK 527
Cdd:cd14878 394 EVLFLQEQTECVQEGVTMETAYSPGNQTgVLDFFFQKPSGFLSLLDEESQMIWSVEPNLPKKLqsllessntnavYSPMK 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 528 EHERFAKPKLSRTDFTISHYAGEVTYQSNHFIDKNKDYIVAEHQALFTASNCKFVAGLFHAlhedssrssKFSSIGSRFK 607
Cdd:cd14878 474 DGNGNVALKDQGTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQS---------KLVTIASQLR 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 608 QQLHSLMESLNGTEPHYIRCIKPNNVLKPGIFENFNVIHQLRCGGVLEAIRISCAGYPTRLAFYDFLDRFGLLApEVLEG 687
Cdd:cd14878 545 KSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLA-DTLLG 623
|
650 660 670
....*....|....*....|....*....|...
gi 30685403 688 NYDDKVA---CQMILDKKSLTDYQIGKTKIFLR 717
Cdd:cd14878 624 EKKKQSAeerCRLVLQQCKLQGWQMGVRKVFLK 656
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
73-717 |
1.32e-108 |
|
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: 362.04 E-value: 1.32e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 73 PGVLRNLETRY--------ELNEIYTYTGNILIAVNPFqRLPHIYETDMMEQYKGIALGELSPHVFAIGDAAYRAMINEG 144
Cdd:cd14887 1 PNLLENLYQRYnkayinkeNRNCIYTYTGTLLIAVNPY-RFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 145 KNNSILVSGESGAGKTETTKMLMRYLAFLGG-RSGVEGRTVEQQVLESNPVLEAFGNAKTLRNNNSSRFGKFVEIQFDKN 223
Cdd:cd14887 80 RSQSILISGESGAGKTETSKHVLTYLAAVSDrRHGADSQGLEARLLQSGPVLEAFGNAHTVLNANSSRFGKMLLLHFTGR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 224 GRISGAAIRTYLLERSRVCQISDPERNYHCFYLLCAAPPEDiKKYKLENPHKFHYLnqsscYKLDGVDdaseyletrRAM 303
Cdd:cd14887 160 GKLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAVAA-ATQKSSAGEGDPES-----TDLRRIT---------AAM 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 304 DVVGISNEEQEAIFRVVAAILHLGNIDFGKGEE------------------------------IDSSVIKDKD-SRSHLN 352
Cdd:cd14887 225 KTVGIGGGEQADIFKLLAAILHLGNVEFTTDQEpetskkrkltsvsvgceetaadrshssevkCLSSGLKVTEaSRKHLK 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 353 MAAELLMCNAQSLEDALIRRVMVTPEEIITRT-LDPDNAIASRDTLAKTIYSHLFDWIVNKINTSIGQD----------- 420
Cdd:cd14887 305 TVARLLGLPPGVEGEEMLRLALVSRSVRETRSfFDLDGAAAARDAACKNLYSRAFDAVVARINAGLQRSakpsesdsded 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 421 -PRSKSI--IGVLDIYGFESFK---CNSFEQFCINFTNEKLQQHFNQHVFKMEQEEYTKEEIAWSYIEFIDN-------- 486
Cdd:cd14887 385 tPSTTGTqtIGILDLFGFEDLRnhsKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGVFQNQDCSAFPfsfplast 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 487 -----QDVLELI--------------EKKPGGIISLLDEACMFPKSTHETFSQKLF--QTFKEHERFAK-----PKLSRT 540
Cdd:cd14887 465 ltsspSSTSPFSptpsfrsssafatsPSLPSSLSSLSSSLSSSPPVWEGRDNSDLFyeKLNKNIINSAKyknitPALSRE 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 541 --DFTISHYAGEVTYQSNHFIDKNKDYIVAEHQALFTASNCKFVAGLFHALHEDSSRSSKFSSIGSRFKQQLHSLMESLN 618
Cdd:cd14887 545 nlEFTVSHFACDVTYDARDFCRANREATSDELERLFLACSTYTRLVGSKKNSGVRAISSRRSTLSAQFASQLQQVLKALQ 624
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 619 GTEPHYIRCIKPNNVLKPGIFENFNVIHQLRCGGVLEAIRISCAGYPTRLAFYDFLDRFGLLAPEVLEGNYDDKVACQMI 698
Cdd:cd14887 625 ETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVELWRRYETKLPMALREALTPKMFCKIV 704
|
730 740
....*....|....*....|.
gi 30685403 699 LDKKSLT--DYQIGKTKIFLR 717
Cdd:cd14887 705 LMFLEINsnSYTFGKTKIFFR 725
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
75-717 |
1.17e-102 |
|
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: 342.77 E-value: 1.17e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 75 VLRNLETRYELNEIYTYTGNILIAVNPFQrlphIYETDMMEqYKGIALGELSPHVFAIGDAAYRAMINEGKNNSILVSGE 154
Cdd:cd14937 3 VLNMLALRYKKNYIYTIAEPMLISINPYQ----VIDVDINE-YKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 155 SGAGKTETTKMLMRYlaFLggrSGV-EGRTVEQQVLESNPVLEAFGNAKTLRNNNSSRFGKFVEIQFDKNGRISGAAIRT 233
Cdd:cd14937 78 SGSGKTEASKLVIKY--YL---SGVkEDNEISNTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIVSSSIEI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 234 YLLERSRVCQISDPERNYHCFYLLCAAPPEDIK-KYKLENPHKFHYLNQSSCyKLDGVDDASEYLETRRAMDVVGIsNEE 312
Cdd:cd14937 153 FLLENIRVVSQEEEERGYHIFYQIFNGMSQELKnKYKIRSENEYKYIVNKNV-VIPEIDDAKDFGNLMISFDKMNM-HDM 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 313 QEAIFRVVAAILHLGNIDFG---KGEEIDSSVIkDKDSRSHLNMAAELLMCNAQSLEDALIRRVMVTPEEIITRTLDPDN 389
Cdd:cd14937 231 KDDLFLTLSGLLLLGNVEYQeieKGGKTNCSEL-DKNNLELVNEISNLLGINYENLKDCLVFTEKTIANQKIEIPLSVEE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 390 AIASRDTLAKTIYSHLFDWIVNKINTSIGQDPRSKSIIGVLDIYGFESFKCNSFEQFCINFTNEKLQQHFNQHVFKMEQE 469
Cdd:cd14937 310 SVSICKSISKDLYNKIFSYITKRINNFLNNNKELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIHSIYLYIVYEKETE 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 470 EYTKEEIAWSYIEFIDNQDVLELIEKKPgGIISLLDEACMFPKSTHETFSQKLFQTFKEHERFAKPKLSRT-DFTISHYA 548
Cdd:cd14937 390 LYKAEDILIESVKYTTNESIIDLLRGKT-SIISILEDSCLGPVKNDESIVSVYTNKFSKHEKYASTKKDINkNFVIKHTV 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 549 GEVTYQSNHFIDKNKDYIVAEHQALFTASNCKFVAGLFHALhEDSSRSSKFSSIGSRFKQQLHSLMESLNGTEPHYIRCI 628
Cdd:cd14937 469 SDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDV-EVSESLGRKNLITFKYLKNLNNIISYLKSTNIYFIKCI 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 629 KPNNVLKPGIFENFNVIHQLRCGGVLEAIRISCAgYPTRLAFYDFLDRFGLLAPEVL-EGNYDDKVACQMILDKKSLTD- 706
Cdd:cd14937 548 KPNENKEKNNFNQKKVFPQLFSLSIIETLNISFF-FQYKYTFDVFLSYFEYLDYSTSkDSSLTDKEKVSMILQNTVDPDl 626
|
650
....*....|.
gi 30685403 707 YQIGKTKIFLR 717
Cdd:cd14937 627 YKVGKTMVFLK 637
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
75-717 |
1.51e-101 |
|
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: 337.64 E-value: 1.51e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 75 VLRNLETRYELNEIYTYTGNILIAVNPFQrlpHIYETDMMEQYKGiALGELSPHVFAIGDAAYRAMINEGkNNSILVSGE 154
Cdd:cd14898 3 TLEILEKRYASGKIYTKSGLVFLALNPYE---TIYGAGAMKAYLK-NYSHVEPHVYDVAEASVQDLLVHG-NQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 155 SGAGKTETTKMLMRYLafLGGRSGVEgrTVEQQVLESNPVLEAFGNAKTLRNNNSSRFGKFVEIQFDknGRISGAAIRTY 234
Cdd:cd14898 78 SGSGKTENAKLVIKYL--VERTASTT--SIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKFD--GKITGAKFETY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 235 LLERSRVCQISDPERNYHCFYLLCAAppediKKYKLENphkfHYLNQSSCY--KLDGVDDASEYLETRRAMDVVGISNee 312
Cdd:cd14898 152 LLEKSRVTHHEKGERNFHIFYQFCAS-----KRLNIKN----DFIDTSSTAgnKESIVQLSEKYKMTCSAMKSLGIAN-- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 313 QEAIFRVVAAILHLGNIDFgkgeeIDSSVIKDKDSRShLNMAAELLMCNAQSLEDALIRRVMVTPEEIITRTLDPDNAIA 392
Cdd:cd14898 221 FKSIEDCLLGILYLGSIQF-----VNDGILKLQRNES-FTEFCKLHNIQEEDFEESLVKFSIQVKGETIEVFNTLKQART 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 393 SRDTLAKTIYSHLFDWIVNKINTSIGQDprSKSIIGVLDIYGFESFKCNSFEQFCINFTNEKLQQHFNQHVFKMEQEEYT 472
Cdd:cd14898 295 IRNSMARLLYSNVFNYITASINNCLEGS--GERSISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMFRAKQGMYK 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 473 KEEIAWSYIEFIDNQDVLELIEkKPGGIISLLDEACMFPKSTHETFSQKLfQTFKEHerFAKPKlSRTDFTISHYAGEVT 552
Cdd:cd14898 373 EEGIEWPDVEFFDNNQCIRDFE-KPCGLMDLISEESFNAWGNVKNLLVKI-KKYLNG--FINTK-ARDKIKVSHYAGDVE 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 553 YQSNHFIDKNKDyivaehqalftASNCKFVAGLFHALHEDSSRSSKFssigsrFKQQLHSLMESLNGTEPHYIRCIKPNN 632
Cdd:cd14898 448 YDLRDFLDKNRE-----------KGQLLIFKNLLINDEGSKEDLVKY------FKDSMNKLLNSINETQAKYIKCIRPNE 510
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 633 VLKPGIFENFNVIHQLRCGGVLEAIRISCAGYPTRLAFYDFLDRFGLLAPEVLEgnyddkvacqmildkksLTDYQIGKT 712
Cdd:cd14898 511 ECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRILGITLFE-----------------VVDYRKGRT 573
|
....*
gi 30685403 713 KIFLR 717
Cdd:cd14898 574 RYFMK 578
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
73-717 |
2.53e-101 |
|
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: 340.35 E-value: 2.53e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 73 PGVLRNLETRYELNEIYTYTGNILIAVNPFQRLPHIYETDMMEQY-------KGIALGELSPHVFAIGDAAYRAMINEGK 145
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKELYDQDVMNVYlhkksnsAASAAPFPKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 146 NNSILVSGESGAGKTETTKMLMRYLAFLGGRSGVEGRtvEQQVLESNPVLEAFGNAKTLRNNNSSRFGKFVEIQFDK--- 222
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYFHYIQTDSQMTER--IDKLIYINNILESMSNATTIKNNNSSRCGRINLLIFEEven 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 223 ------NGRISGAAIRTYLLERSRVCQISDPERNYHCFY-LLCAAPPED---------IKKYKLENPHKFHYLNQSS--- 283
