|
Name |
Accession |
Description |
Interval |
E-value |
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
2-1567 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 1805.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 2 SFEVGTRCWYPHKELGWIGAEVIKNEFNDGKYHLELQLEDDEIVSVDTKDLNNDKDqslpllrNPPILEATEDLTSLSYL 81
Cdd:COG5022 5 NAEVGSGCWIPDEEKGWIWAEIIKEAFNKGKVTEEGKKEDGESVSVKKKVLGNDRI-------KLPKFDGVDDLTELSYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 82 NEPAVLHAIKQRYSQLNIYTYSGIVLIATNPFDRVDqLYTQDMIQAYAGKRRGELEPHLFAIAEEAYRLMKNDKQNQTIV 161
Cdd:COG5022 78 NEPAVLHNLEKRYNNGQIYTYSGLVLIAVNPYRDLG-IYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTII 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 162 VSGESGAGKTVSAKYIMRYFASVEEEnsatvqHQVEMSETEQKILATNPIMEAFGNAKTTRNDNSSRFGKYLEILFDKDT 241
Cdd:COG5022 157 ISGESGAGKTENAKRIMQYLASVTSS------STVEISSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 242 SIIGARIRTYLLERSRLVYQPPTERNYHIFYQLMAGLPAQTKEELHLTDASDYFYMNQGGDTKINGIDDAKEYKITVDAL 321
Cdd:COG5022 231 EICGAKIETYLLEKSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLSQGGCDKIDGIDDAKEFKITLDAL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 322 TLVGITKETQHQIFKILAALLHIGNIEIKKTRNDASLSADEPNLKLACELLGIDAYNFAKWVTKKQIITRSEKIVSNLNY 401
Cdd:COG5022 311 KTIGIDEEEQDQIFKILAAILHIGNIEFKEDRNGAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 402 NQALVAKDSVAKFIYSALFDWLVENINTVLCNPAVndqISSFIGVLDIYGFEHFEKNSFEQFCINYANEKLQQEFNQHVF 481
Cdd:COG5022 391 EQALAIRDSLAKALYSNLFDWIVDRINKSLDHSAA---ASNFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMF 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 482 KLEQEEYVKEEIEWSFIEFNDNQPCIDLIE--NKLGILSLLDEESRLPAGSDESWTQKLYQTLDKsPTNKVFSKPRFGQT 559
Cdd:COG5022 468 KLEQEEYVKEGIEWSFIDYFDNQPCIDLIEkkNPLGILSLLDEECVMPHATDESFTSKLAQRLNK-NSNPKFKKSRFRDN 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 560 KFIVSHYALDVAYDVEGFIEKNRDTVSDGHLEVLKASTNETLINILEGLEKAAKKleeakkleleqagskkpgpirtvNR 639
Cdd:COG5022 547 KFVVKHYAGDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDEENIESK-----------------------GR 603
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 640 KPTLGSMFKQSLIELMNTINSTNVHYIRCIKPNADKEAWQFDNLMVLSQLRACGVLETIRISCAGFPSRWTFEEFVLRYY 719
Cdd:COG5022 604 FPTLGSRFKESLNSLMSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYR 683
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 720 ILIPHEQWDLIFKKKetteEDIISVVKMILDATVKDKSKYQIGNTKIFFKAGMLAYLEKLRSNKMHNSIVMIQKKIRAKY 799
Cdd:COG5022 684 ILSPSKSWTGEYTWK----EDTKNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRY 759
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 800 YRKQYLQISQAIKYLQNNIKGFIIRQRVNDEMKVNCATLLQAAYRGHSIRANVFSVLRTITNLQKKIRKELKQRQ-LKQE 878
Cdd:COG5022 760 LRRRYLQALKRIKKIQVIQHGFRLRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKLQKTIKREKKLREtEEVE 839
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 879 HEYNAAVTIQSKVRTFEPRSRFLRTKKDTVVVQSLIRRRAAQRKLKQLKADAKSVNHLKEVSYKLENKVIELTQNLASkv 958
Cdd:COG5022 840 FSLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAERQLQELKIDVKSISSLKLVNLELESEIIELKKSLSS-- 917
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 959 kenkemtERIKELQVQVEESAKLQETLENmkkehlIDIDNQKSKDMELQKtIENNLQSTEQTLKDAQLELEDMVKQHDEL 1038
Cdd:COG5022 918 -------DLIENLEFKTELIARLKKLLNN------IDLEEGPSIEYVKLP-ELNKLHEVESKLKETSEEYEDLLKKSTIL 983
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 1039 KEESKKQLEELEQTKKTLVEYQTLNGDLQNEVKSLKE---EIARLQTAMSLG-TVTTSVLPQTPLKDVMgggasnfNNMM 1114
Cdd:COG5022 984 VREGNKANSELKNFKKELAELSKQYGALQESTKQLKElpvEVAELQSASKIIsSESTELSILKPLQKLK-------GLLL 1056
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 1115 LENSDLSPNDLNLKsrstplsgnnhidslsVDRENGvnatqineelyrLLEDTEILNQEITEGLLKGFEVPDagvaIQLS 1194
Cdd:COG5022 1057 LENNQLQARYKALK----------------LRRENS------------LLDDKQLYQLESTENLLKTINVKD----LEVT 1104
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 1195 KRDVVYPARILIIVLSEMWRFGLTKQSESFLAQVLTTIQKVVTQLKGNDLIPSGVFWLANVRELYSFVVFALNSilTEET 1274
Cdd:COG5022 1105 NRNLVKPANVLQFIVAQMIKLNLLQEISKFLSQLVNTLEPVFQKLSVLQLELDGLFWEANLEALPSPPPFAALS--EKRL 1182
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 1275 FKNGMTDEEYKEYVSLVTELKDDFEALSYNIYNIWLK-KLQKQLQKKAINAVVISESLPGFSAgetsgfLNKIFANTEEY 1353
Cdd:COG5022 1183 YQSALYDEKSKLSSSEVNDLKNELIALFSKIFSGWPRgDKLKKLISEGWVPTEYSTSLKGFNN------LNKKFDTPASM 1256
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 1354 TMDDILTFFNSIYWCMKSFHIENEVFHAVVTTLLNYVDAICFNELIMKRNFLSWKRGLQLNYNVTRLEEWCKTHGLTDGT 1433
Cdd:COG5022 1257 SNEKLLSLLNSIDNLLSSYKLEEEVLPATINSLLQYINVGLFNALRTKASSLRWKSATEVNYNSEELDDWCREFEISDVD 1336
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 1434 ECLQHLIQTAKLLQVRKYTIEDIDILRGICYSLTPAQLQKLISQYQVADYESPIPQEIL-RYVADIVKKEAALSSSGNDs 1512
Cdd:COG5022 1337 EELEELIQAVKVLQLLKDDLNKLDELLDACYSLNPAEIQNLKSRYDPADKENNLPKEILkKIEALLIKQELQLSLEGKD- 1415
|
1530 1540 1550 1560 1570
....*....|....*....|....*....|....*....|....*....|....*
gi 768464868 1513 KGHEHSSSIFITPETGPFTDPFSLIKTRKFDQVEAyipawlsLPSTKRIVDLVAQ 1567
Cdd:COG5022 1416 ETEVHLSEIFSEEKSLISLDRNSIYKEEVLSSLSA-------LLTKEKIALLDRK 1463
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
84-769 |
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: 1230.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 84 PAVLHAIKQRYSQLN-IYTYSGIVLIATNPFDRVDqLYTQDMIQAYAGKRRGELEPHLFAIAEEAYRLMKNDKQNQTIVV 162
Cdd:cd01380 1 PAVLHNLKVRFCQRNaIYTYCGIVLVAINPYEDLP-IYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 163 SGESGAGKTVSAKYIMRYFASVEEENSatvqhqvEMSETEQKILATNPIMEAFGNAKTTRNDNSSRFGKYLEILFDKDTS 242
Cdd:cd01380 80 SGESGAGKTVSAKYAMRYFATVGGSSS-------GETQVEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 243 IIGARIRTYLLERSRLVYQPPTERNYHIFYQLMAGLPAQTKEELHLTDASDYFYMNQGGDTKINGIDDAKEYKITVDALT 322
Cdd:cd01380 153 IIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNQGGSPVIDGVDDAAEFEETRKALT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 323 LVGITKETQHQIFKILAALLHIGNIEIKKTRN-DASLSADEPNLKLACELLGIDAYNFAKWVTKKQIITRSEKIVSNLNY 401
Cdd:cd01380 233 LLGISEEEQMEIFRILAAILHLGNVEIKATRNdSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPLTL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 402 NQALVAKDSVAKFIYSALFDWLVENINTVLCNPaVNDQISSFIGVLDIYGFEHFEKNSFEQFCINYANEKLQQEFNQHVF 481
Cdd:cd01380 313 QQAIVARDALAKHIYAQLFDWIVDRINKALASP-VKEKQHSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHVF 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 482 KLEQEEYVKEEIEWSFIEFNDNQPCIDLIENKLGILSLLDEESRLPAGSDESWTQKLYQTLDKSPtNKVFSKPRFGQTKF 561
Cdd:cd01380 392 KLEQEEYVKEEIEWSFIDFYDNQPCIDLIEGKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKP-NKHFKKPRFSNTAF 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 562 IVSHYALDVAYDVEGFIEKNRDTVSDGHLEVLKASTNetlinileglekaakkleeakkleleqagskkpgpirtvnRKP 641
Cdd:cd01380 471 IVKHFADDVEYQVEGFLEKNRDTVSEEHLNVLKASKN----------------------------------------RKK 510
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 642 TLGSMFKQSLIELMNTINSTNVHYIRCIKPNADKEAWQFDNLMVLSQLRACGVLETIRISCAGFPSRWTFEEFVLRYYIL 721
Cdd:cd01380 511 TVGSQFRDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVL 590
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 768464868 722 IPHEQWDLIFKKKETteediisvvKMILDATVKDKSKYQIGNTKIFFK 769
Cdd:cd01380 591 LPSKEWLRDDKKKTC---------ENILENLILDPDKYQFGKTKIFFR 629
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
72-769 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 1079.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 72 TEDLTSLSYLNEPAVLHAIKQRYSQLNIYTYSGIVLIATNPFDRVDqLYTQDMIQAYAGKRRGELEPHLFAIAEEAYRLM 151
Cdd:pfam00063 1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLP-IYSEDMIKAYRGKRRGELPPHIFAIADEAYRSM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 152 KNDKQNQTIVVSGESGAGKTVSAKYIMRYFASVEEENSAtvqhqVEMSETEQKILATNPIMEAFGNAKTTRNDNSSRFGK 231
Cdd:pfam00063 80 LQDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSA-----GNVGRLEEQILQSNPILEAFGNAKTVRNNNSSRFGK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 232 YLEILFDKDTSIIGARIRTYLLERSRLVYQPPTERNYHIFYQLMAGLPAQTKEELHLTDASDYFYMNQGGDTKINGIDDA 311
Cdd:pfam00063 155 YIEIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYLSQSGCYTIDGIDDS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 312 KEYKITVDALTLVGITKETQHQIFKILAALLHIGNIEIKKTRND-ASLSADEPNLKLACELLGIDAYNFAKWVTKKQIIT 390
Cdd:pfam00063 235 EEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDeQAVPDDTENLQKAASLLGIDSTELEKALCKRRIKT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 391 RSEKIVSNLNYNQALVAKDSVAKFIYSALFDWLVENINTVLCNPAVndQISSFIGVLDIYGFEHFEKNSFEQFCINYANE 470
Cdd:pfam00063 315 GRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTI--EKASFIGVLDIYGFEIFEKNSFEQLCINYVNE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 471 KLQQEFNQHVFKLEQEEYVKEEIEWSFIEFNDNQPCIDLIENK-LGILSLLDEESRLPAGSDESWTQKLYQTLDKSPtnk 549
Cdd:pfam00063 393 KLQQFFNHHMFKLEQEEYVREGIEWTFIDFGDNQPCIDLIEKKpLGILSLLDEECLFPKATDQTFLDKLYSTFSKHP--- 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 550 VFSKPRF-GQTKFIVSHYALDVAYDVEGFIEKNRDTVSDGHLEVLKASTNETLINILEGLEKAAKKLeeakkleLEQAGS 628
Cdd:pfam00063 470 HFQKPRLqGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESAA-------ANESGK 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 629 KKPGPIRTVnRKPTLGSMFKQSLIELMNTINSTNVHYIRCIKPNADKEAWQFDNLMVLSQLRACGVLETIRISCAGFPSR 708
Cdd:pfam00063 543 STPKRTKKK-RFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNR 621
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768464868 709 WTFEEFVLRYYILIPHEQwdlifkkkETTEEDIISVVKMILDATVKDKSKYQIGNTKIFFK 769
Cdd:pfam00063 622 ITFQEFVQRYRILAPKTW--------PKWKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
65-780 |
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: 990.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 65 NPPILEATEDLTSLSYLNEPAVLHAIKQRYSQLNIYTYSGIVLIATNPFDRVDqLYTQDMIQAYAGKRRGELEPHLFAIA 144
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLP-IYTDEVIKKYRGKSRGELPPHVFAIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 145 EEAYRLMKNDKQNQTIVVSGESGAGKTVSAKYIMRYFASVEEENSATVQhqvemseTEQKILATNPIMEAFGNAKTTRND 224
Cdd:smart00242 80 DNAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNTEVGS-------VEDQILESNPILEAFGNAKTLRNN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 225 NSSRFGKYLEILFDKDTSIIGARIRTYLLERSRLVYQPPTERNYHIFYQLMAGLPAQTKEELHLTDASDYFYMNQGGDTK 304
Cdd:smart00242 153 NSSRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSPEDYRYLNQGGCLT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 305 INGIDDAKEYKITVDALTLVGITKETQHQIFKILAALLHIGNIEIKKTRND--ASLSADEPNLKLACELLGIDAYNFAKW 382
Cdd:smart00242 233 VDGIDDAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDnaASTVKDKEELSNAAELLGVDPEELEKA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 383 VTKKQIITRSEKIVSNLNYNQALVAKDSVAKFIYSALFDWLVENINTVLCNPavnDQISSFIGVLDIYGFEHFEKNSFEQ 462
Cdd:smart00242 313 LTKRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFK---DGSTYFIGVLDIYGFEIFEVNSFEQ 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 463 FCINYANEKLQQEFNQHVFKLEQEEYVKEEIEWSFIEFNDNQPCIDLIENK-LGILSLLDEESRLPAGSDESWTQKLYQT 541
Cdd:smart00242 390 LCINYANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFFDNQDCIDLIEKKpPGILSLLDEECRFPKGTDQTFLEKLNQH 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 542 LDKSPtnkVFSKP-RFGQTKFIVSHYALDVAYDVEGFIEKNRDTVSDGHLEVLKASTNETLINILEGlekaakkleeakk 620
Cdd:smart00242 470 HKKHP---HFSKPkKKGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPS------------- 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 621 lELEQAGSKKpgpirtvnRKPTLGSMFKQSLIELMNTINSTNVHYIRCIKPNADKEAWQFDNLMVLSQLRACGVLETIRI 700
Cdd:smart00242 534 -GVSNAGSKK--------RFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRI 604
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 701 SCAGFPSRWTFEEFVLRYYILIPheqwdlifKKKETTEEDIISVVKMILDATVKDKSKYQIGNTKIFFKAGMLAYLEKLR 780
Cdd:smart00242 605 RRAGFPYRLPFDEFLQRYRVLLP--------DTWPPWGGDAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELR 676
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
84-769 |
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: 841.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 84 PAVLHAIKQRYSQLNIYTYSGIVLIATNPFdRVDQLYTQDMIQAYAGKRRG-ELEPHLFAIAEEAYRLMKNDKQNQTIVV 162
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPF-KWLPLYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 163 SGESGAGKTVSAKYIMRYFASVEEenSATVQHQVEMSETEQKILATNPIMEAFGNAKTTRNDNSSRFGKYLEILFDKDTS 242
Cdd:cd00124 80 SGESGAGKTETTKLVLKYLAALSG--SGSSKSSSSASSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPTGR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 243 IIGARIRTYLLERSRLVYQPPTERNYHIFYQLMAGLPAQTKEELHLTDASDYFYMN----QGGDTKINGIDDAKEYKITV 318
Cdd:cd00124 158 LVGASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYYYLNdylnSSGCDRIDGVDDAEEFQELL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 319 DALTLVGITKETQHQIFKILAALLHIGNIEIKKTRNDASLSADEPN---LKLACELLGIDAYNFAKWVTKKQIITRSEKI 395
Cdd:cd00124 238 DALDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDEDSSAEVADdesLKAAAKLLGVDAEDLEEALTTRTIKVGGETI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 396 VSNLNYNQALVAKDSVAKFIYSALFDWLVENINTVLCNPAVNDQiSSFIGVLDIYGFEHFEKNSFEQFCINYANEKLQQE 475
Cdd:cd00124 318 TKPLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAES-TSFIGILDIFGFENFEVNSFEQLCINYANEKLQQF 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 476 FNQHVFKLEQEEYVKEEIEWSFIEFNDNQPCIDLIENK-LGILSLLDEESRLPAGSDESWTQKLYQTLDKSPTNkvFSKP 554
Cdd:cd00124 397 FNQHVFKLEQEEYEEEGIDWSFIDFPDNQDCLDLIEGKpLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRF--FSKK 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 555 RFGQTKFIVSHYALDVAYDVEGFIEKNRDTVSDGHLEVLKASTNetlinileglekaakkleeakkleleqagskkpgpi 634
Cdd:cd00124 475 RKAKLEFGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSGSQ------------------------------------ 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 635 rtvnrkptlgsmFKQSLIELMNTINSTNVHYIRCIKPNADKEAWQFDNLMVLSQLRACGVLETIRISCAGFPSRWTFEEF 714
Cdd:cd00124 519 ------------FRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEF 586
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 768464868 715 VLRYYILIPHEQWDLIFKKKETTEEdiisvvkmILDATVKDKSKYQIGNTKIFFK 769
Cdd:cd00124 587 LKRYRILAPGATEKASDSKKAAVLA--------LLLLLKLDSSGYQLGKTKVFLR 633
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
84-769 |
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: 777.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 84 PAVLHAIKQRYSQLNIYTYSGIVLIATNPFDRVDqLYTQDMIQAYAGKRRGELEPHLFAIAEEAYRLMKNDKQNQTIVVS 163
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLP-IYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 164 GESGAGKTVSAKYIMRYFASVEEENSATVQHQVEMSETEQKILATNPIMEAFGNAKTTRNDNSSRFGKYLEILFDKDTSI 243
Cdd:cd01377 80 GESGAGKTENTKKVIQYLASVAASSKKKKESGKKKGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTGKI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 244 IGARIRTYLLERSRLVYQPPTERNYHIFYQLMAGLPAQTKEELHLTDASDYFYMNQGGDTKINGIDDAKEYKITVDALTL 323
Cdd:cd01377 160 AGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYFFLSQGELTIDGVDDAEEFKLTDEAFDI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 324 VGITKETQHQIFKILAALLHIGNIEIKKTRND--ASLSADEPNLKlACELLGIDAYNFAKWVTKKQIITRSEKIVSNLNY 401
Cdd:cd01377 240 LGFSEEEKMSIFKIVAAILHLGNIKFKQRRREeqAELDGTEEADK-AAHLLGVNSSDLLKALLKPRIKVGREWVTKGQNK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 402 NQALVAKDSVAKFIYSALFDWLVENINTVLCNpavNDQISSFIGVLDIYGFEHFEKNSFEQFCINYANEKLQQEFNQHVF 481
Cdd:cd01377 319 EQVVFSVGALAKALYERLFLWLVKRINKTLDT---KSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMF 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 482 KLEQEEYVKEEIEWSFIEF-NDNQPCIDLIENK-LGILSLLDEESRLPAGSDESWTQKLYQTLDKSPTNKVFSKPRFGQT 559
Cdd:cd01377 396 VLEQEEYKKEGIEWTFIDFgLDLQPTIDLIEKPnMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKNFKKPKPKKSEA 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 560 KFIVSHYALDVAYDVEGFIEKNRDTVSDGHLEVLKASTNETLINILEglekaakklEEAKKLELEQAGSKKPGPIRTVnr 639
Cdd:cd01377 476 HFILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFK---------DYEESGGGGGKKKKKGGSFRTV-- 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 640 kptlGSMFKQSLIELMNTINSTNVHYIRCIKPNADKEAWQFDNLMVLSQLRACGVLETIRISCAGFPSRWTFEEFVLRYY 719
Cdd:cd01377 545 ----SQLHKEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYS 620
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 768464868 720 ILIPHEQWDLIFKKKETTEediisvvkMILDATVKDKSKYQIGNTKIFFK 769
Cdd:cd01377 621 ILAPNAIPKGFDDGKAACE--------KILKALQLDPELYRIGNTKVFFK 662
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
84-769 |
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: 772.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 84 PAVLHAIKQRYSQLNIYTYSGIVLIATNPFDRVDQLYTQDMIQAYAGKRRGELEPHLFAIAEEAYRLMKNDKQNQTIVVS 163
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPHLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 164 GESGAGKTVSAKYIMRYFASVeeensaTVQHQVEMSETEQKILATNPIMEAFGNAKTTRNDNSSRFGKYLEILFDKDTSI 243
Cdd:cd01384 81 GESGAGKTETTKMLMQYLAYM------GGRAVTEGRSVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAGRI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 244 IGARIRTYLLERSRLVYQPPTERNYHIFYQLMAGLPAQTKEELHLTDASDYFYMNQGGDTKINGIDDAKEYKITVDALTL 323
Cdd:cd01384 155 SGAAIRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKDPKQFHYLNQSKCFELDGVDDAEEYRATRRAMDV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 324 VGITKETQHQIFKILAALLHIGNIE-IKKTRNDASLSADEP---NLKLACELLGIDAYNFAKWVTKKQIITRSEKIVSNL 399
Cdd:cd01384 235 VGISEEEQDAIFRVVAAILHLGNIEfSKGEEDDSSVPKDEKsefHLKAAAELLMCDEKALEDALCKRVIVTPDGIITKPL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 400 NYNQALVAKDSVAKFIYSALFDWLVENINTVLCnpavNDQIS-SFIGVLDIYGFEHFEKNSFEQFCINYANEKLQQEFNQ 478
Cdd:cd01384 315 DPDAATLSRDALAKTIYSRLFDWLVDKINRSIG----QDPNSkRLIGVLDIYGFESFKTNSFEQFCINLANEKLQQHFNQ 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 479 HVFKLEQEEYVKEEIEWSFIEFNDNQPCIDLIENK-LGILSLLDEESRLPAGSDESWTQKLYQTLDkspTNKVFSKPRFG 557
Cdd:cd01384 391 HVFKMEQEEYTKEEIDWSYIEFVDNQDVLDLIEKKpGGIIALLDEACMFPRSTHETFAQKLYQTLK---DHKRFSKPKLS 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 558 QTKFIVSHYALDVAYDVEGFIEKNRDTVSDGHLEVLKASTNETLINILEglekaakkleeakklELEQAGSKKPGPIRTV 637
Cdd:cd01384 468 RTDFTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLFP---------------PLPREGTSSSSKFSSI 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 638 nrkptlGSMFKQSLIELMNTINSTNVHYIRCIKPNADKEAWQFDNLMVLSQLRACGVLETIRISCAGFPSRWTFEEFVLR 717
Cdd:cd01384 533 ------GSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDR 606
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 768464868 718 YYILIPhEQWDLIFKKKEtteediisVVKMILDAtvKDKSKYQIGNTKIFFK 769
Cdd:cd01384 607 FGLLAP-EVLKGSDDEKA--------ACKKILEK--AGLKGYQIGKTKVFLR 647
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
85-769 |
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: 707.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 85 AVLHAIKQRYSQLNIYTYSGIVLIATNPFDRVDqLYTQDMIQAYAGKRRGELEPHLFAIAEEAYRLMKNDKQNQTIVVSG 164
Cdd:cd01381 2 GILRNLLIRYREKLIYTYTGSILVAVNPYQILP-IYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 165 ESGAGKTVSAKYIMRYFASVeeenSAtvQHqvemSETEQKILATNPIMEAFGNAKTTRNDNSSRFGKYLEILFDKDTSII 244
Cdd:cd01381 81 ESGAGKTESTKLILQYLAAI----SG--QH----SWIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 245 GARIRTYLLERSRLVYQPPTERNYHIFYQLMAGLPAQTKEELHLTDASDYFYMNQGGDTKINGIDDAKEYKITVDALTLV 324
Cdd:cd01381 151 GAKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDASDYYYLTQGNCLTCEGRDDAAEFADIRSAMKVL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 325 GITKETQHQIFKILAALLHIGNIEIK-KTRN--DASLSADEPNLKLACELLGIDAYNFAKWVTKKQIITRSEKIVSNLNY 401
Cdd:cd01381 231 MFTDEEIWDIFKLLAAILHLGNIKFEaTVVDnlDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSPLSA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 402 NQALVAKDSVAKFIYSALFDWLVENINTVLCNPAVNDQISSFIGVLDIYGFEHFEKNSFEQFCINYANEKLQQEFNQHVF 481
Cdd:cd01381 311 EQALDVRDAFVKGIYGRLFIWIVNKINSAIYKPRGTDSSRTSIGVLDIFGFENFEVNSFEQLCINFANENLQQFFVRHIF 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 482 KLEQEEYVKEEIEWSFIEFNDNQPCIDLIENK-LGILSLLDEESRLPAGSDESWTQKLYQTLDkspTNKVFSKPRF-GQT 559
Cdd:cd01381 391 KLEQEEYDKEGINWQHIEFVDNQDVLDLIALKpMNIMSLIDEESKFPKGTDQTMLEKLHSTHG---NNKNYLKPKSdLNT 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 560 KFIVSHYALDVAYDVEGFIEKNRDTVSDGHLEVLKASTNETLINILEglekaakkLEEAKKLEleqagskkpgpirTVNR 639
Cdd:cd01381 468 SFGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFN--------EDISMGSE-------------TRKK 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 640 KPTLGSMFKQSLIELMNTINSTNVHYIRCIKPNADKEAWQFDNLMVLSQLRACGVLETIRISCAGFPSRWTFEEFVLRYY 719
Cdd:cd01381 527 SPTLSSQFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYR 606
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 768464868 720 ILIPheqwdlifKKKETTEEDIISVVKMILDATVKDKSKYQIGNTKIFFK 769
Cdd:cd01381 607 VLVP--------GIPPAHKTDCRAATRKICCAVLGGDADYQLGKTKIFLK 648
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
84-769 |
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: 703.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 84 PAVLHAIKQRYSQLNIYTYSGIVLIATNPFDRVdQLYTQDMIQAYagKRRGELEPHLFAIAEEAYRLMKNDKQNQTIVVS 163
Cdd:cd01383 1 PSVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDV-PLYGNEFITAY--RQKLLDSPHVYAVADTAYREMMRDEINQSIIIS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 164 GESGAGKTVSAKYIMRYFASVEEENSATvqhqvemsetEQKILATNPIMEAFGNAKTTRNDNSSRFGKYLEILFDKDTSI 243
Cdd:cd01383 78 GESGAGKTETAKIAMQYLAALGGGSSGI----------ENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 244 IGARIRTYLLERSRLVYQPPTERNYHIFYQLMAGLPAQTKEELHLTDASDYFYMNQGGDTKINGIDDAKEYKITVDALTL 323
Cdd:cd01383 148 CGAKIQTYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKSASEYKYLNQSNCLTIDGVDDAKKFHELKEALDT 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 324 VGITKETQHQIFKILAALLHIGNIEIKKTRN-DASLSADEPNLKLACELLGIDAYNFAKWVTKKQIITRSEKIVSNLNYN 402
Cdd:cd01383 228 VGISKEDQEHIFQMLAAVLWLGNISFQVIDNeNHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKLTLQ 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 403 QALVAKDSVAKFIYSALFDWLVENINTVLcnPAVNDQISSFIGVLDIYGFEHFEKNSFEQFCINYANEKLQQEFNQHVFK 482
Cdd:cd01383 308 QAIDARDALAKAIYASLFDWLVEQINKSL--EVGKRRTGRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLFK 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 483 LEQEEYVKEEIEWSFIEFNDNQPCIDLIENK-LGILSLLDEESRLPAGSDESWTQKLYQTLDkspTNKVFSKPRfgQTKF 561
Cdd:cd01383 386 LEQEEYELDGIDWTKVDFEDNQECLDLIEKKpLGLISLLDEESNFPKATDLTFANKLKQHLK---SNSCFKGER--GGAF 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 562 IVSHYALDVAYDVEGFIEKNRDTVSDGHLEVLkASTNETLINILeglekAAKKLEEAKKLELEQAGSKKPGPIRTVNRKp 641
Cdd:cd01383 461 TIRHYAGEVTYDTSGFLEKNRDLLHSDLIQLL-SSCSCQLPQLF-----ASKMLDASRKALPLTKASGSDSQKQSVATK- 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 642 tlgsmFKQSLIELMNTINSTNVHYIRCIKPNADKEAWQFDNLMVLSQLRACGVLETIRISCAGFPSRWTFEEFVLRYYIL 721
Cdd:cd01383 534 -----FKGQLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFL 608
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 768464868 722 IPheqwdlifkKKETTEEDIISVVKMILDATVKDKSKYQIGNTKIFFK 769
Cdd:cd01383 609 LP---------EDVSASQDPLSTSVAILQQFNILPEMYQVGYTKLFFR 647
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
90-769 |
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: 699.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 90 IKQRYSQLNIYTYSGIVLIATNPFDRVDqLYTQDMIQAYAGKRRGELEPHLFAIAEEAYRLMKNDKQNQTIVVSGESGAG 169
Cdd:cd14883 7 LKVRYKKDLIYTYTGSILVAVNPYKELP-IYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGESGAG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 170 KTVSAKYIMRYFASVeeensaTVQHqvemSETEQKILATNPIMEAFGNAKTTRNDNSSRFGKYLEILFDKDTSIIGARIR 249
Cdd:cd14883 86 KTETTKLILQYLCAV------TNNH----SWVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGHIKGAIIQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 250 TYLLERSRLVYQPPTERNYHIFYQLMAG--LPAQTKEELHLTDASDYFYMNQGGDTKINGIDDAKEYKITVDALTLVGIT 327
Cdd:cd14883 156 DYLLEQSRITFQAPGERNYHVFYQLLAGakHSKELKEKLKLGEPEDYHYLNQSGCIRIDNINDKKDFDHLRLAMNVLGIP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 328 KETQHQIFKILAALLHIGNIE---IKKTRNdASLSADEPNLKLACELLGIDAYNFAKWVTKKQIITRSEKIVSNLNYNQA 404
Cdd:cd14883 236 EEMQEGIFSVLSAILHLGNLTfedIDGETG-ALTVEDKEILKIVAKLLGVDPDKLKKALTIRQINVRGNVTEIPLKVQEA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 405 LVAKDSVAKFIYSALFDWLVENINTVLCNPAVNdqiSSFIGVLDIYGFEHFEKNSFEQFCINYANEKLQQEFNQHVFKLE 484
Cdd:cd14883 315 RDNRDAMAKALYSRTFAWLVNHINSCTNPGQKN---SRFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHYVFKLE 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 485 QEEYVKEEIEWSFIEFNDNQPCIDLIENK-LGILSLLDEESRLPAGSDESWTQKLYQTLDKSPTnkvFSKP--RFGQTKF 561
Cdd:cd14883 392 QEEYEKEGINWSHIVFTDNQECLDLIEKPpLGILKLLDEECRFPKGTDLTYLEKLHAAHEKHPY---YEKPdrRRWKTEF 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 562 IVSHYALDVAYDVEGFIEKNRDTVSDGHLEVLKASTNEtLINILEGLEK--AAKKLEEAKKLELEQAGSKKpgpirtvnR 639
Cdd:cd14883 469 GVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNK-FVKELFTYPDllALTGLSISLGGDTTSRGTSK--------G 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 640 KPTLGSMFKQSLIELMNTINSTNVHYIRCIKPNADKEAWQFDNLMVLSQLRACGVLETIRISCAGFPSRWTFEEFVLRYY 719
Cdd:cd14883 540 KPTVGDTFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYL 619
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 768464868 720 ILIPHEqwdlifkkKETTEEDIISVVKMILDATVKDKSKYQIGNTKIFFK 769
Cdd:cd14883 620 CLDPRA--------RSADHKETCGAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
85-769 |
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: 693.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 85 AVLHAIKQRYSQLNIYTYSGIVLIATNPFdRVDQLYTQDMIQAYAGKRRGELEPHLFAIAEEAYRLMKNDKQNQTIVVSG 164
Cdd:cd01378 2 AINENLKKRFENDEIYTYIGHVLISVNPF-KDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 165 ESGAGKTVSAKYIMRYFASVEEENSATVQHQVEMseteqkILATNPIMEAFGNAKTTRNDNSSRFGKYLEILFDKDTSII 244
Cdd:cd01378 81 ESGAGKTEASKRIMQYIAAVSGGSESEVERVKDM------LLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEPV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 245 GARIRTYLLERSRLVYQPPTERNYHIFYQLMAGLPAQTKEELHLTDASDYFYMNQGGDTKINGIDDAKEYKITVDALTLV 324
Cdd:cd01378 155 GGHITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGCFDVDGIDDAADFKEVLNAMKVI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 325 GITKETQHQIFKILAALLHIGNIEIKKTRNDASLSADEPNLKLACELLGIDAYNFAKWVTKKQIITRSEK---IVSNLNY 401
Cdd:cd01378 235 GFTEEEQDSIFRILAAILHLGNIQFAEDEEGNAAISDTSVLDFVAYLLGVDPDQLEKALTHRTIETGGGGrsvYEVPLNV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 402 NQALVAKDSVAKFIYSALFDWLVENINTVLCNPavNDQISSFIGVLDIYGFEHFEKNSFEQFCINYANEKLQQEFNQHVF 481
Cdd:cd01378 315 EQAAYARDALAKAIYSRLFDWIVERINKSLAAK--SGGKKKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFIELTL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 482 KLEQEEYVKEEIEWSFIEFNDNQPCIDLIENK-LGILSLLDEE-SRLPAGSDESWTQKLYQTLDKSP-TNKVFSKPRFGQ 558
Cdd:cd01378 393 KAEQEEYVREGIEWTPIKYFNNKIICDLIEEKpPGIFAILDDAcLTAGDATDQTFLQKLNQLFSNHPhFECPSGHFELRR 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 559 TKFIVSHYALDVAYDVEGFIEKNRDTVSDGHLEVLKASTNETLINIL-EGLEKAAKKleeakkleleqagskkpgpirtv 637
Cdd:cd01378 473 GEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFpEGVDLDSKK----------------------- 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 638 nRKPTLGSMFKQSLIELMNTINSTNVHYIRCIKPNADKEAWQFDNLMVLSQLRACGVLETIRISCAGFPSRWTFEEFVLR 717
Cdd:cd01378 530 -RPPTAGTKFKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLER 608
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 768464868 718 YYILIPhEQWdliFKKKETTEEDIISvvkmILDATVKDKSKYQIGNTKIFFK 769
Cdd:cd01378 609 YKLLSP-KTW---PAWDGTWQGGVES----ILKDLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
85-769 |
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: 622.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 85 AVLHAIKQRYSQLNIYTYSGIVLIATNPFDRVDQLYTQDMIQAYAGKRRGELEPHLFAIAEEAY-RLMKN---DKQNQTI 160
Cdd:cd14890 2 SLLHTLRLRYERDEIYTYVGPILISINPYKSIPDLYSEERMLLYHGTTAGELPPHVFAIADHAYtQLIQSgvlDPSNQSI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 161 VVSGESGAGKTVSAKYIMRYFASV---------EEENSATVQHQVEMSETEQKILATNPIMEAFGNAKTTRNDNSSRFGK 231
Cdd:cd14890 82 IISGESGAGKTEATKIIMQYLARItsgfaqgasGEGEAASEAIEQTLGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 232 YLEILFDKDTSIIGARIRTYLLERSRLVYQPPTERNYHIFYQLMAGLPAQTKEELHLTDASDYFYMnQGGDTKINGIDDA 311
Cdd:cd14890 162 FIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPVEYFYL-RGECSSIPSCDDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 312 KEYKITVDALTLVGITKETQHQIFKILAALLHIGNIEIKKTrNDASLSADE---PNLKLACELLGIDAYNFAKWVTKKQI 388
Cdd:cd14890 241 KAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESE-NDTTVLEDAttlQSLKLAAELLGVNEDALEKALLTRQL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 389 ITRSEKIVSNLNYNQALVAKDSVAKFIYSALFDWLVENINTVLCNPavnDQISSFIGVLDIYGFEHFEKNSFEQFCINYA 468
Cdd:cd14890 320 FVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSP---DDKWGFIGVLDIYGFEKFEWNTFEQLCINYA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 469 NEKLQQEFNQHVFKLEQEEYVKEEIEWSFIEFNDNQPCIDLIENKL----GILSLLDEESRLPAG-SDESWTQKLYQ--- 540
Cdd:cd14890 397 NEKLQRHFNQHMFEVEQVEYSNEGIDWQYITFNDNQACLELIEGKVngkpGIFITLDDCWRFKGEeANKKFVSQLHAsfg 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 541 -------TLDKSPTNKVFSKPRFGQTK-FIVSHYALDVAYDVEGFIEKNRDTVSDGHLEVLKASTnetlinileglekaa 612
Cdd:cd14890 477 rksgsggTRRGSSQHPHFVHPKFDADKqFGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSR--------------- 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 613 kkleeakkleleqagskkpgpiRTVnRKPTLGSMFKQSLIELMNTINSTNVHYIRCIKPNADKEAWQFDNLMVLSQLRAC 692
Cdd:cd14890 542 ----------------------RSI-REVSVGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYS 598
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768464868 693 GVLETIRISCAGFPSRWTFEEFVLRYYILIPheqwdlifkkketTEEDIISVVKMILDATVKDKSKYQIGNTKIFFK 769
Cdd:cd14890 599 GMMEAIQIRQQGFALREEHDSFFYDFQVLLP-------------TAENIEQLVAVLSKMLGLGKADWQIGSSKIFLK 662
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
85-769 |
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: 615.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 85 AVLHAIKQRYSQLNIYTYSGIVLIATNPFDRVDqLYTQDMIQAYAGKRRGELEPHLFAIAEEAYRLMKNDKQNQTIVVSG 164
Cdd:cd01387 2 TVLWNLKTRYERNLIYTYIGSILVSVNPYKMFD-IYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 165 ESGAGKTVSAKYIMRYFASVEEENSATVQHQvemseteqkILATNPIMEAFGNAKTTRNDNSSRFGKYLEILFdKDTSII 244
Cdd:cd01387 81 ESGSGKTEATKLIMQYLAAVNQRRNNLVTEQ---------ILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFF-EGGVIV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 245 GARIRTYLLERSRLVYQPPTERNYHIFYQLMAGLPAQTKEELHLTDASDYFYMNQGGDTKINGIDDAKEYKITVDALTLV 324
Cdd:cd01387 151 GAITSQYLLEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQEAEKYFYLNQGGNCEIAGKSDADDFRRLLAAMQVL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 325 GITKETQHQIFKILAALLHIGNI-----EIKKTRNDASLSADEpNLKLACELLGIDAYNFAKWVTKKQIITRSEKIVSNL 399
Cdd:cd01387 231 GFSSEEQDSIFRILASVLHLGNVyfhkrQLRHGQEGVSVGSDA-EIQWVAHLLQISPEGLQKALTFKVTETRRERIFTPL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 400 NYNQALVAKDSVAKFIYSALFDWLVENINTVLCNPAvndQISSFIGVLDIYGFEHFEKNSFEQFCINYANEKLQQEFNQH 479
Cdd:cd01387 310 TIDQALDARDAIAKALYALLFSWLVTRVNAIVYSGT---QDTLSIAILDIFGFEDLSENSFEQLCINYANENLQYYFNKH 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 480 VFKLEQEEYVKEEIEWSFIEFNDNQPCIDLIENK-LGILSLLDEESRLPAGSDESWTQKLYQTLDkspTNKVFSKPRFGQ 558
Cdd:cd01387 387 VFKLEQEEYIREQIDWTEIAFADNQPVINLISKKpVGILHILDDECNFPQATDHSFLEKCHYHHA---LNELYSKPRMPL 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 559 TKFIVSHYALDVAYDVEGFIEKNRDTVSDGHLEVLKASTNETLINILEGLekAAKKLEEAKKLELEQAGSKKPgpirtvn 638