Cdd:cd14884 159 tqknmfNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYqVLRGLSDEDlarrnlvrnCGVYGLLNPDESHQKRSVKgtl 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 284 --------CYKLDGVDDASEYLETRRAMDVVGISNEEQEAIFRVVAAILHLGNidfgkgeeidssvikdkdsrSHLNMAA 355
Cdd:cd14884 239 rlgsdsldPSEEEKAKDEKNFVALLHGLHYIKYDERQINEFFDIIAGILHLGN--------------------RAYKAAA 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 356 ELLMCNAQSLEDALIRRVMVTPEEIITRTLDPDNAIASRDTLAKTIYSHLFDWIVNKINTSIGQDPRSKS---------- 425
Cdd:cd14884 299 ECLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNVLKCKEKDEsdnediysin 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 426 --IIGVLDIYGFESFKCNSFEQFCINFTNEKLQQHFNQHVFKMEQEEYTKEEIAWSYIEFIDNQDVLELIEKkpggIISL 503
Cdd:cd14884 379 eaIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDVAPSYSDTLIFIAK----IFRR 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 504 LDEACMFPKSTHETFSQKLFQTFKEHERF---------------------AKPKLSRTDFTISHYAGEVTYQSNHFIDKN 562
Cdd:cd14884 455 LDDITKLKNQGQKKTDDHFFRYLLNNERQqqlegkvsygfvlnhdadgtaKKQNIKKNIFFIRHYAGLVTYRINNWIDKN 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 563 KDYIVAEHQALFTASNCKFvagLFHALheDSSRSSKFSSIGSRFKQQLHSLMESLNGTEPHYIRCIKPNNVLKPGIFENF 642
Cdd:cd14884 535 SDKIETSIETLISCSSNRF---LREAN--NGGNKGNFLSVSKKYIKELDNLFTQLQSTDMYYIRCFLPNAKMLPNTFKRL 609
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30685403 643 NVIHQLRCGGVLEAIRISCAGYPTRLAFYDFLDRFG-LLAPEVLEGNYDDKVACQMILDKKSLTDYQIGKTKIFLR 717
Cdd:cd14884 610 LVYRQLKQCGSNEMIKILNRGLSHKIPKKETAAALKeQIAKELEKCNSNTDIEYQRRLAALDVQFIPDGRLYAFMK 685
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
74-717 |
1.55e-94 |
|
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: 319.51 E-value: 1.55e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 74 GVLRNLETRYELNEIYTYTGNILIAVNPFQRLPhIYETDMMEQYkgialgelspHVFAIGDAAYRAMI-NEGKNNSILVS 152
Cdd:cd14874 2 GIAQNLHERFKKGQTYTKASNVLVFVNDFNKLS-IQDQLVIKKC----------HISGVAENALDRIKsMSSNAESIVFG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 153 GESGAGKTETTKMLMRYLAflgGRSGVEGRTVEQQVLESnpVLEAFGNAKTLRNNNSSRFGKFVEIQFdKNGRISGAAIR 232
Cdd:cd14874 71 GESGSGKSYNAFQVFKYLT---SQPKSKVTTKHSSAIES--VFKSFGCAKTLKNDEATRFGCSIDLLY-KRNVLTGLNLK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 233 -TYLLERSRVCQISDPERNYHCFYLLCAAPPEDIK-KYKLENPHKFHYLNQSSCYKlDGVDDASEYLETRRAMDVVGISN 310
Cdd:cd14874 145 yTVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKaKFGIKGLQKFFYINQGNSTE-NIQSDVNHFKHLEDALHVLGFSD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 311 EEQEAIFRVVAAILHLGNIDF----GKGEEIDSSVIKDKdsrSHLNMAAELLMCNAQSLEDALirrvmvTPEEIITRTLD 386
Cdd:cd14874 224 DHCISIYKIISTILHIGNIYFrtkrNPNVEQDVVEIGNM---SEVKWVAFLLEVDFDQLVNFL------LPKSEDGTTID 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 387 PDNAIASRDTLAKTIYSHLFDWIVNKINTSIgQDPRSKSIIGVLDIYGFESFKCNSFEQFCINFTNEKLQQHFNQHVFKM 466
Cdd:cd14874 295 LNAALDNRDSFAMLIYEELFKWVLNRIGLHL-KCPLHTGVISILDHYGFEKYNNNGVEEFLINSVNERIENLFVKHSFHD 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 467 EQEEYTKEEIAWSYI--EFIDNQDVLELIEKKPGGIISLLDEACMFPKSTHETFSQKLFQTFKEHERFAKPKL-SRTDFT 543
Cdd:cd14874 374 QLVDYAKDGISVDYKvpNSIENGKTVELLFKKPYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRSSYGKARNkERLEFG 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 544 ISHYAGEVTYQSNHFIDKNKDYIVAEHQALFTASNCKFVAGLFhalheDSSRSSKFSSIGSRFKQQLHS---LMESLNGT 620
Cdd:cd14874 454 VRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLF-----ESYSSNTSDMIVSQAQFILRGaqeIADKINGS 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 621 EPHYIRCIKPNNVLKPGIFENFNVIHQLRCGGVLEAIRISCAGYPTRLAFYDFLDRFGLLAPEVLEGNYDDKVACQMILD 700
Cdd:cd14874 529 HAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYRCLLPGDIAMCQNEKEIIQDILQ 608
|
650 660
....*....|....*....|
gi 30685403 701 K---KSLTDYQIGKTKIFLR 717
Cdd:cd14874 609 GqgvKYENDFKIGTEYVFLR 628
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
75-716 |
1.04e-92 |
|
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: 314.36 E-value: 1.04e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 75 VLRNLETRYELNEIYTYTGNILIAVNPFQRLP---HIYETDMMEQYkgialgelsPHVFAIGDAAYRAMINEGKNNSILV 151
Cdd:cd14881 3 VMKCLQARFYAKEFFTNVGPILLSVNPYRDVGnplTLTSTRSSPLA---------PQLLKVVQEAVRQQSETGYPQAIIL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 152 SGESGAGKTETTKMLMRYL-AFLGGRSGVEGRtveQQVLESNPVLEAFGNAKTLRNNNSSRFGKFVEIQFdKNGRISGAA 230
Cdd:cd14881 74 SGTSGSGKTYASMLLLRQLfDVAGGGPETDAF---KHLAAAFTVLRSLGSAKTATNSESSRIGHFIEVQV-TDGALYRTK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 231 IRTYLLERSRVCQISDPERNYHCFY-LLCAAPPEDIKKYKLE--NPHKFHYLNQSSCYKlDGVDDASEYLETRRAMDVVG 307
Cdd:cd14881 150 IHCYFLDQTRVIRPLPGEKNYHIFYqMLAGLSQEERVKLHLDgySPANLRYLSHGDTRQ-NEAEDAARFQAWKACLGILG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 308 ISNEEqeaIFRVVAAILHLGNIDFGKGEEIDSSVIKDkdsrSHLNMAAELLMCNAQSLEDALIRRVMVTPEEIITRTLDP 387
Cdd:cd14881 229 IPFLD---VVRVLAAVLLLGNVQFIDGGGLEVDVKGE----TELKSVAALLGVSGAALFRGLTTRTHNARGQLVKSVCDA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 388 DNAIASRDTLAKTIYSHLFDWIVNKINT-----SIGQDPRSKSIIGVLDIYGFESFKCNSFEQFCINFTNEKLQQHFNQH 462
Cdd:cd14881 302 NMSNMTRDALAKALYCRTVATIVRRANSlkrlgSTLGTHATDGFIGILDMFGFEDPKPSQLEHLCINLCAETMQHFYNTH 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 463 VFKMEQEEYTKEEIAWSY-IEFIDNQDVLELIEKKPGGIISLLDEACMfPKSTHETFSQKLFQTFKEHERFAKPK-LSRT 540
Cdd:cd14881 382 IFKSSIESCRDEGIQCEVeVDYVDNVPCIDLISSLRTGLLSMLDVECS-PRGTAESYVAKIKVQHRQNPRLFEAKpQDDR 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 541 DFTISHYAGEVTYQSNHFIDKNKDYIVAEHQALFTASNCKFvaGLfhALHEdssrsskfssigSRFKQQLHSLMESLNGT 620
Cdd:cd14881 461 MFGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYKQNCNF--GF--ATHT------------QDFHTRLDNLLRTLVHA 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 621 EPHYIRCIKPNNVLKPGIFENFNVIHQLRCGGVLEAIRISCAGYPTRLAFYDFLDRFGLLAPEVLEGNYDDKVA--CQMI 698
Cdd:cd14881 525 RPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAGGYPHRMRFKAFNARYRLLAPFRLLRRVEEKALedCALI 604
|
650 660
....*....|....*....|....*...
gi 30685403 699 L------DKKSL----TDYQIGKTKIFL 716
Cdd:cd14881 605 LqfleaqPPSKLssvsTSWALGKRHIFL 632
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
75-717 |
2.88e-90 |
|
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: 307.82 E-value: 2.88e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 75 VLRNLETRYELNEIYTYTGNILIAVNPFQRLPhIYETDMMEQYKGIALGELSPHVFAIGDAAYRAMINEGKNNSILVSGE 154
Cdd:cd14882 3 ILEELRHRYLMGESYTFIGDILLSLNPNEIKQ-EYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 155 SGAGKTETTKMLMRYLAFLG-GRSGVEGRtveqqVLESNPVLEAFGNAKTLRNNNSSRFGKFVEIQFDKNGRISGAAIRT 233
Cdd:cd14882 82 SYSGKTTNARLLIKHLCYLGdGNRGATGR-----VESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMSGAIFWM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 234 YLLERSRVCQISDPERNYHCFYLLCAA--PPEDIKKYKLENPHKFHYL-----NQSSCYKL---DGVDDASEYLETRRAM 303
Cdd:cd14882 157 YQLEKLRVSTTDGNQSNFHIFYYFYDFieAQNRLKEYNLKAGRNYRYLrippeVPPSKLKYrrdDPEGNVERYKEFEEIL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 304 DVVGISNEEQEAIFRVVAAILHLGNIDF--GKGE-EIDSSVIKDKdsrshlnmAAELLMCNAQSLEDALIRRVMVTPEEI 380
Cdd:cd14882 237 KDLDFNEEQLETVRKVLAAILNLGEIRFrqNGGYaELENTEIASR--------VAELLRLDEKKFMWALTNYCLIKGGSA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 381 ITRTLDPDNAIASRDTLAKTIYSHLFDWIVNKINTSIGQdPRS----KSIIGVLDIYGFESFKCNSFEQFCINFTNEKLQ 456
Cdd:cd14882 309 ERRKHTTEEARDARDVLASTLYSRLVDWIINRINMKMSF-PRAvfgdKYSISIHDMFGFECFHRNRLEQLMVNTLNEQMQ 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 457 QHFNQHVFKMEQEEYTKEEIAWSYIEFIDNQDVLELIEKKPGGIISLLDEAcmfPKSTHEtfSQKLFQTFKEHER-FAKP 535
Cdd:cd14882 388 YHYNQRIFISEMLEMEEEDIPTINLRFYDNKTAVDQLMTKPDGLFYIIDDA---SRSCQD--QNYIMDRIKEKHSqFVKK 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 536 kLSRTDFTISHYAGEVTYQSNHFIDKNKDYIVAEHQALFTASNCKFVAGLFhalheDSSRSSKFSSIGSRFK----QQLH 611
Cdd:cd14882 463 -HSAHEFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMF-----TNSQVRNMRTLAATFRatslELLK 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 612 SLMESLNGTEPHYIRCIKPNNVLKPGIFENFNVIHQLRCGGVLEAIRISCAGYPTRLAFYDFLDRFGLLAPEVLEGNYDD 691
Cdd:cd14882 537 MLSIGANSGGTHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRIPFQEFLRRYQFLAFDFDETVEMT 616
|
650 660
....*....|....*....|....*.
gi 30685403 692 KVACQMILDKKSLTDYQIGKTKIFLR 717
Cdd:cd14882 617 KDNCRLLLIRLKMEGWAIGKTKVFLK 642
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
74-717 |
5.86e-87 |
|
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: 299.61 E-value: 5.86e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 74 GVLRNLETRYELNEIYTYTGNILIAVNPFQRLPhIYETDMMEQYKGIALGELSPHVFAIGDAAYRAMINEGKNNSILVSG 153
Cdd:cd01386 2 SVLHTLRQRYGANLIHTYAGPSLIVINPRHPLA-VYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 154 ESGAGKTETTKMLMRYLAFLGGRSGveGR-TVEqqVLES-NPVLEAFGNAKTLRNNNSSRFGKFVEIQFDKNGRISGAAI 231
Cdd:cd01386 81 RSGSGKTTNCRHILEYLVTAAGSVG--GVlSVE--KLNAaLTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQLASASI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 232 RTYLLERSRVCQISDPERNYHCFYLLCA-APPEDIKKYKLENPHKFHYLNQSSCYKL-DGVDDASEYLETRRAMDVVGIS 309
Cdd:cd01386 157 QTLLLERSRVARRPEGESNFNVFYYLLAgADAALRTELHLNQLAESNSFGIVPLQKPeDKQKAAAAFSKLQAAMKTLGIS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 310 NEEQEAIFRVVAAILHLGNIdfgkGEEIDSSVIKDKDSR-SHLNMAAELLMCNAQSLEDALIRRVMV-------TPEEII 381
Cdd:cd01386 237 EEEQRAIWSILAAIYHLGAA----GATKAASAGRKQFARpEWAQRAAYLLGCTLEELSSAIFKHHLSggpqqstTSSGQE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 382 TRTLDPD-----NAIASRDTLAKTIYSHLFDWIVNKINTSIGQDPRSKSIIGVLDIYGFESFKCN------SFEQFCINF 450
Cdd:cd01386 313 SPARSSSggpklTGVEALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSSITIVDTPGFQNPAHSgsqrgaTFEDLCHNY 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 451 TNEKLQQHFNQHVFKMEQEEYTKE--EIAWSYIEFIDNQDVlELIEKKP--------------GGIISLLDEACMFPKST 514
Cdd:cd01386 393 AQERLQLLFHERTFVAPLERYKQEnvEVDFDLPELSPGALV-ALIDQAPqqalvrsdlrdedrRGLLWLLDEEALYPGSS 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 515 HETFSQKLF-----QTFKEHERFAKPKLSRTDFTISHYAG--EVTYQSNHFIDKNKDYIVAEHQ-ALFTASNCKFVAglf 586
Cdd:cd01386 472 DDTFLERLFshygdKEGGKGHSLLRRSEGPLQFVLGHLLGtnPVEYDVSGWLKAAKENPSAQNAtQLLQESQKETAA--- 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 587 halhedssrsSKFSSIGSRFKQQLHSLMESLNGTEPHYIRCIKPN-----NVLKPGIFEN----FNVI---HQLRCGGVL 654
Cdd:cd01386 549 ----------VKRKSPCLQIKFQVDALIDTLRRTGLHFVHCLLPQhnagkDERSTSSPAAgdelLDVPllrSQLRGSQLL 618
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30685403 655 EAIRISCAGYPTRLAFYDFLDRFGLLAPEV---LEGNY---DDKVACQMIL-----DKKSltdYQIGKTKIFLR 717
Cdd:cd01386 619 DALRLYRQGFPDHMPLGEFRRRFQVLAPPLtkkLGLNSevaDERKAVEELLeeldlEKSS---YRIGLSQVFFR 689
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
79-717 |
2.23e-82 |
|
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: 285.83 E-value: 2.23e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 79 LETRYELNEIYTYTGNILIAVNPFQRLPHIYETDMMEQYKgiALGELSPHVFAIGDAAYRAMINEGKNNSILVSGESGAG 158
Cdd:cd14905 7 IQARYKKEIIYTYIGPILVSVNPLRYLPFLHSQELVRNYN--QRRGLPPHLFALAAKAISDMQDFRRDQLIFIGGESGSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 159 KTETTKMLMRYLAFLG-GRSgvegRTVEQQVLESNPVLEAFGNAKTLRNNNSSRFGKFVEIQFDKNGRISGAAIRTYLLE 237
Cdd:cd14905 85 KSENTKIIIQYLLTTDlSRS----KYLRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQGAKLYSYFLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 238 RSRVCQISDPERNYHCFY-LLCAAPPEDIKKYKLENPHKFHYLNQSSCYKLDGVDDASEYLETRRAMDVVGISNEEQEAI 316
Cdd:cd14905 161 ENRVTYQNKGERNFHIFYqFLKGITDEEKAAYQLGDINSYHYLNQGGSISVESIDDNRVFDRLKMSFVFFDFPSEKIDLI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 317 FRVVAAILHLGNIDF----GKGEEIDSSVIkdkDSRSHlnmaaeLLMCNAQSLEDALIRrvmvtpeeiiTRTLDPDNAIA 392
Cdd:cd14905 241 FKTLSFIIILGNVTFfqknGKTEVKDRTLI---ESLSH------NITFDSTKLENILIS----------DRSMPVNEAVE 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 393 SRDTLAKTIYSHLFDWIVNKINTSIGQDPRSKSiIGVLDIYGFESFKCNSFEQFCINFTNEKLQQHFNQHVFKMEQEEYT 472
Cdd:cd14905 302 NRDSLARSLYSALFHWIIDFLNSKLKPTQYSHT-LGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVLKQEQREYQ 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 473 KEEIAW-SYIEFIDNQDVLELIEKkpggIISLLDEACMFPKSTHETFSQKLFQTFKEHERFAKPKlsrTDFTISHYAGEV 551
Cdd:cd14905 381 TERIPWmTPISFKDNEESVEMMEK----IINLLDQESKNINSSDQIFLEKLQNFLSRHHLFGKKP---NKFGIEHYFGQF 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 552 TYQSNHFIDKNKDYIVAEHQALFTASNCKFV---AGLF--HALHEDSSRSSKFSSIGSRFKQQLHSLMESLNGTEP---- 622
Cdd:cd14905 454 YYDVRGFIIKNRDEILQRTNVLHKNSITKYLfsrDGVFniNATVAELNQMFDAKNTAKKSPLSIVKVLLSCGSNNPnnvn 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 623 -------------------------------------------HYIRCIKPNNVLKPGIFENFNVIHQLRCGGVLEAIRI 659
Cdd:cd14905 534 npnnnsgggggggnsgggsgsggstyttysstnkainnsncdfHFIRCIKPNSKKTHLTFDVKSVNEQIKSLCLLETTRI 613
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30685403 660 SCAGYPTRLAFYDFLDRFGLLapevlegnYDDKVACQMILDKKSLTD----------YQIGKTKIFLR 717
Cdd:cd14905 614 QRFGYTIHYNNKIFFDRFSFF--------FQNQRNFQNLFEKLKENDinidsilpppIQVGNTKIFLR 673
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
76-716 |
1.51e-71 |
|
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: 255.67 E-value: 1.51e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 76 LRNLETRYELNEIYTYTGNILIAVNPFQRLPhIYETDMMEQY----------KGIALGELSPHVFAIGDAAYRAMINEGK 145
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLP-IYTPDHMQAYnksreqtplyEKDTVNDAPPHVFALAQNALRCMQDAGE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 146 NNSILVSGESGAGKTETTKMLMRYLAFLG----------GRSGVeGRTVEQQVLESNPVLEAFGNAKTLRNNNSSRFGKF 215
Cdd:cd14893 83 DQAVILLGGMGAGKSEAAKLIVQYLCEIGdeteprpdseGASGV-LHPIGQQILHAFTILEAFGNAATRQNRNSSRFAKM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 216 VEIQFDKNGRISGAAIRTYLLERSRVCQISDPERNYHCFYLLCAAPPEDIK-KYKLE---NPHKFHYLNQSSCYKLDGVD 291
Cdd:cd14893 162 ISVEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQHDPTlRDSLEmnkCVNEFVMLKQADPLATNFAL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 292 DASEYLETRRAMDVVGISNEEQEAIFRVVAAILHLGNIDFGKGEEIDSSVIK-DKDSRSH-----------LNMAAELLM 359
Cdd:cd14893 242 DARDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFVPDPEGGKSVGGaNSTTVSDaqscalkdpaqILLAAKLLE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 360 CNAQSLEDALIRRVMVTPEEIIT----RTLDPDNAIASRDTLAKTIYSHLFDWIVNKINTSIGQ--DPRSKSII------ 427
Cdd:cd14893 322 VEPVVLDNYFRTRQFFSKDGNKTvsslKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILGGifDRYEKSNIvinsqg 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 428 -GVLDIYGFESFKC--NSFEQFCINFTNEKLQQHFNQHVFKMEQEEYTKEEIAW-------SYIEFIDNQD-VLELIEKK 496
Cdd:cd14893 402 vHVLDMVGFENLTPsqNSFDQLCFNYWSEKVHHFYVQNTLAINFSFLEDESQQVenrltvnSNVDITSEQEkCLQLFEDK 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 497 PGGIISLLDEACMFPKSTHETFSQKLFQTFKE--------------HERFAKPKLSRTDFTISHYAGEVTYQSNHFIDKN 562
Cdd:cd14893 482 PFGIFDLLTENCKVRLPNDEDFVNKLFSGNEAvgglsrpnmgadttNEYLAPSKDWRLLFIVQHHCGKVTYNGKGLSSKN 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 563 KDYIVAEHQALFTASNckfvAGLFHAL-----------------HEDSSRSSKFSSIGSRFKQ--------------QLH 611
Cdd:cd14893 562 MLSISSTCAAIMQSSK----NAVLHAVgaaqmaaassekaakqtEERGSTSSKFRKSASSAREsknitdsaatdvynQAD 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 612 SLMESLNGTEPHYIRCIKPNNVLKPGIFENFNVIHQLRCGGVLEAIRISCAGYPTRLAFYDFLDRFGLLAPE--VLEGNY 689
Cdd:cd14893 638 ALLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRYKNVCGHrgTLESLL 717
|
730 740
....*....|....*....|....*..
gi 30685403 690 DDKVACQMILDKKsltdYQIGKTKIFL 716
Cdd:cd14893 718 RSLSAIGVLEEEK----FVVGKTKVYL 740
|
|
| Myo5-like_CBD |
cd14945 |
Cargo binding domain of myosin 5 and similar proteins; Class V myosins are well studied ... |
1103-1462 |
1.43e-69 |
|
Cargo binding domain of myosin 5 and similar proteins; Class V myosins are well studied unconventional myosins, represented by three paralogs (Myo5 a,b,c) in vertebrates and two (myo2 and myo4) in fungi and related to plant class XI myosins. Their C-terminal cargo binding domains is important for the binding of a diverse set of cargos, including membrane vesicles, organelles, proteins and mRNA. MyoV-CBDs interact with several adaptor proteins that in turn interact with the cargo.