Cdd:cd01387 464 PEFTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSSH--RAQTDKAPPRLGKGRFVTMKP------- 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 639 RKPTLGSMFKQSLIELMNTINSTNVHYIRCIKPNADKEAWQFDNLMVLSQLRACGVLETIRISCAGFPSRWTFEEFVLRY 718
Cdd:cd01387 535 RTPTVAARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRY 614
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 768464868 719 YILIPHeqwdlifKKKETTEEDIISVVKMILDATVKdKSKYQIGNTKIFFK 769
Cdd:cd01387 615 RCLVAL-------KLPRPAPGDMCVSLLSRLCTVTP-KDMYRLGATKVFLR 657
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
84-769 |
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: 611.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 84 PAVLHAIKQRYSQLNIYTYSGIVLIATNPFDRVDQLYTQDMIQAYAGKRRGELEPHLFAIAEEAYRLMKNDKQNQTIVVS 163
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPELYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 164 GESGAGKTVSAKYIMRYFASVeeensATVQHQvemsETEQKILATNPIMEAFGNAKTTRNDNSSRFGKYLEILFDKDTSI 243
Cdd:cd14903 81 GESGAGKTETTKILMNHLATI-----AGGLND----STIKKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKNGTL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 244 IGARIRTYLLERSRLVYQPPTERNYHIFYQLMAGlpAQTKEELHLTDASDYFYMNQGGDTKINGIDDAKEYKITVDALTL 323
Cdd:cd14903 152 VGAKCRTYLLEKTRVISHERPERNYHIFYQLLAS--PDVEERLFLDSANECAYTGANKTIKIEGMSDRKHFARTKEALSL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 324 VGITKETQHQIFKILAALLHIGNIEIKKTRNDASLSADEPN---LKLACELLGIDAYNFAKWVTKKQIITRSEKIVSNLN 400
Cdd:cd14903 230 IGVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSAIAPGdqgAVYATKLLGLSPEALEKALCSRTMRAAGDVYTVPLK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 401 YNQALVAKDSVAKFIYSALFDWLVENINTVLCNPAvndQISSFIGVLDIYGFEHFEKNSFEQFCINYANEKLQQEFNQHV 480
Cdd:cd14903 310 KDQAEDCRDALAKAIYSNVFDWLVATINASLGNDA---KMANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFTQDV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 481 FKLEQEEYVKEEIEWSFIEFNDNQPCIDLIENKLGILSLLDEESRLPAGSDESWTQKLyQTLDKSPTNkVFSKPRFGQTK 560
Cdd:cd14903 387 FKTVQIEYEEEGIRWAHIDFADNQDVLAVIEDRLGIISLLNDEVMRPKGNEESFVSKL-SSIHKDEQD-VIEFPRTSRTQ 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 561 FIVSHYALDVAYDVEGFIEKNRDTVSDGHLEVLKASTNETLINILEglekaaKKLEEAKKLELEQAGSKKPGPIRTVNRK 640
Cdd:cd14903 465 FTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFK------EKVESPAAASTSLARGARRRRGGALTTT 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 641 pTLGSMFKQSLIELMNTINSTNVHYIRCIKPNADKEAWQFDNLMVLSQLRACGVLETIRISCAGFPSRWTFEEFVLRYYI 720
Cdd:cd14903 539 -TVGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWL 617
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 768464868 721 LIP-HEQWDLIFKKKettEEDIISVVKMildatvKDKSKYQIGNTKIFFK 769
Cdd:cd14903 618 FLPeGRNTDVPVAER---CEALMKKLKL------ESPEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
85-769 |
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: 599.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 85 AVLHAIKQRYSQLNIYTYSGIVLIATNPFDRVDQLYTQDMIQAYAGKRRGELEPHLFAIAEEAYRLMKNDKQNQTIVVSG 164
Cdd:cd14873 2 SIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAGLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 165 ESGAGKTVSAKYIMRyFASVEEENSATVQHQVEMSETEQKILATNPIMEAFGNAKTTRNDNSSRFGKYLEILFDKDTSII 244
Cdd:cd14873 82 ESGAGKTESTKLILK-FLSVISQQSLELSLKEKTSCVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 245 GARIRTYLLERSRLVYQPPTERNYHIFYQLMAGLPAQTKEELHLTDASDYFYMNQGGDTKINGIDDAKEYKITVDALTLV 324
Cdd:cd14873 161 GGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTPENYHYLNQSGCVEDKTISDQESFREVITAMEVM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 325 GITKETQHQIFKILAALLHIGNIEIkKTRNDASLSaDEPNLKLACELLGIDAYNFAKWVTKKQIITRSEKIVSNLNYNQA 404
Cdd:cd14873 241 QFSKEEVREVSRLLAGILHLGNIEF-ITAGGAQVS-FKTALGRSAELLGLDPTQLTDALTQRSMFLRGEEILTPLNVQQA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 405 LVAKDSVAKFIYSALFDWLVENINTVLCNpavNDQISSfIGVLDIYGFEHFEKNSFEQFCINYANEKLQQEFNQHVFKLE 484
Cdd:cd14873 319 VDSRDSLAMALYARCFEWVIKKINSRIKG---KEDFKS-IGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKHIFSLE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 485 QEEYVKEEIEWSFIEFNDNQPCIDLIENKLGILSLLDEESRLPAGSDESWTQKLYqtlDKSPTNKVFSKPRFGQTKFIVS 564
Cdd:cd14873 395 QLEYSREGLVWEDIDWIDNGECLDLIEKKLGLLALINEESHFPQATDSTLLEKLH---SQHANNHFYVKPRVAVNNFGVK 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 565 HYALDVAYDVEGFIEKNRDTVSDGHLEVLKASTNETLINILEglekaakKLEEAKKLELEQAGSKKpgpirtvnRKPTLG 644
Cdd:cd14873 472 HYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFE-------HVSSRNNQDTLKCGSKH--------RRPTVS 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 645 SMFKQSLIELMNTINSTNVHYIRCIKPNADKEAWQFDNLMVLSQLRACGVLETIRISCAGFPSRWTFEEFVLRYYILIPH 724
Cdd:cd14873 537 SQFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMRN 616
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 768464868 725 EQWDLIFKKKETTeediisvVKMILDATvkdKSKYQIGNTKIFFK 769
Cdd:cd14873 617 LALPEDVRGKCTS-------LLQLYDAS---NSEWQLGKTKVFLR 651
|
|
| fMyo2p_CBD |
cd15480 |
cargo binding domain of fungal myosin 2; Yeast myosin V travels along actin cables, actin ... |
1154-1564 |
0e+00 |
|
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: 598.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 1154 TQINEELYRLLEDTEILNQEITEGLLKGFEVPDAGVAIQLSKRDVVYPARILIIVLSEMWRFGLTKQSESFLAQVLTTIQ 1233
Cdd:cd15480 1 DDINDELIRLLEDEEALNEEVLEGLIKGLKIPLPSVANPLSRKEVLFPAHLIILILSEMWRLGLTKESERFLANVMQTIQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 1234 KVVTQLKGNDLIPSGVFWLANVRELYSFVVFALNSILTEETFKNGMTDEEYKEYVSLVTELKDDFEALSYNIYNIWLKkl 1313
Cdd:cd15480 81 QHVMSLKGEDAIVPGAFWLSNVHELLSFVCLAESDILQGIGPGKDMREEEWEEYERLVTVVKHDLESLEYNIYHTWMK-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 1314 qkqlqkkainavviseslpgfsagETSGFLNKifanteeyTMDDILTFFNSIYWCMKSFHIENEVFHAVVTTLLNYVDAI 1393
Cdd:cd15480 159 ------------------------ELKKRLEK--------TMDDILNFFNKVYKSMKSYYIEESVIRQVVTELLKLIGVT 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 1394 CFNELIMKRNFLSWKRGLQLNYNVTRLEEWCKTHGLTDGTECLQHLIQTAKLLQVRKYTIEDIDILRGICYSLTPAQLQK 1473
Cdd:cd15480 207 AFNDLLMRRNFLSWKRGLQINYNITRLEEWCKSHDIPEGTLQLEHLMQATKLLQLKKATLEDIEIIYDVCWILTPAQIQK 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 1474 LISQYQVADYESPIPQEILRYVADIVKKEAALSssgndskgheHSSSIFITPETGPFTDPFSliktRKFDQVEAYIPAWL 1553
Cdd:cd15480 287 LISQYYVADYENPISPEILKAVAARVKPEDKSD----------HLLLIPLVEEVGPFEDPFP----REIAGLEAYIPAWL 352
|
410
....*....|.
gi 768464868 1554 SLPSTKRIVDL 1564
Cdd:cd15480 353 NLPHIRRLVEL 363
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
87-769 |
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: 593.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 87 LHAIKQRYSQLNIYTYSGIVLIATNPFDRVDQLYTQDMIQAYAGKRRGELEPHLFAIAEEAYRLMKNDKQNQTIVVSGES 166
Cdd:cd01382 4 LNNIRVRYSKDKIYTYVANILIAVNPYFDIPKLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVSGES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 167 GAGKTVSAKYIMRYFASVEEENSATVqhqvemsetEQKILATNPIMEAFGNAKTTRNDNSSRFGKYLEILFDKDTSIIGA 246
Cdd:cd01382 84 GAGKTESTKYILRYLTESWGSGAGPI---------EQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 247 RIRTYLLERSRLVYQPPTERNYHIFYQLMAGLPAQTKEELhLTDASdyfymnqggdtkingIDDAKEYKITVDALTLVGI 326
Cdd:cd01382 155 FVSHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKL-LKDPL---------------LDDVGDFIRMDKAMKKIGL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 327 TKETQHQIFKILAALLHIGNIEIK----KTRNDASLSAD-EPNLKLACELLGIDAYNFAKWVTKKQIITRSEKIVSN--- 398
Cdd:cd01382 219 SDEEKLDIFRVVAAVLHLGNIEFEengsDSGGGCNVKPKsEQSLEYAAELLGLDQDELRVSLTTRVMQTTRGGAKGTvik 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 399 --LNYNQALVAKDSVAKFIYSALFDWLVENINTvlCNPAvnDQISSFIGVLDIYGFEHFEKNSFEQFCINYANEKLQQEF 476
Cdd:cd01382 299 vpLKVEEANNARDALAKAIYSKLFDHIVNRINQ--CIPF--ETSSYFIGVLDIAGFEYFEVNSFEQFCINYCNEKLQQFF 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 477 NQHVFKLEQEEYVKEEIEWSFIEFNDNQPCIDLIENKL-GILSLLDEESRLPAGSDESWTQKLYQtldKSPTNKVFSKPR 555
Cdd:cd01382 375 NERILKEEQELYEKEGLGVKEVEYVDNQDCIDLIEAKLvGILDLLDEESKLPKPSDQHFTSAVHQ---KHKNHFRLSIPR 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 556 FGQTK----------FIVSHYALDVAYDVEGFIEKNRDTVSDGhLEVL-KASTNETLINILEGLE-KAAKKLEEAKKLEL 623
Cdd:cd01382 452 KSKLKihrnlrddegFLIRHFAGAVCYETAQFIEKNNDALHAS-LESLiCESKDKFIRSLFESSTnNNKDSKQKAGKLSF 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 624 EQAGSKkpgpirtvnrkptlgsmFKQSLIELMNTINSTNVHYIRCIKPNADKEAWQFDNLMVLSQLRACGVLETIRISCA 703
Cdd:cd01382 531 ISVGNK-----------------FKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQG 593
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768464868 704 GFPSRWTFEEFVLRYYILIPHEQWDLifkkketteeDIISVVKMILDATVKDKSKYQIGNTKIFFK 769
Cdd:cd01382 594 GFPSRTSFHDLYNMYKKYLPPKLARL----------DPRLFCKALFKALGLNENDFKFGLTKVFFR 649
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
87-769 |
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: 585.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 87 LHAIKQRYSQLNIYTYSGIVLIATNPFdRVDQLYTQDMIQAYAGKRRGELEPHLFAIAEEAYRLMKNDKQNQTIVVSGES 166
Cdd:cd01385 4 LENLRARFKHGKIYTYVGSILIAVNPF-KFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 167 GAGKTVSAKYIMRYFASVEEENSAtvqhqvemSETEQKILATNPIMEAFGNAKTTRNDNSSRFGKYLEILFDKDTSIIGA 246
Cdd:cd01385 83 GSGKTESTNFLLHHLTALSQKGYG--------SGVEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRGA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 247 RIRTYLLERSRLVYQPPTERNYHIFYQLMAGLPAQTKEELHLTDASDYFYMNQGGDTKINGIDDAKEYKITVDALTLVGI 326
Cdd:cd01385 155 VVEKYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHYLNQSDCYTLEGEDEKYEFERLKQAMEMVGF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 327 TKETQHQIFKILAALLHIGNIEIKKTRNDASLSADEPN---LKLACELLGIDAYNFAKWVTKKQIITRSEKIVSNLNYNQ 403
Cdd:cd01385 235 LPETQRQIFSVLSAVLHLGNIEYKKKAYHRDESVTVGNpevLDIISELLRVKEETLLEALTTKKTVTVGETLILPYKLPE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 404 ALVAKDSVAKFIYSALFDWLVENINTVLCNPAVNDQISS-FIGVLDIYGFEHFEKNSFEQFCINYANEKLQQEFNQHVFK 482
Cdd:cd01385 315 AIATRDAMAKCLYSALFDWIVLRINHALLNKKDLEEAKGlSIGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQHIFK 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 483 LEQEEYVKEEIEWSFIEFNDNQPCIDLIENK-LGILSLLDEESRLPAGSDESWTQKLYQTLDKsptNKVFSKPRFGQTKF 561
Cdd:cd01385 395 LEQEEYKKEGISWHNIEYTDNTGCLQLISKKpTGLLCLLDEESNFPGATNQTLLAKFKQQHKD---NKYYEKPQVMEPAF 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 562 IVSHYALDVAYDVEGFIEKNRDTVSDGHLEVLKASTN---ETLI----------NILEGLEKAAKKLEEAKK-------- 620
Cdd:cd01385 472 IIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSafvRELIgidpvavfrwAVLRAFFRAMAAFREAGRrraqrtag 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 621 --LELEQAGSKKPGPIRTVNRKPTLGSMFKQSLIELMNTINSTNVHYIRCIKPNADKEAWQFDNLMVLSQLRACGVLETI 698
Cdd:cd01385 552 hsLTLHDRTTKSLLHLHKKKKPPSVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVLRQLRYTGMLETV 631
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768464868 699 RISCAGFPSRWTFEEFVLRYYILIPheqwdlifKKKETTEEDIisvvKMILDATVKDKSKYQIGNTKIFFK 769
Cdd:cd01385 632 RIRRSGYSVRYTFQEFITQFQVLLP--------KGLISSKEDI----KDFLEKLNLDRDNYQIGKTKVFLK 690
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
87-769 |
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: 582.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 87 LHAIKQRYSQLNIYTYSGIVLIATNPFDRVDQLY------TQDMIQAYAGKRRgelePHLFAIAEEAYRLMKNDKQNQT- 159
Cdd:cd14892 4 LDVLRRRYERDAIYTFTADILISINPYKSIPLLYdvpgfdSQRKEEATASSPP----PHVFSIAERAYRAMKGVGKGQGt 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 160 ---IVVSGESGAGKTVSAKYIMRYFASVEE--ENSATVQHQVEMSET-EQKILATNPIMEAFGNAKTTRNDNSSRFGKYL 233
Cdd:cd14892 80 pqsIVVSGESGAGKTEASKYIMKYLATASKlaKGASTSKGAANAHESiEECVLLSNLILEAFGNAKTIRNDNSSRFGKYI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 234 EILFDKDTSIIGARIRTYLLERSRLVYQPPTERNYHIFYQLMAGLPAQTKEELHLTDASDYFYMNQGGDTKINGIDDAKE 313
Cdd:cd14892 160 QIHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAESFLFLNQGNCVEVDGVDDATE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 314 YKITVDALTLVGITKETQHQIFKILAALLHIGNIEIKKTRNDASL---SADEPNLKLACELLGIDAYNFAKWVTKKQIIT 390
Cdd:cd14892 240 FKQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEENADDEDVfaqSADGVNVAKAAGLLGVDAAELMFKLVTQTTST 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 391 RSEKIVS-NLNYNQALVAKDSVAKFIYSALFDWLVENIN-------TVLCNPAVNDQISSFIGVLDIYGFEHFEKNSFEQ 462
Cdd:cd14892 320 ARGSVLEiKLTAREAKNALDALCKYLYGELFDWLISRINachkqqtSGVTGGAASPTFSPFIGILDIFGFEIMPTNSFEQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 463 FCINYANEKLQQEFNQHVFKLEQEEYVKEEIEWSFIEFNDNQPCIDLIENK-LGILSLLDEESRLP-AGSDESWTQKLYQ 540
Cdd:cd14892 400 LCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQDNQDCLDLIQKKpLGLLPLLEEQMLLKrKTTDKQLLTIYHQ 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 541 TldKSPTNKVFSKPRFGQTKFIVSHYALDVAYDVEGFIEKNRDTVSDGHLEVLKAStnetlinileglekaakkleeakk 620
Cdd:cd14892 480 T--HLDKHPHYAKPRFECDEFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSS------------------------ 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 621 leleqagskkpgpirtvnrkptlgSMFKQSLIELMNTINSTNVHYIRCIKPNADKEAWQFDNLMVLSQLRACGVLETIRI 700
Cdd:cd14892 534 ------------------------SKFRTQLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVRI 589
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768464868 701 SCAGFPSRWTFEEFVLRYYILiphEQWdliFKKKETTEEDIISVVKMILDATVK----DKSKYQIGNTKIFFK 769
Cdd:cd14892 590 RREGFPIRRQFEEFYEKFWPL---ARN---KAGVAASPDACDATTARKKCEEIVaralERENFQLGRTKVFLR 656
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
84-767 |
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: 581.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 84 PAVLHAIKQRYSQLNIYTYSGIVLIATNPFDRVdQLYTQDMIQAY---AGKR---RGELEPHLFAIAEEAYRLMKND--- 154
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRL-PLYDDETKEAYyehGERRaagERKLPPHVYAVADKAFRAMLFAsrg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 155 -KQNQTIVVSGESGAGKTVSAKYIMRYFASVEEENSATvQHQVEMSETEQKILATNPIMEAFGNAKTTRNDNSSRFGKYL 233
Cdd:cd14901 80 qKCDQSILVSGESGAGKTETTKIIMNYLASVSSATTHG-QNATERENVRDRVLESNPILEAFGNARTNRNNNSSRFGKFI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 234 EILFDKDTSIIGARIRTYLLERSRLVYQPPTERNYHIFYQLMAGLPAQTKEELHLTDASDYFYMNQGG--DTKiNGIDDA 311
Cdd:cd14901 159 RLGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYLNSSQcyDRR-DGVDDS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 312 KEYKITVDALTLVGITKETQHQIFKILAALLHIGNIE-IKKTRNDASLSAD-EPNLKLACELLGIDAYNFAKWVTKKQII 389
Cdd:cd14901 238 VQYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCfVKKDGEGGTFSMSsLANVRAACDLLGLDMDVLEKTLCTREIR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 390 TRSEKIVSNLNYNQALVAKDSVAKFIYSALFDWLVENINTVLCNPAVNDQiSSFIGVLDIYGFEHFEKNSFEQFCINYAN 469
Cdd:cd14901 318 AGGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSESTGA-SRFIGIVDIFGFEIFATNSLEQLCINFAN 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 470 EKLQQEFNQHVFKLEQEEYVKEEIEWSFIEFNDNQPCIDLIENK-LGILSLLDEESRLPAGSDESWTQKLYQTLDKSPTN 548
Cdd:cd14901 397 EKLQQLFGKFVFEMEQDEYVAEAIPWTFVEYPNNDACVAMFEARpTGLFSLLDEQCLLPRGNDEKLANKYYDLLAKHASF 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 549 KVfSKPRFGQTKFIVSHYALDVAYDVEGFIEKNRDTVSDGHLEVLKASTNETLinileglekaakkleeakkleleqags 628
Cdd:cd14901 477 SV-SKLQQGKRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFL--------------------------- 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 629 kkpgpirtvnrKPTLGSMFKQSLIELMNTINSTNVHYIRCIKPNADKEAWQFDNLMVLSQLRACGVLETIRISCAGFPSR 708
Cdd:cd14901 529 -----------SSTVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVR 597
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 768464868 709 WTFEEFVLRYYILIPheQWDLIFKKKETTEEDIISVVKMILdATVKDKSKYQIGNTKIF 767
Cdd:cd14901 598 FPHDAFVHTYSCLAP--DGASDTWKVNELAERLMSQLQHSE-LNIEHLPPFQVGKTKVF 653
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
84-769 |
0e+00 |
|
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or C-terminal to their motor domain and a tail with a MyTH4 domain followed by a SH3 domain in some instances. The monomeric Acanthamoebas were the first identified members of this group and have been joined by Stramenopiles. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276839 Cd Length: 644 Bit Score: 570.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 84 PAVLHAIKQRYSQLNIYTYSGIVLIATNPFDRVdQLYTQDMIQAYAGKRRGELEPHLFAIAEEAYRLMKNDKQNQTIVVS 163
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRL-PLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 164 GESGAGKTVSAKYIMRYFASVEEENSATvqhqvemsetEQKILATNPIMEAFGNAKTTRNDNSSRFGKYLEILFDKDTSI 243
Cdd:cd14872 80 GESGAGKTEATKQCLSFFAEVAGSTNGV----------EQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 244 IGARIRTYLLERSRLVYQPPTERNYHIFYQLMAGLPAQTKEElhLTDASDYFYMNQGGDTKINGIDDAKEYKITVDALTL 323
Cdd:cd14872 150 CGASTENYLLEKSRVVYQIKGERNFHIFYQLLASPDPASRGG--WGSSAAYGYLSLSGCIEVEGVDDVADFEEVVLAMEQ 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 324 VGITKETQHQIFKILAALLHIGNIEIK----KTRNDASLSADEPNLKLACELLGIDAYNFAKWVTKKQIITR-SEKIVSN 398
Cdd:cd14872 228 LGFDDADINNVMSLIAAILKLGNIEFAsgggKSLVSGSTVANRDVLKEVATLLGVDAATLEEALTSRLMEIKgCDPTRIP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 399 LNYNQALVAKDSVAKFIYSALFDWLVENINTVLcnPAVNDQISSFIGVLDIYGFEHFEKNSFEQFCINYANEKLQQEFNQ 478
Cdd:cd14872 308 LTPAQATDACDALAKAAYSRLFDWLVKKINESM--RPQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEKLQQHFNQ 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 479 HVFKLEQEEYVKEEIEWSFIEFNDNQPCIDLIENKL-GILSLLDEESRLPAGSDESWTQKLYQTLDKSpTNKVFSKPRFG 557
Cdd:cd14872 386 YTFKLEEALYQSEGVKFEHIDFIDNQPVLDLIEKKQpGLMLALDDQVKIPKGSDATFMIAANQTHAAK-STFVYAEVRTS 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 558 QTKFIVSHYALDVAYDVEGFIEKNRDTVSDGHLEVLKASTNEtLINILeglekaakkleeakkleleqagsKKPGPIRTV 637
Cdd:cd14872 465 RTEFIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNK-LIAVL-----------------------FPPSEGDQK 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 638 NRKPTLGSMFKQSLIELMNTINSTNVHYIRCIKPNADKEAWQFDNLMVLSQLRACGVLETIRISCAGFPSRWTFEEFVLR 717
Cdd:cd14872 521 TSKVTLGGQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKR 600
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 768464868 718 YYILI-PHEQWDLifKKKETTEEDIISVVKmildatvKDKSKYQIGNTKIFFK 769
Cdd:cd14872 601 YRFLVkTIAKRVG--PDDRQRCDLLLKSLK-------QDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
84-769 |
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: 564.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 84 PAVLHAIKQRYSQLNIYTYSGIVLIATNPFDRVDQLYTQDMIQAYAGKRRGELEPHLFAIAEEAYRLMKNDKQNQTIVVS 163
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDNLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 164 GESGAGKTVSAKYIMRYFASVEEENSatvqhqvemSETEQKILATNPIMEAFGNAKTTRNDNSSRFGKYLEILFDKDTSI 243
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVAGGRK---------DKTIAKVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRGKL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 244 IGARIRTYLLERSRLVYQPPTERNYHIFYQLMAGLPAQTKEELHLTDASDYFYMNQGGD-TKINGIDDAKEYKITVDALT 322
Cdd:cd14904 152 IGAKCETYLLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQYLGDSLAqMQIPGLDDAKLFASTQKSLS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 323 LVGITKETQHQIFKILAALLHIGNIEIKKTRNDASLSADEPNLKLACELLGIDAYNFAKWVTKKQIITRSEKIVSNLNYN 402
Cdd:cd14904 232 LIGLDNDAQRTLFKILSGVLHLGEVMFDKSDENGSRISNGSQLSQVAKMLGLPTTRIEEALCNRSVVTRNESVTVPLAPV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 403 QALVAKDSVAKFIYSALFDWLVENINTVLCNPavNDQISSFIGVLDIYGFEHFEKNSFEQFCINYANEKLQQEFNQHVFK 482
Cdd:cd14904 312 EAEENRDALAKAIYSKLFDWMVVKINAAISTD--DDRIKGQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDVFK 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 483 LEQEEYVKEEIEWSFIEFNDNQPCIDLIENKLGILSLLDEESRLPAGSDESWTQKLYQTLDKSPTNKVFSKPRFGQTKFI 562
Cdd:cd14904 390 TVEEEYIREGLQWDHIEYQDNQGIVEVIDGKMGIIALMNDHLRQPRGTEEALVNKIRTNHQTKKDNESIDFPKVKRTQFI 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 563 VSHYALDVAYDVEGFIEKNRDTVSDGHLEVLKASTNETLINILEGLEkaakkleeakkLELEQAGSKKPgpiRTVNRKPT 642
Cdd:cd14904 470 INHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFGSSE-----------APSETKEGKSG---KGTKAPKS 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 643 LGSMFKQSLIELMNTINSTNVHYIRCIKPNADKEAWQFDNLMVLSQLRACGVLETIRISCAGFPSRWTFEEFVLRYYILI 722
Cdd:cd14904 536 LGSQFKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAIMF 615
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 768464868 723 PHEQWDlifKKKETTEEDIISVVKMildatvKDKSKYQIGNTKIFFK 769
Cdd:cd14904 616 PPSMHS---KDVRRTCSVFMTAIGR------KSPLEYQIGKSLIYFK 653
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
84-733 |
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: 558.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 84 PAVLHAIKQRYSQLNIYTYSGIVLIATNPFDRVDQLYTQDMIQAYAgKRRGELEPHLFAIAEEAYRLMKNDKQNQTIVVS 163
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPGLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 164 GESGAGKTVSAKYIMRYFA---SVEEENSATVqhqvemsetEQKILATNPIMEAFGNAKTTRNDNSSRFGKYLEILFDKD 240
Cdd:cd14888 80 GESGAGKTESTKYVMKFLAcagSEDIKKRSLV---------EAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFSKL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 241 TS---------IIGARIRTYLLERSRLVYQPPTERNYHIFYQLMAGLPAQTKEELHLTDASDYF---------------- 295
Cdd:cd14888 151 KSkrmsgdrgrLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAREAKNTGLSYEENDEKLakgadakpisidmssf 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 296 -------YMNQGGDTKINGIDDAKEYKITVDALTLVGITKETQHQIFKILAALLHIGNI--EIKKTRNDASLSADEP--N 364
Cdd:cd14888 231 ephlkfrYLTKSSCHELPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNIlfENNEACSEGAVVSASCtdD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 365 LKLACELLGIDAYNFAKWVTKKQIITRSEKIVSNLNYNQALVAKDSVAKFIYSALFDWLVENINTVLcnPAVNDQISSFI 444
Cdd:cd14888 311 LEKVASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESI--GYSKDNSLLFC 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 445 GVLDIYGFEHFEKNSFEQFCINYANEKLQQEFNQHVFKLEQEEYVKEEIEWSFIEFNDNQPCIDLIENK-LGILSLLDEE 523
Cdd:cd14888 389 GVLDIFGFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFPDNQDCVDLLQEKpLGIFCMLDEE 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 524 SRLPAGSDESWTQKLYQtldKSPTNKVFSKPRFGQTKFIVSHYALDVAYDVEGFIEKNRDTVSDGHLEVLKASTNETLIN 603
Cdd:cd14888 469 CFVPGGKDQGLCNKLCQ---KHKGHKRFDVVKTDPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKNPFISN 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 604 ILEGLEKAAKKLEEAKKleleqagskkpgpirtvnRKPTLGSMFKQSLIELMNTINSTNVHYIRCIKPNADKEAWQFDNL 683
Cdd:cd14888 546 LFSAYLRRGTDGNTKKK------------------KFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRI 607
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 684 MVLSQLRACGVLETIRISCAGFPSRWTFEEFVLRYYILIP------HEQW----DLIFKK 733
Cdd:cd14888 608 SVNEQLKYGGVLQAVQVSRAGYPVRLSHAEFYNDYRILLNgegkkqLSIWavgkTLCFFK 667
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
84-769 |
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: 555.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 84 PAVLHAIKQRYSQLNIYTYSGIVLIATNPFDRVDqLYTQDMIQAYAGKRRGELEPHLFAIAEEAYRLMKNDKQNQTIVVS 163
Cdd:cd01379 1 DTIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLG-IYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 164 GESGAGKTVSAKYImryfasveeensatVQHQVEMSET-----EQKILATNPIMEAFGNAKTTRNDNSSRFGKYLEILFD 238
Cdd:cd01379 80 GESGAGKTESANLL--------------VQQLTVLGKAnnrtlEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 239 KDTSIIGARIRTYLLERSRLVYQPPTERNYHIFYQLMAGLPAQTK-EELHLTDASDYFYMNQGGDTKINGIDDA---KEY 314
Cdd:cd01379 146 STGAVTGARISEYLLEKSRVVHQAIGERNFHIFYYIYAGLAEDKKlAKYKLPENKPPRYLQNDGLTVQDIVNNSgnrEKF 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 315 KITVDALTLVGITKETQHQIFKILAALLHIGNIEIKKTRN-----DASLSADEPNLKLACELLGIDAYNFAKWVTKKQII 389
Cdd:cd01379 226 EEIEQCFKVIGFTKEEVDSVYSILAAILHIGDIEFTEVESnhqtdKSSRISNPEALNNVAKLLGIEADELQEALTSHSVV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 390 TRSEKIVSNLNYNQALVAKDSVAKFIYSALFDWLVENINTVLC--NPAVNDQISsfIGVLDIYGFEHFEKNSFEQFCINY 467
Cdd:cd01379 306 TRGETIIRNNTVEEATDARDAMAKALYGRLFSWIVNRINSLLKpdRSASDEPLS--IGILDIFGFENFQKNSFEQLCINI 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 468 ANEKLQQEFNQHVFKLEQEEYVKEEIEWSFIEFNDNQPCIDLIENK-LGILSLLDEESRLPAGSDESWTQKLYQTLdKSp 546
Cdd:cd01379 384 ANEQIQYYFNQHIFAWEQQEYLNEGIDVDLIEYEDNRPLLDMFLQKpMGLLALLDEESRFPKATDQTLVEKFHNNI-KS- 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 547 tnKVFSKPRFGQTKFIVSHYALDVAYDVEGFIEKNRDTVSDGHLEVLKASTNETLinileglekaakkleeakkleleqa 626
Cdd:cd01379 462 --KYYWRPKSNALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLV------------------------- 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 627 gskkpgpirtvnrKPTLGSMFKQSLIELMNTINSTNVHYIRCIKPNADKEAWQFDNLMVLSQLRACGVLETIRISCAGFP 706
Cdd:cd01379 515 -------------RQTVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFS 581
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768464868 707 SRWTFEEFVLRYYIlipheqwdLIFKKKETTEEDIISVVKMILDATVkdkSKYQIGNTKIFFK 769
Cdd:cd01379 582 HRILFADFLKRYYF--------LAFKWNEEVVANRENCRLILERLKL---DNWALGKTKVFLK 633
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
85-769 |
1.01e-174 |
|
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: 540.37 E-value: 1.01e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 85 AVLHAIKQRYSQLNIYTYSGIVLIATNPFDRVdQLYTQDMIQAYAGKRRGELEPHLFAIAEEAYRLMKNDKQNQTIVVSG 164
Cdd:cd14920 2 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNL-PIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 165 ESGAGKTVSAKYIMRYFASVEEENSATVQHQVEmSETEQKILATNPIMEAFGNAKTTRNDNSSRFGKYLEILFDKDTSII 244
Cdd:cd14920 81 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIP-GELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 245 GARIRTYLLERSRLVYQPPTERNYHIFYQLMAGLPAQTKEELHLTDASDYFYMNqGGDTKINGIDDAKEYKITVDALTLV 324
Cdd:cd14920 160 GANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLS-NGYIPIPGQQDKDNFQETMEAMHIM 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 325 GITKETQHQIFKILAALLHIGNIEIKKTRN--DASLSADEPNLKLaCELLGIDAYNFAKWVTKKQIITRSEKIVSNLNYN 402
Cdd:cd14920 239 GFSHEEILSMLKVVSSVLQFGNISFKKERNtdQASMPENTVAQKL-CHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 403 QALVAKDSVAKFIYSALFDWLVENINTVLcnPAVNDQISSFIGVLDIYGFEHFEKNSFEQFCINYANEKLQQEFNQHVFK 482
Cdd:cd14920 318 QADFAVEALAKATYERLFRWLVHRINKAL--DRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFI 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 483 LEQEEYVKEEIEWSFIEFN-DNQPCIDLIE---NKLGILSLLDEESRLPAGSDESWTQKLYQTLDKSPTnkvFSKPR--F 556
Cdd:cd14920 396 LEQEEYQREGIEWNFIDFGlDLQPCIDLIErpaNPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSK---FQKPRqlK 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 557 GQTKFIVSHYALDVAYDVEGFIEKNRDTVSDGHLEVLKASTNETLINILEGLEKAAKKLEEAKKLELEQAGS--KKPGPI 634
Cdd:cd14920 473 DKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTETAFGSAykTKKGMF 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 635 RTVnrkptlGSMFKQSLIELMNTINSTNVHYIRCIKPNADKEAWQFDNLMVLSQLRACGVLETIRISCAGFPSRWTFEEF 714
Cdd:cd14920 553 RTV------GQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEF 626
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 768464868 715 VLRYYILIPHEQWDLIFKKKETTEediisvvkMILDATVKDKSKYQIGNTKIFFK 769
Cdd:cd14920 627 RQRYEILTPNAIPKGFMDGKQACE--------RMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
84-769 |
2.27e-170 |
|
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: 527.69 E-value: 2.27e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 84 PAVLH--AIKQRYSQLNIYTYSGIVLIATNPFDRVDQLYTQDmiqaYAGKRRGELEPHLFAIAEEAYRLM---KNDKQNQ 158
Cdd:cd14891 1 AGILHnlEERSKLDNQRPYTFMANVLIAVNPLRRLPEPDKSD----YINTPLDPCPPHPYAIAEMAYQQMclgSGRMQNQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 159 TIVVSGESGAGKTVSAKYIMRYFASVEEENSATVQHQVEMS---------ETEQKILATNPIMEAFGNAKTTRNDNSSRF 229
Cdd:cd14891 77 SIVISGESGAGKTETSKIILRFLTTRAVGGKKASGQDIEQSskkrklsvtSLDERLMDTNPILESFGNAKTLRNHNSSRF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 230 GKYLEILFDKDT-SIIGARIRTYLLERSRLVYQPPTERNYHIFYQLMAGLPAQTKEELHLTDASDYFYMNQGGDTKINGI 308
Cdd:cd14891 157 GKFMKLQFTKDKfKLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSPEDFIYLNQSGCVSDDNI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 309 DDAKEYKITVDALTLVGITKETQHQIFKILAALLHIGNIEIKKTRNDASLS-----ADEPNLKLACELLGIDAYNFAKWV 383
Cdd:cd14891 237 DDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEEDTSEGEAeiaseSDKEALATAAELLGVDEEALEKVI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 384 TKKQIITRSEKIVSNLNYNQALVAKDSVAKFIYSALFDWLVENINTVLcnpAVNDQISSFIGVLDIYGFEHFE-KNSFEQ 462
Cdd:cd14891 317 TQREIVTRGETFTIKRNAREAVYSRDAIAKSIYERLFLWIVQQINTSL---GHDPDPLPYIGVLDIFGFESFEtKNDFEQ 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 463 FCINYANEKLQQEFNQHVFKLEQEEYVKEEIEWSFIEFNDNQPCIDLIENKL-GILSLLDEESRLPAGSDESWTQKLYQT 541
Cdd:cd14891 394 LLINYANEALQATFNQQVFIAEQELYKSEGIDVGVITWPDNRECLDLIASKPnGILPLLDNEARNPNPSDAKLNETLHKT 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 542 LDKSPTnkvF--SKPRFGQTKFIVSHYALDVAYDVEGFIEKNRDTVSDGhlevlkastnetliniLEGLEKAAKKleeak 619
Cdd:cd14891 474 HKRHPC---FprPHPKDMREMFIVKHYAGTVSYTIGSFIDKNNDIIPED----------------FEDLLASSAK----- 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 620 kleleqagskkpgpirtvnrkptlgsmFKQSLIELMNTINSTNVHYIRCIKPNADKEAWQFDNLMVLSQLRACGVLETIR 699
Cdd:cd14891 530 ---------------------------FSDQMQELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCE 582
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 700 ISCAGFPSRWTFEEFVLRYYILIPhEQWDLIFKKKETTeediisVVKMILDATVKDKSKYQIGNTKIFFK 769
Cdd:cd14891 583 VLKVGLPTRVTYAELVDVYKPVLP-PSVTRLFAENDRT------LTQAILWAFRVPSDAYRLGRTRVFFR 645
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
86-721 |
1.06e-169 |
|
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: 526.52 E-value: 1.06e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 86 VLHAIKQRYSQLNIYTYSGIVLIATNPFDRVDQLYTQDMIQAY--AGKRRGEL------EPHLFAIAEEAYRLMKNDKQN 157
Cdd:cd14907 3 LLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDNLFSEEVMQMYkeQIIQNGEYfdikkePPHIYAIAALAFKQLFENNKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 158 QTIVVSGESGAGKTVSAKYIMRYFASVEEENSATVQHQVEMSET----------EQKILATNPIMEAFGNAKTTRNDNSS 227
Cdd:cd14907 83 QAIVISGESGAGKTENAKYAMKFLTQLSQQEQNSEEVLTLTSSIratskstksiEQKILSCNPILEAFGNAKTVRNDNSS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 228 RFGKYLEILFDKDTS-IIGARIRTYLLERSRLVYQPPTERNYHIFYQLMAGLPAQTKEELHLTDASD---YFYMNQGGDT 303
Cdd:cd14907 163 RFGKYVSILVDKKKRkILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLKNQLSgdrYDYLKKSNCY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 304 KINGIDDAKEYKITVDALTLVGITKETQHQIFKILAALLHIGNIEIkktrNDASLSADEPN-------LKLACELLGIDA 376
Cdd:cd14907 243 EVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQF----DDSTLDDNSPCcvknketLQIIAKLLGIDE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 377 YNFAKWVTKKQIITRSEKIVSNLNYNQALVAKDSVAKFIYSALFDWLVENIN-TVLCNPAVNDQISSF----IGVLDIYG 451
Cdd:cd14907 319 EELKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNdTIMPKDEKDQQLFQNkylsIGLLDIFG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 452 FEHFEKNSFEQFCINYANEKLQQEFNQHVFKLEQEEYVKEEIE--WSFIEFNDNQPCIDLIE-NKLGILSLLDEESRLPA 528
Cdd:cd14907 399 FEVFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEdyLNQLSYTDNQDVIDLLDkPPIGIFNLLDDSCKLAT 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 529 GSDESWTQKLYQTLDKSPTNKVFSKprFGQTKFIVSHYALDVAYDVEGFIEKNRDTVSDGHLEVLKASTNETLINILEGl 608
Cdd:cd14907 479 GTDEKLLNKIKKQHKNNSKLIFPNK--INKDTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIFSG- 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 609 ekaakkleeakklELEQAGSKKPGPIRTVNRKPTLGSMFKQSLIELMNTINSTNVHYIRCIKPNADKEAWQFDNLMVLSQ 688
Cdd:cd14907 556 -------------EDGSQQQNQSKQKKSQKKDKFLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQ 622
|
650 660 670
....*....|....*....|....*....|...