Pssm-ID: 271253 [Multi-domain] Cd Length: 288 Bit Score: 235.76 E-value: 1.43e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 1103 ENQELLLKSISEDIGFSEG--KPVAACLIYKCLIHWRSF--EVERTSIFNRIIETIASAIEMQENSDVLC-YWLSNSATL 1177
Cdd:cd14945 1 SEEDSLLRGIVTDFEPSSGdhKLTPAYILYLCIRHAASNglTGQSTSLLNKVLKTIQQVVQQHNDDMQLLaFWLSNASEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 1178 LMFLQRTLKAgatgsittprrrgmpsslfgrvsqsfrgspqsagfpfmTGRAIGGGLDELRQVEAKYPALLFKQQLTAFL 1257
Cdd:cd14945 81 LYFLKQDSKL--------------------------------------YGAAGEAPQKEEEQKLTVSDLNELKQDLEAVS 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 1258 EKIYGMIRDKMKKEISPllasciqvprtprsglvkgrsqntqnnvvapkpmiaHWQNIVTCLNGHLRTMRANYVPSLLIS 1337
Cdd:cd14945 123 IKIYQQALKYLNKNLQP------------------------------------KIRDIVKFLNSFLDLLKSFHVHPEIRS 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 1338 KVFGQIFSFINVQLFNSLLLRRECCSFSNGEYVKTGLAELEKWCHDATEEfvGSAWDELKHIRQAVGFLVIHQKPKKSLk 1417
Cdd:cd14945 167 QVFTQLFSFINARLFNQLITKKDALSWSRGMQIRANISRLEEWCEGRGLE--HLAVDFLSKLIQAVQLLQLKKYTQEDI- 243
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 30685403 1418 EITTELCPVLSIQQLYRISTMYWDDKYGTHSVSTEVIATMRAEVS 1462
Cdd:cd14945 244 EILCELCPSLNPAQLQAILTQYQPANYGESPVPKEILRTLAAEVS 288
|
|
| MYSc_Myo24B |
cd14938 |
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
73-716 |
3.29e-56 |
|
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a coiled-coil region in their C-terminal tail. The functions of these myosins remain elusive. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276898 [Multi-domain] Cd Length: 713 Bit Score: 209.31 E-value: 3.29e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 73 PGVLRNLETRYELNEIYTYTGNILIAVNPFQRLpHIYETDMMEQYKGI-ALGELSPHVFAIGDAAYRAMINEGKNNSILV 151
Cdd:cd14938 1 PSVLYHLKERFKNNKFYTKMGPLLIFINPKINN-NINNEETIEKYKCIdCIEDLSLNEYHVVHNALKNLNELKRNQSIII 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 152 SGESGAGKTETTKMLMRYLAF--LGGRSGVEGRTVEQQVLES------------------NPVLEAFGNAKTLRNNNSSR 211
Cdd:cd14938 80 SGESGSGKSEIAKNIINFIAYqvKGSRRLPTNLNDQEEDNIHneentdyqfnmsemlkhvNVVMEAFGNAKTVKNNNSSR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 212 FGKFVEIQFDkNGRISGAAIRTYLLERSRVCQISDPERNYHCFYLLCAAPPEDIKK-YKLENPHKFHYLNQSSCYKLDGv 290
Cdd:cd14938 160 FSKFCTIHIE-NEEIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKmYFLKNIENYSMLNNEKGFEKFS- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 291 DDASEYLETRRAMDVVGISNEEQEAIFRVVAAILHLGNIDFGKG-------------------EEIDSSVIKDKDSRSHL 351
Cdd:cd14938 238 DYSGKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNTEIVKAfrkksllmgknqcgqninyETILSELENSEDIGLDE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 352 NMAAELLMCNAQSLEDALIRRVMVTP---EEIITRTLDPDNAIASR-DTLAKTIYSHLFDWIVNKINTSIGQDPR---SK 424
Cdd:cd14938 318 NVKNLLLACKLLSFDIETFVKYFTTNyifNDSILIKVHNETKIQKKlENFIKTCYEELFNWIIYKINEKCTQLQNiniNT 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 425 SIIGVLDIYGFESFKCNSFEQFCINFTNEKLQQHFNQHVFKMEQEEYTKEEIAWSY-IEFIDNQDVLE-LIEKKPGGIIS 502
Cdd:cd14938 398 NYINVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYnSENIDNEPLYNlLVGPTEGSLFS 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 503 LLDEAC---MFPKSTHETFSQKLFQTFKEHERFAKPKLSRTDFTISHYAGEVTYQSNHFIDKNKDYIVAEHQALFTASNC 579
Cdd:cd14938 478 LLENVStktIFDKSNLHSSIIRKFSRNSKYIKKDDITGNKKTFVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQSEN 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 580 KFVAGLFHALHEDSS----RSSKFSSIGSRFK------------------QQLHSLMESLNGTEPHYIRCIKPN-NVLKP 636
Cdd:cd14938 558 EYMRQFCMFYNYDNSgnivEEKRRYSIQSALKlfkrrydtknqmavsllrNNLTELEKLQETTFCHFIVCMKPNeSKREL 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 637 GIFENFNVIHQLRCGGVLEAIRISCAGYPTRLAFYDFLDRFGLLapevlegNYDDKVACQMILDKKSLTDYQ--IGKTKI 714
Cdd:cd14938 638 CSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIK-------NEDLKEKVEALIKSYQISNYEwmIGNNMI 710
|
..
gi 30685403 715 FL 716
Cdd:cd14938 711 FL 712
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
95-221 |
5.19e-38 |
|
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: 140.56 E-value: 5.19e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 95 ILIAVNPFQRLPHIYETDMMEQYKGIALGELSPHVFAIGDAAYRAMInEGKNN-SILVSGESGAGKTETTKMLMRYLAFL 173
Cdd:cd01363 1 VLVRVNPFKELPIYRDSKIIVFYRGFRRSESQPHVFAIADPAYQSML-DGYNNqSIFAYGESGAGKTETMKGVIPYLASV 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 174 GGR----------SGVEGRTV--EQQVLESNPVLEAFGNAKTLRNNNSSRFGKFVEIQFD 221
Cdd:cd01363 80 AFNginkgetegwVYLTEITVtlEDQILQANPILEAFGNAKTTRNENSSRFGKFIEILLD 139
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
79-683 |
4.05e-35 |
|
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: 145.66 E-value: 4.05e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 79 LETRYELNEIYTYTGNILIAV-NPFQ-----RLPHIYETDMMEQYKGIALGE--LSPHVFAIGD---------------- 134
Cdd:cd14894 7 LTSRFDDDRIYTYINHHTMAVmNPYRllqtaRFTSIYDEQVVLTYADTANAEtvLAPHPFAIAKqslvrlffdnehtmpl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 135 ----AAYRAMiNEGKNNSILVSGESGAGKTETTKMLMRYLAFLG-----------------------------GRSGVEG 181
Cdd:cd14894 87 pstiSSNRSM-TEGRGQSLFLCGESGSGKTELAKDLLKYLVLVAqpalskgseetckvsgstrqpkiklftssTKSTIQM 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 182 RTVEQQ-------------------------------------------------------------------------- 187
Cdd:cd14894 166 RTEEARtialleakgvekyeivlldlhperwdemtsvsrskrlpqvhvdglffgfyeklehledeeqlrmyfknphaakk 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 188 ---VLESNPVLEAFGNAKTLRNNNSSRFGKFVEIQF-----DKNGRISGAAIRTYLLERSRVCQI------SDPERNYHC 253
Cdd:cd14894 246 lsiVLDSNIVLEAFGHATTSMNLNSSRFGKMTTLQVafglhPWEFQICGCHISPFLLEKSRVTSErgresgDQNELNFHI 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 254 FYLLCAA----PPEDIKKYKLE----NPHKFHYLNQSScYKLDGV--------DDASEYLETRRAMDVVGISNEEQEAIF 317
Cdd:cd14894 326 LYAMVAGvnafPFMRLLAKELHldgiDCSALTYLGRSD-HKLAGFvskedtwkKDVERWQQVIDGLDELNVSPDEQKTIF 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 318 RVVAAILHLGNIDFGKGEEIDSSVIKDKDSRSHLNMAAELL-MCNAQSLEDALIRR--VMVTPEEIITRTLDPDNAIASR 394
Cdd:cd14894 405 KVLSAVLWLGNIELDYREVSGKLVMSSTGALNAPQKVVELLeLGSVEKLERMLMTKsvSLQSTSETFEVTLEKGQVNHVR 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 395 DTLAKTIYSHLFDWIVNKIN-----TSIGQD------------PRSKSIIGVLDIYGFESFKCNSFEQFCINFTNEKLqq 457
Cdd:cd14894 485 DTLARLLYQLAFNYVVFVMNeatkmSALSTDgnkhqmdsnasaPEAVSLLKIVDVFGFEDLTHNSLDQLCINYLSEKL-- 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 458 hfnqhvfkmeqeeYTKEE--IAWSY------IEFIDNQDVLeLIEKKPGGIISLLDEACMFPKSTHETFSQ-----KLF- 523
Cdd:cd14894 563 -------------YAREEqvIAVAYssrphlTARDSEKDVL-FIYEHPLGVFASLEELTILHQSENMNAQQeekrnKLFv 628
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 524 ---------------QTFKEHERFAKPKLSRTDFTISHYAGEVTYQSNHFIDKNKDYIVAEHQ-ALFTASNCKFVAGLFH 587
Cdd:cd14894 629 rniydrnssrlpeppRVLSNAKRHTPVLLNVLPFVIPHTRGNVIYDANDFVKKNSDFVYANLLvGLKTSNSSHFCRMLNE 708
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 588 ALHEDSSRSSKFSSIGS-------------RFKQQLHSLMESLNGTEPHYIRCIKPNNVLKPGIFENFNVIHQLRCGGV- 653
Cdd:cd14894 709 SSQLGWSPNTNRSMLGSaesrlsgtksfvgQFRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCRSQRLi 788
|
810 820 830
....*....|....*....|....*....|...
gi 30685403 654 --LEAIRISCAGYPT-RLAFYDFLDRFGLLAPE 683
Cdd:cd14894 789 rqMEICRNSSSSYSAiDISKSTLLTRYGSLLRE 821
|
|
| DIL |
pfam01843 |
DIL domain; The DIL domain has no known function. |
1338-1442 |
3.23e-34 |
|
DIL domain; The DIL domain has no known function.
Pssm-ID: 460359 [Multi-domain] Cd Length: 103 Bit Score: 126.94 E-value: 3.23e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 1338 KVFGQIFSFINVQLFNSLLLRRECCSFSNGEYVKTGLAELEKWCHDAteEFVGSAWDELKHIRQAVGFLVIHQKPKKSLK 1417
Cdd:pfam01843 1 QLFSQLFYFINAELFNRLLLRKKYCSWSKGMQIRYNLSRLEEWARSN--GLESEARDHLAPLIQAAQLLQLRKSTLEDLD 78
|
90 100
....*....|....*....|....*
gi 30685403 1418 EItTELCPVLSIQQLYRISTMYWDD 1442
Cdd:pfam01843 79 SI-LQVCPALNPLQLHRLLTLYQPD 102
|
|
| Myo5_CBD |
cd15470 |
Cargo binding domain of myosin 5; Class V myosins are well studied unconventional myosins, ... |
1311-1439 |
1.04e-11 |
|
Cargo binding domain of myosin 5; Class V myosins are well studied unconventional myosins, represented by three paralogs (Myo5a,b,c) in vertebrates. Their C-terminal cargo binding domains (CBDs) are important for the binding of a diverse set of cargos, including membrane vesicles, organelles, proteins and mRNA. The MyoV-CBDs directly interact with several adaptor proteins, in case of Myo5a, melanophilin (MLPH), Rab interacting lysosomal protein-like 2 (RILPL2), and granuphilin, and in case of Myo5b, Rab11-family interacting protein 2.