gi 768464868 689 LRACGVLETIRISCAGFPSRWTFEEFVLRYYIL 721
Cdd:cd14907 623 IRYLGVLESIRVRKQGYPYRKSYEDFYKQYSLL 655
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
84-769 |
2.46e-169 |
|
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: 525.56 E-value: 2.46e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 84 PAVLHAIKQRYSQLNIYTYSGIVLIATNPFDRVdQLYTQDMIQAYAGKRRGELEPHLFAIAEEAYRLMKNDKQNQTIVVS 163
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRY-PVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 164 GESGAGKTVSAKYIMRYFASVEEeNSATVQHQVEMSETEQKILATNPIMEAFGNAKTTRNDNSSRFGKYLEILFDKDTSI 243
Cdd:cd14909 80 GESGAGKTENTKKVIAYFATVGA-SKKTDEAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 244 IGARIRTYLLERSRLVYQPPTERNYHIFYQLMAGLPAQTKEELHLT-DASDYFYMNQgGDTKINGIDDAKEYKITVDALT 322
Cdd:cd14909 159 AGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLSdNIYDYYIVSQ-GKVTVPNVDDGEEFSLTDQAFD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 323 LVGITKETQHQIFKILAALLHIGNIEIKKTRNDASLSAD--EPNLKLAcELLGIDAYNFAKWVTKKQIITRSEKIVSNLN 400
Cdd:cd14909 238 ILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDgeEEGGRVS-KLFGCDTAELYKNLLKPRIKVGNEFVTQGRN 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 401 YNQALVAKDSVAKFIYSALFDWLVENINTVLcnpAVNDQISSFIGVLDIYGFEHFEKNSFEQFCINYANEKLQQEFNQHV 480
Cdd:cd14909 317 VQQVTNSIGALCKGVFDRLFKWLVKKCNETL---DTQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHM 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 481 FKLEQEEYVKEEIEWSFIEFN-DNQPCIDLIENKLGILSLLDEESRLPAGSDESWTQKLYQT-LDKSPTNKVFSKPRFGQ 558
Cdd:cd14909 394 FVLEQEEYKREGIDWAFIDFGmDLLACIDLIEKPMGILSILEEESMFPKATDQTFSEKLTNThLGKSAPFQKPKPPKPGQ 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 559 --TKFIVSHYALDVAYDVEGFIEKNRDTVSDGHLEVLKASTNETLINILEGLEKAAKKLEEAKKleleqAGSKKPGPIRT 636
Cdd:cd14909 474 qaAHFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAGQSGGGEQAKG-----GRGKKGGGFAT 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 637 VNrkptlgSMFKQSLIELMNTINSTNVHYIRCIKPNADKEAWQFDNLMVLSQLRACGVLETIRISCAGFPSRWTFEEFVL 716
Cdd:cd14909 549 VS------SAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKM 622
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 768464868 717 RYYILIPHEQwdlifkKKETTEEdiiSVVKMILDATVKDKSKYQIGNTKIFFK 769
Cdd:cd14909 623 RYKILNPAGI------QGEEDPK---KAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
85-769 |
2.80e-169 |
|
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: 525.70 E-value: 2.80e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 85 AVLHAIKQRYSQLNIYTYSGIVLIATNPFDRVdQLYTQDMIQAYAGKRRGELEPHLFAIAEEAYRLMKNDKQNQTIVVSG 164
Cdd:cd14911 2 SVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKL-PIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 165 ESGAGKTVSAKYIMRYFASV---EEENSATVQH-----QVEMSETEQKILATNPIMEAFGNAKTTRNDNSSRFGKYLEIL 236
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVaasKPKGSGAVPHpavnpAVLIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 237 FDKDTSIIGARIRTYLLERSRLVYQPPTERNYHIFYQLMAGLPAQTKEELHLTDASDYFYMNQgGDTKINGIDDAKEYKI 316
Cdd:cd14911 161 FDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSN-GSLPVPGVDDYAEFQA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 317 TVDALTLVGITKETQHQIFKILAALLHIGNIEIKKTRND--ASLSADEPNLKLAcELLGIDAYNFAKWVTKKQIITRSEK 394
Cdd:cd14911 240 TVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNdqATLPDNTVAQKIA-HLLGLSVTDMTRAFLTPRIKVGRDF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 395 IVSNLNYNQALVAKDSVAKFIYSALFDWLVENINTVLcnPAVNDQISSFIGVLDIYGFEHFEKNSFEQFCINYANEKLQQ 474
Cdd:cd14911 319 VTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSL--DRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQ 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 475 EFNQHVFKLEQEEYVKEEIEWSFIEFN-DNQPCIDLIENKLGILSLLDEESRLPAGSDESWTQKLYQTLDKSPTnkvFSK 553
Cdd:cd14911 397 LFNHTMFILEQEEYQREGIEWKFIDFGlDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLVSAHSMHPK---FMK 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 554 PRF-GQTKFIVSHYALDVAYDVEGFIEKNRDTVSDGHLEVLKASTNETLINILEGLEKAAkkLEEAKKLELEQAGSKKPG 632
Cdd:cd14911 474 TDFrGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAEIVG--MAQQALTDTQFGARTRKG 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 633 PIRTVNRkptlgsMFKQSLIELMNTINSTNVHYIRCIKPNADKEAWQFDNLMVLSQLRACGVLETIRISCAGFPSRWTFE 712
Cdd:cd14911 552 MFRTVSH------LYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQ 625
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 768464868 713 EFVLRYYILIPHEQWDLIFKKKETTEediisvvKMILdATVKDKSKYQIGNTKIFFK 769
Cdd:cd14911 626 EFRQRYELLTPNVIPKGFMDGKKACE-------KMIQ-ALELDSNLYRVGQSKIFFR 674
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
84-769 |
1.09e-168 |
|
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: 523.77 E-value: 1.09e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 84 PAVLHAIKQRYSQLNIYTYSGIVLIATNPFDRVdQLYTQDMIQAYAGKRRGELEPHLFAIAEEAYRLMKNDKQNQTIVVS 163
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWL-PVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 164 GESGAGKTVSAKYIMRYFASVeeenSATVQHQVEMSETEQKILATNPIMEAFGNAKTTRNDNSSRFGKYLEILFDKDTSI 243
Cdd:cd14929 80 GESGAGKTVNTKHIIQYFATI----AAMIESKKKLGALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGML 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 244 IGARIRTYLLERSRLVYQPPTERNYHIFYQLMAGlpaqtKEELH-----LTDASDyFYMNQGGDTKINGIDDAKEYKITV 318
Cdd:cd14929 156 SSADIDIYLLEKSRVIFQQPGERNYHIFYQILSG-----KKELRdlllvSANPSD-FHFCSCGAVAVESLDDAEELLATE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 319 DALTLVGITKETQHQIFKILAALLHIGNIEIKKTRNDASLSAD-EPNLKLACELLGIDAYNFAKWVTKKQIITRSEKIVS 397
Cdd:cd14929 230 QAMDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADgTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 398 NLNYNQALVAKDSVAKFIYSALFDWLVENINTVLcnpavNDQISS--FIGVLDIYGFEHFEKNSFEQFCINYANEKLQQE 475
Cdd:cd14929 310 SQNIEQVTYAVGALSKSIYERMFKWLVARINRVL-----DAKLSRqfFIGILDITGFEILDYNSLEQLCINFTNEKLQQF 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 476 FNQHVFKLEQEEYVKEEIEWSFIEFN-DNQPCIDLIENKLGILSLLDEESRLPAGSDESWTQKLYQT-LDKSPTnkvFSK 553
Cdd:cd14929 385 FNQHMFVLEQEEYRKEGIDWVSIDFGlDLQACIDLIEKPMGIFSILEEECMFPKATDLTFKTKLFDNhFGKSVH---FQK 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 554 PRFGQTKFIV----SHYALDVAYDVEGFIEKNRDTVSDGHLEVLKASTNETLINILEglekaaKKLEEAKKLELEQAGSK 629
Cdd:cd14929 462 PKPDKKKFEAhfelVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFE------NYISTDSAIQFGEKKRK 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 630 KPGPIRTVnrkptlGSMFKQSLIELMNTINSTNVHYIRCIKPNADKEAWQFDNLMVLSQLRACGVLETIRISCAGFPSRW 709
Cdd:cd14929 536 KGASFQTV------ASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRL 609
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768464868 710 TFEEFVLRYYILIPHeqwdlIFKK------KETTEEdiisvvkmILDATVKDKSKYQIGNTKIFFK 769
Cdd:cd14929 610 LYADFKQRYCILNPR-----TFPKskfvssRKAAEE--------LLGSLEIDHTQYRFGITKVFFK 662
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
86-769 |
4.03e-166 |
|
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: 515.78 E-value: 4.03e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 86 VLHAIKQRYSQLNIYTYSGIVLIATNPFDRVDqLYTQDMIQAYAGKR-RGELEPHLFAIAEEAYRLMKNDKQNQTIVVSG 164
Cdd:cd14897 3 IVQTLKSRYNKDKFYTYIGDILVAVNPCKPLP-IFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 165 ESGAGKTVSAKYImryfasveeensatVQHQVEMSETEQ-----KILATNPIMEAFGNAKTTRNDNSSRFGKYLEILFDK 239
Cdd:cd14897 82 ESGAGKTESTKYM--------------IKHLMKLSPSDDsdlldKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 240 DTSIIGARIRTYLLERSRLVYQPPTERNYHIFYQLMAGLPAQTKEELHLTDASDYFYMnQGGDTKINGIDDAKE---YKI 316
Cdd:cd14897 148 NGQLLGAKIDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDPDCHRIL-RDDNRNRPVFNDSEEleyYRQ 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 317 TVDALT----LVGITKETQHQIFKILAALLHIGNIE-IKKTRNDASLSADEPNLKLACELLGIDAYNFAKWVTKKQIITR 391
Cdd:cd14897 227 MFHDLTnimkLIGFSEEDISVIFTILAAILHLTNIVfIPDEDTDGVTVADEYPLHAVAKLLGIDEVELTEALISNVNTIR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 392 SEKIVSNLNYNQALVAKDSVAKFIYSALFDWLVENINTVLcNPAVNDQI---SSFIGVLDIYGFEHFEKNSFEQFCINYA 468
Cdd:cd14897 307 GERIQSWKSLRQANDSRDALAKDLYSRLFGWIVGQINRNL-WPDKDFQImtrGPSIGILDMSGFENFKINSFDQLCINLS 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 469 NEKLQQEFNQHVFKLEQEEYVKEEIEWSFIEFNDNQPCIDLI-ENKLGILSLLDEESRLPAGSDESWTQKLYqtlDKSPT 547
Cdd:cd14897 386 NERLQQYFNDYVFPRERSEYEIEGIEWRDIEYHDNDDVLELFfKKPLGILPLLDEESTFPQSTDSSLVQKLN---KYCGE 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 548 NKVFSKPRFGQTKFIVSHYALDVAYDVEGFIEKNRDTVSDGHLEVLKASTNEtLINILeglekaakkleeakkleleqag 627
Cdd:cd14897 463 SPRYVASPGNRVAFGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNE-FISDL---------------------- 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 628 skkpgpirtvnrkptLGSMFKQSLIELMNTINSTNVHYIRCIKPNADKEAWQFDNLMVLSQLRACGVLETIRISCAGFPS 707
Cdd:cd14897 520 ---------------FTSYFKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPI 584
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768464868 708 RWTFEEFVLRYYilipheqwDLIFKKKETTEEDIISVVKMILDATVKDkskYQIGNTKIFFK 769
Cdd:cd14897 585 RIKYEDFVKRYK--------EICDFSNKVRSDDLGKCQKILKTAGIKG---YQFGKTKVFLK 635
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
85-769 |
1.69e-165 |
|
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: 516.04 E-value: 1.69e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 85 AVLHAIKQRYSQLNIYTYSGIVLIATNPFDRVdQLYTQDMIQAYAGKRRGELEPHLFAIAEEAYRLMKNDKQNQTIVVSG 164
Cdd:cd14927 2 SVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWL-PVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 165 ESGAGKTVSAKYIMRYFASVEE--ENSATvQHQVEMSET----EQKILATNPIMEAFGNAKTTRNDNSSRFGKYLEILFD 238
Cdd:cd14927 81 ESGAGKTVNTKRVIQYFAIVAAlgDGPGK-KAQFLATKTggtlEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 239 KDTSIIGARIRTYLLERSRLVYQPPTERNYHIFYQLMAGLPAQTKEELHL-TDASDYFYMNQgGDTKINGIDDAKEYKIT 317
Cdd:cd14927 160 PTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLVsMNPYDYHFCSQ-GVTTVDNMDDGEELMAT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 318 VDALTLVGITKETQHQIFKILAALLHIGNIEIKKTRNDASLSAD-EPNLKLACELLGIDAYNFAKWVTKKQIITRSEKIV 396
Cdd:cd14927 239 DHAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADgTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYVT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 397 SNLNYNQALVAKDSVAKFIYSALFDWLVENINTVLcNPAVNDQIssFIGVLDIYGFEHFEKNSFEQFCINYANEKLQQEF 476
Cdd:cd14927 319 KGQSVEQVVYAVGALAKATYDRMFKWLVSRINQTL-DTKLPRQF--FIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFF 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 477 NQHVFKLEQEEYVKEEIEWSFIEFN-DNQPCIDLIENKLGILSLLDEESRLPAGSDESWTQKLYQT-LDKSPTnkvFSKP 554
Cdd:cd14927 396 NHHMFILEQEEYKREGIEWVFIDFGlDLQACIDLIEKPLGILSILEEECMFPKASDASFKAKLYDNhLGKSPN---FQKP 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 555 RFG-----QTKFIVSHYALDVAYDVEGFIEKNRDTVSDGHLEVLKASTNETLINILEGLekAAKKLEEAKKLELEQAgSK 629
Cdd:cd14927 473 RPDkkrkyEAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYENY--VGSDSTEDPKSGVKEK-RK 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 630 KPGPIRTVNRkptlgsMFKQSLIELMNTINSTNVHYIRCIKPNADKEAWQFDNLMVLSQLRACGVLETIRISCAGFPSRW 709
Cdd:cd14927 550 KAASFQTVSQ------LHKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRI 623
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 710 TFEEFVLRYYILIPHEQWDLIFKKKETTEEDIISVVKMildatvkDKSKYQIGNTKIFFK 769
Cdd:cd14927 624 LYADFKQRYRILNPSAIPDDKFVDSRKATEKLLGSLDI-------DHTQYQFGHTKVFFK 676
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
86-769 |
3.98e-165 |
|
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: 514.07 E-value: 3.98e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 86 VLHAIKQRYSQLNIYTYSGIVLIATNPFdRVDQLYTQDMIQAYAGKRRGELEPHLFAIAEEAYRLM----KNDKQNQTIV 161
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPF-KYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMlgrlARGPKNQCIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 162 VSGESGAGKTVSAKYIMRYFASVEEENSatvqhqvemsETEQKILATNPIMEAFGNAKTTRNDNSSRFGKYLEILFdKDT 241
Cdd:cd14889 82 ISGESGAGKTESTKLLLRQIMELCRGNS----------QLEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRF-RNG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 242 SIIGARIRTYLLERSRLVYQPPTERNYHIFYQLMAGLPAQTKEELHLTDASDYFYMNQGGDTKINGIDDAKEYKITVDAL 321
Cdd:cd14889 151 HVKGAKINEYLLEKSRVVHQDGGEENFHIFYYMFAGISAEDRENYGLLDPGKYRYLNNGAGCKREVQYWKKKYDEVCNAM 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 322 TLVGITKETQHQIFKILAALLHIGNIEIKKTRNDASLSADEPN--LKLACELLGIDAYNFAKWVTKKQIITRSEKIVSNL 399
Cdd:cd14889 231 DMVGFTEQEEVDMFTILAGILSLGNITFEMDDDEALKVENDSNgwLKAAAGQFGVSEEDLLKTLTCTVTFTRGEQIQRHH 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 400 NYNQALVAKDSVAKFIYSALFDWLVENINTVLCNPAVNDQISSFIGVLDIYGFEHFEKNSFEQFCINYANEKLQQEFNQH 479
Cdd:cd14889 311 TKQQAEDARDSIAKVAYGRVFGWIVSKINQLLAPKDDSSVELREIGILDIFGFENFAVNRFEQACINLANEQLQYFFNHH 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 480 VFKLEQEEYVKEEIEWSFIEFNDNQPCIDLIENK-LGILSLLDEESRLPAGSDESWTQKLYQTLDKSPTnkvFSKPRFGQ 558
Cdd:cd14889 391 IFLMEQKEYKKEGIDWKEITYKDNKPILDLFLNKpIGILSLLDEQSHFPQATDESFVDKLNIHFKGNSY---YGKSRSKS 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 559 TKFIVSHYALDVAYDVEGFIEKNRDTvsdghlevLKASTNETLINILEGLEKAAKKLEEAKKLELEQAGSKKPGPIRTVN 638
Cdd:cd14889 468 PKFTVNHYAGKVTYNASGFLEKNRDT--------IPASIRTLFINSATPLLSVLFTATRSRTGTLMPRAKLPQAGSDNFN 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 639 --RKPTLGSMFKQSLIELMNTINSTNVHYIRCIKPNADKEAWQFDNLMVLSQLRACGVLETIRISCAGFPSRWTFEEFVL 716
Cdd:cd14889 540 stRKQSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFSWRPSFAEFAE 619
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 768464868 717 RYYILipheqwdLIFKKKETTEEDIISvvkmILDATvkDKSKYQIGNTKIFFK 769
Cdd:cd14889 620 RYKIL-------LCEPALPGTKQSCLR----ILKAT--KLVGWKCGKTRLFFK 659
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
84-715 |
5.95e-164 |
|
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: 513.29 E-value: 5.95e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 84 PAVLHAIKQRYSQLNIYTYSGIVLIATNPFDRVDQLYTQDMIQAY--------AGKRRGELEPHLFAIAEEAYR-LMKND 154
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPDLYSESQLNAYkasmtstsPVSQLSELPPHVFAIGGKAFGgLLKPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 155 KQNQTIVVSGESGAGKTVSAKYIMRYFASVEEENSATVQHQVEMSETEQKILATNPIMEAFGNAKTTRNDNSSRFGKYLE 234
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLTSVGRDQSSTEQEGSDAVEIGKRILQTNPILESFGNAQTIRNDNSSRFGKFIK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 235 ILFDKDTSIIGARIRTYLLERSRLVYQPPTERNYHIFYQLMAGLPAQTKEELHLTDASDYFYMNQGGDT----KINGIDD 310
Cdd:cd14902 161 IQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKGGKYELLNSYGPSfarkRAVADKY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 311 AKEYKITVDALTLVGITKETQHQIFKILAALLHIGNIEIK----KTRNDASLSADEPNLKLACELLGIDAYNFAKWVTKK 386
Cdd:cd14902 241 AQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTaengQEDATAVTAASRFHLAKCAELMGVDVDKLETLLSSR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 387 QIITRSEKIVSNLNYNQALVAKDSVAKFIYSALFDWLVENINTVLCNPAVNDQISSF------IGVLDIYGFEHFEKNSF 460
Cdd:cd14902 321 EIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINYFDSAVSISDEdeelatIGILDIFGFESLNRNGF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 461 EQFCINYANEKLQQEFNQHVFKLEQEEYVKEEIEWSFIEFNDNQPCIDLIENKL-GILSLLDEESRLPAGSDESWTQKLY 539
Cdd:cd14902 401 EQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYPSNAACLALFDDKSnGLFSLLDQECLMPKGSNQALSTKFY 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 540 QTldksptnkvfskpRFGQTKFIVSHYALDVAYDVEGFIEKNRDTVSDGHLEVLKASTNETLINILeGLEKAAKKLEEAK 619
Cdd:cd14902 481 RY-------------HGGLGQFVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVVVAIG-ADENRDSPGADNG 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 620 KleleqAGSKKPGPIRTvnrkPTLGSMFKQSLIELMNTINSTNVHYIRCIKPNADKEAWQFDNLMVLSQLRACGVLETIR 699
Cdd:cd14902 547 A-----AGRRRYSMLRA----PSVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLEAVR 617
|
650
....*....|....*.
gi 768464868 700 ISCAGFPSRWTFEEFV 715
Cdd:cd14902 618 IARHGYSVRLAHASFI 633
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
84-769 |
9.10e-162 |
|
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: 505.98 E-value: 9.10e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 84 PAVLHAIKQRYSQLNIYTYSGIVLIATNPFDRVdQLYTQDMIQAY--AGKRRGE-------LEPHLFAIAEEAYR-LMKN 153
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRL-PLYGKEILESYrqEGLLRSQgiespqaLGPHVFAIADRSYRqMMSE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 154 DKQNQTIVVSGESGAGKTVSAKYIMRYFASVEEENSATVQHQVEMSETE--QKILATNPIMEAFGNAKTTRNDNSSRFGK 231
Cdd:cd14908 80 IRASQSILISGESGAGKTESTKIVMLYLTTLGNGEEGAPNEGEELGKLSimDRVLQSNPILEAFGNARTLRNDNSSRFGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 232 YLEILFDKDTSIIGARIRTYLLERSRLVYQPPTERNYHIFYQLMAGLPAQTKEELHLTD--------ASDYFYMNQGGDT 303
Cdd:cd14908 160 FIELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEEEHEKYEFHDgitgglqlPNEFHYTGQGGAP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 304 KINGIDDAKEYKITVDALTLVGITKETQHQIFKILAALLHIGNIEIK-KTRNDASLSADEPNLKL---ACELLGIDAYNF 379
Cdd:cd14908 240 DLREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFEsKEEDGAAEIAEEGNEKClarVAKLLGVDVDKL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 380 AKWVTKKQIITRSEKIVSNLNYNQALVAKDSVAKFIYSALFDWLVENINTVLcNPAVNDQISSFIGVLDIYGFEHFEKNS 459
Cdd:cd14908 320 LRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSI-NWENDKDIRSSVGVLDIFGFECFAHNS 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 460 FEQFCINYANEKLQQEFNQHVFKLEQEEYVKEEIEWSFIEFNDNQPCIDLIE-NKLGILSLLDEESRLPA-GSDESWTQK 537
Cdd:cd14908 399 FEQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFPDNQDCLDTIQaKKKGILTMLDDECRLGIrGSDANYASR 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 538 LYQTLDKSPTNKVFSKPRFGQTK-------FIVSHYALDVAYDVE-GFIEKNRDTvsdghlevlkastnetlinilegLE 609
Cdd:cd14908 479 LYETYLPEKNQTHSENTRFEATSiqktkliFAVRHFAGQVQYTVEtTFCEKNKDE-----------------------IP 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 610 KAAKKLEEAkkleleqagskkpgpirtvnrkptlGSMFKQSLIELMNTINSTNVHYIRCIKPNADKEAWQFDNLMVLSQL 689
Cdd:cd14908 536 LTADSLFES-------------------------GQQFKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQL 590
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 690 RACGVLETIRISCAGFPSRWTFEEFVLRYYILIPHEQWDLIFKKKETTEEDIISVVKMILD--------ATVKDKS---- 757
Cdd:cd14908 591 RYGGVLEAVRVARSGYPVRLPHKDFFKRYRMLLPLIPEVVLSWSMERLDPQKLCVKKMCKDlvkgvlspAMVSMKNiped 670
|
730
....*....|..
gi 768464868 758 KYQIGNTKIFFK 769
Cdd:cd14908 671 TMQLGKSKVFMR 682
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
86-723 |
1.62e-160 |
|
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: 502.07 E-value: 1.62e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 86 VLHAIKQRYSQLNIYTYSGIVLIATNPFDRVDQLYTQDMIQAY-AGKRRGELEPHLFAIAEEAYRLMKNDKQ--NQTIVV 162
Cdd:cd14880 3 VLRCLQARYTADTFYTNAGCTLVALNPFKPVPQLYSPELMREYhAAPQPQKLKPHIFTVGEQTYRNVKSLIEpvNQSIVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 163 SGESGAGKTVSAKYIMRYFASVEEENSATVQHqvEMSE-TEQKILATNPIMEAFGNAKTTRNDNSSRFGKYLEILFDKDT 241
Cdd:cd14880 83 SGESGAGKTWTSRCLMKFYAVVAASPTSWESH--KIAErIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQLNRAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 242 SIIGARIRTYLLERSRLVYQPPTERNYHIFYQLMAGLPAQTKEELHLTDASDYFYMNQGGDTKingidDAKEYKITVDAL 321
Cdd:cd14880 161 QMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAAFSWLPNPERNL-----EEDCFEVTREAM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 322 TLVGITKETQHQIFKILAALLHIGNIEIKKTRNDAS----LSADEPNLKLACELLGIDAYNFAKWVTKKQIITRSEKIVS 397
Cdd:cd14880 236 LHLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQpcqpMDDTKESVRTSALLLKLPEDHLLETLQIRTIRAGKQQQVF 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 398 NLNYNQAL--VAKDSVAKFIYSALFDWLVENINTVLCnpAVNDQISSFIGVLDIYGFEHFEKNSFEQFCINYANEKLQQE 475
Cdd:cd14880 316 KKPCSRAEcdTRRDCLAKLIYARLFDWLVSVINSSIC--ADTDSWTTFIGLLDVYGFESFPENSLEQLCINYANEKLQQH 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 476 FNQHVFKLEQEEYVKEEIEWSFIEFNDNQPCIDLIE-NKLGILSLLDEESRLPAGSDESWTQ-KLYQTLDKSPT---NKV 550
Cdd:cd14880 394 FVAHYLRAQQEEYAVEGLEWSFINYQDNQTCLDLIEgSPISICSLINEECRLNRPSSAAQLQtRIESALAGNPClghNKL 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 551 FSKPrfgqtKFIVSHYALDVAYDVEGFIEKNRDTVSDGHLEVLKAStNETLINILEGLEKAAKKLEEakkleleqagskk 630
Cdd:cd14880 474 SREP-----SFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQS-QDPLLQKLFPANPEEKTQEE------------- 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 631 pgpIRTVNRKP--TLGSMFKQSLIELMNTINSTNVHYIRCIKPNADKEAWQFDNLMVLSQLRACGVLETIRISCAGFPSR 708
Cdd:cd14880 535 ---PSGQSRAPvlTVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIR 611
|
650
....*....|....*
gi 768464868 709 WTFEEFVLRYYILIP 723
Cdd:cd14880 612 VSHQNFVERYKLLRR 626
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
85-769 |
4.64e-157 |
|
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: 493.39 E-value: 4.64e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 85 AVLHAIKQRYSQLNIYTYSGIVLIATNPFDRVdQLYTQDMIQAYAGKRRGELEPHLFAIAEEAYRLMKNDKQNQTIVVSG 164
Cdd:cd14932 2 SVLHNLKERYYSGLIYTYSGLFCVVINPYKYL-PIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 165 ESGAGKTVSAKYIMRYFASV-------EEENSATVQHqvemSETEQKILATNPIMEAFGNAKTTRNDNSSRFGKYLEILF 237
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVassfktkKDQSSIALSH----GELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 238 DKDTSIIGARIRTYLLERSRLVYQPPTERNYHIFYQLMAGLPAQTKEELHLTDASDYFYMNQGGDTkINGIDDAKEYKIT 317
Cdd:cd14932 157 DVNGYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNVT-IPGQQDKELFAET 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 318 VDALTLVGITKETQHQIFKILAALLHIGNIEIKKTRN-DASLSADEPNLKLACELLGIDAYNFAKWVTKKQIITRSEKIV 396
Cdd:cd14932 236 MEAFRIMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNsDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQ 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 397 SNLNYNQALVAKDSVAKFIYSALFDWLVENINTVLcnPAVNDQISSFIGVLDIYGFEHFEKNSFEQFCINYANEKLQQEF 476
Cdd:cd14932 316 KAQTQEQAEFAVEALAKASYERMFRWLVMRINKAL--DKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLF 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 477 NQHVFKLEQEEYVKEEIEWSFIEFN-DNQPCIDLIENKL---GILSLLDEESRLPAGSDESWTQKLYQTLDKSPTnkvFS 552
Cdd:cd14932 394 NHTMFILEQEEYQREGIEWSFIDFGlDLQPCIELIEKPNgppGILALLDEECWFPKATDKSFVEKVVQEQGNNPK---FQ 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 553 KPR--FGQTKFIVSHYALDVAYDVEGFIEKNRDTVSDGHLEVLKASTNETL------INILEGLEKAAKKLEEAkklelE 624
Cdd:cd14932 471 KPKklKDDADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVselwkdVDRIVGLDKVAGMGESL-----H 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 625 QAGSKKPGPIRTVnrkptlGSMFKQSLIELMNTINSTNVHYIRCIKPNADKEAWQFDNLMVLSQLRACGVLETIRISCAG 704
Cdd:cd14932 546 GAFKTRKGMFRTV------GQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQG 619
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768464868 705 FPSRWTFEEFVLRYYILIPHEQWDLIFKKKEtteediiSVVKMIlDATVKDKSKYQIGNTKIFFK 769
Cdd:cd14932 620 FPNRIVFQEFRQRYEILTPNAIPKGFMDGKQ-------ACVLMV-KALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
84-769 |
9.81e-157 |
|
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: 492.26 E-value: 9.81e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 84 PAVLHAIKQRYSQLNIYTYSGIVLIATNPFDRVdQLYTQDMIQAYAGKRRGELEPHLFAIAEEAYRLMKNDKQNQTIVVS 163
Cdd:cd14913 1 PAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWL-PVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 164 GESGAGKTVSAKYIMRYFASVEEENSATVQHQVEMSET-EQKILATNPIMEAFGNAKTTRNDNSSRFGKYLEILFDKDTS 242
Cdd:cd14913 80 GESGAGKTVNTKRVIQYFATIAATGDLAKKKDSKMKGTlEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 243 IIGARIRTYLLERSRLVYQPPTERNYHIFYQLMAGLPAQTKEELHL-TDASDYFYMNQgGDTKINGIDDAKEYKITVDAL 321
Cdd:cd14913 160 LASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLItTNPYDYPFISQ-GEILVASIDDAEELLATDSAI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 322 TLVGITKETQHQIFKILAALLHIGNIEIKKTRNDASLSAD--EPNLKLAcELLGIDAYNFAKWVTKKQIITRSEKIVSNL 399
Cdd:cd14913 239 DILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDgtEVADKTA-YLMGLNSSDLLKALCFPRVKVGNEYVTKGQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 400 NYNQALVAKDSVAKFIYSALFDWLVENINTVLcNPAVNDQisSFIGVLDIYGFEHFEKNSFEQFCINYANEKLQQEFNQH 479
Cdd:cd14913 318 TVDQVHHAVNALSKSVYEKLFLWMVTRINQQL-DTKLPRQ--HFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHH 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 480 VFKLEQEEYVKEEIEWSFIEFN-DNQPCIDLIENKLGILSLLDEESRLPAGSDESWTQKLY-QTLDKSPTnkvFSKPRFG 557
Cdd:cd14913 395 MFVLEQEEYKKEGIEWTFIDFGmDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYdQHLGKSNN---FQKPKVV 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 558 QTK----FIVSHYALDVAYDVEGFIEKNRDTVSDGHLEVLKASTNETLINILEGLEKAAKKLEEAKkleleqaGSKKPGp 633
Cdd:cd14913 472 KGRaeahFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFATADADSGKKK-------VAKKKG- 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 634 irtvNRKPTLGSMFKQSLIELMNTINSTNVHYIRCIKPNADKEAWQFDNLMVLSQLRACGVLETIRISCAGFPSRWTFEE 713
Cdd:cd14913 544 ----SSFQTVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGD 619
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 714 FVLRYYIL----IPHEQwdliFKKKETTEEDIISVVKMildatvkDKSKYQIGNTKIFFK 769
Cdd:cd14913 620 FKQRYRVLnasaIPEGQ----FIDSKKACEKLLASIDI-------DHTQYKFGHTKVFFK 668
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
84-769 |
1.86e-156 |
|
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: 492.93 E-value: 1.86e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 84 PAVLHAIKQRYSQLNIYTYSGIVLIATNPFDRVDQLYTqdmIQAYAGKRRG--ELEPHLFAIAEEAYRLMK-------ND 154
Cdd:cd14895 1 PAFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIPGLYD---LHKYREEMPGwtALPPHVFSIAEGAYRSLRrrlhepgAS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 155 KQNQTIVVSGESGAGKTVSAKYIMRYFASVEEENSATVQHQVEMSETEQKILATNPIMEAFGNAKTTRNDNSSRFGKYLE 234
Cdd:cd14895 78 KKNQTILVSGESGAGKTETTKFIMNYLAESSKHTTATSSSKRRRAISGSELLSANPILESFGNARTLRNDNSSRFGKFVR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 235 ILF-----DKDTSIIGARIRTYLLERSRLVYQPPTERNYHIFYQLMAGLPAQTKEELHLTD--ASDYFYMNQGGDTKIN- 306
Cdd:cd14895 158 MFFeghelDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQLELlsAQEFQYISGGQCYQRNd 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 307 GIDDAKEYKITVDALTLVGITKETQHQIFKILAALLHIGNIEIKKTRNDAS----LSADEP---------------NLKL 367
Cdd:cd14895 238 GVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEGeednGAASAPcrlasaspssltvqqHLDI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 368 ACELLGIDAYNFAKWVTKKQIITRSEKIVSNLNYNQALVAKDSVAKFIYSALFDWLVENINTVL--------CNPAVNDQ 439
Cdd:cd14895 318 VSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASpqrqfalnPNKAANKD 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 440 ISSFIGVLDIYGFEHFEKNSFEQFCINYANEKLQQEFNQHVFKLEQEEYVKEEIEWSFIEFNDNQPCIDLIENK-LGILS 518
Cdd:cd14895 398 TTPCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDNSVCLEMLEQRpSGIFS 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 519 LLDEESRLPAGSDESWTQKLYQTLDKsptNKVFSKPRFGQTK--FIVSHYALDVAYDVEGFIEKNRDTVSDGHLEVLKAS 596
Cdd:cd14895 478 LLDEECVVPKGSDAGFARKLYQRLQE---HSNFSASRTDQADvaFQIHHYAGAVRYQAEGFCEKNKDQPNAELFSVLGKT 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 597 TNETLINILEGLekaakKLEEAKKLELEQagskkpgpIRTVNRKPTL-----GSMFKQSLIELMNTINSTNVHYIRCIKP 671
Cdd:cd14895 555 SDAHLRELFEFF-----KASESAELSLGQ--------PKLRRRSSVLssvgiGSQFKQQLASLLDVVQQTQTHYIRCIKP 621
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 672 NADKEAWQFDNLMVLSQLRACGVLETIRISCAGFPSRWTFEEFVLRYYILIPHEqwdlifKKKETTEEDIISVVKMIlda 751
Cdd:cd14895 622 NDESASDQFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLVAAK------NASDATASALIETLKVD--- 692
|
730
....*....|....*...
gi 768464868 752 tvkdksKYQIGNTKIFFK 769
Cdd:cd14895 693 ------HAELGKTRVFLR 704
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
74-833 |
8.02e-153 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 486.84 E-value: 8.02e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 74 DLTSLSYLNEPAVLHAIKQRYSQLNIYTYSGIVLIATNPFDRVDqLYTQDMIQAYA-GKRRGELEPHLFAIAEEAYRLMK 152
Cdd:PTZ00014 100 DIGLLPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLG-NTTNDWIRRYRdAKDSDKLPPHVFTTARRALENLH 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 153 NDKQNQTIVVSGESGAGKTVSAKYIMRYFAS-VEEENSATVQhqvemseteQKILATNPIMEAFGNAKTTRNDNSSRFGK 231
Cdd:PTZ00014 179 GVKKSQTIIVSGESGAGKTEATKQIMRYFASsKSGNMDLKIQ---------NAIMAANPVLEAFGNAKTIRNNNSSRFGR 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 232 YLEILFDKDTSIIGARIRTYLLERSRLVYQPPTERNYHIFYQLMAGLPAQTKEELHLTDASDYFYMNQGGdTKINGIDDA 311
Cdd:PTZ00014 250 FMQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKLKSLEEYKYINPKC-LDVPGIDDV 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 312 KEYKITVDALTLVGITKETQHQIFKILAALLHIGNIEIKKTR----NDASLSADEpNLKL---ACELLGIDAYNFAKWVT 384
Cdd:PTZ00014 329 KDFEEVMESFDSMGLSESQIEDIFSILSGVLLLGNVEIEGKEegglTDAAAISDE-SLEVfneACELLFLDYESLKKELT 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 385 KKQIITRSEKIVSNLNYNQALVAKDSVAKFIYSALFDWLVENINTVLCNPavnDQISSFIGVLDIYGFEHFEKNSFEQFC 464
Cdd:PTZ00014 408 VKVTYAGNQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPP---GGFKVFIGMLDIFGFEVFKNNSLEQLF 484
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 465 INYANEKLQQEFNQHVFKLEQEEYVKEEIEWSFIEFNDNQPCIDLIENKL-GILSLLDEESRLPAGSDESWTQKLYQTLD 543
Cdd:PTZ00014 485 INITNEMLQKNFVDIVFERESKLYKDEGISTEELEYTSNESVIDLLCGKGkSVLSILEDQCLAPGGTDEKFVSSCNTNLK 564
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 544 KSPtnkVFSKPRFGQTK-FIVSHYALDVAYDVEGFIEKNRDTVSDGHLEVLKASTNETLINILEGLEKAAKKLeeAKKLe 622
Cdd:PTZ00014 565 NNP---KYKPAKVDSNKnFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLFEGVEVEKGKL--AKGQ- 638
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 623 leqagskkpgpirtvnrkpTLGSMFKQSLIELMNTINSTNVHYIRCIKPNADKEAWQFDNLMVLSQLRACGVLETIRISC 702
Cdd:PTZ00014 639 -------------------LIGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQ 699
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 703 AGFPSRWTFEEFvLRYYiliphEQWDLIFKKKETTEEDIIsvVKMILDATVKDKSKYQIGNTKIFFK---AGMLAYLEKL 779
Cdd:PTZ00014 700 LGFSYRRTFAEF-LSQF-----KYLDLAVSNDSSLDPKEK--AEKLLERSGLPKDSYAIGKTMVFLKkdaAKELTQIQRE 771
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....
gi 768464868 780 RSNKMHNSIVMIQKKIRAKYYRKQYLQISQAIKYLQNNIKgfiiRQRVNDEMKV 833
Cdd:PTZ00014 772 KLAAWEPLVSVLEALILKIKKKRKVRKNIKSLVRIQAHLR----RHLVIAEIKP 821
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
85-769 |
8.75e-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: 479.13 E-value: 8.75e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 85 AVLHAIKQRYSQLNIYTYSGIVLIATNPFDRVdQLYTQDMIQAYAGKRRGELEPHLFAIAEEAYRLMKNDKQNQTIVVSG 164
Cdd:cd14921 2 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKHL-PIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 165 ESGAGKTVSAKYIMRYFASVEEENSATVQHQVeMSETEQKILATNPIMEAFGNAKTTRNDNSSRFGKYLEILFDKDTSII 244
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVVASSHKGKKDTSI-TGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 245 GARIRTYLLERSRLVYQPPTERNYHIFYQLMAGLPAQTKEELHLTDASDYFYMNQgGDTKINGIDDAKEYKITVDALTLV 324
Cdd:cd14921 160 GANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYTFLSN-GFVPIPAAQDDEMFQETLEAMSIM 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 325 GITKETQHQIFKILAALLHIGNIEIKKTRN-DASLSADEPNLKLACELLGIDAYNFAKWVTKKQIITRSEKIVSNLNYNQ 403
Cdd:cd14921 239 GFSEEEQLSILKVVSSVLQLGNIVFKKERNtDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 404 ALVAKDSVAKFIYSALFDWLVENINTVLcnPAVNDQISSFIGVLDIYGFEHFEKNSFEQFCINYANEKLQQEFNQHVFKL 483
Cdd:cd14921 319 ADFAIEALAKATYERLFRWILTRVNKAL--DKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFIL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 484 EQEEYVKEEIEWSFIEFN-DNQPCIDLIE---NKLGILSLLDEESRLPAGSDESWTQKLYQTLDKSPTnkvFSKPR--FG 557
Cdd:cd14921 397 EQEEYQREGIEWNFIDFGlDLQPCIELIErpnNPPGVLALLDEECWFPKATDKSFVEKLCTEQGNHPK---FQKPKqlKD 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 558 QTKFIVSHYALDVAYDVEGFIEKNRDTVSDGHLEVLKASTNETLINILE------GLEKAAKKLEEAkkleLEQAGSKKP 631
Cdd:cd14921 474 KTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKdvdrivGLDQMAKMTESS----LPSASKTKK 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 632 GPIRTVnrkptlGSMFKQSLIELMNTINSTNVHYIRCIKPNADKEAWQFDNLMVLSQLRACGVLETIRISCAGFPSRWTF 711
Cdd:cd14921 550 GMFRTV------GQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVF 623
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 768464868 712 EEFVLRYYILIPHEQWDLIFKKKETteediisvVKMILDATVKDKSKYQIGNTKIFFK 769
Cdd:cd14921 624 QEFRQRYEILAANAIPKGFMDGKQA--------CILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
84-769 |
1.99e-149 |
|
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: 471.57 E-value: 1.99e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 84 PAVLHAIKQRYSQLNIYTYSGIVLIATNPFdRVDQLYTQDMIQAYAGKRRGELEPHLFAIAEEAYRLMKNDKQNQTIVVS 163
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPH-RSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 164 GESGAGKTVSAKYIMRYFASVEEENSATVQHQVEmseteqKILatnPIMEAFGNAKTTRNDNSSRFGKYLEILFDKDTsI 243
Cdd:cd14896 80 GHSGSGKTEAAKKIVQFLSSLYQDQTEDRLRQPE------DVL---PILESFGHAKTILNANASRFGQVLRLHLQHGV-I 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 244 IGARIRTYLLERSRLVYQPPTERNYHIFYQLMAGLPAQTKEELHLTDASDYFYMNQGGDTKINGIDDAKEYKITVDALTL 323
Cdd:cd14896 150 VGASVSHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQGPETYYYLNQGGACRLQGKEDAQDFEGLLKALQG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 324 VGITKETQHQIFKILAALLHIGNIEIKKTRND----ASLSADEpNLKLACELLGIDAYNFAKWVTKKQIITRSEKIVSNL 399
Cdd:cd14896 230 LGLCAEELTAIWAVLAAILQLGNICFSSSEREsqevAAVSSWA-EIHTAARLLQVPPERLEGAVTHRVTETPYGRVSRPL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 400 NYNQALVAKDSVAKFIYSALFDWLVENINTVLCNPAVNDQISSfIGVLDIYGFEHFEKNSFEQFCINYANEKLQQEFNQH 479
Cdd:cd14896 309 PVEGAIDARDALAKTLYSRLFTWLLKRINAWLAPPGEAESDAT-IGVVDAYGFEALRVNGLEQLCINLASERLQLFSSQT 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 480 VFKLEQEEYVKEEIEWSFIEFNDNQPCIDLIENK-LGILSLLDEESRLPAGSDESWTQKLYQTLDKSPTnkvFSKPRFGQ 558
Cdd:cd14896 388 LLAQEEEECQRELLPWVPIPQPPRESCLDLLVDQpHSLLSILDDQTWLSQATDHTFLQKCHYHHGDHPS---YAKPQLPL 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 559 TKFIVSHYALDVAYDVEGFIEKNRDTVSDGHLEVLKASTnetlinilegLEKAAKKLEEAKklelEQAGSKKPgpirtvn 638
Cdd:cd14896 465 PVFTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQ----------LQLVGSLFQEAE----PQYGLGQG------- 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 639 rKPTLGSMFKQSLIELMNTINSTNVHYIRCIKPNADKEAWQFDNLMVLSQLRACGVLETIRISCAGFPSRWTFEEFVLRY 718
Cdd:cd14896 524 -KPTLASRFQQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARF 602
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 768464868 719 YILIPHEQWDLifkkkeTTEEDIISVVKMILDAtvkDKSKYQIGNTKIFFK 769
Cdd:cd14896 603 GALGSERQEAL------SDRERCGAILSQVLGA---ESPLYHLGATKVLLK 644
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
85-769 |
6.77e-149 |
|
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: 471.05 E-value: 6.77e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 85 AVLHAIKQRYSQLNIYTYSGIVLIATNPFDRVdQLYTQDMIQAYAGKRRGELEPHLFAIAEEAYRLMKNDKQNQTIVVSG 164
Cdd:cd14934 2 SVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWL-PIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 165 ESGAGKTVSAKYIMRYFASVeeeNSATVQHQVEMSETEQKILATNPIMEAFGNAKTTRNDNSSRFGKYLEILFDKDTSII 244
Cdd:cd14934 81 ESGAGKTENTKKVIQYFANI---GGTGKQSSDGKGSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 245 GARIRTYLLERSRLVYQPPTERNYHIFYQLMAGLPAQTKEELHLT-DASDYFYMNQgGDTKINGIDDAKEYKITVDALTL 323
Cdd:cd14934 158 GADIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLLVpNPKEYHWVSQ-GVTVVDNMDDGEELQITDVAFDV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 324 VGITKETQHQIFKILAALLHIGNIEIK-KTRND-ASLSADEPNLKLAcELLGIDAYNFAKWVTKKQIITRSEKIVSNLNY 401
Cdd:cd14934 237 LGFSAEEKIGVYKLTGGIMHFGNMKFKqKPREEqAEVDTTEVADKVA-HLMGLNSGELQKGITRPRVKVGNEFVQKGQNM 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 402 NQALVAKDSVAKFIYSALFDWLVENINTVLcnpAVNDQISSFIGVLDIYGFEHFEKNSFEQFCINYANEKLQQEFNQHVF 481
Cdd:cd14934 316 EQCNNSIGALGKAVYDKMFKWLVVRINKTL---DTKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMF 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 482 KLEQEEYVKEEIEWSFIEFN-DNQPCIDLIENKLGILSLLDEESRLPAGSDESWTQKLYQT-LDKSPTnkvFSKPRFGQT 559
Cdd:cd14934 393 VLEQEEYKREGIEWVFIDFGlDLQACIDLLEKPMGIFSILEEQCVFPKATDATFKAALYDNhLGKSSN---FLKPKGGKG 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 560 K-----FIVSHYALDVAYDVEGFIEKNRDTVsdghlevlkastNETLINILEglEKAAKKLEEAKKLELEQAGSKKPgpi 634
Cdd:cd14934 470 KgpeahFELVHYAGTVGYNITGWLEKNKDPL------------NETVVGLFQ--KSSLGLLALLFKEEEAPAGSKKQ--- 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 635 RTVNRKPTLGSMFKQSLIELMNTINSTNVHYIRCIKPNADKEAWQFDNLMVLSQLRACGVLETIRISCAGFPSRWTFEEF 714
Cdd:cd14934 533 KRGSSFMTVSNFYREQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEF 612
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 768464868 715 VLRYYILIPHEQWDLIFKKKETTEediisvvkMILDATVKDKSKYQIGNTKIFFK 769
Cdd:cd14934 613 KQRYQVLNPNVIPQGFVDNKKASE--------LLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
85-769 |
9.76e-149 |
|
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: 470.73 E-value: 9.76e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 85 AVLHAIKQRYSQLNIYTYSGIVLIATNPFDRVdQLYTQDMIQAYAGKRRGELEPHLFAIAEEAYRLMKNDKQNQTIVVSG 164
Cdd:cd14930 2 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQL-PIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 165 ESGAGKTVSAKYIMRYFASVEEENSATVQHQVEmSETEQKILATNPIMEAFGNAKTTRNDNSSRFGKYLEILFDKDTSII 244
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVP-GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 245 GARIRTYLLERSRLVYQPPTERNYHIFYQLMAGLPAQTKEELHLTDASDYFYMNQGGDTKINgiDDAKEYKITVDALTLV 324
Cdd:cd14930 160 GANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPG--QERELFQETLESLRVL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 325 GITKETQHQIFKILAALLHIGNIEIKKTRN-DASLSADEPNLKLACELLGIDAYNFAKWVTKKQIITRSEKIVSNLNYNQ 403
Cdd:cd14930 238 GFSHEEITSMLRMVSAVLQFGNIVLKRERNtDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 404 ALVAKDSVAKFIYSALFDWLVENINTVLCNPAvnDQISSFIGVLDIYGFEHFEKNSFEQFCINYANEKLQQEFNQHVFKL 483
Cdd:cd14930 318 ADFALEALAKATYERLFRWLVLRLNRALDRSP--RQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 484 EQEEYVKEEIEWSFIEFN-DNQPCIDLIE---NKLGILSLLDEESRLPAGSDESWTQKLYQTLDKSPTnkvFSKPR--FG 557
Cdd:cd14930 396 EQEEYQREGIPWTFLDFGlDLQPCIDLIErpaNPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPK---FQRPRhlRD 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 558 QTKFIVSHYALDVAYDVEGFIEKNRDTVSDGHLEVLKASTNETLINILEGLEKAAkKLEEAKKLeleqaGSKKPG--PIR 635
Cdd:cd14930 473 QADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIV-GLEQVSSL-----GDGPPGgrPRR 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 636 TVNRkpTLGSMFKQSLIELMNTINSTNVHYIRCIKPNADKEAWQFDNLMVLSQLRACGVLETIRISCAGFPSRWTFEEFV 715
Cdd:cd14930 547 GMFR--TVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFR 624
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 768464868 716 LRYYILIPHEQWDLIFKKKETTEediisvvKMIlDATVKDKSKYQIGNTKIFFK 769
Cdd:cd14930 625 QRYEILTPNAIPKGFMDGKQACE-------KMI-QALELDPNLYRVGQSKIFFR 670
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
86-721 |
2.20e-148 |
|
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276865 Cd Length: 627 Bit Score: 468.25 E-value: 2.20e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 86 VLHAIKQRYSQLNIYTYSGIVLIATNPFDRVDQLYTQDMIQAYA-----------GKRRGELEPHLFAIAEEAYRLMKN- 153
Cdd:cd14900 3 ILSALETRFYAQKIYTNTGAILLAVNPFQKLPGLYSSDTMAKYLlsfearssstrNKGSDPMPPHIYQVAGEAYKAMMLg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 154 ---DKQNQTIVVSGESGAGKTVSAKYIMRYFASV-EEENSATVQHQVEMSETEQKILATNPIMEAFGNAKTTRNDNSSRF 229
Cdd:cd14900 83 lngVMSDQSILVSGESGSGKTESTKFLMEYLAQAgDNNLAASVSMGKSTSGIAAKVLQTNILLESFGNARTLRNDNSSRF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 230 GKYLEILFDKDTSIIGARIRTYLLERSRLVYQPPTERNYHIFYQLMAGL-PAQTKEelhltdasdyfymnqggdtkingi 308
Cdd:cd14900 163 GKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGAsEAARKR------------------------ 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 309 ddaKEYKITVDALTLVGITKETQHQIFKILAALLHIGNIEIKKTRNDASLSADEPNLKLACE--------LLGIDAYNFA 380
Cdd:cd14900 219 ---DMYRRVMDAMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDRLGQLKSDLAPSSIwsrdaaatLLSVDATKLE 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 381 KWVTKKQIITRSEKIVSNLNYNQALVAKDSVAKFIYSALFDWLVENINTVLC--NPAVNDQISSFIGVLDIYGFEHFEKN 458
Cdd:cd14900 296 KALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLKmdDSSKSHGGLHFIGILDIFGFEVFPKN 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 459 SFEQFCINYANEKLQQEFNQHVFKLEQEEYVKEEIEWSFIEFNDNQPCIDLIENK-LGILSLLDEESRLPAGSDESWTQK 537
Cdd:cd14900 376 SFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFCDNQDCVNLISQRpTGILSLIDEECVMPKGSDTTLASK 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 538 LYQTLDKSPTnkvFSKPRFGQTK--FIVSHYALDVAYDVEGFIEKNRDtvsdghleVLKASTNETLINileglekaakkl 615
Cdd:cd14900 456 LYRACGSHPR---FSASRIQRARglFTIVHYAGHVEYSTDGFLEKNKD--------VLHQEAVDLFVY------------ 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 616 eeakkleleqagskkpgpirtvnrkptlGSMFKQSLIELMNTINSTNVHYIRCIKPNADKEAWQFDNLMVLSQLRACGVL 695
Cdd:cd14900 513 ----------------------------GLQFKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVM 564
|
650 660
....*....|....*....|....*.
gi 768464868 696 ETIRISCAGFPSRWTFEEFVLRYYIL 721
Cdd:cd14900 565 EAVRVARAGFPIRLLHDEFVARYFSL 590
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
84-769 |
7.02e-148 |
|
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: 468.43 E-value: 7.02e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 84 PAVLHAIKQRYSQLNIYTYSGIVLIATNPFDRVdQLYTQDMIQAYAGKRRGELEPHLFAIAEEAYRLMKNDKQNQTIVVS 163
Cdd:cd14917 1 PAVLYNLKERYASWMIYTYSGLFCVTVNPYKWL-PVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 164 GESGAGKTVSAKYIMRYFASVEEENSATVQHQVEMSET-EQKILATNPIMEAFGNAKTTRNDNSSRFGKYLEILFDKDTS 242
Cdd:cd14917 80 GESGAGKTVNTKRVIQYFAVIAAIGDRSKKDQTPGKGTlEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 243 IIGARIRTYLLERSRLVYQPPTERNYHIFYQLMAGLPAQTKEELHLTDAS-DYFYMNQgGDTKINGIDDAKEYKITVDAL 321
Cdd:cd14917 160 LASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPyDYAFISQ-GETTVASIDDAEELMATDNAF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 322 TLVGITKETQHQIFKILAALLHIGNIEIK-KTRNDASLSADEPNLKLACELLGIDAYNFAKWVTKKQIITRSEKIVSNLN 400
Cdd:cd14917 239 DVLGFTSEEKNSMYKLTGAIMHFGNMKFKqKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 401 YNQALVAKDSVAKFIYSALFDWLVENINTVLcnpAVNDQISSFIGVLDIYGFEHFEKNSFEQFCINYANEKLQQEFNQHV 480
Cdd:cd14917 319 VQQVIYATGALAKAVYEKMFNWMVTRINATL---ETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHM 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 481 FKLEQEEYVKEEIEWSFIEFN-DNQPCIDLIENKLGILSLLDEESRLPAGSDESWTQKLYQT-LDKSPTnkvFSKPRFGQ 558
Cdd:cd14917 396 FVLEQEEYKKEGIEWTFIDFGmDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNhLGKSNN---FQKPRNIK 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 559 TK----FIVSHYALDVAYDVEGFIEKNRDTVSDGHLEVLKASTNETLINILEGLEKAAKKLEEAKkleleqAGSKKPGPI 634
Cdd:cd14917 473 GKpeahFSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFANYAGADAPIEKGK------GKAKKGSSF 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 635 RTVNrkptlgSMFKQSLIELMNTINSTNVHYIRCIKPNADKEAWQFDNLMVLSQLRACGVLETIRISCAGFPSRWTFEEF 714
Cdd:cd14917 547 QTVS------ALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDF 620
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 768464868 715 VLRYYILIPHEQWDLIFKKKETTEEDIISVVKMildatvkDKSKYQIGNTKIFFK 769
Cdd:cd14917 621 RQRYRILNPAAIPEGQFIDSRKGAEKLLSSLDI-------DHNQYKFGHTKVFFK 668
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
85-769 |
1.71e-147 |
|
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: 467.65 E-value: 1.71e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 85 AVLHAIKQRYSQLNIYTYSGIVLIATNPFDRVdQLYTQDMIQAYAGKRRGELEPHLFAIAEEAYRLMKNDKQNQTIVVSG 164
Cdd:cd14919 2 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNL-PIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 165 ESGAGKTVSAKYIMRYFASVeeenSATVQHQVEMSETEQKILATNPIMEAFGNAKTTRNDNSSRFGKYLEILFDKDTSII 244
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHV----ASSHKSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 245 GARIRTYLLERSRLVYQPPTERNYHIFYQLMAGLPAQTKEELHLTDASDYFYMNQGGDTkINGIDDAKEYKITVDALTLV 324
Cdd:cd14919 157 GANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVT-IPGQQDKDMFQETMEAMRIM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 325 GITKETQHQIFKILAALLHIGNIEIKKTRN-DASLSADEPNLKLACELLGIDAYNFAKWVTKKQIITRSEKIVSNLNYNQ 403
Cdd:cd14919 236 GIPEEEQMGLLRVISGVLQLGNIVFKKERNtDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQ 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 404 ALVAKDSVAKFIYSALFDWLVENINTVLcnPAVNDQISSFIGVLDIYGFEHFEKNSFEQFCINYANEKLQQEFNQHVFKL 483
Cdd:cd14919 316 ADFAIEALAKATYERMFRWLVLRINKAL--DKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFIL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 484 EQEEYVKEEIEWSFIEFN-DNQPCIDLIENKL---GILSLLDEESRLPAGSDESWTQKLYQTLDKSPTnkvFSKPRFGQT 559
Cdd:cd14919 394 EQEEYQREGIEWNFIDFGlDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVVQEQGTHPK---FQKPKQLKD 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 560 K--FIVSHYALDVAYDVEGFIEKNRDTVSDGHLEVLKASTNETL------INILEGLEKAAKKLEEAkkleLEQAGSKKP 631
Cdd:cd14919 471 KadFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVselwkdVDRIIGLDQVAGMSETA----LPGAFKTRK 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 632 GPIRTVnrkptlGSMFKQSLIELMNTINSTNVHYIRCIKPNADKEAWQFDNLMVLSQLRACGVLETIRISCAGFPSRWTF 711
Cdd:cd14919 547 GMFRTV------GQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVF 620
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 768464868 712 EEFVLRYYILIPHEQWDLIFKKKETteediisvVKMILDATVKDKSKYQIGNTKIFFK 769
Cdd:cd14919 621 QEFRQRYEILTPNSIPKGFMDGKQA--------CVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
85-769 |
8.72e-146 |
|
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: 463.00 E-value: 8.72e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 85 AVLHAIKQRYSQLNIYTYSGIVLIATNPFDRVdQLYTQDMIQAYAGKRRGELEPHLFAIAEEAYRLMKNDKQNQTIVVSG 164
Cdd:cd15896 2 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNL-PIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 165 ESGAGKTVSAKYIMRYFASV-------EEENSATVQHqvemSETEQKILATNPIMEAFGNAKTTRNDNSSRFGKYLEILF 237
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVasshktkKDQNSLALSH----GELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 238 DKDTSIIGARIRTYLLERSRLVYQPPTERNYHIFYQLMAGLPAQTKEELHLTDASDYFYMNQGGDTkINGIDDAKEYKIT 317
Cdd:cd15896 157 DVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYNNYRFLSNGNVT-IPGQQDKDLFTET 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 318 VDALTLVGITKETQHQIFKILAALLHIGNIEIKKTRN-DASLSADEPNLKLACELLGIDAYNFAKWVTKKQIITRSEKIV 396
Cdd:cd15896 236 MEAFRIMGIPEDEQIGMLKVVASVLQLGNMSFKKERHtDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQ 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 397 SNLNYNQALVAKDSVAKFIYSALFDWLVENINTVLcnPAVNDQISSFIGVLDIYGFEHFEKNSFEQFCINYANEKLQQEF 476
Cdd:cd15896 316 KAQTQEQAEFAVEALAKATYERMFRWLVMRINKAL--DKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLF 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 477 NQHVFKLEQEEYVKEEIEWSFIEFN-DNQPCIDLIENKL---GILSLLDEESRLPAGSDESWTQKLYQTLDKSPTnkvFS 552
Cdd:cd15896 394 NHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIEKPAsppGILALLDEECWFPKATDKSFVEKVLQEQGTHPK---FF 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 553 KPR--FGQTKFIVSHYALDVAYDVEGFIEKNRDTVSDGHLEVLKASTNETLINILEGLEKAAKKLEEAKKLELEQAGSKK 630
Cdd:cd15896 471 KPKklKDEADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVDRIVGLDKVSGMSEMPGAFKTR 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 631 PGPIRTVnrkptlGSMFKQSLIELMNTINSTNVHYIRCIKPNADKEAWQFDNLMVLSQLRACGVLETIRISCAGFPSRWT 710