Pssm-ID: 271254 [Multi-domain] Cd Length: 332 Bit Score: 68.01 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 1311 HWQNIVTCLNGHLRTMRANYVPSLLISKVFGQIFSFINVQLFNSLLLRRECCSFSNGEYVKTGLAELEKWCHDATEEFVG 1390
Cdd:cd15470 142 TLDSLLQQLNSFHTTLTQHGLDPELIKQVFRQLFYLICASTLNNLLLRKDLCSWSKGMQIRYNVSQLEEWLRDKGLQDSG 221
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 30685403 1391 sAWDELKHIRQAVGFLvihQKPKKSLKEITT--ELCPVLSIQQLYRISTMY 1439
Cdd:cd15470 222 -ARETLEPLIQAAQLL---QVKKTTEEDAQSicEMCTKLTTAQIVKILNLY 268
|
|
| Myosin_N |
pfam02736 |
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ... |
8-47 |
1.20e-10 |
|
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: 57.83 E-value: 1.20e-10
10 20 30 40
....*....|....*....|....*....|....*....|
gi 30685403 8 VGSHVWVEDPHLAWIDGEVTRIDGINVHVKTKKGKTVVTN 47
Cdd:pfam02736 2 AKKLVWVPDPKEGFVKGEIKEEEGDKVTVETEDGKTVTVK 41
|
|
| fMyo2p_CBD |
cd15480 |
cargo binding domain of fungal myosin 2; Yeast myosin V travels along actin cables, actin ... |
1314-1483 |
2.62e-09 |
|
cargo binding domain of fungal myosin 2; Yeast myosin V travels along actin cables, actin filaments that are bundled by fimbrin, in the presence of tropomyosin. This is in contrast to the other vertebrate class V myosins. Like other class V myosins, fungal myosin 2 and 4 contain a C-terminal cargo binding domain. Myo 2 binds to Vac17, vacuole-specific cargo adaptor, and Mmr1, mitochondria-specific cargo adaptor. Both adaptors bind competitivly at the same site.
Pssm-ID: 271264 Cd Length: 363 Bit Score: 61.05 E-value: 2.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 1314 NIVTCLNGHLRTMRANYVPSLLISKVFGQIFSFINVQLFNSLLLRRECCSFSNGEYVKTGLAELEKWC--HDATEefvGS 1391
Cdd:cd15480 170 DILNFFNKVYKSMKSYYIEESVIRQVVTELLKLIGVTAFNDLLMRRNFLSWKRGLQINYNITRLEEWCksHDIPE---GT 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 1392 awDELKHIRQAVGFLvihQKPKKSLK--EITTELCPVLSIQQLYRISTMYWDDKYgTHSVSTEVIATMRAEVSDVSKSAI 1469
Cdd:cd15480 247 --LQLEHLMQATKLL---QLKKATLEdiEIIYDVCWILTPAQIQKLISQYYVADY-ENPISPEILKAVAARVKPEDKSDH 320
|
170
....*....|....
gi 30685403 1470 SNSFLLDDDSSiPF 1483
Cdd:cd15480 321 LLLIPLVEEVG-PF 333
|
|
| Myo5b_CBD |
cd15477 |
Cargo binding domain of myosin 5b; Class V myosins are well studied unconventional myosins, ... |
1335-1439 |
7.50e-09 |
|
Cargo binding domain of myosin 5b; Class V myosins are well studied unconventional myosins, represented by three paralogs (Myo5a,b,c) in vertebrates. Their C-terminal cargo binding domains (CBDs) are important for the binding of a diverse set of cargos, including membrane vesicles, organelles, proteins and mRNA. They interact with several adaptor proteins, in case of Myo5b-CBD, Rab11-family interacting protein 2.
Pssm-ID: 271261 Cd Length: 372 Bit Score: 59.49 E-value: 7.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 1335 LISKVFGQIFSFINVQLFNSLLLRRECCSFSNGEYVKTGLAELEKWCHDATEEFVGSAwDELKHIRQAVGFLVIHQKPKK 1414
Cdd:cd15477 204 IIQQVFKQLFYMINAVTLNNLLLRKDVCSWSTGMQLRYNISQLEEWLRGRNLHQSGAA-QTMEPLIQAAQLLQLKKKTSE 282
|
90 100
....*....|....*....|....*
gi 30685403 1415 SLKEITTeLCPVLSIQQLYRISTMY 1439
Cdd:cd15477 283 DAEAICS-LCTALSTQQIVKILNLY 306
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
868-1047 |
2.77e-07 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 54.15 E-value: 2.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 868 RRELRMLKMAARDTGALKDAKNKLEQRVEelslrlHLEKRLRT---DLEEAK--VQEVAKLQEALHTMRLQLKETTAMVV 942
Cdd:COG1340 91 REELDELRKELAELNKAGGSIDKLRKEIE------RLEWRQQTevlSPEEEKelVEKIKELEKELEKAKKALEKNEKLKE 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 943 KEQEAARVAiEEASSVNKEpvVVEDTEKIDSLSNEIDRLKGLLSSETHKADEAQHayqsalvQNEELCKKLEEAGRKIDQ 1022
Cdd:COG1340 165 LRAELKELR-KEAEEIHKK--IKELAEEAQELHEEMIELYKEADELRKEADELHK-------EIVEAQEKADELHEEIIE 234
|
170 180
....*....|....*....|....*
gi 30685403 1023 LQDSVQRFQEKVFSLESENKVLRQQ 1047
Cdd:COG1340 235 LQKELRELRKELKKLRKKQRALKRE 259
|
|
| Myo5p-like_CBD_fungal |
cd15474 |
cargo binding domain of fungal myosin V -like proteins; Yeast myosin V travels along actin ... |
1250-1439 |
5.03e-07 |
|
cargo binding domain of fungal myosin V -like proteins; Yeast myosin V travels along actin cables, actin filaments that are bundled by fimbrin, in the presence of tropomyosin. This is in contrast to the other vertebrate class V myosins. Like other class V myosins, fungal myosin 2 and 4 contain a C-terminal cargo binding domain. In case of Myo4 it has been shown to bind to the adapter protein She3p (Swi5p-dependent HO expression 3), which in turn anchors myosin 4 to its cargos, zip-coded mRNP (messenger ribonucleoprotein particles) and tER (tubular endoplasmic reticulum). Myo 2 binds to Vac17, vacuole-specific cargo adaptor, and Mmr1, mitochondria-specific cargo adaptor. Both adaptors bind competitivly at the same site.
Pssm-ID: 271258 Cd Length: 352 Bit Score: 53.58 E-value: 5.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 1250 KQQLTAFLEKIYGMIRDKMKKEISPLLASCIQVprtprSGLVKGRSQNTQNNVVAPKPMIAHWQNIVTCLNGHLRTMRAN 1329
Cdd:cd15474 124 FDKTLKHLSNIYSTWIDKLNKHLSPKIEGAVLV-----LLTSLDLSELIDLNKEFFNKPKKKMADLITFLNEVYDLLQSF 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 1330 YVPSLLISKVFGQIFSFINVQLFNSLLLRRECCSFSNGEYVKTGLAELEKWCHdatEEFVGSAWDELKHIRQAVGFLVIH 1409
Cdd:cd15474 199 SVQPELLNAIVSSTLQYINVEAFNSLITKRSALSWKRGSQISYNVSRLKEWCH---QHGLSDANLQLEPLIQASKLLQLR 275
|
170 180 190
....*....|....*....|....*....|
gi 30685403 1410 QKPKKSLKEITTeLCPVLSIQQLYRISTMY 1439
Cdd:cd15474 276 KDDENDFKIILS-VCYALNPAQIQKLLDKY 304
|
|
| Myo5a_CBD |
cd15478 |
Cargo binding domain of myosin 5a; Class V myosins are well studied unconventional myosins, ... |
1335-1497 |
9.28e-07 |
|
Cargo binding domain of myosin 5a; Class V myosins are well studied unconventional myosins, represented by three paralogs (Myo5a,b,c) in vertebrates. Their C-terminal cargo binding domains (CBDs) are important for the binding of a diverse set of cargos, including membrane vesicles, organelles, proteins and mRNA. They interact with several adaptor proteins, in case of Myo5a-CBD, melanophilin (MLPH), Rab interacting lysosomal protein-like 2 (RILPL2), and granuphilin. Mutations in human Myo5a (many of which map to the cargo binding domain) lead to Griscelli syndrome, a severe neurological disease.
Pssm-ID: 271262 Cd Length: 375 Bit Score: 53.11 E-value: 9.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 1335 LISKVFGQIFSFINVQLFNSLLLRRECCSFSNGEYVKTGLAELEKWCHDATEEFVGsAWDELKHIRQAVGFLVIHQKPKK 1414
Cdd:cd15478 204 LIKQVVKQMFYIIGAITLNNLLLRKDMCSWSKGMQIRYNVSQLEEWLRDKNLMNSG-AKETLEPLIQAAQLLQVKKKTDD 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 1415 SLKEITTeLCPVLSIQQLYRISTMYWDDKYGTHSVSTEVIATMRAEVSDVSKSAisnSFLLDDDSSIP--FSLDDISKSM 1492
Cdd:cd15478 283 DAEAICS-MCNALTTAQIVKVLNLYTPVNEFEERVSVSFIRTIQMRLRDRKDSP---QLLMDAKHIFPvtFPFNPSSLAL 358
|
....*
gi 30685403 1493 QNVEV 1497
Cdd:cd15478 359 ETIQI 363
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
829-1124 |
1.86e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.84 E-value: 1.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 829 RKAAIVLQAHWRGRQAFSYYTRLQKAAIVTQC--AWRCRLARRELRMLKMAARDTGALKDAKNKLEQRVEELSLRLHLEK 906
Cdd:PTZ00121 1558 KKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAeeARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQ 1637
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 907 RLRTDLEEA-KVQEVAKLQEALHTMRLQLKEttamvvKEQEAARVAIEEASSVNKEPVVVEDTEKIDSLSNEIDRLKGLL 985
Cdd:PTZ00121 1638 LKKKEAEEKkKAEELKKAEEENKIKAAEEAK------KAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKE 1711
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 986 SSETHKADEAQHAYQSALVQNEELCKKLEEAGRKIDQLQDSVQRfQEKVFSLESENKVLRQQTLTISPTTRALALRPKTT 1065
Cdd:PTZ00121 1712 AEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEE-KKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDE 1790
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30685403 1066 IIQRTPE---KDTFSNGETtqLQEPETEDRPQKSlNQKQQENQELLLKSISEDIGFSEGKPV 1124
Cdd:PTZ00121 1791 KRRMEVDkkiKDIFDNFAN--IIEGGKEGNLVIN-DSKEMEDSAIKEVADSKNMQLEEADAF 1849
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
824-1114 |
2.52e-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: 2.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 824 RLRRQRKAAivlqahwrgRQafsyYTRLQKAAivtqcawrcRLARRELRMLKMAArdtgaLKDAKNKLEQRVEELSLRLh 903
Cdd:COG1196 204 PLERQAEKA---------ER----YRELKEEL---------KELEAELLLLKLRE-----LEAELEELEAELEELEAEL- 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 904 lekrlrtdleEAKVQEVAKLQEALHTMRLQLKETTAMVVKEQEAARVAIEEASSVNKEpvVVEDTEKIDSLSNEIDRLKG 983
Cdd:COG1196 256 ----------EELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD--IARLEERRRELEERLEELEE 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 984 LLSSETHKADEAQHAYQSALVQNEELCKKLEEAGRKIDQLQDSVQRFQEKVFSLESENKVLRQQTLTISPTTRALA---L 1060
Cdd:COG1196 324 ELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAaqlE 403
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 30685403 1061 RPKTTIIQRTPEKDTFSNGETTQLQEPETEDRPQKSLNQKQQENQELLLKSISE 1114
Cdd:COG1196 404 ELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
722-1032 |
1.54e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.94 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 722 AELDARRAEVLGNAARVIQRQFRTCMAR-KNYRSIRNAAIVLQSFLRGEIARAVHKKLRIEAAALRVQknfRRYVDRKSF 800
Cdd:COG1196 538 AALEAALAAALQNIVVEDDEVAAAAIEYlKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVA---SDLREADAR 614
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 801 VTTRSSTIVLQTGLRAMIARSEFRLRRQRKAAIVLQAHWRGRQAFSYYTRLQKAAIVTqcawrcRLARRELRMLKMAARD 880
Cdd:COG1196 615 YYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLA------ALLEAEAELEELAERL 688
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 881 TGALKDAKNKLEQRVEELSLRLHLEKRLRTDLEEAKVQEVAKLQEALHTMRLQLKEttamvvkEQEAARVAIEEAssvnk 960
Cdd:COG1196 689 AEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEE-------EELLEEEALEEL----- 756
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 961 epvvvEDTEKIDSLSNEIDRLKG---------LLSSETHKADEAQHAYQSAlvQNEELC---KKLEEAGRKIDQLqdSVQ 1028
Cdd:COG1196 757 -----PEPPDLEELERELERLEReiealgpvnLLAIEEYEELEERYDFLSE--QREDLEearETLEEAIEEIDRE--TRE 827
|
....