Cdd:cd15896 551 KGMFRTV------GQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIV 624
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 768464868 711 FEEFVLRYYILIPHEQWDLIFKKKETteediisvVKMILDATVKDKSKYQIGNTKIFFK 769
Cdd:cd15896 625 FQEFRQRYEILTPNAIPKGFMDGKQA--------CVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
84-769 |
8.88e-144 |
|
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: 457.66 E-value: 8.88e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 84 PAVLHAIKQRYSQLNIYTYSGIVLIATNPFDRVdQLYTQDMIQAYAGKRRGELEPHLFAIAEEAYRLMKNDKQNQTIVVS 163
Cdd:cd14910 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWL-PVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 164 GESGAGKTVSAKYIMRYFASV--------EEENSATVQHQVEmseteQKILATNPIMEAFGNAKTTRNDNSSRFGKYLEI 235
Cdd:cd14910 80 GESGAGKTVNTKRVIQYFATIavtgekkkEEATSGKMQGTLE-----DQIISANPLLEAFGNAKTVRNDNSSRFGKFIRI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 236 LFDKDTSIIGARIRTYLLERSRLVYQPPTERNYHIFYQLMAGLPAQTKEELHL-TDASDYFYMNQgGDTKINGIDDAKEY 314
Cdd:cd14910 155 HFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLItTNPYDYAFVSQ-GEITVPSIDDQEEL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 315 KITVDALTLVGITKETQHQIFKILAALLHIGNIEIKKTRNDASLSADEPNL-KLACELLGIDAYNFAKWVTKKQIITRSE 393
Cdd:cd14910 234 MATDSAIEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVaDKAAYLQNLNSADLLKALCYPRVKVGNE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 394 KIVSNLNYNQALVAKDSVAKFIYSALFDWLVENINTVLcnpAVNDQISSFIGVLDIYGFEHFEKNSFEQFCINYANEKLQ 473
Cdd:cd14910 314 YVTKGQTVQQVYNAVGALAKAVYDKMFLWMVTRINQQL---DTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQ 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 474 QEFNQHVFKLEQEEYVKEEIEWSFIEFN-DNQPCIDLIENKLGILSLLDEESRLPAGSDESWTQKLY-QTLDKSPTnkvF 551
Cdd:cd14910 391 QFFNHHMFVLEQEEYKKEGIEWEFIDFGmDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYeQHLGKSNN---F 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 552 SKPRFGQTK----FIVSHYALDVAYDVEGFIEKNRDTVSDGHLEVLKASTNETLINILEGlekaakkleeAKKLELEQAG 627
Cdd:cd14910 468 QKPKPAKGKveahFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSG----------AAAAEAEEGG 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 628 SKKPGPIRTVNRKpTLGSMFKQSLIELMNTINSTNVHYIRCIKPNADKEAWQFDNLMVLSQLRACGVLETIRISCAGFPS 707
Cdd:cd14910 538 GKKGGKKKGSSFQ-TVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPS 616
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768464868 708 RWTFEEFVLRYYIL----IPHEQWdliFKKKETTEEdiisvvkmILDATVKDKSKYQIGNTKIFFK 769
Cdd:cd14910 617 RILYADFKQRYKVLnasaIPEGQF---IDSKKASEK--------LLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
84-769 |
1.08e-143 |
|
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: 456.37 E-value: 1.08e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 84 PAVLHAIKQRYSQLNIYTYSGIVLIATNPFDRVDQLyTQDMIQAYAG-KRRGELEPHLFAIAEEAYRLMKNDKQNQTIVV 162
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNA-TDEWIRKYRDaPDLTKLPPHVFYTARRALENLHGVNKSQTIIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 163 SGESGAGKTVSAKYIMRYFASVEEEN-SATVQhqvemseteQKILATNPIMEAFGNAKTTRNDNSSRFGKYLEILFDKDT 241
Cdd:cd14876 80 SGESGAGKTEATKQIMRYFASAKSGNmDLRIQ---------TAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVASEG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 242 SIIGARIRTYLLERSRLVYQPPTERNYHIFYQLMAGLPAQTKEELHLTDASDYFYMNqGGDTKINGIDDAKEYKITVDAL 321
Cdd:cd14876 151 GIRYGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLGLKEYKFLN-PKCLDVPGIDDVADFEEVLESL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 322 TLVGITKETQHQIFKILAALLHIGNIEIKKTRND-----ASLSADEPN-LKLACELLGIDAYNFAKWVTKKQIITRSEKI 395
Cdd:cd14876 230 KSMGLTEEQIDTVFSIVSGVLLLGNVKITGKTEQgvddaAAISNESLEvFKEACSLLFLDPEALKRELTVKVTKAGGQEI 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 396 VSNLNYNQALVAKDSVAKFIYSALFDWLVENINTVLCNPavnDQISSFIGVLDIYGFEHFEKNSFEQFCINYANEKLQQE 475
Cdd:cd14876 310 EGRWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIEPP---GGFKNFMGMLDIFGFEVFKNNSLEQLFINITNEMLQKN 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 476 FNQHVFKLEQEEYVKEEIEWSFIEFNDNQPCID-LIENKLGILSLLDEESRLPAGSDESWTQKLYQTLDkspTNKVFSKP 554
Cdd:cd14876 387 FIDIVFERESKLYKDEGIPTAELEYTSNAEVIDvLCGKGKSVLSILEDQCLAPGGSDEKFVSACVSKLK---SNGKFKPA 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 555 RFGQT-KFIVSHYALDVAYDVEGFIEKNRDTVSDGHLEVLKASTNETLINILEGLEKAAKKLeeAKkleleqaGSkkpgp 633
Cdd:cd14876 464 KVDSNiNFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEGVVVEKGKI--AK-------GS----- 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 634 irtvnrkpTLGSMFKQSLIELMNTINSTNVHYIRCIKPNADKEAWQFDNLMVLSQLRACGVLETIRISCAGFPSRWTFEE 713
Cdd:cd14876 530 --------LIGSQFLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEE 601
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 768464868 714 FVLRYYILipheqwDL-IFKKKETTEEDIIsvvKMILDATVKDKSKYQIGNTKIFFK 769
Cdd:cd14876 602 FLYQFKFL------DLgIANDKSLDPKVAA---LKLLESSGLSEDEYAIGKTMVFLK 649
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
84-769 |
2.66e-143 |
|
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: 456.50 E-value: 2.66e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 84 PAVLHAIKQRYSQLNIYTYSGIVLIATNPFDRVdQLYTQDMIQAYAGKRRGELEPHLFAIAEEAYRLMKNDKQNQTIVVS 163
Cdd:cd14912 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWL-PVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 164 GESGAGKTVSAKYIMRYFASV--------EEENSATVQHQVEmseteQKILATNPIMEAFGNAKTTRNDNSSRFGKYLEI 235
Cdd:cd14912 80 GESGAGKTVNTKRVIQYFATIavtgekkkEEITSGKMQGTLE-----DQIISANPLLEAFGNAKTVRNDNSSRFGKFIRI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 236 LFDKDTSIIGARIRTYLLERSRLVYQPPTERNYHIFYQLMAGLPAQTKEELHL-TDASDYFYMNQgGDTKINGIDDAKEY 314
Cdd:cd14912 155 HFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLItTNPYDYPFVSQ-GEISVASIDDQEEL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 315 KITVDALTLVGITKETQHQIFKILAALLHIGNIEIKKTRNDASLSADEPNL-KLACELLGIDAYNFAKWVTKKQIITRSE 393
Cdd:cd14912 234 MATDSAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVaDKAAYLQSLNSADLLKALCYPRVKVGNE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 394 KIVSNLNYNQALVAKDSVAKFIYSALFDWLVENINTVLcnpAVNDQISSFIGVLDIYGFEHFEKNSFEQFCINYANEKLQ 473
Cdd:cd14912 314 YVTKGQTVEQVTNAVGALAKAVYEKMFLWMVARINQQL---DTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQ 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 474 QEFNQHVFKLEQEEYVKEEIEWSFIEFN-DNQPCIDLIENKLGILSLLDEESRLPAGSDESWTQKLY-QTLDKSPTnkvF 551
Cdd:cd14912 391 QFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYeQHLGKSAN---F 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 552 SKPRF----GQTKFIVSHYALDVAYDVEGFIEKNRDTVSDGHLEVLKASTNETLINILEGLEKAAKkleEAKKLELEQAG 627
Cdd:cd14912 468 QKPKVvkgkAEAHFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSGAQTAEG---ASAGGGAKKGG 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 628 SKKPGPIRTVNrkptlgSMFKQSLIELMNTINSTNVHYIRCIKPNADKEAWQFDNLMVLSQLRACGVLETIRISCAGFPS 707
Cdd:cd14912 545 KKKGSSFQTVS------ALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPS 618
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768464868 708 RWTFEEFVLRYYIL----IPHEQwdliFKKKETTEEDIISVVKMildatvkDKSKYQIGNTKIFFK 769
Cdd:cd14912 619 RILYADFKQRYKVLnasaIPEGQ----FIDSKKASEKLLASIDI-------DHTQYKFGHTKVFFK 673
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
84-769 |
8.72e-142 |
|
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: 451.88 E-value: 8.72e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 84 PAVLHAIKQRYSQLNIYTYSGIVLIATNPFDRVdQLYTQDMIQAYAGKRRGELEPHLFAIAEEAYRLMKNDKQNQTIVVS 163
Cdd:cd14918 1 PGVLYNLKERYAAWMIYTYSGLFCVTVNPYKWL-PVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 164 GESGAGKTVSAKYIMRYFASVEEENSATVQHQVEMSET-EQKILATNPIMEAFGNAKTTRNDNSSRFGKYLEILFDKDTS 242
Cdd:cd14918 80 GESGAGKTVNTKRVIQYFATIAVTGEKKKEESGKMQGTlEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 243 IIGARIRTYLLERSRLVYQPPTERNYHIFYQLMAGLPAQTKEELHL-TDASDYFYMNQgGDTKINGIDDAKEYKITVDAL 321
Cdd:cd14918 160 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLItTNPYDYAFVSQ-GEITVPSIDDQEELMATDSAI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 322 TLVGITKETQHQIFKILAALLHIGNIEIKKTRNDASLSADEPNL-KLACELLGIDAYNFAKWVTKKQIITRSEKIVSNLN 400
Cdd:cd14918 239 DILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVaDKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 401 YNQALVAKDSVAKFIYSALFDWLVENINTVLcnpAVNDQISSFIGVLDIYGFEHFEKNSFEQFCINYANEKLQQEFNQHV 480
Cdd:cd14918 319 VQQVYNAVGALAKAVYEKMFLWMVTRINQQL---DTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHM 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 481 FKLEQEEYVKEEIEWSFIEFN-DNQPCIDLIENKLGILSLLDEESRLPAGSDESWTQKLY-QTLDKSPTnkvFSKPRF-- 556
Cdd:cd14918 396 FVLEQEEYKKEGIEWTFIDFGmDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYdQHLGKSAN---FQKPKVvk 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 557 --GQTKFIVSHYALDVAYDVEGFIEKNRDTVSDGHLEVLKASTNETLINILEGLeKAAKKLEEAKKleleqaGSKKPGpi 634
Cdd:cd14918 473 gkAEAHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTY-ASAEADSGAKK------GAKKKG-- 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 635 rtvNRKPTLGSMFKQSLIELMNTINSTNVHYIRCIKPNADKEAWQFDNLMVLSQLRACGVLETIRISCAGFPSRWTFEEF 714
Cdd:cd14918 544 ---SSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDF 620
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 768464868 715 VLRYYIL----IPHEQwdliFKKKETTEEDIISVVKMildatvkDKSKYQIGNTKIFFK 769
Cdd:cd14918 621 KQRYKVLnasaIPEGQ----FIDSKKASEKLLASIDI-------DHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
84-769 |
1.33e-140 |
|
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: 448.79 E-value: 1.33e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 84 PAVLHAIKQRYSQLNIYTYSGIVLIATNPFDRVdQLYTQDMIQAYAGKRRGELEPHLFAIAEEAYRLMKNDKQNQTIVVS 163
Cdd:cd14915 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWL-PVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 164 GESGAGKTVSAKYIMRYFASV--------EEENSATVQHQVEmseteQKILATNPIMEAFGNAKTTRNDNSSRFGKYLEI 235
Cdd:cd14915 80 GESGAGKTVNTKRVIQYFATIavtgekkkEEAASGKMQGTLE-----DQIISANPLLEAFGNAKTVRNDNSSRFGKFIRI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 236 LFDKDTSIIGARIRTYLLERSRLVYQPPTERNYHIFYQLMAGLPAQTKEELHL-TDASDYFYMNQgGDTKINGIDDAKEY 314
Cdd:cd14915 155 HFGATGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLItTNPYDFAFVSQ-GEITVPSIDDQEEL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 315 KITVDALTLVGITKETQHQIFKILAALLHIGNIEIKKTRNDASLSADEPNL-KLACELLGIDAYNFAKWVTKKQIITRSE 393
Cdd:cd14915 234 MATDSAVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVaDKAAYLTSLNSADLLKALCYPRVKVGNE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 394 KIVSNLNYNQALVAKDSVAKFIYSALFDWLVENINTVLcnpAVNDQISSFIGVLDIYGFEHFEKNSFEQFCINYANEKLQ 473
Cdd:cd14915 314 YVTKGQTVQQVYNSVGALAKAIYEKMFLWMVTRINQQL---DTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQ 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 474 QEFNQHVFKLEQEEYVKEEIEWSFIEFN-DNQPCIDLIENKLGILSLLDEESRLPAGSDESWTQKLY-QTLDKSPTnkvF 551
Cdd:cd14915 391 QFFNHHMFVLEQEEYKKEGIEWEFIDFGmDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYeQHLGKSNN---F 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 552 SKPRFGQTK----FIVSHYALDVAYDVEGFIEKNRDTVsdghlevlkastNETLINILE--GLEKAAKKLEEAKKLELEQ 625
Cdd:cd14915 468 QKPKPAKGKaeahFSLVHYAGTVDYNIAGWLDKNKDPL------------NETVVGLYQksGMKTLAFLFSGGQTAEAEG 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 626 AGSKKPGPIRTVNRKpTLGSMFKQSLIELMNTINSTNVHYIRCIKPNADKEAWQFDNLMVLSQLRACGVLETIRISCAGF 705
Cdd:cd14915 536 GGGKKGGKKKGSSFQ-TVSALFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGF 614
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768464868 706 PSRWTFEEFVLRYYIL----IPHEQWdliFKKKETTEEdiisvvkmILDATVKDKSKYQIGNTKIFFK 769
Cdd:cd14915 615 PSRILYADFKQRYKVLnasaIPEGQF---IDSKKASEK--------LLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
84-769 |
1.03e-139 |
|
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: 446.43 E-value: 1.03e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 84 PAVLHAIKQRYSQLNIYTYSGIVLIATNPFDRVdQLYTQDMIQAYAGKRRGELEPHLFAIAEEAYRLMKNDKQNQTIVVS 163
Cdd:cd14916 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWL-PVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 164 GESGAGKTVSAKYIMRYFASVEEENSATVQHQVEMSE--TEQKILATNPIMEAFGNAKTTRNDNSSRFGKYLEILFDKDT 241
Cdd:cd14916 80 GESGAGKTVNTKRVIQYFASIAAIGDRSKKENPNANKgtLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 242 SIIGARIRTYLLERSRLVYQPPTERNYHIFYQLMAGLPAQTKEELHLTDAS-DYFYMNQgGDTKINGIDDAKEYKITVDA 320
Cdd:cd14916 160 KLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPyDYAFVSQ-GEVSVASIDDSEELLATDSA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 321 LTLVGITKETQHQIFKILAALLHIGNIEIKKTRNDASLSAD-EPNLKLACELLGIDAYNFAKWVTKKQIITRSEKIVSNL 399
Cdd:cd14916 239 FDVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDgTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 400 NYNQALVAKDSVAKFIYSALFDWLVENINTVLcnpAVNDQISSFIGVLDIYGFEHFEKNSFEQFCINYANEKLQQEFNQH 479
Cdd:cd14916 319 SVQQVYYSIGALAKSVYEKMFNWMVTRINATL---ETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHH 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 480 VFKLEQEEYVKEEIEWSFIEFN-DNQPCIDLIENKLGILSLLDEESRLPAGSDESWTQKLYQT-LDKSPTnkvFSKPRFG 557
Cdd:cd14916 396 MFVLEQEEYKKEGIEWEFIDFGmDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLYDNhLGKSNN---FQKPRNV 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 558 QTK----FIVSHYALDVAYDVEGFIEKNRDTVSDGHLEVLKASTNETLINILEGLEKAakkleEAKKLELEQAGSKKPGP 633
Cdd:cd14916 473 KGKqeahFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYASA-----DTGDSGKGKGGKKKGSS 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 634 IRTVNrkptlgSMFKQSLIELMNTINSTNVHYIRCIKPNADKEAWQFDNLMVLSQLRACGVLETIRISCAGFPSRWTFEE 713
Cdd:cd14916 548 FQTVS------ALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGD 621
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 768464868 714 FVLRYYILIPHEQWDLIFKKKETTEEDIISVVKMildatvkDKSKYQIGNTKIFFK 769
Cdd:cd14916 622 FRQRYRILNPAAIPEGQFIDSRKGAEKLLGSLDI-------DHNQYKFGHTKVFFK 670
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
84-769 |
2.12e-138 |
|
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: 442.97 E-value: 2.12e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 84 PAVLHAIKQRYSQLNIYTYSGIVLIATNPFDRVdQLYTQDMIQAYAGKRRGELEPHLFAIAEEAYRLMKNDKQNQTIVVS 163
Cdd:cd14923 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWL-PVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 164 GESGAGKTVSAKYIMRYFAS--VEEENSATVQHQVEMSETEQKILATNPIMEAFGNAKTTRNDNSSRFGKYLEILFDKDT 241
Cdd:cd14923 80 GESGAGKTVNTKRVIQYFATiaVTGDKKKEQQPGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 242 SIIGARIRTYLLERSRLVYQPPTERNYHIFYQLMAGLPAQTKEELHL-TDASDYFYMNQgGDTKINGIDDAKEYKITVDA 320
Cdd:cd14923 160 KLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLIsTNPFDFPFVSQ-GEVTVASIDDSEELLATDNA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 321 LTLVGITKETQHQIFKILAALLHIGNIEIKKTRNDASLSADEPNL-KLACELLGIDAYNFAKWVTKKQIITRSEKIVSNL 399
Cdd:cd14923 239 IDILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVaDKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 400 NYNQALVAKDSVAKFIYSALFDWLVENINTVLcnpAVNDQISSFIGVLDIYGFEHFEKNSFEQFCINYANEKLQQEFNQH 479
Cdd:cd14923 319 NVQQVTNSVGALAKAVYEKMFLWMVTRINQQL---DTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHH 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 480 VFKLEQEEYVKEEIEWSFIEFN-DNQPCIDLIENKLGILSLLDEESRLPAGSDESWTQKLY-QTLDKSPTnkvFSKPRFG 557
Cdd:cd14923 396 MFVLEQEEYKKEGIEWEFIDFGmDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYdQHLGKSNN---FQKPKPA 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 558 QTK----FIVSHYALDVAYDVEGFIEKNRDTVSDGHLEVLKASTnetlINILEGLEKAAKKLEEAKKLELEQAGSKKPGP 633
Cdd:cd14923 473 KGKaeahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSS----LKLLSFLFSNYAGAEAGDSGGSKKGGKKKGSS 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 634 IRTVNrkptlgSMFKQSLIELMNTINSTNVHYIRCIKPNADKEAWQFDNLMVLSQLRACGVLETIRISCAGFPSRWTFEE 713
Cdd:cd14923 549 FQTVS------AVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYAD 622
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 714 FVLRYYIL----IPHEQwdliFKKKETTEEDIISVVKMildatvkDKSKYQIGNTKIFFK 769
Cdd:cd14923 623 FKQRYRILnasaIPEGQ----FIDSKNASEKLLNSIDV-------DREQYRFGHTKVFFK 671
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
86-769 |
5.04e-137 |
|
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: 438.86 E-value: 5.04e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 86 VLHAIKQRYSQLNI-YTYSGIVLIATNPFDRVDQLYTQDMIQAYAGKRRGELEPHLFAIAEEAY-RLMKNDKQNQTIVVS 163
Cdd:cd14875 3 LLHCIKERFEKLHQqYSLMGEMVLSVNPFRLMPFNSEEERKKYLALPDPRLLPPHIWQVAHKAFnAIFVQGLGNQSVVIS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 164 GESGAGKTVSAKYIMRYFASVEEENSATVQHQVEMSETEQKILATNPIMEAFGNAKTTRNDNSSRFGKYLEILFDKDTSI 243
Cdd:cd14875 83 GESGSGKTENAKMLIAYLGQLSYMHSSNTSQRSIADKIDENLKWSNPVMESFGNARTVRNDNSSRFGKYIKLYFDPTSGV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 244 -IGARIRTYLLERSRLVYQPPTERNYHIFYQLMAGLPAQTKEEL-HLTDASDYFYMNqGGDTKI------NGIDDAKEYK 315
Cdd:cd14875 163 mVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELgGLKTAQDYKCLN-GGNTFVrrgvdgKTLDDAHEFQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 316 ITVDALTLVGITKETQHQIFKILAALLHIGNIEIKKTRNDASLSADEPNLKLACELLGIDaynfAKWVTKKQIITRSEKI 395
Cdd:cd14875 242 NVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQNDKAQIADETPFLTACRLLQLD----PAKLRECFLVKSKTSL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 396 VSNL-NYNQALVAKDSVAKFIYSALFDWLVENINTVLcNPAVNDQISSFIGVLDIYGFEHFEKNSFEQFCINYANEKLQQ 474
Cdd:cd14875 318 VTILaNKTEAEGFRNAFCKAIYVGLFDRLVEFVNASI-TPQGDCSGCKYIGLLDIFGFENFTRNSFEQLCINYANESLQN 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 475 EFNQHVFKLEQEEYVKEEIEWSFIEFNDNQPCIDLIE-NKLGILSLLDEESRLPAGSDESWTQKLYQTLdkSPTNKVFSK 553
Cdd:cd14875 397 HYNKYTFINDEEECRREGIQIPKIEFPDNSECVNMFDqKRTGIFSMLDEECNFKGGTTERFTTNLWDQW--ANKSPYFVL 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 554 PRFG-QTKFIVSHYALDVAYDVEGFIEKNRDTVSDGHLEVLKASTNETLINILeglekaakkleeakkleleqagSKKPG 632
Cdd:cd14875 475 PKSTiPNQFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTLL----------------------STEKG 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 633 PIRtvnRKPTLGSMFKQSLIELMNTINSTNVHYIRCIKPNADKEAWQFDNLMVLSQLRACGVLETIRISCAGFPSRWTFE 712
Cdd:cd14875 533 LAR---RKQTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRRPIE 609
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 768464868 713 EFVLRYYILIPHEQWDLiFKKKETTE--EDIISVVKMILDATvkdKSKYQIGNTKIFFK 769
Cdd:cd14875 610 QFCRYFYLIMPRSTASL-FKQEKYSEaaKDFLAYYQRLYGWA---KPNYAVGKTKVFLR 664
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
86-769 |
9.45e-134 |
|
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: 429.69 E-value: 9.45e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 86 VLHAIKQRYSQLNIYTYSGIVLIATNPFDRVDQLYTQDMIQAYAG--KRRG---ELEPHLFAIAEEAYRLMKNDKQNQTI 160
Cdd:cd14886 3 VIDILRDRFAKDKIYTYAGKLLVALNPFKQIRNLYGTEVIGRYRQadTSRGfpsDLPPHSYAVAQSALNGLISDGISQSC 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 161 VVSGESGAGKTVSAKYIMRYFASVEEENSATVQhqvemseteQKILATNPIMEAFGNAKTTRNDNSSRFGKYLEILFDKD 240
Cdd:cd14886 83 IVSGESGAGKTETAKQLMNFFAYGHSTSSTDVQ---------SLILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGPD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 241 TSIIGARIRTYLLERSRLVYQPPTERNYHIFYQLMAGLPAQTKEELHLTDASDYFYMNQGGDTKINGIDDAKEYKITVDA 320
Cdd:cd14886 154 GGLKGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLESYNFLNASKCYDAPGIDDQKEFAPVRSQ 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 321 LTLVgITKETQHQIFKILAALLHIGNIEIKK-----TRNDASLSADEPNLKLaCELLGIDAYNFAKWVTKKQIITRSEKI 395
Cdd:cd14886 234 LEKL-FSKNEIDSFYKCISGILLAGNIEFSEegdmgVINAAKISNDEDFGKM-CELLGIESSKAAQAIITKVVVINNETI 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 396 VSNLNYNQALVAKDSVAKFIYSALFDWLVENINTVLcnpAVNDQISSFIGVLDIYGFEHFEKNSFEQFCINYANEKLQQE 475
Cdd:cd14886 312 ISPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEII---QFDADARPWIGILDIYGFEFFERNTYEQLLINYANERLQQY 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 476 FNQHVFKLEQEEYVKEEIEWSFIEFNDNQPCIDLIEN-KLGILSLLDEESRLPAGSDESWTqklyQTLDKSPTNKVFSKP 554
Cdd:cd14886 389 FINQVFKSEIQEYEIEGIDHSMITFTDNSNVLAVFDKpNLSIFSFLEEQCLIQTGSSEKFT----SSCKSKIKNNSFIPG 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 555 RFGQTKFIVSHYALDVAYDVEGFIEKNRDTVSDGHLEVLKASTNeTLINilegleKAAKKLeeakkleleqagskkpgPI 634
Cdd:cd14886 465 KGSQCNFTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTN-PIVN------KAFSDI-----------------PN 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 635 RTVNRKPT-LGSMFKQSLIELMNTINSTNVHYIRCIKPNADKEAWQFDNLMVLSQLRACGVLETIRISCAGFPSRWTFEE 713
Cdd:cd14886 521 EDGNMKGKfLGSTFQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFEE 600
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 768464868 714 FVLRYYILIPHEQwdlifkKKETTEEDIISVVKMILDATVKDKSKYQIGNTKIFFK 769
Cdd:cd14886 601 FFHRNKILISHNS------SSQNAGEDLVEAVKSILENLGIPCSDYRIGKTKVFLR 650
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
85-718 |
1.08e-128 |
|
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: 417.96 E-value: 1.08e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 85 AVLHAIKQRYSQLNIYTYSGIVLIATNPFDRVDQLYTQDMIQAYAGKRRGEL----------EPHLFAIAEEAYRLMKND 154
Cdd:cd14899 2 SILNALRLRYERHAIYTHIGDILISINPFQDLPQLYGDEILRGYAYDHNSQFgdrvtstdprEPHLFAVARAAYIDIVQN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 155 KQNQTIVVSGESGAGKTVSAKYIMRYFA------SVEEENSATVQHQVEMSET--EQKILATNPIMEAFGNAKTTRNDNS 226
Cdd:cd14899 82 GRSQSILISGESGAGKTEATKIIMTYFAvhcgtgNNNLTNSESISPPASPSRTtiEEQVLQSNPILEAFGNARTVRNDNS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 227 SRFGKYLEILF-DKDTSIIGARIRTYLLERSRLVYQPPTERNYHIFYQLMAG----LPAQTKEELHLTDASDYF-YMNQG 300
Cdd:cd14899 162 SRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSAdnncVSKEQKQVLALSGGPQSFrLLNQS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 301 GDTKI-NGIDDAKEYKITVDALTLVGITKETQHQIFKILAALLHIGNIEIKKT--RNDASLSADEP-----------NLK 366
Cdd:cd14899 242 LCSKRrDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEQIphKGDDTVFADEArvmssttgafdHFT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 367 LACELLGIDAYNFAKWVTKKQIITRSEKIVSNLNYNQALVAKDSVAKFIYSALFDWLVENINTVLCNPA----------V 436
Cdd:cd14899 322 KAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLQRQAsapwgadesdV 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 437 NDQISS--FIGVLDIYGFEHFEKNSFEQFCINYANEKLQQEFNQHVFKLEQEEYVKEEIEWSFIEFNDNQPCIDLIENK- 513
Cdd:cd14899 402 DDEEDAtdFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFPNNRACLELFEHRp 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 514 LGILSLLDEESRLPAGSDESWTQKLYQTLDKSPTNKVFSKPRFGQ--TKFIVSHYALDVAYDVEGFIEKNRDTVSDGHLE 591
Cdd:cd14899 482 IGIFSLTDQECVFPQGTDRALVAKYYLEFEKKNSHPHFRSAPLIQrtTQFVVAHYAGCVTYTIDGFLAKNKDSFCESAAQ 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 592 VLKASTNEtlinILEGLEKAAKKLEEAKKLELEQAGSKKPGPIRTVNRKPTLGSMFKQSLIELMNTINSTNVHYIRCIKP 671
Cdd:cd14899 562 LLAGSSNP----LIQALAAGSNDEDANGDSELDGFGGRTRRRAKSAIAAVSVGTQFKIQLNELLSTVRATTPRYVRCIKP 637
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 768464868 672 NADKEAWQFDNLMVLSQLRACGVLETIRISCAGFPSRWTFEEFVLRY 718
Cdd:cd14899 638 NDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRY 684
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
86-767 |
5.83e-127 |
|
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: 413.22 E-value: 5.83e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 86 VLHAIKQRYSQLNIYTYSGIVLIATNPFDRVDQLYTQDMIQAYAGKRR-GELEPHLFAIAEEAYRLMKNDKQNQTIVVSG 164
Cdd:cd14906 3 ILNNLGKRYKSDSIYTYIGNVLISINPYKDISSIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIIISG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 165 ESGAGKTVSAKYIMRYFASVEEENSATVQHQVEMSET-EQKILATNPIMEAFGNAKTTRNDNSSRFGKYLEILFDKDTSI 243
Cdd:cd14906 83 ESGSGKTEASKTILQYLINTSSSNQQQNNNNNNNNNSiEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFRSSDGK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 244 I-GARIRTYLLERSRLVYQPPTER-NYHIFYQLMAGLPAQTKEELHL-TDASDYFYMN-------------QGGDTKING 307
Cdd:cd14906 163 IdGASIETYLLEKSRISHRPDNINlSYHIFYYLVYGASKDERSKWGLnNDPSKYRYLDarddvissfksqsSNKNSNHNN 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 308 IDDAKE-YKITVDALTLVGITKETQHQIFKILAALLHIGNIEIKKTRNDASLSADEPN----LKLACELLGIDAYNFAKW 382
Cdd:cd14906 243 KTESIEsFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSDFSKYAYQKDKvtasLESVSKLLGYIESVFKQA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 383 VTKKQIIT--RSEKIVSNLNYNQALVAKDSVAKFIYSALFDWLVENINTVLCN--------PAVNDQISSFIGVLDIYGF 452
Cdd:cd14906 323 LLNRNLKAggRGSVYCRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRKFNQntqsndlaGGSNKKNNLFIGVLDIFGF 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 453 EHFEKNSFEQFCINYANEKLQQEFNQHVFKLEQEEYVKEEIEWSFIEFNDNQPCIDLIENK-LGILSLLDEESRLPAGSD 531
Cdd:cd14906 403 ENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNFIDNKECIELIEKKsDGILSLLDDECIMPKGSE 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 532 ESWTQKLYQTLDKSPTnkvFSKPRFGQTKFIVSHYALDVAYDVEGFIEKNRDTVSdGHLEVLKASTNETLINILEGLEKA 611
Cdd:cd14906 483 QSLLEKYNKQYHNTNQ---YYQRTLAKGTLGIKHFAGDVTYQTDGWLEKNRDSLY-SDVEDLLLASSNFLKKSLFQQQIT 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 612 AKKLEEAKKleleqagskkpgpirtvNRKPTLGSMFKQSLIELMNTINSTNVHYIRCIKPNADKEAWQFDNLMVLSQLRA 691
Cdd:cd14906 559 STTNTTKKQ-----------------TQSNTVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLSQLRN 621
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 692 CGVLETIRISCAGFPSRWTFEEFVLRYYIL------------IPHEQWDLIFKKKETTEEDIISVVK----MILDATVKD 755
Cdd:cd14906 622 VGVLNTIKVRKMGYSYRRDFNQFFSRYKCIvdmynrknnnnpKLASQLILQNIQSKLKTMGISNNKKknnsNSNSNTTND 701
|
730
....*....|..
gi 768464868 756 KSKYQIGNTKIF 767
Cdd:cd14906 702 KPLFQIGKTKIF 713
|
|
| Myo5p-like_CBD_fungal |
cd15474 |
cargo binding domain of fungal myosin V -like proteins; Yeast myosin V travels along actin ... |
1169-1533 |
2.23e-124 |
|
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: 392.55 E-value: 2.23e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 1169 ILNQEITEGLLKGFEVPDAGV-AIQLSKRDVVYPARILIIVLSEMWRFG--LTKQSESFLAQVLTTIQKVVTQLKGNDLI 1245
Cdd:cd15474 1 DYTLEFTEGLLKSVEVLELKDiSDEVSGDNLLFLGHVNFLIYSQMWKSLleLLTQSERFLSHVLSYIASIVDSLPKKETI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 1246 PSGVFWLANVRELYSFVVFALNSILTEETFkngmtdEEYKEYVSLVTELKDDFEALSYNIYNIWLKKLQKQLQKKAINAV 1325
Cdd:cd15474 81 PDGAFWLANLHELRSFVVYLLSLIEHSSSD------EFSKESEEYWNTLFDKTLKHLSNIYSTWIDKLNKHLSPKIEGAV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 1326 VISESLPGFSageTSGFLNKIFANTEEYTMDDILTFFNSIYWCMKSFHIENEVFHAVVTTLLNYVDAICFNELIMKRNFL 1405
Cdd:cd15474 155 LVLLTSLDLS---ELIDLNKEFFNKPKKKMADLITFLNEVYDLLQSFSVQPELLNAIVSSTLQYINVEAFNSLITKRSAL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 1406 SWKRGLQLNYNVTRLEEWCKTHGLTDGTECLQHLIQTAKLLQVRKYTIEDIDILRGICYSLTPAQLQKLISQYQVADYES 1485
Cdd:cd15474 232 SWKRGSQISYNVSRLKEWCHQHGLSDANLQLEPLIQASKLLQLRKDDENDFKIILSVCYALNPAQIQKLLDKYQPANYEA 311
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 768464868 1486 PIPQEILRYVADIVKKEAALSSSGNdskghehSSSIFITPETGPFTDP 1533
Cdd:cd15474 312 PVPKEFLNALEKLIKKENLSLPGRK-------NNSKMEIPESSNFDVL 352
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
85-723 |
7.50e-113 |
|
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: 369.61 E-value: 7.50e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 85 AVLHAIKQRYSQLNIYTYSGIVLIATNPFDRVdqlYTQDMIQAYAgKRRGELEPHLFAIAEEAYRLMkNDKQNQTIVVSG 164
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYETI---YGAGAMKAYL-KNYSHVEPHVYDVAEASVQDL-LVHGNQTIVISG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 165 ESGAGKTVSAKYIMRYFasVEEENSATvqhqvemsETEQKILATNPIMEAFGNAKTTRNDNSSRFGKYLEILFDKDtsII 244
Cdd:cd14898 77 ESGSGKTENAKLVIKYL--VERTASTT--------SIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKFDGK--IT 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 245 GARIRTYLLERSRLVYQPPTERNYHIFYQLMAglpaqtKEELHLTDasDYFYMNQGGDTKINGIDDAKEYKITVDALTLV 324
Cdd:cd14898 145 GAKFETYLLEKSRVTHHEKGERNFHIFYQFCA------SKRLNIKN--DFIDTSSTAGNKESIVQLSEKYKMTCSAMKSL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 325 GITKetQHQIFKILAALLHIGNIEIKktrNDASLSA-DEPNLKLACELLGIDAYNFAKWVTKKQIITRSEKIVSNLNYNQ 403
Cdd:cd14898 217 GIAN--FKSIEDCLLGILYLGSIQFV---NDGILKLqRNESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIEVFNTLKQ 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 404 ALVAKDSVAKFIYSALFDWLVENINTVL-CNPAVNdqissfIGVLDIYGFEHFEKNSFEQFCINYANEKLQQEFNQHVFK 482
Cdd:cd14898 292 ARTIRNSMARLLYSNVFNYITASINNCLeGSGERS------ISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMFR 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 483 LEQEEYVKEEIEWSFIEFNDNQPCIDLIENKLGILSLLDEESRLPAGSDESWTQKLYQTLDKsptnkvFSKPRFGQtKFI 562
Cdd:cd14898 366 AKQGMYKEEGIEWPDVEFFDNNQCIRDFEKPCGLMDLISEESFNAWGNVKNLLVKIKKYLNG------FINTKARD-KIK 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 563 VSHYALDVAYDVEGFIEKNRDtvsDGHLEVLKastnetliNILeglekaakkleeakkleleqagskkpgpIRTVNRKPT 642
Cdd:cd14898 439 VSHYAGDVEYDLRDFLDKNRE---KGQLLIFK--------NLL----------------------------INDEGSKED 479
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 643 LGSMFKQSLIELMNTINSTNVHYIRCIKPNADKEAWQFDNLMVLSQLRACGVLETIRISCAGFPSRWTFEEFVLRYYILI 722
Cdd:cd14898 480 LVKYFKDSMNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRILG 559
|
.