gi 30685403 1029 RFQE 1032
Cdd:COG1196 828 RFLE 831
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
865-1060 |
1.74e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.38 E-value: 1.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 865 RLARRELRMLKMAARDTGALKDAKNKLEQRVEELSLRLHLEKRLRTDLEEAK-----VQEVAKLQEALHTMRLQLKETTA 939
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLqllplYQELEALEAELAELPERLEELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 940 MvVKEQEAARVAIEEASsvnkepvvvedtEKIDSLSNEIDRLKGLLSSETHKA-DEAQHAYQSALVQNEELCKKLEEAGR 1018
Cdd:COG4717 154 R-LEELRELEEELEELE------------AELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQE 220
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 30685403 1019 KIDQLQDSVQRFQEKVFSLESENKVLRQQTLTISPTTRALAL 1060
Cdd:COG4717 221 ELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALL 262
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
822-955 |
3.09e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 48.41 E-value: 3.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 822 EFRLRRQRkaaivlQAHWRGRQAFSYYTR-LQKAAIVTQCAWRCRLARRELRMLKMAARDTGALKDAKNKleQRVEELSL 900
Cdd:pfam15709 388 EIRLRKQR------LEEERQRQEEEERKQrLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAEAEK--QRQKELEM 459
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 30685403 901 RLHLE-KRLRTDLEEAKVQEVAKLQEALHTMRLQLKETTAmvvKEQEAARVAIEEA 955
Cdd:pfam15709 460 QLAEEqKRLMEMAEEERLEYQRQKQEAEEKARLEAEERRQ---KEEEAARLALEEA 512
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
863-1040 |
3.21e-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: 48.90 E-value: 3.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 863 RCRLARRELRMLKMAARDtgaLKDAKNKLEQRVEELSLRLHLEKRLRTDLEEAKVQ----------EVAKLQEALHTMRL 932
Cdd:TIGR02168 797 ELKALREALDELRAELTL---LNEEAANLRERLESLERRIAATERRLEDLEEQIEElsedieslaaEIEELEELIEELES 873
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 933 QLKETTAMVVKEQEAARVAIEEASSVnkepvvvedTEKIDSLSNEIDRLKGLLSSETHKADEAQHAYQSALVQNEELCKK 1012
Cdd:TIGR02168 874 ELEALLNERASLEEALALLRSELEEL---------SEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQER 944
|
170 180 190
....*....|....*....|....*....|....*.
gi 30685403 1013 L--------EEAGRKIDQLQDSVQRFQEKVFSLESE 1040
Cdd:TIGR02168 945 LseeysltlEEAEALENKIEDDEEEARRRLKRLENK 980
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
721-1047 |
3.62e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.39 E-value: 3.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 721 MAELDARRaEVLGNAARViqrqfrtcmARKnYRSIRNAAIVLQSFLRGEIARAVHKKLRIEAAALRVQKNfrryvdrksf 800
Cdd:COG1196 195 LGELERQL-EPLERQAEK---------AER-YRELKEELKELEAELLLLKLRELEAELEELEAELEELEA---------- 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 801 vtTRSSTIVLQTGLRAMIARSEFRLRRQRKAAIVLQAHWRGRQAfsyytrlQKAAIVTQCAwrcRLARRELRMLKMAARD 880
Cdd:COG1196 254 --ELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA-------ELARLEQDIA---RLEERRRELEERLEEL 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 881 TGALKDAKNKLEQ---RVEELSLRLHLEKRLRTDLEEAKVQEVAKLQEALHTMRLQLKETTAMVVKEQEAARVAIEEASS 957
Cdd:COG1196 322 EEELAELEEELEEleeELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 958 V-NKEPVVVEDTEKIDSLSNEIDRLKGLLSSETHKADEAQHAYQSALVQNEELCKKLEEAGRKIDQLQDSVQRFQEKVFS 1036
Cdd:COG1196 402 LeELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
|
330
....*....|.
gi 30685403 1037 LESENKVLRQQ 1047
Cdd:COG1196 482 LLEELAEAAAR 492
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
810-1045 |
5.12e-05 |
|
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: 48.25 E-value: 5.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 810 LQTGLRAMIARSEFRLRRQRKAAIVLQAHWRGRQAFSYYTRLQKAAIVTQ-CAWRCRLARRE-------LRMLKMAARDT 881
Cdd:pfam01576 181 LKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQiAELRAQLAKKEeelqaalARLEEETAQKN 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 882 GALKDAKnKLEQRVEELSLRLHLEKRLRTDLEEAKvQEVAKLQEALHTMRLQLKETTAM-----VVKEQEAARV--AIEE 954
Cdd:pfam01576 261 NALKKIR-ELEAQISELQEDLESERAARNKAEKQR-RDLGEELEALKTELEDTLDTTAAqqelrSKREQEVTELkkALEE 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 955 ASSVNKEPV----------VVEDTEKID--------------SLSNEIDRLKGLLSSETHKADEAQHAYQSALVQNEELC 1010
Cdd:pfam01576 339 ETRSHEAQLqemrqkhtqaLEELTEQLEqakrnkanlekakqALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQ 418
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 30685403 1011 KKLEEAGRKIDQLQDSVQRFQEKVFSL-----ESENKVLR 1045
Cdd:pfam01576 419 ARLSESERQRAELAEKLSKLQSELESVssllnEAEGKNIK 458
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
868-1047 |
6.75e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 47.64 E-value: 6.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 868 RRELRMLKMAARdtGALKDAKNKL---EQRVEELSLRLHLEKRLRTDLEE---------AKVQEVAKLQEALHTMRLQLK 935
Cdd:COG3096 280 RRELSERALELR--RELFGARRQLaeeQYRLVEMARELEELSARESDLEQdyqaasdhlNLVQTALRQQEKIERYQEDLE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 936 ETTAMVvKEQEAARVAIEEASSVNKEPVvvEDTEKidslsnEIDRLKGLLSsETHKADEAQH----AYQSALVQNEELCK 1011
Cdd:COG3096 358 ELTERL-EEQEEVVEEAAEQLAEAEARL--EAAEE------EVDSLKSQLA-DYQQALDVQQtraiQYQQAVQALEKARA 427
|
170 180 190
....*....|....*....|....*....|....*.
gi 30685403 1012 KLEEAGRKIDQLQDSVQRFQEKVFSLESENKVLRQQ 1047
Cdd:COG3096 428 LCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQK 463
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
870-1037 |
1.26e-04 |
|
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: 46.71 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 870 ELRMLKMAARDTgalKDAKNKLEQRVEELSLRLHLEKRLRTDLEEakvqEVAKLQEALHTMRLQLKETtamvvkEQEAAR 949
Cdd:pfam01576 392 ELRTLQQAKQDS---EHKRKKLEGQLQELQARLSESERQRAELAE----KLSKLQSELESVSSLLNEA------EGKNIK 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 950 VAiEEASSVNKEpvvVEDTE---------------KIDSLSNEIDRLKGLLSSETHKADEAQHAYQSALVQNEELCKKLE 1014
Cdd:pfam01576 459 LS-KDVSSLESQ---LQDTQellqeetrqklnlstRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLE 534
|
170 180
....*....|....*....|...
gi 30685403 1015 EAGRKIDQLQDSVQRFQEKVFSL 1037
Cdd:pfam01576 535 EDAGTLEALEEGKKRLQRELEAL 557
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
947-1034 |
1.45e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.98 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 947 AARVAIEEASSVNKEPVVVEDTEKIDSLSNEIDRLKGLLSSETHKADEAQHAYQSALVQNEELCKKLEEAGRKIDQLQDS 1026
Cdd:COG3883 1 ALALALAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAE 80
|
....*...
gi 30685403 1027 VQRFQEKV 1034
Cdd:COG3883 81 IEERREEL 88
|
|
| Myo5c_CBD |
cd15476 |
Cargo binding domain of myosin 5C; Class V myosins are well studied unconventional myosins, ... |
1325-1439 |
2.03e-04 |
|
Cargo binding domain of myosin 5C; Class V myosins are well studied unconventional myosins, represented by three paralogs (Myo5a,b,c) in vertebrates. Their C-terminal cargo binding domains (CBDs) are important for the binding of a diverse set of cargos, including membrane vesicles, organelles, proteins and mRNA. The MyoV-CBDs directly interact with several adaptor proteins.MyoVb and myoVc areprimarily expressed in epithelial cells, and have been implicated as motors involved in recycling endosomes.
Pssm-ID: 271260 [Multi-domain] Cd Length: 332 Bit Score: 45.16 E-value: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 1325 TMRANYVPSLLISKVFGQIFSFINVQLFNSLLLRRECCSFSNGEYVKTGLAELEKWCHDATEEFVgSAWDELKHIRQAVG 1404
Cdd:cd15476 157 TMCQHGMDPELIKQAVKQLFFLIGAVTLNSIFLRKDMCSCRKGMQIRCNISYLEEWLKEKNLQNS-NAKETLEPLSQAAW 235
|
90 100 110
....*....|....*....|....*....|....*
gi 30685403 1405 FLVIHQKPKKSLKEItTELCPVLSIQQLYRISTMY 1439
Cdd:cd15476 236 LLQVNKTTDDDAKEI-CERCTELSAVQIVKILNSY 269
|
|
| Myo5p-like_CBD_afadin |
cd15471 |
cargo binding domain of myosin 5-like of afadin; Afadin is an actin filament (F-actin) and ... |
1144-1421 |
2.32e-04 |
|
cargo binding domain of myosin 5-like of afadin; Afadin is an actin filament (F-actin) and Rap1 small G protein-binding protein, found in cadherin-based adherens junctions in epithelial cells, endothelial cells, and fibroblasts. It interacts with cell adhesion molecules and signaling molecules and plays a role in the formation of cell junctions, cell polarization, migration, survival, proliferation, and differentiation. Afadin is a multi domain protein, that contains beside a myosin5-like CBD, two Ras-associated domains, a forkhead-associated domain, a PDZ domain, three proline-rich domains, and an F-actin-binding domain.