gi 768464868 723 P 723
Cdd:cd14898 560 I 560
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
85-769 |
3.99e-111 |
|
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: 367.60 E-value: 3.99e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 85 AVLHAIKQRYSQLNIYTYSGIVLIATNPFDRVdQLYTQDMIQAY---AGKRRGELEPHLFAIAEEAYRLMKNDKQNQTIV 161
Cdd:cd14878 2 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKEL-PIYSTMVSQLYlssSGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 162 VSGESGAGKTVSAKYIMRYFASVEEENSATVqhqvemsetEQKILATNPIMEAFGNAKTTRNDNSSRFGKYLEILF-DKD 240
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLTCRASSSRTTF---------DSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFcERK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 241 TSIIGARIRTYLLERSRLVYQPPTERNYHIFYQLMAGLPAQTKEELHLTDASDYFYMNQG--GDTKINGIDDAKEyKITV 318
Cdd:cd14878 152 KHLTGARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTmrEDVSTAERSLNRE-KLAV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 319 --DALTLVGITKETQHQIFKILAALLHIGNIEIKK-TRNDASLSADEPNLKLACELLGIDAYNFAKWVT------KKQII 389
Cdd:cd14878 231 lkQALNVVGFSSLEVENLFVILSAILHLGDIRFTAlTEADSAFVSDLQLLEQVAGMLQVSTDELASALTtdiqyfKGDMI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 390 TRSEKIvsnlnyNQALVAKDSVAKFIYSALFDWLVENINTVLCNpavNDQISSF----IGVLDIYGFEHFEKNSFEQFCI 465
Cdd:cd14878 311 IRRHTI------QIAEFYRDLLAKSLYSRLFSFLVNTVNCCLQS---QDEQKSMqtldIGILDIFGFEEFQKNEFEQLCV 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 466 NYANEKLQQEFNQHVFKLEQEEYVKEEIEWSFIEFNDNQPCI-DLIENK-LGILSLLDEESRLPAGSDESWTQKLYQTLD 543
Cdd:cd14878 382 NMTNEKMHHYINEVLFLQEQTECVQEGVTMETAYSPGNQTGVlDFFFQKpSGFLSLLDEESQMIWSVEPNLPKKLQSLLE 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 544 KSPTNKVFSKPRFGQ---------TKFIVSHYALDVAYDVEGFIEKNRDTVSDGHLEVLKASTNeTLINileglekaakK 614
Cdd:cd14878 462 SSNTNAVYSPMKDGNgnvalkdqgTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSEN-VVIN----------H 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 615 LEEAKKLeleqagskkpgpirtvnrkpTLGSMFKQSLIELMNTINSTNVHYIRCIKPNADKEAWQFDNLMVLSQLRACGV 694
Cdd:cd14878 531 LFQSKLV--------------------TIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGV 590
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768464868 695 LETIRISCAGFPSRWTFEEFVLRYYILIPHEQWDlifKKKETTEEDIISVVKMIldatvkDKSKYQIGNTKIFFK 769
Cdd:cd14878 591 LEMVKIFRYGYPVRLSFSDFLSRYKPLADTLLGE---KKKQSAEERCRLVLQQC------KLQGWQMGVRKVFLK 656
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
81-768 |
5.80e-108 |
|
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: 358.40 E-value: 5.80e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 81 LNEPAVLHAIKQRYSQLNIYTY-SGIVLIATNPF-------DRVDQLYTQDMIQAYAGKRRGeLEPHLFAIAEEAYRLMK 152
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRlGSSALVAVNPYkylssnsDASLGEYGSEYYDTTSGSKEP-LPPHAYDLAARAYLRMR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 153 NDKQNQTIVVSGESGAGKTVSAKYIMRYFASVeeenSAtvqHQVEMSETEQKILATNPIMEAFGNAKTTRNDNSSRFGKY 232
Cdd:cd14879 80 RRSEDQAVVFLGETGSGKSESRRLLLRQLLRL----SS---HSKKGTKLSSQISAAEFVLDSFGNAKTLTNPNASRFGRY 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 233 LEILFDKDTSIIGARIRTYLLERSRLVYQPPTERNYHIFYQLMAGLPAQTKEELHLTDASDYFYMNQGGDTKIN---GID 309
Cdd:cd14879 153 TELQFNERGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPSDYALLASYGCHPLPlgpGSD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 310 DAKEYKITVDALTLVGITKETQHQIFKILAALLHIGNIE--IKKTRNDASLS-ADEPNLKLACELLGIDAYNFAKWVTKK 386
Cdd:cd14879 233 DAEGFQELKTALKTLGFKRKHVAQICQLLAAILHLGNLEftYDHEGGEESAVvKNTDVLDIVAAFLGVSPEDLETSLTYK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 387 QIITRSEKIVSNLNYNQALVAKDSVAKFIYSALFDWLVENINTVLCnpAVNDQISSFIGVLDIYGFEHF---EKNSFEQF 463
Cdd:cd14879 313 TKLVRKELCTVFLDPEGAAAQRDELARTLYSLLFAWVVETINQKLC--APEDDFATFISLLDFPGFQNRsstGGNSLDQF 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 464 CINYANEKLQQEFNQHVFKLEQEEYVKEEIEWSFIEFNDNQPCIDLIENK-LGILSLLDEE-SRLPAGSDESWTQKLYQT 541
Cdd:cd14879 391 CVNFANERLHNYVLRSFFERKAEELEAEGVSVPATSYFDNSDCVRLLRGKpGGLLGILDDQtRRMPKKTDEQMLEALRKR 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 542 LDKSPTNKVFSKP--RFGQTKFIVSHYALDVAYDVEGFIEKNRDTVS-DghlevlkastnetLINILEGlekaakkleea 618
Cdd:cd14879 471 FGNHSSFIAVGNFatRSGSASFTVNHYAGEVTYSVEGFLERNGDVLSpD-------------FVNLLRG----------- 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 619 kkleleqagskkpgpirtvnrkptlGSMFKQSLIELMNTINSTNVHYIRCIKPNADKEAWQFDNLMVLSQLRACGVLETI 698
Cdd:cd14879 527 -------------------------ATQLNAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQIRSLGLPELA 581
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 699 RISCAGFPSRWTFEEFVLRYyilipheqwdlifkKKETTEEDIISVVKMILDATVKDKSKYQIGNTKIFF 768
Cdd:cd14879 582 ARLRVEYVVSLEHAEFCERY--------------KSTLRGSAAERIRQCARANGWWEGRDYVLGNTKVFL 637
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
86-769 |
3.33e-100 |
|
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: 336.22 E-value: 3.33e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 86 VLHAIKQRYSQLNIYTYSGIVLIATNPFDRVDQlytqdMIQAYAGKRRGELEPHLFAIAEEAYRLMKNDKQNQTIVVSGE 165
Cdd:cd14937 3 VLNMLALRYKKNYIYTIAEPMLISINPYQVIDV-----DINEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 166 SGAGKTVSAKYIMRYFAS-VEEENsatvqhqvEMSETeqkILATNPIMEAFGNAKTTRNDNSSRFGKYLEILFDKDTSII 244
Cdd:cd14937 78 SGSGKTEASKLVIKYYLSgVKEDN--------EISNT---LWDSNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 245 GARIRTYLLERSRLVYQPPTERNYHIFYQLMAGLPAQTKEELHLTDASDYFYMNQgGDTKINGIDDAKEYK---ITVDAL 321
Cdd:cd14937 147 SSSIEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSENEYKYIVN-KNVVIPEIDDAKDFGnlmISFDKM 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 322 TLvgitKETQHQIFKILAALLHIGNIE---IKKTRNDASLSADEPNLKL---ACELLGIDAYNFAKWVTKKQIITRSEKI 395
Cdd:cd14937 226 NM----HDMKDDLFLTLSGLLLLGNVEyqeIEKGGKTNCSELDKNNLELvneISNLLGINYENLKDCLVFTEKTIANQKI 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 396 VSNLNYNQALVAKDSVAKFIYSALFDWLVENINTVLCNpavNDQISSFIGVLDIYGFEHFEKNSFEQFCINYANEKLQQE 475
Cdd:cd14937 302 EIPLSVEESVSICKSISKDLYNKIFSYITKRINNFLNN---NKELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIHSI 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 476 FNQHVFKLEQEEYVKEEIEWSFIEFNDNQPCIDLIENKLGILSLLDEESRLPAGSDES----WTQKLYQTLDKSPTNKVF 551
Cdd:cd14937 379 YLYIVYEKETELYKAEDILIESVKYTTNESIIDLLRGKTSIISILEDSCLGPVKNDESivsvYTNKFSKHEKYASTKKDI 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 552 SKprfgqtKFIVSHYALDVAYDVEGFIEKNRDTVSDGHLEVLKASTNETLINILEGLEKAakkleeakkleleqagskkp 631
Cdd:cd14937 459 NK------NFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDVEVS-------------------- 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 632 gpiRTVNRKPTLGSMFKQSLIELMNTINSTNVHYIRCIKPNADKEAWQFDNLMVLSQLRACGVLETIRISCAgFPSRWTF 711
Cdd:cd14937 513 ---ESLGRKNLITFKYLKNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNISFF-FQYKYTF 588
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 768464868 712 EEFvLRYYiliphEQWDLIFKKKETTEEDiiSVVKMILDATVkDKSKYQIGNTKIFFK 769
Cdd:cd14937 589 DVF-LSYF-----EYLDYSTSKDSSLTDK--EKVSMILQNTV-DPDLYKVGKTMVFLK 637
|
|
| Myo5-like_CBD |
cd14945 |
Cargo binding domain of myosin 5 and similar proteins; Class V myosins are well studied ... |
1169-1500 |
2.09e-98 |
|
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: 318.19 E-value: 2.09e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 1169 ILNQEITEGLLKGFEVPdagvaiqlSKRDVVYPARILIIVLSEMWRFGLTKQSESFLAQVLTTIQKVVTQLkgNDLIPSG 1248
Cdd:cd14945 1 SEEDSLLRGIVTDFEPS--------SGDHKLTPAYILYLCIRHAASNGLTGQSTSLLNKVLKTIQQVVQQH--NDDMQLL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 1249 VFWLANVRELYSFVVFALNSILTEETFKNgmTDEEYKEYVSLVTELKDDFEALSYNIYNIWLkklqkqlqkkainavvis 1328
Cdd:cd14945 71 AFWLSNASELLYFLKQDSKLYGAAGEAPQ--KEEEQKLTVSDLNELKQDLEAVSIKIYQQAL------------------ 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 1329 eslpgfsagetsgflnKIFANTEEYTMDDILTFFNSIYWCMKSFHIENEVFHAVVTTLLNYVDAICFNELIMKRNFLSWK 1408
Cdd:cd14945 131 ----------------KYLNKNLQPKIRDIVKFLNSFLDLLKSFHVHPEIRSQVFTQLFSFINARLFNQLITKKDALSWS 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 1409 RGLQLNYNVTRLEEWCKTHGLT-DGTECLQHLIQTAKLLQVRKYTIEDIDILRGICYSLTPAQLQKLISQYQVADY-ESP 1486
Cdd:cd14945 195 RGMQIRANISRLEEWCEGRGLEhLAVDFLSKLIQAVQLLQLKKYTQEDIEILCELCPSLNPAQLQAILTQYQPANYgESP 274
|
330
....*....|....
gi 768464868 1487 IPQEILRYVADIVK 1500
Cdd:cd14945 275 VPKEILRTLAAEVS 288
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
84-769 |
2.08e-95 |
|
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: 325.06 E-value: 2.08e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 84 PAVLHAIKQRYSQL--------NIYTYSGIVLIATNPFDRVDqLYTQDMIQAYAGKRRGELEPHLFAIAEEAYRLMKNDK 155
Cdd:cd14887 1 PNLLENLYQRYNKAyinkenrnCIYTYTGTLLIAVNPYRFFN-LYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 156 QNQTIVVSGESGAGKTVSAKYIMRYFASVEEEnsatvQHQVEMSETEQKILATNPIMEAFGNAKTTRNDNSSRFGKYLEI 235
Cdd:cd14887 80 RSQSILISGESGAGKTETSKHVLTYLAAVSDR-----RHGADSQGLEARLLQSGPVLEAFGNAHTVLNANSSRFGKMLLL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 236 LFDKDTSIIGARIRTYLLERSRLVYQPPTERNYHIFYQLMAGLPAQTKEELHLTDASDYFYmnqggdtkingiddakEYK 315
Cdd:cd14887 155 HFTGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAVAAATQKSSAGEGDPEST----------------DLR 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 316 ITVDALTLVGITKETQHQIFKILAALLHIGNIEIKKTRND-------------------ASLS----------------A 360
Cdd:cd14887 219 RITAAMKTVGIGGGEQADIFKLLAAILHLGNVEFTTDQEPetskkrkltsvsvgceetaADRShssevkclssglkvteA 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 361 DEPNLKLACELLGIDAYNFAKWVTKKQIITRS-EKIVSNLNYNQALVAKDSVAKFIYSALFDWLVENINTVLCNPAVNDQ 439
Cdd:cd14887 299 SRKHLKTVARLLGLPPGVEGEEMLRLALVSRSvRETRSFFDLDGAAAARDAACKNLYSRAFDAVVARINAGLQRSAKPSE 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 440 ISS-----------FIGVLDIYGFEHFE---KNSFEQFCINYANEKLQQEFNQHVFKLEQEEYVKEEIEWSFIEFNDN-- 503
Cdd:cd14887 379 SDSdedtpsttgtqTIGILDLFGFEDLRnhsKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGVFQNQDCSAFPfs 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 504 -------------------------QPCIDLIENKLGILSLLDEESRL--PAGSDESWTQKLYQTLDKSPTNKVFSK--- 553
Cdd:cd14887 459 fplastltsspsstspfsptpsfrsSSAFATSPSLPSSLSSLSSSLSSspPVWEGRDNSDLFYEKLNKNIINSAKYKnit 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 554 PRFGQTK--FIVSHYALDVAYDVEGFIEKNRDTVSDgHLEVLKASTNeTLINILeglekaakkleeakkleleqaGSKKP 631
Cdd:cd14887 539 PALSRENleFTVSHFACDVTYDARDFCRANREATSD-ELERLFLACS-TYTRLV---------------------GSKKN 595
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 632 GPIRTV-NRKPTLGSMFKQSLIELMNTINSTNVHYIRCIKPNADKEAWQFDNLMVLSQLRACGVLETIRISCAGFPSRWT 710
Cdd:cd14887 596 SGVRAIsSRRSTLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCRLP 675
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*....
gi 768464868 711 FEEFVLRYYILIPHEQwdlifkKKETTEEDIISVVKMILDAtvkDKSKYQIGNTKIFFK 769
Cdd:cd14887 676 YVELWRRYETKLPMAL------REALTPKMFCKIVLMFLEI---NSNSYTFGKTKIFFR 725
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
86-769 |
1.75e-94 |
|
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: 321.57 E-value: 1.75e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 86 VLHAIKQRY-SQLnIYTYSGIVLIATNPFDRVdQLYTQDMIQAYAGKRRGELEPHLFAIAEEAYRLMKNDKQNQTIVVSG 164
Cdd:cd01386 3 VLHTLRQRYgANL-IHTYAGPSLIVINPRHPL-AVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 165 ESGAGKTVSAKYIMRYFASVeeenSATVQHQVemseTEQKILATNPIMEAFGNAKTTRNDNSSRFGKYLEILFDKDTSII 244
Cdd:cd01386 81 RSGSGKTTNCRHILEYLVTA----AGSVGGVL----SVEKLNAALTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQLA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 245 GARIRTYLLERSRLVYQPPTERNYHIFYQLMAGLPAQTKEELHLTDA--SDYFYMN--QGGDTKingIDDAKEYKITVDA 320
Cdd:cd01386 153 SASIQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLaeSNSFGIVplQKPEDK---QKAAAAFSKLQAA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 321 LTLVGITKETQHQIFKILAALLHIGNIEIKKTrNDASLS--ADEPNLKLACELLGIDAYNFAKWVTK---KQIITRSEKI 395
Cdd:cd01386 230 MKTLGISEEEQRAIWSILAAIYHLGAAGATKA-ASAGRKqfARPEWAQRAAYLLGCTLEELSSAIFKhhlSGGPQQSTTS 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 396 VSNLNYNQ---------ALVAKDSVAKFIYSALFDWLVENINTVLCNpavNDQISSFIGVLDIYGF---EHFEKN---SF 460
Cdd:cd01386 309 SGQESPARsssggpkltGVEALEGFAAGLYSELFAAVVSLINRSLSS---SHHSTSSITIVDTPGFqnpAHSGSQrgaTF 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 461 EQFCINYANEKLQQEFNQHVFKLEQEEYVKEEIEWSFiEFNDNQPC--IDLI---------------ENKLGILSLLDEE 523
Cdd:cd01386 386 EDLCHNYAQERLQLLFHERTFVAPLERYKQENVEVDF-DLPELSPGalVALIdqapqqalvrsdlrdEDRRGLLWLLDEE 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 524 SRLPAGSDESWTQKLYQTLDKSPTNKVFSKPRFGQT--KFIVSHY--ALDVAYDVEGFIEKNRDTVSDGH-LEVLKASTN 598
Cdd:cd01386 465 ALYPGSSDDTFLERLFSHYGDKEGGKGHSLLRRSEGplQFVLGHLlgTNPVEYDVSGWLKAAKENPSAQNaTQLLQESQK 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 599 ETlinileglekaakkleeakkleleqAGSKKPGPIrtvnrkptlgSMFKQSLIELMNTINSTNVHYIRCIKPNADKEAW 678
Cdd:cd01386 545 ET-------------------------AAVKRKSPC----------LQIKFQVDALIDTLRRTGLHFVHCLLPQHNAGKD 589
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 679 ------------QFDNLMVLSQLRACGVLETIRISCAGFPSRWTFEEFVLRYYILIPHeqwdliFKKKETTEEDIIS--- 743
Cdd:cd01386 590 erstsspaagdeLLDVPLLRSQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPP------LTKKLGLNSEVADerk 663
|
730 740
....*....|....*....|....*.
gi 768464868 744 VVKMILDATVKDKSKYQIGNTKIFFK 769
Cdd:cd01386 664 AVEELLEELDLEKSSYRIGLSQVFFR 689
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
84-708 |
2.31e-92 |
|
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: 315.31 E-value: 2.31e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 84 PAVLHAIKQRYSQLNIYTYSGIVLIATNPFDRVDQLYTQDMIQAYAGKRRGE-------LEPHLFAIAEEAYRLMKNDKQ 156
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKELYDQDVMNVYLHKKSNSaasaapfPKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 157 NQTIVVSGESGAGKTVSAKYIMRYFASVeeensatvQHQVEMSETEQKILATNPIMEAFGNAKTTRNDNSSRFGKYLEIL 236
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYFHYI--------QTDSQMTERIDKLIYINNILESMSNATTIKNNNSSRCGRINLLI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 237 FD--KDTSII-------GARIRTYLLERSRLVYQPPTERNYHIFYQLMAGLPAQTKEELHLT-DASDYFYMNQ------- 299
Cdd:cd14884 153 FEevENTQKNmfngcfrNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGLSDEDLARRNLVrNCGVYGLLNPdeshqkr 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 300 --GGDTKINGID----------DAKEYKITVDALTLVGITKETQHQIFKILAALLHIGNieikktrndaslsadePNLKL 367
Cdd:cd14884 233 svKGTLRLGSDSldpseeekakDEKNFVALLHGLHYIKYDERQINEFFDIIAGILHLGN----------------RAYKA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 368 ACELLGIDAYNFAKWVTKKQIITRSEKIVSNLNYNQALVAKDSVAKFIYSALFDWLVENINTVLCNPAVNDQI------- 440
Cdd:cd14884 297 AAECLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNVLKCKEKDESdnediys 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 441 --SSFIGVLDIYGFEHFEKNSFEQFCINYANEKLQQEFNQHVFKLEQEEYVKEEIEWSFIEFNDNQPCIDLIENklgILS 518
Cdd:cd14884 377 inEAIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDVAPSYSDTLIFIAK---IFR 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 519 LLDEESRLPAG-----SDESWT-----QKLYQTLDKSPTNKVFSKPRFGQTK--------FIVSHYALDVAYDVEGFIEK 580
Cdd:cd14884 454 RLDDITKLKNQgqkktDDHFFRyllnnERQQQLEGKVSYGFVLNHDADGTAKkqnikkniFFIRHYAGLVTYRINNWIDK 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 581 NRDTVSDGHLEVLKASTNETLINILEGlekaakkleeakkleleqagsKKPGPIRTVNRkptlgsMFKQSLIELMNTINS 660
Cdd:cd14884 534 NSDKIETSIETLISCSSNRFLREANNG---------------------GNKGNFLSVSK------KYIKELDNLFTQLQS 586
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 768464868 661 TNVHYIRCIKPNADKEAWQFDNLMVLSQLRACGVLETIRISCAGFPSR 708
Cdd:cd14884 587 TDMYYIRCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHK 634
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
86-769 |
6.18e-92 |
|
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: 313.57 E-value: 6.18e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 86 VLHAIKQRYSQLNIYTYSGIVLIATNPFDRVDQLYTQDMIQAYaGKRRGeLEPHLFAIAEEAYRLMKNDKQNQTIVVSGE 165
Cdd:cd14905 3 LINIIQARYKKEIIYTYIGPILVSVNPLRYLPFLHSQELVRNY-NQRRG-LPPHLFALAAKAISDMQDFRRDQLIFIGGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 166 SGAGKTVSAKYIMRYFASVEEENSATVQhqvemseteQKILATNPIMEAFGNAKTTRNDNSSRFGKYLEILFDKDTSIIG 245
Cdd:cd14905 81 SGSGKSENTKIIIQYLLTTDLSRSKYLR---------DYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 246 ARIRTYLLERSRLVYQPPTERNYHIFYQLMAGLPAQTKEELHLTDASDYFYMNQGGDTKINGIDDAKEYKITVDALTLVG 325
Cdd:cd14905 152 AKLYSYFLDENRVTYQNKGERNFHIFYQFLKGITDEEKAAYQLGDINSYHYLNQGGSISVESIDDNRVFDRLKMSFVFFD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 326 ITKETQHQIFKILAALLHIGNIEIKKtRNDASLSADEPNLKLACELLGIDAynfakwvTKKQIITRSEKivsNLNYNQAL 405
Cdd:cd14905 232 FPSEKIDLIFKTLSFIIILGNVTFFQ-KNGKTEVKDRTLIESLSHNITFDS-------TKLENILISDR---SMPVNEAV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 406 VAKDSVAKFIYSALFDWLVENINTVLcNPAvndQISSFIGVLDIYGFEHFEKNSFEQFCINYANEKLQQEFNQHVFKLEQ 485
Cdd:cd14905 301 ENRDSLARSLYSALFHWIIDFLNSKL-KPT---QYSHTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVLKQEQ 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 486 EEYVKEEIEW-SFIEFNDNQPCIDLIENklgILSLLDEESRLPAGSDESWTQKLYQTLDKsptNKVFSKPrfgQTKFIVS 564
Cdd:cd14905 377 REYQTERIPWmTPISFKDNEESVEMMEK---IINLLDQESKNINSSDQIFLEKLQNFLSR---HHLFGKK---PNKFGIE 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 565 HYALDVAYDVEGFIEKNRDTVSDGHLEVLKASTNETL---------------INILEGLEKAAKKLEEAKKLELEQAGSK 629
Cdd:cd14905 448 HYFGQFYYDVRGFIIKNRDEILQRTNVLHKNSITKYLfsrdgvfninatvaeLNQMFDAKNTAKKSPLSIVKVLLSCGSN 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 630 KPGPIRTVNRKP--------------TLGSMFkQSLIELMNTINSTNV--HYIRCIKPNADKEAWQFDNLMVLSQLRACG 693
Cdd:cd14905 528 NPNNVNNPNNNSgggggggnsgggsgSGGSTY-TTYSSTNKAINNSNCdfHFIRCIKPNSKKTHLTFDVKSVNEQIKSLC 606
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768464868 694 VLETIRISCAGFPSRWTFEEFVLRYYILIPHEQ-WDLIFKKKETTEEDIISVVkmildatvkdKSKYQIGNTKIFFK 769
Cdd:cd14905 607 LLETTRIQRFGYTIHYNNKIFFDRFSFFFQNQRnFQNLFEKLKENDINIDSIL----------PPPIQVGNTKIFLR 673
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
85-769 |
3.63e-89 |
|
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: 304.10 E-value: 3.63e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 85 AVLHAIKQRYSQLNIYTYSGIVLIATNPFDRVDQlYTQDMIQAYagkrrgelepHLFAIAEEAYRLMKNDKQN-QTIVVS 163
Cdd:cd14874 2 GIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSI-QDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 164 GESGAGKTVSAKYIMRYFASVEEENSATVQHQvemseteqkilATNPIMEAFGNAKTTRNDNSSRFGKYLEILFdKDTSI 243
Cdd:cd14874 71 GESGSGKSYNAFQVFKYLTSQPKSKVTTKHSS-----------AIESVFKSFGCAKTLKNDEATRFGCSIDLLY-KRNVL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 244 IGARIR-TYLLERSRLVYQPPTERNYHIFYQLMAGLPAQTKEELHLTDASDYFYMNQGGDTKiNGIDDAKEYKITVDALT 322
Cdd:cd14874 139 TGLNLKyTVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGLQKFFYINQGNSTE-NIQSDVNHFKHLEDALH 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 323 LVGITKETQHQIFKILAALLHIGNIEIKKTRN-----DASLSADEPNLKLACELLGIDaynFAKWVtkkQIITRSEKIVS 397
Cdd:cd14874 218 VLGFSDDHCISIYKIISTILHIGNIYFRTKRNpnveqDVVEIGNMSEVKWVAFLLEVD---FDQLV---NFLLPKSEDGT 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 398 NLNYNQALVAKDSVAKFIYSALFDWLVENINTVLCNPAVNDQISsfigVLDIYGFEHFEKNSFEQFCINYANEKLQQEFN 477
Cdd:cd14874 292 TIDLNAALDNRDSFAMLIYEELFKWVLNRIGLHLKCPLHTGVIS----ILDHYGFEKYNNNGVEEFLINSVNERIENLFV 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 478 QHVFKLEQEEYVKEEIEWSFIEFN--DNQPCIDLIENK-LGILSLLDEESRLPAGSDESWTQKL-YQTLDKSPTNKVFSK 553
Cdd:cd14874 368 KHSFHDQLVDYAKDGISVDYKVPNsiENGKTVELLFKKpYGLLPLLTDECKFPKGSHESYLEHCnLNHTDRSSYGKARNK 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 554 PRFgqtKFIVSHYALDVAYDVEGFIEKNRDTVSDGHLEVLKASTNETLINILEGLEKaakkleEAKKLELEQAgskkpgp 633
Cdd:cd14874 448 ERL---EFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFESYSS------NTSDMIVSQA------- 511
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 634 iRTVNRkptlgsmfkqSLIELMNTINSTNVHYIRCIKPNADKEAWQFDNLMVLSQLRACGVLETIRISCAGFPSRWTFEE 713
Cdd:cd14874 512 -QFILR----------GAQEIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTT 580
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 768464868 714 FVLRYYILIPHEqwdliFKKKETTEEdiisVVKMILDAT-VKDKSKYQIGNTKIFFK 769
Cdd:cd14874 581 FARQYRCLLPGD-----IAMCQNEKE----IIQDILQGQgVKYENDFKIGTEYVFLR 628
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
87-768 |
5.97e-81 |
|
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: 283.79 E-value: 5.97e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 87 LHAIKQRYSQLNIYTYSGIVLIATNPFDRVdQLYTQDMIQAYAGKRR----------GELEPHLFAIAEEAYRLMKNDKQ 156
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPL-PIYTPDHMQAYNKSREqtplyekdtvNDAPPHVFALAQNALRCMQDAGE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 157 NQTIVVSGESGAGKTVSAKYIMRYFASVEEEnsATVQHQVE-----MSETEQKILATNPIMEAFGNAKTTRNDNSSRFGK 231
Cdd:cd14893 83 DQAVILLGGMGAGKSEAAKLIVQYLCEIGDE--TEPRPDSEgasgvLHPIGQQILHAFTILEAFGNAATRQNRNSSRFAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 232 YLEILFDKDTSIIGARIRTYLLERSRLVYQPPTERNYHIFYQLMAGLP--AQTKEELHLTDASDYFYMNQGGDTKINGID 309
Cdd:cd14893 161 MISVEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQhdPTLRDSLEMNKCVNEFVMLKQADPLATNFA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 310 -DAKEYKITVDALTLVGITKETQHQIFKILAALLHIGNIEI--------------KKTRNDASLSA--DEPNLKLACELL 372
Cdd:cd14893 241 lDARDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFvpdpeggksvgganSTTVSDAQSCAlkDPAQILLAAKLL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 373 GIDAYNFAKWVTKKQIITR-SEKIVSNL---NYNQALVAKDSVAKFIYSALFDWLVENINTVL---------CNPAVNDQ 439
Cdd:cd14893 321 EVEPVVLDNYFRTRQFFSKdGNKTVSSLkvvTVHQARKARDTFVRSLYESLFNFLVETLNGILggifdryekSNIVINSQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 440 issFIGVLDIYGFEHFE--KNSFEQFCINYANEKLQQEFNQHVFKL-------EQEEYVKEEIEWSFIEFN-DNQPCIDL 509
Cdd:cd14893 401 ---GVHVLDMVGFENLTpsQNSFDQLCFNYWSEKVHHFYVQNTLAInfsfledESQQVENRLTVNSNVDITsEQEKCLQL 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 510 IENK-LGILSLLDEESRLPAGSDESWTQKLYQ-----------TLDKSPTNKVFSKPRFGQTKFIVSHYALDVAYDVEGF 577
Cdd:cd14893 478 FEDKpFGIFDLLTENCKVRLPNDEDFVNKLFSgneavgglsrpNMGADTTNEYLAPSKDWRLLFIVQHHCGKVTYNGKGL 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 578 IEKNRDTVSDGHLEVLKASTNETLiNILEGLEKAAKKLEEAKKlELEQAGSKKPGPIRTVNRKPTLGSMFKQSLIE---- 653
Cdd:cd14893 558 SSKNMLSISSTCAAIMQSSKNAVL-HAVGAAQMAAASSEKAAK-QTEERGSTSSKFRKSASSARESKNITDSAATDvynq 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 654 ---LMNTINSTNVHYIRCIKPNADKEAWQFDNLMVLSQLRACGVLETIRISCAGFPSRWTFEEFVLRYYILIPHeqwdli 730
Cdd:cd14893 636 adaLLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRYKNVCGH------ 709
|
730 740 750
....*....|....*....|....*....|....*...
gi 768464868 731 fkkKETTEediiSVVKMILDATVKDKSKYQIGNTKIFF 768
Cdd:cd14893 710 ---RGTLE----SLLRSLSAIGVLEEEKFVVGKTKVYL 740
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
85-768 |
4.87e-80 |
|
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: 277.77 E-value: 4.87e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 85 AVLHAIKQRYSQLNIYTYSGIVLIATNPFDRVDQLYTqdmiqaYAGKRRGELEPHLFAIAEEAYRLMKNDKQNQTIVVSG 164
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPYRDVGNPLT------LTSTRSSPLAPQLLKVVQEAVRQQSETGYPQAIILSG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 165 ESGAGKTVSAKYIMRYFASVEEENSATvqhqvemsETEQKILATNPIMEAFGNAKTTRNDNSSRFGKYLEILFdKDTSII 244
Cdd:cd14881 76 TSGSGKTYASMLLLRQLFDVAGGGPET--------DAFKHLAAAFTVLRSLGSAKTATNSESSRIGHFIEVQV-TDGALY 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 245 GARIRTYLLERSRLVYQPPTERNYHIFYQLMAGLPAQTKEELHLT--DASDYFYMNQgGDTKINGIDDAKEYKITVDALT 322
Cdd:cd14881 147 RTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDgySPANLRYLSH-GDTRQNEAEDAARFQAWKACLG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 323 LVGITKEtqhQIFKILAALLHIGNIE-IKKTRNDASLSAdEPNLKLACELLGIDAYNFAKWVTKKQIITRSEKIVSNLNY 401
Cdd:cd14881 226 ILGIPFL---DVVRVLAAVLLLGNVQfIDGGGLEVDVKG-ETELKSVAALLGVSGAALFRGLTTRTHNARGQLVKSVCDA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 402 NQALVAKDSVAKFIYSALFDWLVENINTV--LCNPAVNDQISSFIGVLDIYGFEHFEKNSFEQFCINYANEKLQQEFNQH 479
Cdd:cd14881 302 NMSNMTRDALAKALYCRTVATIVRRANSLkrLGSTLGTHATDGFIGILDMFGFEDPKPSQLEHLCINLCAETMQHFYNTH 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 480 VFKLE----QEEYVKEEIEwsfIEFNDNQPCIDLIEN-KLGILSLLDEESRlPAGSDESWTQKLYQTLDKSPtnKVFSKP 554
Cdd:cd14881 382 IFKSSiescRDEGIQCEVE---VDYVDNVPCIDLISSlRTGLLSMLDVECS-PRGTAESYVAKIKVQHRQNP--RLFEAK 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 555 RFGQTKFIVSHYALDVAYDVEGFIEKNRDTVSDGHLEVL-KASTNETLInileglekaakkleeakkleleqagskkpgp 633
Cdd:cd14881 456 PQDDRMFGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFyKQNCNFGFA------------------------------- 504
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 634 irtvnrkpTLGSMFKQSLIELMNTINSTNVHYIRCIKPNADKEAWQFDNLMVLSQLRACGVLETIRISCAGFPSRWTFEE 713
Cdd:cd14881 505 --------THTQDFHTRLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAGGYPHRMRFKA 576
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768464868 714 FVLRYYILIPheqwdliFKKKETTEEDIISVVKMILD-ATVKDKSK-------YQIGNTKIFF 768
Cdd:cd14881 577 FNARYRLLAP-------FRLLRRVEEKALEDCALILQfLEAQPPSKlssvstsWALGKRHIFL 632
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
86-721 |
5.36e-69 |
|
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: 245.81 E-value: 5.36e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 86 VLHAIKQRYSQLNIYTYSGIVLIATNPfDRVDQLYTQDMIQAYAGKRRGELEPHLFAIAEEAYRLMKNDKQNQTIVVSGE 165
Cdd:cd14882 3 ILEELRHRYLMGESYTFIGDILLSLNP-NEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 166 SGAGKTVSAKYIMRYFASVEEENSATVQhqvemseteqKILATNPIMEAFGNAKTTRNDNSSRFGKYLEILFDKDTSIIG 245
Cdd:cd14882 82 SYSGKTTNARLLIKHLCYLGDGNRGATG----------RVESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMSG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 246 ARIRTYLLERSRLVYQPPTERNYHIFYQLMAGLPAQTK-EELHLTDASDYFYMNQGGDTKINGI----DD----AKEYKI 316
Cdd:cd14882 152 AIFWMYQLEKLRVSTTDGNQSNFHIFYYFYDFIEAQNRlKEYNLKAGRNYRYLRIPPEVPPSKLkyrrDDpegnVERYKE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 317 TVDALTLVGITKETQHQIFKILAALLHIGNIEIKKTRNDASLSADEPNLKLAcELLGIDAYNFAKWVTKKQIITRSEKIV 396
Cdd:cd14882 232 FEEILKDLDFNEEQLETVRKVLAAILNLGEIRFRQNGGYAELENTEIASRVA-ELLRLDEKKFMWALTNYCLIKGGSAER 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 397 SNLNYNQALVAKDSVAKFIYSALFDWLVENINTVLCNP--AVNDQISsfIGVLDIYGFEHFEKNSFEQFCINYANEKLQQ 474
Cdd:cd14882 311 RKHTTEEARDARDVLASTLYSRLVDWIINRINMKMSFPraVFGDKYS--ISIHDMFGFECFHRNRLEQLMVNTLNEQMQY 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 475 EFNQHVFKLEQEEYVKEEIEWSFIEFNDNQPCIDLIENKL-GILSLLDEESRLPAGSDeswtqklyQTLDKSPTNK-VFS 552
Cdd:cd14882 389 HYNQRIFISEMLEMEEEDIPTINLRFYDNKTAVDQLMTKPdGLFYIIDDASRSCQDQN--------YIMDRIKEKHsQFV 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 553 KPRfGQTKFIVSHYALDVAYDVEGFIEKNRDTVSDGHLEVLKASTNETLINILEGLEkaakkleeakkleleqagskkpg 632
Cdd:cd14882 461 KKH-SAHEFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTNSQ----------------------- 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 633 pirtVNRKPTLGSMFKQSLIELMNTI----NSTNVHYIRCIKPNADKEAWQFDNLMVLSQLRACGVLETIRISCAGFPSR 708
Cdd:cd14882 517 ----VRNMRTLAATFRATSLELLKMLsigaNSGGTHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYR 592
|
650
....*....|...
gi 768464868 709 WTFEEFVLRYYIL 721
Cdd:cd14882 593 IPFQEFLRRYQFL 605
|
|
| MYSc_Myo24B |
cd14938 |
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
84-767 |
7.69e-58 |
|
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: 214.31 E-value: 7.69e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 84 PAVLHAIKQRYSQLNIYTYSGIVLIATNPFDRVDQLYTQDMIQAYAGKRRGELEPHLFAIAEEAYRLMKNDKQNQTIVVS 163
Cdd:cd14938 1 PSVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKCIDCIEDLSLNEYHVVHNALKNLNELKRNQSIIIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 164 GESGAGKTVSAKYIMRYFASVEEENSATVQHQVEMSETEQKILATNP--------------IMEAFGNAKTTRNDNSSRF 229
Cdd:cd14938 81 GESGSGKSEIAKNIINFIAYQVKGSRRLPTNLNDQEEDNIHNEENTDyqfnmsemlkhvnvVMEAFGNAKTVKNNNSSRF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 230 GKYLEILFDKDtSIIGARIRTYLLERSRLVYQPPTERNYHIFYQLMAGLPAQTKEELHLTDASDYFYMNQGGDTKINGID 309
Cdd:cd14938 161 SKFCTIHIENE-EIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIENYSMLNNEKGFEKFSDY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 310 DAKeykiTVDALTLVGITKETQHQI---FKILAALLHIGNIEIKKT----------------------------RNDASL 358
Cdd:cd14938 240 SGK----ILELLKSLNYIFDDDKEIdfiFSVLSALLLLGNTEIVKAfrkksllmgknqcgqninyetilselenSEDIGL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 359 SADEPNLKLACELLGIDAYNFAKWVTKKQIITRSEKIVSnlnYNQALVAK--DSVAKFIYSALFDWLVENINTVLCNPAV 436
Cdd:cd14938 316 DENVKNLLLACKLLSFDIETFVKYFTTNYIFNDSILIKV---HNETKIQKklENFIKTCYEELFNWIIYKINEKCTQLQN 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 437 NDQISSFIGVLDIYGFEHFEKNSFEQFCINYANEKLQQEFNQHVFKLEQEEYVKEEIEWSF-IEFNDNQPCIDLI--ENK 513
Cdd:cd14938 393 ININTNYINVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYnSENIDNEPLYNLLvgPTE 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 514 LGILSLLDEESrlpagsdeswTQKLYQ--TLDKSPTNKVFSKPRFGQTK--------FIVSHYALDVAYDVEGFIEKNRD 583
Cdd:cd14938 473 GSLFSLLENVS----------TKTIFDksNLHSSIIRKFSRNSKYIKKDditgnkktFVITHSCGDIIYNAENFVEKNID 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 584 TVSDGHLEVLKASTNETL--INILEGLEKAAKKLEEAKKLELEQAGSKKPGPIRTVNRKPTlgSMFKQSLIELMNTINST 661
Cdd:cd14938 543 ILTNRFIDMVKQSENEYMrqFCMFYNYDNSGNIVEEKRRYSIQSALKLFKRRYDTKNQMAV--SLLRNNLTELEKLQETT 620
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 662 NVHYIRCIKPNADKEA-WQFDNLMVLSQLRACGVLETIRISCAGFPSRWTFEEFVlryyilipheqwdLIFKKKettEED 740
Cdd:cd14938 621 FCHFIVCMKPNESKRElCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFL-------------SIFDIK---NED 684
|
730 740
....*....|....*....|....*..
gi 768464868 741 IISVVKMILDATVKDKSKYQIGNTKIF 767
Cdd:cd14938 685 LKEKVEALIKSYQISNYEWMIGNNMIF 711
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
106-238 |
5.39e-41 |
|
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: 149.03 E-value: 5.39e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 106 VLIATNPFDRVDQLYTQDMIQAYAGKRRGELEPHLFAIAEEAYRLMKNDKQNQTIVVSGESGAGKTVSAKYIMRYFASV- 184
Cdd:cd01363 1 VLVRVNPFKELPIYRDSKIIVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVa 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 768464868 185 -----EEENSATVQHQVEMSETEQKILATNPIMEAFGNAKTTRNDNSSRFGKYLEILFD 238
Cdd:cd01363 81 fnginKGETEGWVYLTEITVTLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEILLD 139
|
|
| DIL |
pfam01843 |
DIL domain; The DIL domain has no known function. |
1382-1482 |
3.26e-35 |
|
DIL domain; The DIL domain has no known function.
Pssm-ID: 460359 [Multi-domain] Cd Length: 103 Bit Score: 130.02 E-value: 3.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 1382 VVTTLLNYVDAICFNELIMKRNFLSWKRGLQLNYNVTRLEEWCKTHGLTDG-TECLQHLIQTAKLLQVRKYTIEDIDILR 1460
Cdd:pfam01843 2 LFSQLFYFINAELFNRLLLRKKYCSWSKGMQIRYNLSRLEEWARSNGLESEaRDHLAPLIQAAQLLQLRKSTLEDLDSIL 81
|
90 100
....*....|....*....|..
gi 768464868 1461 GICYSLTPAQLQKLISQYQVAD 1482
Cdd:pfam01843 82 QVCPALNPLQLHRLLTLYQPDD 103
|
|
| fMyo4p_CBD |
cd15479 |
cargo binding domain of fungal myosin 4; Yeast myosin V travels along actin cables, actin ... |
1173-1502 |
2.07e-31 |
|
cargo binding domain of fungal myosin 4; 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).
Pssm-ID: 271263 Cd Length: 329 Bit Score: 126.63 E-value: 2.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 1173 EITEGLLKGFEVPdagvaiQLSKRDVVYPARILIIVLSEMWRFGLTKQSESFLAQVLTTIQKVVTQLKGNDLIPSGVFWL 1252
Cdd:cd15479 5 EVTEGYLKKVNVT------EVNGDNVLGPIHVITTVVSSLVRNGLLIQSSKFISKVLLTVESIVMSLPKDETMLGGIFWL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 1253 ANVRELYSFVvfALNSILTEetfKNGmTDEEYKEYVSLVTELKDDFEALSYNIYNIWLKKLQK-QLQKKAINAVVISEsl 1331
Cdd:cd15479 79 SNLSRLPAFA--ANQKTLYE---ANG-GDEKDKLTLIYLNDLENETLKVFDKIYSTWLVKFMKhASAHIEIFDMVLNE-- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 1332 pgfsagetsgflnKIFANTEEYTMDDILTFFNSIYWCMKSFHIENEVFHAVVTTLLNYVDAICFNELIMKRNFLSWKRGL 1411
Cdd:cd15479 151 -------------KLFKNSGDEKFAKLFTFLNEFDAVLCKFQVVDSMHTKIFNDTLKYLNVMLFNDLITKCPALNWKYGY 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 1412 QLNYNVTRLEEWCKTHglTDGTEC-LQHLIQTAKLLQVRKYTIEDIDILRGICYSLTPAQLQKLISQYQVADY-ESPIPQ 1489
Cdd:cd15479 218 EVDRNIERLVSWFEPR--IEDVRPnLIQIIQAVKILQLKISNLNEFKLLFDFWYALNPAQIQAILLKYKPANKgEAGVPN 295
|
330
....*....|...
gi 768464868 1490 EILRYVADIVKKE 1502
Cdd:cd15479 296 EILNYLANVIKRE 308
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
205-700 |
5.09e-31 |
|
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276859 [Multi-domain] Cd Length: 871 Bit Score: 132.56 E-value: 5.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 205 ILATNPIMEAFGNAKTTRNDNSSRFGKY--LEILFDK---DTSIIGARIRTYLLERSRLVYQ------PPTERNYHIFYQ 273
Cdd:cd14894 249 VLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLhpwEFQICGCHISPFLLEKSRVTSErgresgDQNELNFHILYA 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 274 LMAGLPA-----QTKEELHL--TDASDYFYMNQGgDTKINGI--------DDAKEYKITVDALTLVGITKETQHQIFKIL 338
Cdd:cd14894 329 MVAGVNAfpfmrLLAKELHLdgIDCSALTYLGRS-DHKLAGFvskedtwkKDVERWQQVIDGLDELNVSPDEQKTIFKVL 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 339 AALLHIGNIEIKKTR--------NDASLSADEPNLKLaCELLGIDAYNFAKWVTKKQIITRSEKIVSNLNYNQALVAKDS 410
Cdd:cd14894 408 SAVLWLGNIELDYREvsgklvmsSTGALNAPQKVVEL-LELGSVEKLERMLMTKSVSLQSTSETFEVTLEKGQVNHVRDT 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 411 VAKFIYSALFDWLVENINTVLCNPAVND--------------QISSFIGVLDIYGFEHFEKNSFEQFCINYANEKLQQef 476
Cdd:cd14894 487 LARLLYQLAFNYVVFVMNEATKMSALSTdgnkhqmdsnasapEAVSLLKIVDVFGFEDLTHNSLDQLCINYLSEKLYA-- 564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 477 nqhvfKLEQEEYVKEEIEWSFIEFNDNQPCIDLIENKLGI------LSLLDEESRLPAGSDESWTQKLYQTLDKSPTNKV 550
Cdd:cd14894 565 -----REEQVIAVAYSSRPHLTARDSEKDVLFIYEHPLGVfasleeLTILHQSENMNAQQEEKRNKLFVRNIYDRNSSRL 639
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 551 FSKPR------------FGQTKFIVSHYALDVAYDVEGFIEKNRDTVSDGHLEVLKASTNETLINILegleKAAKKLEEA 618
Cdd:cd14894 640 PEPPRvlsnakrhtpvlLNVLPFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNSSHFCRML----NESSQLGWS 715
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 619 KKLELEQAGSKKPgpiRTVNRKPTLGSMfkQSLIELMNTINSTNV-HYIRCIKPNADKEAWQFDNLMVLSQLRACGVLET 697
Cdd:cd14894 716 PNTNRSMLGSAES---RLSGTKSFVGQF--RSHVNVLTSQDDKNMpFYFHCIRPNAKKQPSLVNNDLVEQQCRSQRLIRQ 790
|
...
gi 768464868 698 IRI 700
Cdd:cd14894 791 MEI 793
|
|
| Myo5_CBD |
cd15470 |
Cargo binding domain of myosin 5; Class V myosins are well studied unconventional myosins, ... |
1354-1531 |
3.18e-26 |
|
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: 111.53 E-value: 3.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 1354 TMDDILTFFNSIYWCMKSFHIENEVFHAVVTTLLNYVDAICFNELIMKRNFLSWKRGLQLNYNVTRLEEWCKTHGLTDG- 1432
Cdd:cd15470 142 TLDSLLQQLNSFHTTLTQHGLDPELIKQVFRQLFYLICASTLNNLLLRKDLCSWSKGMQIRYNVSQLEEWLRDKGLQDSg 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 1433 -TECLQHLIQTAKLLQVRKYTIEDIDILRGICYSLTPAQLQKLISQYQ-VADYESPIPQEILRYVADIVKKEAALSSSGN 1510
Cdd:cd15470 222 aRETLEPLIQAAQLLQVKKTTEEDAQSICEMCTKLTTAQIVKILNLYTpVDDFEERVTPSFIRKVQARLNERADSNQLQL 301
|
170 180
....*....|....*....|...
gi 768464868 1511 --DSKghehsssiFITPETGPFT 1531
Cdd:cd15470 302 lmDTK--------YIFPVTFPFN 316
|
|
| Myo5a_CBD |
cd15478 |
Cargo binding domain of myosin 5a; Class V myosins are well studied unconventional myosins, ... |
1182-1495 |
9.57e-22 |
|
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: 99.33 E-value: 9.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 1182 FEVPDAGVAIQLSKRdvvYPARILIIVLSEMWRFGLTKQSESFLAQVLTTIQKVVTQlKGNDLiPSGVFWLANVRELysf 1261
Cdd:cd15478 13 LELKPRGVAVNLIPG---LPAYILFMCVRHADYLNDDQKVRSLLTSTINSIKKVLKK-RGDDF-ETVSFWLSNTCRF--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 1262 vVFALNSILTEETFKNGMTDEEYKEYVSL--VTELKDDFEALSYNIYNIWLKKLQKQLQKKAINAVVISESLPGFSAGET 1339
Cdd:cd15478 85 -LHCLKQYSGEEGFMKHNTSRQNEHCLTNfdLAEYRQVLSDLAIQIYQQLVRVLENILQPMIVSGMLEHETIQGVSGVKP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 1340 SGFLNKIFANTEE--YTMDDILTFFNSIYWCMKSFHIENEVFHAVVTTLLNYVDAICFNELIMKRNFLSWKRGLQLNYNV 1417
Cdd:cd15478 164 TGLRKRTSSIADEgtYTLDSILRQLNSFHSVMCQHGMDPELIKQVVKQMFYIIGAITLNNLLLRKDMCSWSKGMQIRYNV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 1418 TRLEEWCKTHGLTD--GTECLQHLIQTAKLLQVRKYTIEDIDILRGICYSLTPAQLQKLISQYQ-VADYESPIPQEILRY 1494
Cdd:cd15478 244 SQLEEWLRDKNLMNsgAKETLEPLIQAAQLLQVKKKTDDDAEAICSMCNALTTAQIVKVLNLYTpVNEFEERVSVSFIRT 323
|
.
gi 768464868 1495 V 1495
Cdd:cd15478 324 I 324
|
|
| Myo5b_CBD |
cd15477 |
Cargo binding domain of myosin 5b; Class V myosins are well studied unconventional myosins, ... |
1223-1478 |
7.01e-21 |
|
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: 96.47 E-value: 7.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 1223 SFLAQVLTTIQKVVTqlKGNDLIPSGVFWLANVRELysfvVFALNSILTEETFkngMTDEEYKEYVSLV-----TELKDD 1297
Cdd:cd15477 50 SLLTSTINGIKKVLK--KHNDDFEMTSFWLANTCRL----LHCLKQYSGDEGF---MTQNTAKQNEHCLknfdlTEYRQV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 1298 FEALSYNIYNIWLKKLQKQLQKKAINAVVISESLPGFSAGETSGFLNKIFANTE---EYTMDDILTFFNSIYWCMKSFHI 1374
Cdd:cd15477 121 LSDLSIQIYQQLIKIAEGILQPMIVSAMLENESIQGLSGVKPMGYRKRSSSMADgdnSYTLEALIRQLNTFHSIMCDQGL 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 1375 ENEVFHAVVTTLLNYVDAICFNELIMKRNFLSWKRGLQLNYNVTRLEEWCKTHGL--TDGTECLQHLIQTAKLLQVRKYT 1452
Cdd:cd15477 201 DPEIIQQVFKQLFYMINAVTLNNLLLRKDVCSWSTGMQLRYNISQLEEWLRGRNLhqSGAAQTMEPLIQAAQLLQLKKKT 280
|
250 260
....*....|....*....|....*.
gi 768464868 1453 IEDIDILRGICYSLTPAQLQKLISQY 1478
Cdd:cd15477 281 SEDAEAICSLCTALSTQQIVKILNLY 306
|
|
| Myo5p-like_CBD_afadin |
cd15471 |
cargo binding domain of myosin 5-like of afadin; Afadin is an actin filament (F-actin) and ... |
1386-1503 |
5.16e-14 |
|
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: 75.04 E-value: 5.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 1386 LLNYVDAICFNELIMKRN--FLSWKRGLQLNYNVTRLEEWCKTHGLTDGTEC-LQHLIQTAKLLQVRKYTIEDIDILRGI 1462
Cdd:cd15471 180 LFHFINAWLFNSLVSNPDsgLCTRYWGKRLRQRLAHVEAWAERQGLELAADChLDRIVQAANLLTAPKYSAEDVANLSST 259
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 768464868 1463 CYSLTPAQLQKLISQYQVADYESPIPQEILRYVADIVKKEA 1503
Cdd:cd15471 260 CFKLNSLQLRALLSHYQPPPGEPPIPPDLIERVVRLAESQA 300
|
|
| Myo5c_CBD |
cd15476 |
Cargo binding domain of myosin 5C; Class V myosins are well studied unconventional myosins, ... |
1346-1495 |
5.37e-12 |
|
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: 69.04 E-value: 5.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 1346 IFANTEEYTMDDILTFFNSIYWCMKSFHIENEVFHAVVTTLLNYVDAICFNELIMKRNFLSWKRGLQLNYNVTRLEEWCK 1425
Cdd:cd15476 135 VMENNLQPTISSILQQLSYFYSTMCQHGMDPELIKQAVKQLFFLIGAVTLNSIFLRKDMCSCRKGMQIRCNISYLEEWLK 214
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768464868 1426 THGLTDGT--ECLQHLIQTAKLLQVRKYTIEDIDILRGICYSLTPAQLQKLISQYQ-VADYESPIPQEILRYV 1495
Cdd:cd15476 215 EKNLQNSNakETLEPLSQAAWLLQVNKTTDDDAKEICERCTELSAVQIVKILNSYTpIDDFEKRVTPSFVRKV 287
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
857-1081 |
2.08e-11 |
|
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: 69.32 E-value: 2.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 857 RTITNLQK--KIRKELKqRQLKqeheynaavTIQSKVRTFEpRSRFLRTKKDTVVVQSLIRR-RAAQRKLKQLKADAKSV 933
Cdd:TIGR02168 183 RTRENLDRleDILNELE-RQLK---------SLERQAEKAE-RYKELKAELRELELALLVLRlEELREELEELQEELKEA 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 934 NHLKEvsyKLENKVIELTQNLASKVKENKEMTERIKELQVQVEESAKLQETLENMKKEHLIDIDNQKSKDMELQKTIENN 1013
Cdd:TIGR02168 252 EEELE---ELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEEL 328
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768464868 1014 lqstEQTLKDAQLELEDMVKQHDELKEESKKQLEELEQTKKTLVEYQTLNGDLQNEVKSLKEEIARLQ 1081
Cdd:TIGR02168 329 ----ESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE 392
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
864-1083 |
1.85e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.65 E-value: 1.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 864 KKIRKELKQRQLK-QEHEYNAAvtiQSKVRTFEPRSRFLRTKKDTVVVQSLIRRRAAQRKLKQLKADAKSVNHLKEVSYK 942
Cdd:COG1196 216 RELKEELKELEAElLLLKLREL---EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 943 LENKVIELTQNLASKVKENKEMTERIKELQVQVEESAKLQETLEnmkkEHLIDIDNQKSKDMELQKTIENNLQSTEQTLK 1022
Cdd:COG1196 293 LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELE----EELEELEEELEEAEEELEEAEAELAEAEEALL 368
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768464868 1023 DAQLELEDMVKQHDELKEESKKQLEELEQTKKTLVEYQTLNGDLQNEVKSLKEEIARLQTA 1083
Cdd:COG1196 369 EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA 429
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
864-1094 |
1.01e-08 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 60.14 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 864 KKIRKELKQRQLKQEHEYNAAVTIqSKVRTFEpRSRFLRTKKDTVVVQSL-------IRRRAAQRKLKQLKADAKSVNHL 936
Cdd:pfam17380 351 ERIRQEERKRELERIRQEEIAMEI-SRMRELE-RLQMERQQKNERVRQELeaarkvkILEEERQRKIQQQKVEMEQIRAE 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 937 KEVSYKLENKVIEltqnlaskvkenkemTERIKELQVQVEESAKLQETLENMKKEHlidiDNQKSKDMELQKTIENNLQS 1016
Cdd:pfam17380 429 QEEARQREVRRLE---------------EERAREMERVRLEEQERQQQVERLRQQE----EERKRKKLELEKEKRDRKRA 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 1017 TEQTLKDAQLELEDmvKQHDELKEESKKQL--EELEQTKKTLVEYQTLNGDLQNEVKSLK-EEIARLQTAMSLGTVTTSV 1093
Cdd:pfam17380 490 EEQRRKILEKELEE--RKQAMIEEERKRKLleKEMEERQKAIYEEERRREAEEERRKQQEmEERRRIQEQMRKATEERSR 567
|
.
gi 768464868 1094 L 1094
Cdd:pfam17380 568 L 568
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
861-1080 |
5.41e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 57.72 E-value: 5.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 861 NLQKKIRKELKQRQLKQEHEYNAAVTIQSKVRTFEPRSRFLRTKKDTVVVQSLIRRRAAQRKLKQLKADAKSVNHLKEVS 940
Cdd:TIGR04523 307 DWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEI 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 941 YKLENKVIELTQNLASKVKENKEMTERIKELQVQVEESAKLQETLENMKKEHLIDIDNQKSKDMELQKTIENnlqsTEQT 1020
Cdd:TIGR04523 387 KNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKN----LDNT 462
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 1021 LKDAQLELEDMVKQHDELKEESKKQLEELEQTKKTLVEYQTLNGDLQNEVKSLKEEIARL 1080
Cdd:TIGR04523 463 RESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSL 522
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
864-1084 |
5.76e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.77 E-value: 5.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 864 KKIRKELKQRQLKQEH--EYNAavtIQSKVRTFEPRSRFLRTKKDTVVVQSLIRRRAAQRKL-----KQLKADAKSVNHL 936
Cdd:TIGR02169 194 DEKRQQLERLRREREKaeRYQA---LLKEKREYEGYELLKEKEALERQKEAIERQLASLEEElekltEEISELEKRLEEI 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 937 KEVSYKLENKVIELTQNLASKVKEN-KEMTERIKELQVQVEESAKLQETLENMKKEHLIDIDNQKSKDMELQKTIE---- 1011
Cdd:TIGR02169 271 EQLLEELNKKIKDLGEEEQLRVKEKiGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEeerk 350
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768464868 1012 ------NNLQSTEQTLKDAQLELEDMVKQHDELKEESKKQLEELEQTKKTLVEYQTLNGDLQNEVKSLKEEIARLQTAM 1084
Cdd:TIGR02169 351 rrdkltEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAI 429
|
|
| Myo5p-like_CBD_Rasip1 |
cd15472 |
cargo binding domain of myosin 5-like of Ras-interacting protein 1; Ras-interacting protein 1 ... |
1370-1481 |
5.92e-08 |
|
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: 56.90 E-value: 5.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 1370 KSFHIENEVFHAVVTTLLNYVDAICFNELIMK---RNFLSWKRGLQLNYNVTRLEEWCKTHGLTD-GTECLQHLIQTAKL 1445
Cdd:cd15472 212 RQYQVHPEIASQMFAYLFFFSNASLFNQLMEKgsgGGFFQWSRGVQIRANLDLLLDWLQGAGLGDlAEEFFRKLSSTVNL 291
|
90 100 110
....*....|....*....|....*....|....*...
gi 768464868 1446 LQVRKYTIEDID--ILRGICYSLTPAQLQKLISQYQVA 1481
Cdd:cd15472 292 LATPKEQLLQMSwsSLRAEFPALNPAQLHHLLRQYQLG 329
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
890-1085 |
7.76e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 57.37 E-value: 7.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 890 KVRTFEPRSRFLRTKKDTVVVQSLIRRRaaQRKLKQLKADAKSVNHLKEVSYKLENKVIELTqnlaskVKENKEMTERIK 969
Cdd:TIGR02168 171 KERRKETERKLERTRENLDRLEDILNEL--ERQLKSLERQAEKAERYKELKAELRELELALL------VLRLEELREELE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 970 ELQVQVEESAKLQETLENMKKEHLIDIDNQKSKDMELQKTIeNNLQSTEQTLKDAQLELEDMVKQHDELKEESKKQLEE- 1048
Cdd:TIGR02168 243 ELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEI-EELQKELYALANEISRLEQQKQILRERLANLERQLEEl 321
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 768464868 1049 ---LEQTKKTLVEYQTLNGDLQNEVKSLKEEIARLQTAMS 1085
Cdd:TIGR02168 322 eaqLEELESKLDELAEELAELEEKLEELKEELESLEAELE 361
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
773-1081 |
9.51e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.00 E-value: 9.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 773 LAYLEKLRSNKMHNSIVMIQKKIraKYYRKQYLQISQAIKYLQNNIKGfiIRQRVNDEMK-VN-----------CATLLQ 840
Cdd:PRK03918 371 KEELERLKKRLTGLTPEKLEKEL--EELEKAKEEIEEEISKITARIGE--LKKEIKELKKaIEelkkakgkcpvCGRELT 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 841 AAYRGHSIR------ANVFSVLRTITNLQKKIRKELKqrqlkqeheynaavtiqsKVRTFEPRSRFLRTKKDTVVVQSLI 914
Cdd:PRK03918 447 EEHRKELLEeytaelKRIEKELKEIEEKERKLRKELR------------------ELEKVLKKESELIKLKELAEQLKEL 508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 915 RRRAAQRKLKQLKADAKSVNHLKEVSYKLENKVIELTQNLASKVKENKEMTERIKELQVQVEESAKLQETLENMKKEhli 994
Cdd:PRK03918 509 EEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFE--- 585
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 995 DIDNQKSKDMELQ---------KTIENNLQSTEQTLKDAQLELEDMVKQHDELK---EESKKQLEELEQtKKTLVEYQTL 1062
Cdd:PRK03918 586 SVEELEERLKELEpfyneylelKDAEKELEREEKELKKLEEELDKAFEELAETEkrlEELRKELEELEK-KYSEEEYEEL 664
|
330 340
....*....|....*....|..
gi 768464868 1063 NG---DLQNEVKSLKEEIARLQ 1081
Cdd:PRK03918 665 REeylELSRELAGLRAELEELE 686
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
840-1080 |
1.32e-07 |
|
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: 56.60 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 840 QAAYRGHSIRANVFSVLRTITNLQKKIRKELKQ-RQLKQEHEYNAAVTIQSKVRTFEPRSRFLRTKKDTVVVQSLIRRRA 918
Cdd:TIGR02168 716 QLRKELEELSRQISALRKDLARLEAEVEQLEERiAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLK 795
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 919 AQRKL--KQLKADAKSVNHLKEVSYKLENKVIELTQNLASKVKENKEMTERIKELQVQVEESA----KLQETLENMKKEh 992
Cdd:TIGR02168 796 EELKAlrEALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAaeieELEELIEELESE- 874
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 993 LIDIDNQKSKDMELQKTIENNLQSTEQTLKDAQLELEDMVKQHDELKE---ESKKQLEELEQTKKTL-----VEYQTLNG 1064
Cdd:TIGR02168 875 LEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREklaQLELRLEGLEVRIDNLqerlsEEYSLTLE 954
|
250 260 270
....*....|....*....|....*....|
gi 768464868 1065 D--------------LQNEVKSLKEEIARL 1080
Cdd:TIGR02168 955 EaealenkieddeeeARRRLKRLENKIKEL 984
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
917-1081 |
1.37e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 55.61 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 917 RAAQRKLKQLKADAKSVNhlKEVSyKLENKVIELTQNLASKVKENKEMTERIKELQVQVEE-SAKLQETLENMKKeHLID 995
Cdd:COG3883 19 QAKQKELSELQAELEAAQ--AELD-ALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEaEAEIEERREELGE-RARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 996 IDNQ-----------KSKD-------MELQKTIENNLQSTEQTLKDAQLELEDMVKQHDELKEESKKQLEELEQTKKTLV 1057
Cdd:COG3883 95 LYRSggsvsyldvllGSESfsdfldrLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180
....*....|....*....|....*...
gi 768464868 1058 ----EYQTLNGDLQNEVKSLKEEIARLQ 1081
Cdd:COG3883 175 aqqaEQEALLAQLSAEEAAAEAQLAELE 202
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
915-1081 |
2.11e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.16 E-value: 2.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 915 RRRAAQRKLKQLKADAKSVnhLKEVSyKLENKVIELTQNLASKVKENKEMTERIKELQVQVEESAKLQETLENMKKEHLI 994
Cdd:COG4942 35 EIAELEKELAALKKEEKAL--LKQLA-ALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 995 DID-----------------NQKSKDMELQKTIENNLQSTEQTLKDAQLELEDMVKQHDELKEESKKQLEELEQTKKTL- 1056
Cdd:COG4942 112 ALYrlgrqpplalllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALe 191
|
170 180
....*....|....*....|....*...
gi 768464868 1057 ---VEYQTLNGDLQNEVKSLKEEIARLQ 1081
Cdd:COG4942 192 alkAERQKLLARLEKELAELAAELAELQ 219
|
|
| Myo5p-like_CBD_DIL_ANK |
cd15473 |
cargo binding domain of myosin 5-like of dil and ankyrin domain containing protein; DIL and ... |
1357-1500 |
4.61e-07 |
|
cargo binding domain of myosin 5-like of dil and ankyrin domain containing protein; DIL and ankyrin domain-containing protein are a group of fungal proteins that contain a domain homologous to the cargo binding domain of class V myosins and ankyrin repeats. Their function is unknown.
Pssm-ID: 271257 [Multi-domain] Cd Length: 316 Bit Score: 53.71 E-value: 4.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 1357 DILTFFNSIYWCMKSFHIenevfHAVVTT-----LLNYVDAICFNELIMKRNFLSWKRGLQLNYNVTRLEEWCKTHGLT- 1430
Cdd:cd15473 138 NITSLLSSTLYVLELYDV-----HPAIIIqalsqLFYWLGCELFNRILTNKKYLCRSKAMQIRMNLSALEDWARSNNLQp 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 1431 --------DGTECLQHLIQTAKLLQVRkYTIEDIDILRGICYS---LTPAQLQKLISQYQVADYESPIPQEILRYVADIV 1499
Cdd:cd15473 213 ekgespprIARSHLAPVIQLLQWLQCL-SSLDDFESLIATIQQldaLNPLQLLRAVKDYRYEVNEGRMPEECVKYLAQLQ 291
|
.
gi 768464868 1500 K 1500
Cdd:cd15473 292 K 292
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
902-1081 |
7.51e-07 |
|
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: 54.30 E-value: 7.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 902 RTKKDTVVVQSLIRRRAAQRKLKQLKADAKSVNH----LKEVSYKLENKVIELTQNLASKVKENKEMTERIKELQVQVEE 977
Cdd:TIGR02169 697 LRRIENRLDELSQELSDASRKIGEIEKEIEQLEQeeekLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHK 776
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 978 SAKLQETLENMKKEHLID-IDNQKSKDMELQKTIENNLQSTEQTLKDAQLELE-------DMVKQHDELK---------- 1039
Cdd:TIGR02169 777 LEEALNDLEARLSHSRIPeIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEylekeiqELQEQRIDLKeqiksiekei 856
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 768464868 1040 EESKKQLEELEQ----TKKTLVEYQTLNGDLQNEVKSLKEEIARLQ 1081
Cdd:TIGR02169 857 ENLNGKKEELEEeleeLEAALRDLESRLGDLKKERDELEAQLRELE 902
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
944-1086 |
1.72e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.14 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 944 ENKVIELTQNLASKVKENKEMTERIKELQVQVEESAKLQETLENM--KKEHLIDIDNQKSKDMELQ-KTIENNLQSTEQT 1020
Cdd:TIGR02168 669 NSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEEleQLRKELEELSRQISALRKDlARLEAEVEQLEER 748
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768464868 1021 LKDAQLELEDMVKQHDELKEESKKQLEELEQTKKTLVEYQTLNGDLQNEVKSLKEEIARLQTAMSL 1086
Cdd:TIGR02168 749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTL 814
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
910-1084 |
2.80e-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: 2.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 910 VQSLIRRRAAQRKLKQLKADAKsvnhLKEVSYKLeNKVIELTQNLASKVKENKEMTERIKELQVQVEEsakLQETLENMK 989
Cdd:COG1196 202 LEPLERQAEKAERYRELKEELK----ELEAELLL-LKLRELEAELEELEAELEELEAELEELEAELAE---LEAELEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 990 KEHL---IDIDNQKSKDMELQKTI---ENNLQSTEQTLKDAQLELEDMVKQHDELKEESKKQLEELEQTKKTLVEYQTLN 1063
Cdd:COG1196 274 LELEeleLELEEAQAEEYELLAELarlEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEL 353
|
170 180
....*....|....*....|.
gi 768464868 1064 GDLQNEVKSLKEEIARLQTAM 1084
Cdd:COG1196 354 EEAEAELAEAEEALLEAEAEL 374
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
881-1081 |
3.43e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.84 E-value: 3.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 881 YNAAVTIQSKVRTFEP----RSRFLRTKKDTVVVQSLIRRR---AAQRKLKQLKADAKSVNHLKEvsyKLENKVIELTQN 953
Cdd:COG4913 241 HEALEDAREQIELLEPirelAERYAAARERLAELEYLRAALrlwFAQRRLELLEAELEELRAELA---RLEAELERLEAR 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 954 LaskvkenKEMTERIKELQVQVEESAklQETLENMKKEhlidIDNQKSKdmelQKTIENNLQSTEQTLKDAQLELEDMVK 1033
Cdd:COG4913 318 L-------DALREELDELEAQIRGNG--GDRLEQLERE----IERLERE----LEERERRRARLEALLAALGLPLPASAE 380
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 768464868 1034 QHDELKEESKKQLEELEQTKKTLVEYQTLNG----DLQNEVKSLKEEIARLQ 1081
Cdd:COG4913 381 EFAALRAEAAALLEALEEELEALEEALAEAEaalrDLRRELRELEAEIASLE 432
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
864-1083 |
3.43e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.99 E-value: 3.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 864 KKIRKELKQRQLKQEHEYNAAVTIQSKVRtfEPRSRFLRTKKDTVVVQSLIRRraaqrkLKQLKADAKSVNHLKEVSYKL 943
Cdd:PRK03918 234 EELKEEIEELEKELESLEGSKRKLEEKIR--ELEERIEELKKEIEELEEKVKE------LKELKEKAEEYIKLSEFYEEY 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 944 ENKVIELTQNLASKVKENKEMTERIKELQVQVEESAKLQETLENMKKEhlIDIDNQKSKDMELQKTIENNLQSTEQTLKD 1023
Cdd:PRK03918 306 LDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKR--LEELEERHELYEEAKAKKEELERLKKRLTG 383
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768464868 1024 aqLELEDMVKQHDEL---KEESKKQLEELEQTKktlveyqtlnGDLQNEVKSLKEEIARLQTA 1083
Cdd:PRK03918 384 --LTPEKLEKELEELekaKEEIEEEISKITARI----------GELKKEIKELKKAIEELKKA 434
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
915-1058 |
5.38e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 49.54 E-value: 5.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 915 RRRAAQRKLKQLKADAKSVNhlKEVSyKLENKVIELTQNLA------SKVKENKEMteriKELQVQVEESAKLQETLEnm 988
Cdd:COG1579 39 ELAALEARLEAAKTELEDLE--KEIK-RLELEIEEVEARIKkyeeqlGNVRNNKEY----EALQKEIESLKRRISDLE-- 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 989 kkEHLIDIdnqkskdMELQKTIENNLQSTEQTLKDAQLELEDMVKQHDELKEESKKQLEELEQTKKTLVE 1058
Cdd:COG1579 110 --DEILEL-------MERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAA 170
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
925-1077 |
7.72e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 50.88 E-value: 7.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 925 QLKADAKSVNH----LKEVSYKLEN---KVIELTQNLASKVKENKEMTERIKELQVQVeesaklqetlenmkKEHLIDID 997
Cdd:pfam05483 458 QLTAIKTSEEHylkeVEDLKTELEKeklKNIELTAHCDKLLLENKELTQEASDMTLEL--------------KKHQEDII 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 998 NQKSKDMELQKTIENnLQSTEQTLKDaQLEL--EDMVKQHDELKEESKKQLEELEQTKKTLVEYQTLNGDLQNEVKSLKE 1075
Cdd:pfam05483 524 NCKKQEERMLKQIEN-LEEKEMNLRD-ELESvrEEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKK 601
|
..
gi 768464868 1076 EI 1077
Cdd:pfam05483 602 QI 603
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
864-1084 |
8.94e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 8.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 864 KKIRKELKQRQlKQEHEYNAAVTIQSKVRTfeprsrflrtkkdtvvvqsliRRRAAQRKLKQLKADAKSVNHLKEVsYKL 943
Cdd:COG4717 74 KELEEELKEAE-EKEEEYAELQEELEELEE---------------------ELEELEAELEELREELEKLEKLLQL-LPL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 944 ENKVIELTQNLAskvkenkEMTERIKELQVQVEESAKLQETLENMKKEHlididnqkskdMELQKTIEnnlQSTEQTLKD 1023
Cdd:COG4717 131 YQELEALEAELA-------ELPERLEELEERLEELRELEEELEELEAEL-----------AELQEELE---ELLEQLSLA 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768464868 1024 AQLELEDMVKQHDELKEESKKQLEELEQtkktlveyqtlngdLQNEVKSLKEEIARLQTAM 1084
Cdd:COG4717 190 TEEELQDLAEELEELQQRLAELEEELEE--------------AQEELEELEEELEQLENEL 236
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
862-1074 |
9.15e-06 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 50.51 E-value: 9.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 862 LQKKIRKELKQRQLKQEHEYNAAVTIQSKVRTFEPRSRFLRTKKDTVV----VQSLI------RRRAAQRKLKQLKADAK 931
Cdd:pfam05557 53 LQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEKESQLAdareVISCLknelseLRRQIQRAELELQSTNS 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 932 SVNHLKEVSYKLENKVIELTQ---NLASKVKENKEMTERIKELQVQVEESAKLQETLENMKKEHL------IDIDNQKSK 1002
Cdd:pfam05557 133 ELEELQERLDLLKAKASEAEQlrqNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSKSELAripeleKELERLREH 212
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768464868 1003 DMELQKTIENNLQSTEQtlkdaqleledmvkqhdelKEESKKQLEELEQTKKTLVEYQTLNGDLQNEVKSLK 1074
Cdd:pfam05557 213 NKHLNENIENKLLLKEE-------------------VEDLKRKLEREEKYREEAATLELEKEKLEQELQSWV 265
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
855-1086 |
9.17e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.45 E-value: 9.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 855 VLRTITNLQK---------KIRKELKQRQLKQEHEYNAAVTIQSKVRTFEprSRFLRTKKDTVVVQSLIRRRAaqRKLKQ 925
Cdd:PRK03918 150 VVRQILGLDDyenayknlgEVIKEIKRRIERLEKFIKRTENIEELIKEKE--KELEEVLREINEISSELPELR--EELEK 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 926 LKADAKSVNHLKEvsyklenKVIELTQNLASKVKENKEMTERIKELQVQVEESAKLQETLENMKKEhLIDIDNQKSKDME 1005
Cdd:PRK03918 226 LEKEVKELEELKE-------EIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKE-LKELKEKAEEYIK 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 1006 LQKTIENnlqsteqtLKDAQLELEDMVKQHDELKEESKKQLEELEQTKKTLVEYQTLNGDLQNEVKSLKEEIARLQTAMS 1085
Cdd:PRK03918 298 LSEFYEE--------YLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKA 369
|
.
gi 768464868 1086 L 1086
Cdd:PRK03918 370 K 370
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
913-1080 |
1.22e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 49.78 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 913 LIRRRAAQRKLKQLKADAKSV--NHLKEVSYKLENKVIELTQ-NLASKVKENKEMTERIKELQvqveesaKLQETLENmK 989
Cdd:PRK12704 23 FVRKKIAEAKIKEAEEEAKRIleEAKKEAEAIKKEALLEAKEeIHKLRNEFEKELRERRNELQ-------KLEKRLLQ-K 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 990 KEHLididNQKSKDMELQktiENNLQSTEQTLKDAQLELEDMVKQHDELKEESKKQLEEL-----EQTKKTLVEyqtlng 1064
Cdd:PRK12704 95 EENL----DRKLELLEKR---EEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERIsgltaEEAKEILLE------ 161
|
170
....*....|....*..
gi 768464868 1065 dlqnEVKS-LKEEIARL 1080
Cdd:PRK12704 162 ----KVEEeARHEAAVL 174
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
954-1083 |
1.46e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.91 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 954 LASKVKENKEMTERIKELQVQVEESAKLQETLENmKKEHLIDIDNQKSKdmelqktiENNLQSTEQTLKDAQLELEDMVK 1033
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQE-RREALQRLAEYSWD--------EIDVASAEREIAELEAELERLDA 682
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 768464868 1034 QHDELkEESKKQLEELEQTKKTLVE----YQTLNGDLQNEVKSLKEEIARLQTA 1083
Cdd:COG4913 683 SSDDL-AALEEQLEELEAELEELEEeldeLKGEIGRLEKELEQAEEELDELQDR 735
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
860-1083 |
2.39e-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: 49.40 E-value: 2.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 860 TNLQKKIRKELKQR--QLKQeheynaavTIQSKVRTFEPRSRFLRTKKDTVV------VQSLIRRRAAQRKLKQ------ 925
Cdd:pfam01576 315 TAAQQELRSKREQEvtELKK--------ALEEETRSHEAQLQEMRQKHTQALeelteqLEQAKRNKANLEKAKQalesen 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 926 --LKADAKSVNHLKEVS----YKLENKVIELTQNLASKVKENKEMTERIKELQVQVEESAKLQETLEnmkkehlididnq 999
Cdd:pfam01576 387 aeLQAELRTLQQAKQDSehkrKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAE------------- 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 1000 kSKDMELQK---TIENNLQSTEQTLKD---AQLELEDMVKQHDELKEESKKQLEELEQTKKTLV-EYQTLNGDLQNEVKS 1072
Cdd:pfam01576 454 -GKNIKLSKdvsSLESQLQDTQELLQEetrQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVErQLSTLQAQLSDMKKK 532
|
250
....*....|.
gi 768464868 1073 LKEEIARLQTA 1083
Cdd:pfam01576 533 LEEDAGTLEAL 543
|
|
| PLC-beta_C |
pfam08703 |
PLC-beta C terminal; This domain corresponds to the alpha helical C terminal domain of ... |
910-1087 |
2.58e-05 |
|
PLC-beta C terminal; This domain corresponds to the alpha helical C terminal domain of phospholipase C beta.