Pssm-ID: 271255 Cd Length: 322 Bit Score: 44.99 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 1144 TSIFNRIIETIASAIEMQENS-DVLCYWLSNSATLLMFLQRTlkagatgsittprrrgmpsslfgRVSQSFRGSPQSAgf 1222
Cdd:cd15471 55 TAFLNKIASLIQQVIQEQRNIaGALAFWMANASELLNFLKQD-----------------------RDLSAFSVQAQDV-- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 1223 pfmtgraigggLDELRQveakypallfkqqlTAFLEKIYGMIRDkMKKEISPLLASCIQVPRTPRSGLVkgrsqntqnnv 1302
Cdd:cd15471 110 -----------LAEAVQ--------------SAFSYLVRCLQEE-LERSLPAFLDSLVSLDDEPAIGDV----------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 1303 vapkpmiahwqniVTCLNGHLRTMRANYV-PSLLIsKVFGQIFSFINVQLFNSLLL--RRECCSFSNGEYVKTGLAELEK 1379
Cdd:cd15471 153 -------------LHTLSSAMRLLRRCRVnAALTI-QLFSQLFHFINAWLFNSLVSnpDSGLCTRYWGKRLRQRLAHVEA 218
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 30685403 1380 WchdATEEFVGSAWD-ELKHIRQAVGFLvihQKPKKSLKEITT 1421
Cdd:cd15471 219 W---AERQGLELAADcHLDRIVQAANLL---TAPKYSAEDVAN 255
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
884-1059 |
4.68e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 4.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 884 LKDAKNKLEQRVEEL-SLRLHLEKrLRTDLEEAKvQEVAKLQEALHTMRLQLKETTAMVVKEQEA----ARVAIEEASSV 958
Cdd:COG3883 25 LSELQAELEAAQAELdALQAELEE-LNEEYNELQ-AELEALQAEIDKLQAEIAEAEAEIEERREElgerARALYRSGGSV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 959 NKEPVVVE--------------------DTEKIDSLSNEIDRLKGLLSSETHKADEAQHAYQSALVQNEELCKKLEEAGR 1018
Cdd:COG3883 103 SYLDVLLGsesfsdfldrlsalskiadaDADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEA 182
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 30685403 1019 KIDQLQDSVQRFQEKVFSLESENKVLRQQTLTISPTTRALA 1059
Cdd:COG3883 183 LLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAA 223
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
718-1117 |
4.95e-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: 44.96 E-value: 4.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 718 AGQMAELDARRAEVLGNAARViqrqFRTCMARKNYRSIRNAAI--VLQSFLRGEI-ARAVHKKLRIEAAALRVQKNFRRY 794
Cdd:TIGR00618 409 QATIDTRTSAFRDLQGQLAHA----KKQQELQQRYAELCAAAItcTAQCEKLEKIhLQESAQSLKEREQQLQTKEQIHLQ 484
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 795 VDRKSfvTTRSSTIVLQTGLRAMIARSEFRLRRQRKAAIVLQAHWRGRQAFSY-YTRLQKAAIVT--QC-AWRCRLARRE 870
Cdd:TIGR00618 485 ETRKK--AVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQtYAQLETSEEDVyhQLtSERKQRASLK 562
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 871 LRM-------LKMAARDTgALKDAKNKLEQRVEELSLRLHLEKRLRTDLEEAKVQEVAKLQEALHTMRLQLKEttamvvk 943
Cdd:TIGR00618 563 EQMqeiqqsfSILTQCDN-RSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHL------- 634
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 944 EQEAARVAIEEASSVNKEPVVVEDTEKIDSLSNEIDRLKgLLSSETHKADEAQHAYQSALVQNEELCKKLEEAGRKIDQL 1023
Cdd:TIGR00618 635 QQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKE-LLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHI 713
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 1024 QDSVQRFQEKVFSLESENKVLRQQTLTISPTTRALALRPKTTIIQRTPEKDTFSNGETTQLQEPETEDRPQKSLNQKQQE 1103
Cdd:TIGR00618 714 EEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRL 793
|
410
....*....|....*.
gi 30685403 1104 NQEL--LLKSISEDIG 1117
Cdd:TIGR00618 794 REEDthLLKTLEAEIG 809
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
878-1059 |
5.32e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.62 E-value: 5.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 878 ARDTGALKDAKNKLEQRVEELSLRLH-LEKRLR--------TDLEE---AKVQEVAKLQEALHTMRLQLKETTAMVVKEQ 945
Cdd:COG3206 167 ELRREEARKALEFLEEQLPELRKELEeAEAALEefrqknglVDLSEeakLLLQQLSELESQLAEARAELAEAEARLAALR 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 946 EAARVAIEEASSVNKEPVVVEDTEKIDSLSNEIDRLKGLLSsethkadeAQH-AYQSALVQNEELCKKL-EEAGRKIDQL 1023
Cdd:COG3206 247 AQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYT--------PNHpDVIALRAQIAALRAQLqQEAQRILASL 318
|
170 180 190
....*....|....*....|....*....|....*.
gi 30685403 1024 QDSVQRFQEKVFSLESENKVLRQQTLTISPTTRALA 1059
Cdd:COG3206 319 EAELEALQAREASLQAQLAQLEARLAELPELEAELR 354
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
867-1038 |
5.98e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.56 E-value: 5.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 867 ARRELRM-LKMAARDTGALKDAKNKLE---QRVEELSLRLHLEKRLRTDLEEAKVQEVAKLQEALHTMRLQLKETTAmvV 942
Cdd:PRK04863 277 HANERRVhLEEALELRRELYTSRRQLAaeqYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALRQQEKIERY--Q 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 943 KEQEAARVAIEEASSVNKEP--VVVEDTEKIDSLSNEIDRLKGLLSSETHKADEAQH---AYQ---SALVQNEELCKK-- 1012
Cdd:PRK04863 355 ADLEELEERLEEQNEVVEEAdeQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTraiQYQqavQALERAKQLCGLpd 434
|
170 180
....*....|....*....|....*...
gi 30685403 1013 --LEEAGRKIDQLQDSVQRFQEKVFSLE 1038
Cdd:PRK04863 435 ltADNAEDWLEEFQAKEQEATEELLSLE 462
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
888-1047 |
6.04e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 44.43 E-value: 6.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 888 KNKLEQRVEELSLR----LHLEKRLRT------D-------LEE---AKVQEVAKLQEALHTMRLQLKETTAMVVKEQEA 947
Cdd:pfam10174 288 KNKIDQLKQELSKKeselLALQTKLETltnqnsDckqhievLKEsltAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQ 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 948 ARVAIEEASSVNKEPVVVEDT------------EKIDSLSNEI-----------DRLKGlLSSETHKADEAQHAYQSALV 1004
Cdd:pfam10174 368 LQDLTEEKSTLAGEIRDLKDMldvkerkinvlqKKIENLQEQLrdkdkqlaglkERVKS-LQTDSSNTDTALTTLEEALS 446
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 30685403 1005 QNEELCKKLEEagrkidQLQDSVQRFQEKVFSLESENKVLRQQ 1047
Cdd:pfam10174 447 EKERIIERLKE------QREREDRERLEELESLKKENKDLKEK 483
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
878-1042 |
6.43e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.75 E-value: 6.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 878 ARDTGALKDAKNKleQRVEEL----SLRLHLEKRlrtDLEEAKVQEVAK---LQEALHTMRLQLKETTAMVVKEQEAARV 950
Cdd:PTZ00121 1533 AKKADEAKKAEEK--KKADELkkaeELKKAEEKK---KAEEAKKAEEDKnmaLRKAEEAKKAEEARIEEVMKLYEEEKKM 1607
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 951 AIEEASSVNKEPVVVEDTEKIDSLSNEIDRLKGLLSSETHKADEAQHAYQSALVQNEELCKKLEEAGRKIDQLQ--DSVQ 1028
Cdd:PTZ00121 1608 KAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKkaEEDE 1687
|
170
....*....|....
gi 30685403 1029 RFQEKVFSLESENK 1042
Cdd:PTZ00121 1688 KKAAEALKKEAEEA 1701
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
865-1185 |
6.45e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.74 E-value: 6.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 865 RLARRELRMLKMAARDTGALKDAKNKLEQRVEELslrlhleKRLRTDLEEAKvQEVAKLQEALHTMRLQLKETTamvvKE 944
Cdd:COG4372 7 KVGKARLSLFGLRPKTGILIAALSEQLRKALFEL-------DKLQEELEQLR-EELEQAREELEQLEEELEQAR----SE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 945 QEAARVAIEEAssvnkepvvvedTEKIDSLSNEIDRLKGLLSSETHKADEAQHAYQSALVQNEELCKKLEEAGRKIDQLQ 1024
Cdd:COG4372 75 LEQLEEELEEL------------NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 1025 DSVQRFQEKVFSLESENKVLRQQTLTISPTTRALALRPKTTIIQRTpEKDTFSNGETTQLQEPETEDRPQKSLNQKQQEN 1104
Cdd:COG4372 143 SEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDEL-LKEANRNAEKEEELAEAEKLIESLPRELAEELL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 1105 QELLLKSISEDIGFSEGKPVAACLIYKCLIHWRSFEVERTSIFNRI---IETIASAIEMQENSDVLCYWLSNSATLLMFL 1181
Cdd:COG4372 222 EAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAIlveKDTEEEELEIAALELEALEEAALELKLLALL 301
|
....
gi 30685403 1182 QRTL 1185
Cdd:COG4372 302 LNLA 305
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
605-630 |
7.25e-04 |
|
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.
Pssm-ID: 276814 [Multi-domain] Cd Length: 170 Bit Score: 41.95 E-value: 7.25e-04
10 20
....*....|....*....|....*.
gi 30685403 605 RFKQQLHSLMESLNGTEPHYIRCIKP 630
Cdd:cd01363 145 IINESLNTLMNVLRATRPHFVRCISP 170
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
884-1107 |
7.56e-04 |
|
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: 44.28 E-value: 7.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 884 LKDAKNKLEQRVEelSLRLHLEK-----RLRTDLEEAK----VQEVAKLQEALHTMRLQLKETTAMVVKEQEAARVAIEE 954
Cdd:TIGR02168 191 LEDILNELERQLK--SLERQAEKaerykELKAELRELElallVLRLEELREELEELQEELKEAEEELEELTAELQELEEK 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 955 ASSVNKEPVVVED-----TEKIDSLSNEIDRL---KGLLSSETHKADEAQHAYQSALVQNE-----------ELCKKLEE 1015
Cdd:TIGR02168 269 LEELRLEVSELEEeieelQKELYALANEISRLeqqKQILRERLANLERQLEELEAQLEELEskldelaeelaELEEKLEE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 1016 AGRKIDQLQDSVQRFQEKVFSLESENKVLRQQTLTISpTTRALALRPKTTI---IQRTPEKDTFSNGETTQLQEPETEDR 1092
Cdd:TIGR02168 349 LKEELESLEAELEELEAELEELESRLEELEEQLETLR-SKVAQLELQIASLnneIERLEARLERLEDRRERLQQEIEELL 427
|
250
....*....|....*
gi 30685403 1093 PQKSLNQKQQENQEL 1107
Cdd:TIGR02168 428 KKLEEAELKELQAEL 442
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
766-1034 |
1.47e-03 |
|
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: 43.51 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 766 LRGEIARAVHK--KLRIEAAALRVQ----KNFRRYVDRKSFVTTRSST---IVLQTgLRAMIARSEFRLRRQRKAAIVLQ 836
Cdd:TIGR02168 682 LEEKIEELEEKiaELEKALAELRKEleelEEELEQLRKELEELSRQISalrKDLAR-LEAEVEQLEERIAQLSKELTELE 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 837 AhwrgrQAFSYYTRLQKAAIVTQCAWRcRLARRELRMLKMAARdTGALKDAKNKLEQRVEELSLRLHlEKRLRTDLEEAK 916
Cdd:TIGR02168 761 A-----EIEELEERLEEAEEELAEAEA-EIEELEAQIEQLKEE-LKALREALDELRAELTLLNEEAA-NLRERLESLERR 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 917 VQEVAKLQEALHTMRLQLKETTAMVVKEQEAARVAIEEASSVnkepvVVEDTEKIDSLSNEIDRLKGLLSSETHKADEAQ 996
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESE-----LEALLNERASLEEALALLRSELEELSEELRELE 907
|
250 260 270
....*....|....*....|....*....|....*...
gi 30685403 997 HAYQSALVQNEELCKKLEEAGRKIDQLQDSVQRFQEKV 1034
Cdd:TIGR02168 908 SKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL 945
|
|
| Myo5p-like_CBD_Rasip1 |
cd15472 |
cargo binding domain of myosin 5-like of Ras-interacting protein 1; Ras-interacting protein 1 ... |
1335-1439 |
1.49e-03 |
|
cargo binding domain of myosin 5-like of Ras-interacting protein 1; Ras-interacting protein 1 (Rasip1 or RAIN) is an effector of the small G protein Rap1 and plays an important role in endothelial junction stabilization. Rasip1, like afadin, is a multi domain protein, that contains beside a myosin5-like CBD, a Ras-associated domain and a PDZ domain.
Pssm-ID: 271256 Cd Length: 366 Bit Score: 42.64 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 1335 LISKVFGQIFSFINVQLFNSLLLR---RECCSFSNGEYVKTGLAELEKW-----CHDATEEFvgsawdeLKHIRQAVGFL 1406
Cdd:cd15472 220 IASQMFAYLFFFSNASLFNQLMEKgsgGGFFQWSRGVQIRANLDLLLDWlqgagLGDLAEEF-------FRKLSSTVNLL 292
|
90 100 110
....*....|....*....|....*....|....*..
gi 30685403 1407 VIhqkPKKSLKEIT-TELC---PVLSIQQLYRISTMY 1439
Cdd:cd15472 293 AT---PKEQLLQMSwSSLRaefPALNPAQLHHLLRQY 326
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
684-1110 |
2.05e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.03 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 684 VLEGNYDDKVACQMILDKKSLT------DYQIGKTKIFLRAGQMAEL----DARRAEVLGNAARVIQRQFRTCMARKNYR 753
Cdd:TIGR00618 111 LEQKKGRGRILAAKKSETEEVIhdllklDYKTFTRVVLLPQGEFAQFlkakSKEKKELLMNLFPLDQYTQLALMEFAKKK 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 754 SIRNAAIVLQSFLRGEI-----------------------ARAVHKKLRIEAAALRVQKNFRRYVDRK----SFVTTRSS 806
Cdd:TIGR00618 191 SLHGKAELLTLRSQLLTlctpcmpdtyherkqvlekelkhLREALQQTQQSHAYLTQKREAQEEQLKKqqllKQLRARIE 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 807 TIvlqTGLRAMIARSEFRLRRQRKAAIVLQ-----AHWRgRQAFSYYTRLQ--KAAIVTQCAWRCRLARREL------RM 873
Cdd:TIGR00618 271 EL---RAQEAVLEETQERINRARKAAPLAAhikavTQIE-QQAQRIHTELQskMRSRAKLLMKRAAHVKQQSsieeqrRL 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 874 LKMAARDTGALKDAKNKLEQRVEELSLRLHLEKRLRT---------DLEEAKVQEVAKLQEALHT----------MRLQL 934
Cdd:TIGR00618 347 LQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTlqqqkttltQKLQSLCKELDILQREQATidtrtsafrdLQGQL 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 935 KETTAMVVKEQEAA---RVAIEEA--SSVNKEPVVVEDTEKIDSLSNEIDRLKGLLSSETHKADEAQHAYQSALVQNEEL 1009
Cdd:TIGR00618 427 AHAKKQQELQQRYAelcAAAITCTaqCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPL 506
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 1010 CKKLEEAGRKIDQL------QDSVQRFQEKVFSLESENKVLRQQtlTISPTTRALALRPKTTIIQRT----PEKDTFSNG 1079
Cdd:TIGR00618 507 CGSCIHPNPARQDIdnpgplTRRMQRGEQTYAQLETSEEDVYHQ--LTSERKQRASLKEQMQEIQQSfsilTQCDNRSKE 584
|
490 500 510
....*....|....*....|....*....|....*.
gi 30685403 1080 ETTQLQEPETEDRPQKSLN-----QKQQENQELLLK 1110
Cdd:TIGR00618 585 DIPNLQNITVRLQDLTEKLseaedMLACEQHALLRK 620
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
824-1103 |
2.38e-03 |
|
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: 42.75 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 824 RLRRQRKAAIVLQAHWRGRQAFSYYTRLQKAaivtqcawrcRLARRELRMLKmaaRDTGALKDAKNKLEQRVEELSLRLH 903
Cdd:TIGR02169 202 RLRREREKAERYQALLKEKREYEGYELLKEK----------EALERQKEAIE---RQLASLEEELEKLTEEISELEKRLE 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 904 lekRLRTDLEEAKvqevAKLQEALHTMRLQLKETTAMVVKEQEAARVAIEEASSVNK--EPVVVEDTEKIDSLSNEIDRL 981
Cdd:TIGR02169 269 ---EIEQLLEELN----KKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEdaEERLAKLEAEIDKLLAEIEEL 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 982 KGLLSSETHKADEAQHAYQSA------LVQN----------------------EELCKKLEEAGRKIDQLQDSVQRFQEK 1033
Cdd:TIGR02169 342 EREIEEERKRRDKLTEEYAELkeeledLRAEleevdkefaetrdelkdyreklEKLKREINELKRELDRLQEELQRLSEE 421
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 1034 VFSLESENKVLRQQTLTISPTTRALALRPKTTIIQRTPEKDTFSNGETTQLQEPETEDRPQKSLNQKQQE 1103
Cdd:TIGR02169 422 LADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRE 491
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
868-1044 |
4.02e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 4.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 868 RRELRMLKMAARDTGALKDAKNKLEQRVEELSLRL-HLEKRLRT-------DLEEaKVQEVAKLQE---ALHTMRLQLKE 936
Cdd:PRK03918 538 KGEIKSLKKELEKLEELKKKLAELEKKLDELEEELaELLKELEElgfesveELEE-RLKELEPFYNeylELKDAEKELER 616
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 937 TTAMVVKEQEAARVAIEEASSVNKEpvvvedtekIDSLSNEIDRLKGLLSSETHKADEAQH-----AYQSALVQNEELCK 1011
Cdd:PRK03918 617 EEKELKKLEEELDKAFEELAETEKR---------LEELRKELEELEKKYSEEEYEELREEYlelsrELAGLRAELEELEK 687
|
170 180 190
....*....|....*....|....*....|...
gi 30685403 1012 KLEEAGRKIDQLQDSVQRFQEKVFSLESENKVL 1044
Cdd:PRK03918 688 RREEIKKTLEKLKEELEEREKAKKELEKLEKAL 720
|
|
| IQ |
smart00015 |
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ... |
850-872 |
5.16e-03 |
|
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln residues.
Pssm-ID: 197470 [Multi-domain] Cd Length: 23 Bit Score: 35.76 E-value: 5.16e-03
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
883-1027 |
5.31e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.29 E-value: 5.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 883 ALKDAKNKLEQRVEELSLRLHLEKRLRTDLE---EAKVQEVAKLQEALHTMRLQlKETTAMvVKEQEAARVAIEEAssvn 959
Cdd:COG1579 35 ELEDELAALEARLEAAKTELEDLEKEIKRLEleiEEVEARIKKYEEQLGNVRNN-KEYEAL-QKEIESLKRRISDL---- 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30685403 960 kEPVVVEDTEKIDSLSNEIDRLKGLLSSETHKADEAQHAYQSALvqnEELCKKLEEAGRKIDQLQDSV 1027
Cdd:COG1579 109 -EDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEEL---AELEAELEELEAEREELAAKI 172
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
824-1024 |
6.63e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 6.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 824 RLRRQRKAAIVLQAHWRgrqafSYYTRLQKAAIVTQC-----AWRcrlARRELRMLKMA-ARDTGALKDAKNKLEQRVEE 897
Cdd:COG4913 246 DAREQIELLEPIRELAE-----RYAAARERLAELEYLraalrLWF---AQRRLELLEAElEELRAELARLEAELERLEAR 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 898 LSLRLHLEKRLRTDLEEAKVQEVAKLQEALHTMRLQLKEttamvvKEQEAARVAiEEASSVNKEpvVVEDTEKIDSLSNE 977
Cdd:COG4913 318 LDALREELDELEAQIRGNGGDRLEQLEREIERLERELEE------RERRRARLE-ALLAALGLP--LPASAEEFAALRAE 388
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 30685403 978 IDRLKGLLSSETHKADEAQHAyqsALVQNEELCKKLEEAGRKIDQLQ 1024
Cdd:COG4913 389 AAALLEALEEELEALEEALAE---AEAALRDLRRELRELEAEIASLE 432
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
884-1058 |
7.69e-03 |
|
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: 40.93 E-value: 7.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 884 LKDAKNKLEQRVEELSLRLHLEKRLRTDLEEAKVQ---EVAKLQEALHTMRLQLKETTAMVVKEQE---AARVAIEEASS 957
Cdd:pfam01576 178 LSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKlegESTDLQEQIAELQAQIAELRAQLAKKEEelqAALARLEEETA 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 958 VNKEPV---------VVEDTEKIDS--------------LSNEIDRLKGLLsSETHKADEAQHAYQSALVQN-EELCKKL 1013
Cdd:pfam01576 258 QKNNALkkireleaqISELQEDLESeraarnkaekqrrdLGEELEALKTEL-EDTLDTTAAQQELRSKREQEvTELKKAL 336
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 30685403 1014 EEAGRKID-QLQDSVQRFQEKVFSLESENKVLRQQTLTISPTTRAL 1058
Cdd:pfam01576 337 EEETRSHEaQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQAL 382
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
831-1047 |
8.13e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 8.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 831 AAIVLQAHWRGRQAFSYYTRLQKAAIVTQCAWRCRLARRELRMLKMAARDTGALKDAKNKLEQR-VEELSLRLHLEKRLR 909
Cdd:COG4717 256 AALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEeLEELLAALGLPPDLS 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 910 TDLEEAKVQEVAKLQEALHTMRLQLKEttaMVVKEQEAARVAIEEASSVNKE---PVVVEDTEKIDSLSNEIDRLKGLLS 986
Cdd:COG4717 336 PEELLELLDRIEELQELLREAEELEEE---LQLEELEQEIAALLAEAGVEDEeelRAALEQAEEYQELKEELEELEEQLE 412
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30685403 987 SETHKADEAQHAYQSALVQNE--ELCKKLEEAGRKIDQLQDSVQRFQEKVFSLESENKV--LRQQ 1047
Cdd:COG4717 413 ELLGELEELLEALDEEELEEEleELEEELEELEEELEELREELAELEAELEQLEEDGELaeLLQE 477
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
882-1123 |
9.86e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 40.33 E-value: 9.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 882 GALKDAKNKLEQRVEELSLRLHLEKRLRTDLEEAKVQEVAKLQEALHTMRLQLKETTAMVVKEQEAARVAI-EEASSVNK 960
Cdd:COG5185 289 KQFENTKEKIAEYTKSIDIKKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIkEEIENIVG 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 961 EPVVVEDTEKIDSLSNEIDRLK----GLLSSETHKADEA----QHAYQSALVQNEEL-------CKKLEEAGRKIDQLQD 1025
Cdd:COG5185 369 EVELSKSSEELDSFKDTIESTKesldEIPQNQRGYAQEIlatlEDTLKAADRQIEELqrqieqaTSSNEEVSKLLNELIS 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30685403 1026 SVQRFQEKVfsLESENKVLRQQTLTISPTTRALALRPKTTIIQRTPEKDTFSNGETTQLQEPE--------TEDRPQKSL 1097
Cdd:COG5185 449 ELNKVMREA--DEESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLErqlegvrsKLDQVAESL 526
|
250 260
....*....|....*....|....*.
gi 30685403 1098 NQKQQENQELLLKSISEDIGFSEGKP 1123
Cdd:COG5185 527 KDFMRARGYAHILALENLIPASELIQ 552
|
|
| |