Pssm-ID: 462571 [Multi-domain] Cd Length: 176 Bit Score: 46.60 E-value: 2.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 910 VQSLIRRRAAQ----RKLKQlkadaksvNHLKEVSYKLENKVIElTQnlASKVKENKEMTER-IKELQVQVEesAKLQET 984
Cdd:pfam08703 11 EQELLELREEQyeqeKKRKE--------QHLTEQIQKLKELARE-KQ--AAELKALKESSESeKKEMKKKLE--RKRLES 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 985 LENMKKehlidIDNQKSKDMELQKTIEN-NLQSTEQTLKdaqlELEDMVKQHDELKEEskKQLEELEQTKKTLVEYQT-L 1062
Cdd:pfam08703 78 IQEAKK-----RTSDKAAQERLKKEINNsHIQEVVQSIK----QLEEKQKRRQEKLEE--KQAECLQQIKEEEPQLQAeL 146
|
170 180
....*....|....*....|....*.
gi 768464868 1063 NGDLQNEVKSLKEEIAR-LQTAMSLG 1087
Cdd:pfam08703 147 NAEYEEKLKGLPAEVREsVKSCLKEG 172
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
961-1081 |
3.04e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.36 E-value: 3.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 961 NKEMTERIKELQVQVEESAKLQETLENMKKE------HLIDIDNQKSKDMELQKTIENNLQSTEQTLKDAQLELEDMVKQ 1034
Cdd:COG4372 44 QEELEQLREELEQAREELEQLEEELEQARSEleqleeELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKE 123
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 768464868 1035 HDELKEESKKQLEELEQTKKTLVEYQTLNGDLQNEVKSLKEEIARLQ 1081
Cdd:COG4372 124 RQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALE 170
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
859-1082 |
4.49e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 48.09 E-value: 4.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 859 ITNLQKKIRKELKQRQLKQEHeynaAVTIQSKVRTFEPRSRFLR-------------TKKDTV---VVQSLIRRRAAQRk 922
Cdd:TIGR04523 393 INDLESKIQNQEKLNQQKDEQ----IKKLQQEKELLEKEIERLKetiiknnseikdlTNQDSVkelIIKNLDNTRESLE- 467
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 923 lKQLKADAKSVNHLKEvsyKLENKVIEL---TQNLASKVKENKEMTERIKELQVQVEESAKLQETLENMKKEHLIDIDNQ 999
Cdd:TIGR04523 468 -TQLKVLSRSINKIKQ---NLEQKQKELkskEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDL 543
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 1000 KSK----DMELQKT-IENNLQSTEQTLKDAQLELEDMVKQHDELKEESKKQLEELEQTKKTLVEYQTLNGDLQNEVKSLK 1074
Cdd:TIGR04523 544 EDElnkdDFELKKEnLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAK 623
|
....*...
gi 768464868 1075 EEIARLQT 1082
Cdd:TIGR04523 624 KENEKLSS 631
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
863-1080 |
4.68e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.14 E-value: 4.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 863 QKKIRKELKQRQLKQeHEYNAAVT------IQSKVRTFEPRSRFLRTkkdtVVVQSLIRRRAAQRKLKQLKADAKSvnhL 936
Cdd:TIGR02169 760 LKELEARIEELEEDL-HKLEEALNdlearlSHSRIPEIQAELSKLEE----EVSRIEARLREIEQKLNRLTLEKEY---L 831
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 937 KEVSYKLENKVIELTQNLASKVKENKEMTERIKELQVQVEESAKLQETLENMKKEHLIDIDNQKSKDMELQKTIennlqs 1016
Cdd:TIGR02169 832 EKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKI------ 905
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768464868 1017 teQTLKDAQLELEDMVKQHDELKEESKKQLEELEQTKKTLVEYQTLN---GDLQNEVKSLKEEIARL 1080
Cdd:TIGR02169 906 --EELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEElslEDVQAELQRVEEEIRAL 970
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
963-1077 |
5.64e-05 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 47.06 E-value: 5.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 963 EMTERIKELQVQVEESAKLQETLENMKKEhLIDIDNQKSKDMELQKTIENNLQSTEQTLKDAQLELEDMVKQhdeLKEES 1042
Cdd:pfam09787 48 ELEELRQERDLLREEIQKLRGQIQQLRTE-LQELEAQQQEEAESSREQLQELEEQLATERSARREAEAELER---LQEEL 123
|
90 100 110
....*....|....*....|....*....|....*
gi 768464868 1043 KKQLEELEQTKKTLVEYQTlngDLQNEVKSLKEEI 1077
Cdd:pfam09787 124 RYLEEELRRSKATLQSRIK---DREAEIEKLRNQL 155
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
839-1077 |
5.77e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 47.79 E-value: 5.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 839 LQAAYRGHSIRANVFSVlrTITNLQKKIRKElKQRQLKQEHEYNA-AVTIQSKVRTFEPRSRFLRTKKdtVVVQSLIRRR 917
Cdd:pfam05483 340 LNKAKAAHSFVVTEFEA--TTCSLEELLRTE-QQRLEKNEDQLKIiTMELQKKSSELEEMTKFKNNKE--VELEELKKIL 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 918 AAQRKLKQLKadaKSVNHLKEvsyKLENKVIELTQNLASKVKEnkemterIKELQVQVEESAKLQETLENMKKEHLIDID 997
Cdd:pfam05483 415 AEDEKLLDEK---KQFEKIAE---ELKGKEQELIFLLQAREKE-------IHDLEIQLTAIKTSEEHYLKEVEDLKTELE 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 998 NQKSKDMELqkTIENNLQSTEQtlKDAQLELEDMV---KQHDELKEESKKQLEELEQTKKTLVEYQTlngDLQNEVKSLK 1074
Cdd:pfam05483 482 KEKLKNIEL--TAHCDKLLLEN--KELTQEASDMTlelKKHQEDIINCKKQEERMLKQIENLEEKEM---NLRDELESVR 554
|
...
gi 768464868 1075 EEI 1077
Cdd:pfam05483 555 EEF 557
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
911-1085 |
7.27e-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: 47.74 E-value: 7.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 911 QSLIRRRAAQRKLKQLKADA-KSVNHLKEVSYKLENKVIELTQNLASKVKENKEMTERIKELQVQVEES----------- 978
Cdd:TIGR02168 705 KELEELEEELEQLRKELEELsRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAeeelaeaeaei 784
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 979 AKLQETLENMKKEHLIDIDNQKSKDMELQKT-------------IENNLQSTEQTLKDAQ--------------LELEDM 1031
Cdd:TIGR02168 785 EELEAQIEQLKEELKALREALDELRAELTLLneeaanlrerlesLERRIAATERRLEDLEeqieelsedieslaAEIEEL 864
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 768464868 1032 VKQHDELKEESKKQLEELEQTKKTLVEYQTLNGDLQNEVKSLKEEIARLQTAMS 1085
Cdd:TIGR02168 865 EELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELE 918
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
911-1081 |
8.84e-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: 47.48 E-value: 8.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 911 QSLIRRRAAQRKLKQLK--ADAKsvnhLKevsyKLENKVIELTQNLASKVKENKEMTERIKELQVQV---EESAKLQETL 985
Cdd:pfam01576 110 EQLDEEEAARQKLQLEKvtTEAK----IK----KLEEDILLLEDQNSKLSKERKLLEERISEFTSNLaeeEEKAKSLSKL 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 986 ENMKKEHLIDIDNQKSKDMELQKTIENNLQSTEQTLKDAQLELEDMVKQHDELKEESKKQLEELEQTKKTLVEYQTLNGD 1065
Cdd:pfam01576 182 KNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNN 261
|
170
....*....|....*.
gi 768464868 1066 LQNEVKSLKEEIARLQ 1081
Cdd:pfam01576 262 ALKKIRELEAQISELQ 277
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
867-1075 |
1.10e-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: 46.97 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 867 RKELKQRQLKQEHEYNAAVTIQSKVRT--FEPRSRFLRTkkdTVVVQSLIRRRAAQRK--------LKQLKADAKSVNH- 935
Cdd:TIGR02168 784 IEELEAQIEQLKEELKALREALDELRAelTLLNEEAANL---RERLESLERRIAATERrledleeqIEELSEDIESLAAe 860
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 936 LKEVSYKLENKVIELTQNLASKVKENKEMTERIKELQVQVEESAKLQEtlENMKKEHLIDIDNQKSKDMELQKT-IENNL 1014
Cdd:TIGR02168 861 IEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES--KRSELRRELEELREKLAQLELRLEgLEVRI 938
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768464868 1015 QSTEQTL-KDAQLELEDMVKQHDELKEESKKQLEELEQTKKTLVEYQTLNGDLQNEVKSLKE 1075
Cdd:TIGR02168 939 DNLQERLsEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKE 1000
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
864-1086 |
1.84e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.29 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 864 KKIRKELKQRQLKQEHEYNAAVTIQSK---VRTFEPRSRflRTKKDTVVVQSLIRRRAAQRKLKQLKADAKSVNHLKEVS 940
Cdd:PTZ00121 1360 EAAEEKAEAAEKKKEEAKKKADAAKKKaeeKKKADEAKK--KAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAK 1437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 941 YKLEN--KVIELTQNL-----ASKVKENKEMTERIKELQVQVEESAKLQET---LENMKK--EHLIDIDNQKSKDMELQK 1008
Cdd:PTZ00121 1438 KKAEEakKADEAKKKAeeakkAEEAKKKAEEAKKADEAKKKAEEAKKADEAkkkAEEAKKkaDEAKKAAEAKKKADEAKK 1517
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 1009 TIE----NNLQSTEQTLKDAQLELEDMVKQHDELKE-ESKKQLEELEQTKKTLVEYQTLNGDLQNEVKSLKEEIARLQTA 1083
Cdd:PTZ00121 1518 AEEakkaDEAKKAEEAKKADEAKKAEEKKKADELKKaEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEV 1597
|
...
gi 768464868 1084 MSL 1086
Cdd:PTZ00121 1598 MKL 1600
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
942-1081 |
2.05e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.53 E-value: 2.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 942 KLENKVIELTQNLASKVKENKEMTERIKELQVQVEEsakLQETLENMKKE------HLIDIDNQKSKDMELQKTIENN-- 1013
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEA---AKTELEDLEKEikrlelEIEEVEARIKKYEEQLGNVRNNke 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768464868 1014 ---LQSTEQTLKDAQLELEDMVKQHDELKEESKKQLEELEQTKKTLVEyqTLNgDLQNEVKS----LKEEIARLQ 1081
Cdd:COG1579 91 yeaLQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEA--ELE-EKKAELDEelaeLEAELEELE 162
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
950-1082 |
2.60e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.14 E-value: 2.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 950 LTQNLASKVKENKEMTERIKELQVQVEESAKLQETLENMKKEHLIDIDNQKSKDMELQKTI---ENNLQSTEQTLKDAQL 1026
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIralEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768464868 1027 ELEDMVKQHDELKEESKKQL------------------EELEQTKKTLVEYQTLNGDLQNEVKSLKEEIARLQT 1082
Cdd:COG4942 91 EIAELRAELEAQKEELAELLralyrlgrqpplalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAA 164
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
919-1047 |
3.17e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 45.21 E-value: 3.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 919 AQRKLKQLKADAKSVNHlkevSYKLENKVIELTQNLAskvKENKEMTERIKELQVQVEESAK----LQETLENMKKeHLI 994
Cdd:PRK04778 322 AKEQNKELKEEIDRVKQ----SYTLNESELESVRQLE---KQLESLEKQYDEITERIAEQEIayseLQEELEEILK-QLE 393
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 768464868 995 DIDNQkskdmelQKTIENNLQSteqtLKDAQLELEDMVKQHDELKEESKKQLE 1047
Cdd:PRK04778 394 EIEKE-------QEKLSEMLQG----LRKDELEAREKLERYRNKLHEIKRYLE 435
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
862-1160 |
3.87e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.52 E-value: 3.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 862 LQKKIRKELKQRQLKQEHEYNAAVTiQSKVRTFEPRSRFLRTKKDtvvvQSLIRRRAAQRKLKQlKADAKSVNHLKevsy 941
Cdd:PTZ00121 1612 AKKAEEAKIKAEELKKAEEEKKKVE-QLKKKEAEEKKKAEELKKA----EEENKIKAAEEAKKA-EEDKKKAEEAK---- 1681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 942 klenKVIELTQNLASKVKENKEMTERIKELQVQVEESAKLQETLENMKKEHLIDIDNQKSKDMELQKTIENNLQSTEQTL 1021
Cdd:PTZ00121 1682 ----KAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKK 1757
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 1022 KDAQLELEDMVKQHDELKEESKKQLEELEQtkktlvEYQTLNGDLQNEVKSLKEEIARLQTAMSLGTVTTSVLPQT---P 1098
Cdd:PTZ00121 1758 KIAHLKKEEEKKAEEIRKEKEAVIEEELDE------EDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMedsA 1831
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768464868 1099 LKDVmgggaSNFNNMMLENSD------LSPNDLNLKSRSTPLSGNNHIDSLSVDRENgVNATQINEEL 1160
Cdd:PTZ00121 1832 IKEV-----ADSKNMQLEEADafekhkFNKNNENGEDGNKEADFNKEKDLKEDDEEE-IEEADEIEKI 1893
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
797-1100 |
3.94e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.01 E-value: 3.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 797 AKYYRKQYLQISQAIKYLQNNIK------GFIIRQRVNDEMKVNCATLLQA---AYRGHSIRANVFSVLRTITNLQKKIr 867
Cdd:COG3206 106 DEDPLGEEASREAAIERLRKNLTvepvkgSNVIEISYTSPDPELAAAVANAlaeAYLEQNLELRREEARKALEFLEEQL- 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 868 KELKQrQLKQeheynaavtIQSKVRTFEPRSRFLRTKKDT-VVVQSLIRRRAAQRKLKQLKADAKSvnhlkevSYKLENK 946
Cdd:COG3206 185 PELRK-ELEE---------AEAALEEFRQKNGLVDLSEEAkLLLQQLSELESQLAEARAELAEAEA-------RLAALRA 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 947 VIELTQNLASKVKENKEMTERIKELQvqvEESAKLQETLENMKKEH--LIDIDNQKSkdmELQKTIEnnlQSTEQTLKDA 1024
Cdd:COG3206 248 QLGSGPDALPELLQSPVIQQLRAQLA---ELEAELAELSARYTPNHpdVIALRAQIA---ALRAQLQ---QEAQRILASL 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 1025 QLELEDMVKQHDELKEESKKQLEELEQTKKTLVEYQTLNGDLQNEVKSLKEEIARLQTA---MSLGTVTTSVL--PQTPL 1099
Cdd:COG3206 319 EAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEArlaEALTVGNVRVIdpAVVPL 398
|
.
gi 768464868 1100 K 1100
Cdd:COG3206 399 K 399
|
|
| mS26_Tt |
cd23695 |
Tetrahymena thermophila ribosomal protein mS26 and similar proteins; Ribosomal protein mS26 is ... |
862-1082 |
4.39e-04 |
|
Tetrahymena thermophila ribosomal protein mS26 and similar proteins; Ribosomal protein mS26 is a component of small subunit (SSU) in Tetrahymena thermophila mitochondrial ribosome (mitoribosome). The structure of the mitoribosome reveals an assembly of 94-ribosomal proteins and four-rRNAs with an additional protein mass of ~700 kDa on the small subunit; the large mitoribosomal subunit (LSU) lacks 5S rRNA.
Pssm-ID: 467909 [Multi-domain] Cd Length: 496 Bit Score: 44.81 E-value: 4.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 862 LQKKIRKELKQRQLKQEHE----YNAAVTIQSKVRTFEPRSRFLRTKKDTVVVQSLIRRRAAQRKLKQLKADAKsvNHLK 937
Cdd:cd23695 17 YRKKHKKDYWESQTIVENEfidkYNKEELKKQRKDLDKWRTSIITISKATQNHIKLLEKKSVKKEENERKYLLE--QDVK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 938 EVSYKLENKVIELT-------QNLASKVKENKEMTERI---KELQVQVEESAKLQET--LENMKKEHLIDIDNQKsKDME 1005
Cdd:cd23695 95 AMNKKIILDVMNEEsknwinlQNMNEKINPNLILPDTIldeTSYYLKLQELAFLFEQgdHEEMDKLLDENEEIEY-KNSL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 1006 LQ------KTIENNLQSTE--QTLKDAQLELEDMVKQHDELKEESKKQLEELEQtkktlvEYQTLngdLQNEVKSLKEEI 1077
Cdd:cd23695 174 LMpiyqdlKSLIKHLKYTElfKLLKEYQDAKAIIIEDFRESSEEGAEKLEKLEK------AFATL---LKNYKEELEEPE 244
|
....*
gi 768464868 1078 ARLQT 1082
Cdd:cd23695 245 KQLEF 249
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
927-1079 |
4.65e-04 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 45.05 E-value: 4.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 927 KADAKSVNHLKEVSYkLENKVIELtQNLASKVKENKEMTERIKELQVqVEESAKLQETLENMKKEHLIDIDNQKSK-DME 1005
Cdd:pfam05911 627 EDEIKKHDCIDKVTL-SENKVAQV-DNGCSEIDNLSSDPEIPSDGPL-VSGSNDLKTEENKRLKEEFEQLKSEKENlEVE 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 1006 LQKTIENN------LQSTEQTLKDAQLEL----------EDMVKQHDELKEESKKQLEELE-QTKKTLVEYQTLNGDLQN 1068
Cdd:pfam05911 704 LASCTENLestksqLQESEQLIAELRSELaslkesnslaETQLKCMAESYEDLETRLTELEaELNELRQKFEALEVELEE 783
|
170
....*....|.
gi 768464868 1069 EVKSLKEEIAR 1079
Cdd:pfam05911 784 EKNCHEELEAK 794
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
862-1096 |
4.87e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 44.50 E-value: 4.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 862 LQKKIRKELKQR-QLKQEHEYNAAVTIQSKVRTFEPRSRFLRtkkdtvvvqsliRRRAAQRKLKQLKADAKsvnHLKEVS 940
Cdd:pfam07888 32 LQNRLEECLQERaELLQAQEAANRQREKEKERYKRDREQWER------------QRRELESRVAELKEELR---QSREKH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 941 YKLENKVIE-------LTQNLASKVKENKEMTERIKELQVQVE---ESAKLQET-LENMkKEHLIDIDNQKSKDMELQKT 1009
Cdd:pfam07888 97 EELEEKYKElsasseeLSEEKDALLAQRAAHEARIRELEEDIKtltQRVLERETeLERM-KERAKKAGAQRKEEEAERKQ 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 1010 IENNLQSTEQTLKDAQLELEDMVKQHDElKEESKKQLEE----LEQTKKTLVEYQTLNGDLQNEVKSLKEEI-ARLQTAM 1084
Cdd:pfam07888 176 LQAKLQQTEEELRSLSKEFQELRNSLAQ-RDTQVLQLQDtittLTQKLTTAHRKEAENEALLEELRSLQERLnASERKVE 254
|
250
....*....|..
gi 768464868 1085 SLGTVTTSVLPQ 1096
Cdd:pfam07888 255 GLGEELSSMAAQ 266
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
916-1082 |
5.05e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 44.63 E-value: 5.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 916 RRAAQRKLKQLKADAKSVNHLKEVSYKLENKVIELTQNLASKVKENKEMTERIKELQVQVEESAKLQETLENMKKEHLID 995
Cdd:TIGR04523 196 LLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 996 IDNQKSKDMELQKTIeNNLQSteqtlkdaqlELEDMVKQ-----HDELKEESKKQLEELEQTKKTLVEYQTLNGDLQNEV 1070
Cdd:TIGR04523 276 LEQNNKKIKELEKQL-NQLKS----------EISDLNNQkeqdwNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQI 344
|
170
....*....|..
gi 768464868 1071 KSLKEEIARLQT 1082
Cdd:TIGR04523 345 SQLKKELTNSES 356
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
647-671 |
5.95e-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: 42.33 E-value: 5.95e-04
10 20
....*....|....*....|....*
gi 768464868 647 FKQSLIELMNTINSTNVHYIRCIKP 671
Cdd:cd01363 146 INESLNTLMNVLRATRPHFVRCISP 170
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
791-1011 |
7.35e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.60 E-value: 7.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 791 IQKKIRAKyyRKQYLQISQAIKYLQNNIKGfiIRQRVNdemkvncatllQAAYRGHSIRANVFSVLRTITNLQKKIrKEL 870
Cdd:COG4942 32 LQQEIAEL--EKELAALKKEEKALLKQLAA--LERRIA-----------ALARRIRALEQELAALEAELAELEKEI-AEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 871 KQRQLKQEHEYNAAVTIQSKVRTfEPRSRFLRTKKDtvvVQSLIRRRAAQRKLkqLKADAKSVNHLKEVSYKLENKVIEL 950
Cdd:COG4942 96 RAELEAQKEELAELLRALYRLGR-QPPLALLLSPED---FLDAVRRLQYLKYL--APARREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768464868 951 TQNLASKVKENKEMTERIKELQVQVEESAKLQETLENMKKEHLIDIDNQKSKDMELQKTIE 1011
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIA 230
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
930-1100 |
7.53e-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: 44.19 E-value: 7.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 930 AKSVNHLKEVSYKLENKVIELTQNL------ASKVKENKEMTERIKELQVQVEESAKLQETLENMKK--------EHLID 995
Cdd:TIGR00618 225 EKELKHLREALQQTQQSHAYLTQKReaqeeqLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKaaplaahiKAVTQ 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 996 IDNQ--------KSKDMELQKTIEN--NLQSTEQTLKDAQLELEDMVKQHDEL----------KEESKKQLeELEQTKKT 1055
Cdd:TIGR00618 305 IEQQaqrihtelQSKMRSRAKLLMKraAHVKQQSSIEEQRRLLQTLHSQEIHIrdahevatsiREISCQQH-TLTQHIHT 383
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 768464868 1056 LVEYQTLNGDLQNEVKSLKEEIARLQtamslGTVTTSVLPQTPLK 1100
Cdd:TIGR00618 384 LQQQKTTLTQKLQSLCKELDILQREQ-----ATIDTRTSAFRDLQ 423
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
880-1077 |
1.01e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 43.89 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 880 EYNAAVT-IQSKVRTFEPRSRFLRTKKDTVVVQSLIRRRAAQRKLKQLKADAKsVNHLKEVSYKLENKVieltqnlASKV 958
Cdd:TIGR01612 1518 QYKKDVTeLLNKYSALAIKNKFAKTKKDSEIIIKEIKDAHKKFILEAEKSEQK-IKEIKKEKFRIEDDA-------AKND 1589
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 959 KENKEMTE-------------RIKELQVQVEESAKLQETLEnmKKEHLIDIDNQKSKdMELQKTIENNLQSTEQTLKDAQ 1025
Cdd:TIGR01612 1590 KSNKAAIDiqlslenfenkflKISDIKKKINDCLKETESIE--KKISSFSIDSQDTE-LKENGDNLNSLQEFLESLKDQK 1666
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 1026 LELEDMVKQHDELKEESKKQLEELEQTKKT--------LVEYQTLNgdlQNEVKSLKEEI 1077
Cdd:TIGR01612 1667 KNIEDKKKELDELDSEIEKIEIDVDQHKKNyeigiiekIKEIAIAN---KEEIESIKELI 1723
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
922-1079 |
1.05e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 43.69 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 922 KLKQLKA--DAKSVNHLKEvsyklenKVIELTQNLASKVKE---NKEMTERIKELQVQVEESA---------KLQETLEN 987
Cdd:PLN03229 536 KLDMLNEfsRAKALSEKKS-------KAEKLKAEINKKFKEvmdRPEIKEKMEALKAEVASSGassgdelddDLKEKVEK 608
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 988 MKKEHLIDIDN-QKSKDMELQKTIENNLQSTEQTLKdaqlelEDMVKQHDELKEESKKQLEELEQTKktlveyqtlngDL 1066
Cdd:PLN03229 609 MKKEIELELAGvLKSMGLEVIGVTKKNKDTAEQTPP------PNLQEKIESLNEEINKKIERVIRSS-----------DL 671
|
170
....*....|...
gi 768464868 1067 QNEVKSLKEEIAR 1079
Cdd:PLN03229 672 KSKIELLKLEVAK 684
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
859-1059 |
1.21e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.46 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 859 ITNLQKKIRKELKQRQLKQEHEYNAAVTIQSKVRtfeprsrfLRTKKDTVVVQSLIRRRAAQRKLKQLKADAKSvnhlke 938
Cdd:PHA02562 204 IEEQRKKNGENIARKQNKYDELVEEAKTIKAEIE--------ELTDELLNLVMDIEDPSAALNKLNTAAAKIKS------ 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 939 vsyKLE--NKVIEL----------TQNLASKVKENKEMTERIKELQVQVEesaKLQETLENMKkEHLIDIDNQKSKDMEL 1006
Cdd:PHA02562 270 ---KIEqfQKVIKMyekggvcptcTQQISEGPDRITKIKDKLKELQHSLE---KLDTAIDELE-EIMDEFNEQSKKLLEL 342
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 768464868 1007 QKTIENN---LQSTEQTLKDAQLELEDMVKQHDELKEESKKQLEELEQTKKTLVEY 1059
Cdd:PHA02562 343 KNKISTNkqsLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSEL 398
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
867-1080 |
1.49e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.39 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 867 RKELKQRQLKQEHEYNAAVTIQSKVRTFEPRSRFLRtkkDTVVVQSLIRRRA--AQRKLKQLKADAKSVNHLKEVSYKLE 944
Cdd:COG1196 584 ARAALAAALARGAIGAAVDLVASDLREADARYYVLG---DTLLGRTLVAARLeaALRRAVTLAGRLREVTLEGEGGSAGG 660
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 945 NKVIELTQNLASKVKENKEMTERIKELQVQVEESAKLQETLENMKKEHLIDIDNQKSKDMELQKTIENNLQSTEQTLKDA 1024
Cdd:COG1196 661 SLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEE 740
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 768464868 1025 QLELEDMVKQHDELKEESKKQLEELEQtkktlveyqtlngdlqnEVKSLKEEIARL 1080
Cdd:COG1196 741 LLEEEELLEEEALEELPEPPDLEELER-----------------ELERLEREIEAL 779
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
921-1084 |
1.58e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.21 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 921 RKLKQLKADAKSvnhLKEVSYKLENKVIELTQNLASKVKENKEMTERIKELQVQ----VEESAKLQETLENMKKEHLIDI 996
Cdd:COG1340 29 EKRDELNEELKE---LAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEErdelNEKLNELREELDELRKELAELN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 997 DNQKSKDmELQKTIEN--NLQSTEQTLKDAQLELEDMVKQHDELKEESKKQLEELEQTKKTLVEYQTLNG---DLQNEVK 1071
Cdd:COG1340 106 KAGGSID-KLRKEIERleWRQQTEVLSPEEEKELVEKIKELEKELEKAKKALEKNEKLKELRAELKELRKeaeEIHKKIK 184
|
170
....*....|...
gi 768464868 1072 SLKEEIARLQTAM 1084
Cdd:COG1340 185 ELAEEAQELHEEM 197
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
858-1073 |
1.76e-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: 43.24 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 858 TITNLQKKIRKELKQRQ----LKQEHEyNAAVTIQSKVRTFEPRSRFLR---TKKDTVVVQSLIR-------RRAAQRKL 923
Cdd:pfam01576 188 MISDLEERLKKEEKGRQelekAKRKLE-GESTDLQEQIAELQAQIAELRaqlAKKEEELQAALARleeetaqKNNALKKI 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 924 KQLKAdaksvnHLKEVSYKLENKviELTQNLASKVKenKEMTERIKELQVQVEE---SAKLQETLENMKKEHLididnqk 1000
Cdd:pfam01576 267 RELEA------QISELQEDLESE--RAARNKAEKQR--RDLGEELEALKTELEDtldTTAAQQELRSKREQEV------- 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 1001 skdMELQKTIENnlqstEQTLKDAQleLEDMVKQHDELKEESKKQLEE-------LEQTKKTLveyQTLNGDLQNEVKSL 1073
Cdd:pfam01576 330 ---TELKKALEE-----ETRSHEAQ--LQEMRQKHTQALEELTEQLEQakrnkanLEKAKQAL---ESENAELQAELRTL 396
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
857-1078 |
2.28e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 857 RTITNLQKKIRKELKQRQLKQE-HEYNAAVTIQSKVRTFEPRSRFLRTKKDTVVVQSLIRRRAAQRKLKQLKA--DAKSV 933
Cdd:PTZ00121 1457 KKAEEAKKKAEEAKKADEAKKKaEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKaeEAKKA 1536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 934 NHLKEVSYKLENKVIELTQNL-----------ASKVKENKEMTERIKELQVQVEES-----AKLQETLENMKKEHLIDID 997
Cdd:PTZ00121 1537 DEAKKAEEKKKADELKKAEELkkaeekkkaeeAKKAEEDKNMALRKAEEAKKAEEArieevMKLYEEEKKMKAEEAKKAE 1616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 998 NQKSKDMELQK------TIENNLQSTEQTLKDAQ----LELEDMVKQHDELK--EESKKQLEEL---EQTKKTLVEYQTL 1062
Cdd:PTZ00121 1617 EAKIKAEELKKaeeekkKVEQLKKKEAEEKKKAEelkkAEEENKIKAAEEAKkaEEDKKKAEEAkkaEEDEKKAAEALKK 1696
|
250
....*....|....*.
gi 768464868 1063 NGDLQNEVKSLKEEIA 1078
Cdd:PTZ00121 1697 EAEEAKKAEELKKKEA 1712
|
|
| DivIVA |
COG3599 |
Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle ... |
949-1042 |
2.44e-03 |
|
Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442818 [Multi-domain] Cd Length: 125 Bit Score: 39.45 E-value: 2.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 949 ELTQNLASKVKENKEMTERIKELQVQVEESAKLQETLENMkkehLI----DIDNQKSK-DMELQKTIENNLQSTEQTLKD 1023
Cdd:COG3599 31 EVAEDYERLIRENKELKEKLEELEEELEEYRELEETLQKT----LVvaqeTAEEVKENaEKEAELIIKEAELEAEKIIEE 106
|
90
....*....|....*....
gi 768464868 1024 AQLELEDMVKQHDELKEES 1042
Cdd:COG3599 107 AQEKARKIVREIEELKRQR 125
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
942-1084 |
2.55e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 942 KLENKVIELT----QNLASKVKENKEMTERIKELQVQVEESAKLQETLENMKKEhlididnqkskdmelQKTIENNLQST 1017
Cdd:COG4717 50 RLEKEADELFkpqgRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEE---------------LEELEAELEEL 114
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768464868 1018 EQTLK--DAQLELEDMVKQHDELKEESKKQLEELEQTKKTLVEYQtlngDLQNEVKSLKEEIARLQTAM 1084
Cdd:COG4717 115 REELEklEKLLQLLPLYQELEALEAELAELPERLEELEERLEELR----ELEEELEELEAELAELQEEL 179
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
919-1082 |
3.00e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 42.31 E-value: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 919 AQRKLKQLKadaksvNHLKEVSYKLENKVIELTQNlaskVKENKEMTERIKELQVQVEE--SAKLQETLENMKKEhlidI 996
Cdd:TIGR04523 251 TQTQLNQLK------DEQNKIKKQLSEKQKELEQN----NKKIKELEKQLNQLKSEISDlnNQKEQDWNKELKSE----L 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 997 DNQKSKDMELQKTIENNLQSTEQtLKDaqlELEDMVKQHDELKEESKKQLEELEQTKKTLVEYQTLNGDLQNEVKSLKEE 1076
Cdd:TIGR04523 317 KNQEKKLEEIQNQISQNNKIISQ-LNE---QISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQ 392
|
....*.
gi 768464868 1077 IARLQT 1082
Cdd:TIGR04523 393 INDLES 398
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
997-1094 |
3.27e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 3.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 997 DNQKSKDMELQKTIENNLQSTEQTLKDAQLELEDMVKQHDELKEESKKQLEELEQTKKtlvEYQTLNGDLQNEVKSLKEE 1076
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQA---EIAEAEAEIEERREELGER 91
|
90
....*....|....*...
gi 768464868 1077 IARLQTAMSLGTVTTSVL 1094
Cdd:COG3883 92 ARALYRSGGSVSYLDVLL 109
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
973-1081 |
3.87e-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: 41.98 E-value: 3.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 973 VQVEESAKLQETlenmkKEHLIDIDNQKSKDMELQKTIENNLQSTEQTLKDAQLELEDMVKQHDELKEESKKQLEELEQT 1052
Cdd:TIGR02169 668 FSRSEPAELQRL-----RERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEEL 742
|
90 100
....*....|....*....|....*....
gi 768464868 1053 KKTLVEYQTLNGDLQNEVKSLKEEIARLQ 1081
Cdd:TIGR02169 743 EEDLSSLEQEIENVKSELKELEARIEELE 771
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
866-1058 |
3.88e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.85 E-value: 3.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 866 IRKELKQRQLKQEHEYNAAVTIqskvRTFEPRSRFLRTKKDTVVVQSLIRRRAAQRKLKQLKADAKSVNHLKEVSYKLEN 945
Cdd:COG1196 618 LGDTLLGRTLVAARLEAALRRA----VTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEEL 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 946 KVIELTQNLASKVKENKEMTERIKELQVQVEESAKLQETLENMKKEHLIDIDNQKSKDMELQKTIENNLQSTEQTLKDAQ 1025
Cdd:COG1196 694 ELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLE 773
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 768464868 1026 LELEDM-------VKQHDELKE---ESKKQLEELEQTKKTLVE 1058
Cdd:COG1196 774 REIEALgpvnllaIEEYEELEErydFLSEQREDLEEARETLEE 816
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
980-1081 |
3.99e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.43 E-value: 3.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 980 KLQETLENMKKEHLIDI---DNQKSKDMELQKTIENNLQSTEQTLKDAQLELEDMVKQHDELKEESKKQLEELEQTKKTL 1056
Cdd:COG4372 10 KARLSLFGLRPKTGILIaalSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQL 89
|
90 100
....*....|....*....|....*
gi 768464868 1057 VEYQTLNGDLQNEVKSLKEEIARLQ 1081
Cdd:COG4372 90 QAAQAELAQAQEELESLQEEAEELQ 114
|
|
| Leu_zip |
pfam15294 |
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ... |
931-1056 |
4.09e-03 |
|
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 (LZTFL1) and Leucine zipper protein 2 (LUZP2).
Pssm-ID: 464620 [Multi-domain] Cd Length: 276 Bit Score: 40.84 E-value: 4.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 931 KSVNHLKEVSYKLENKVIELTQNLASKVKENKEMTERIKELQVQVEESaklqetleNMKKEHLIDIDNQKSKDMELQKTI 1010
Cdd:pfam15294 133 MEIERLKEENEKLKERLKTLESQATQALDEKSKLEKALKDLQKEQGAK--------KDVKSNLKEISDLEEKMAALKSDL 204
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 768464868 1011 ENNLQSTEQTLKDAQLELEDMvkQHDELKEEskkqlEELEQTKKTL 1056
Cdd:pfam15294 205 EKTLNASTALQKSLEEDLAST--KHELLKVQ-----EQLEMAEKEL 243
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
854-1077 |
4.26e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 41.88 E-value: 4.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 854 SVLRTITNLQKKIRKELKQRQLKQEHEYNAAVTIQSKVRTFEPRSRFLrtkkdTVVVQSLIRRRAAQRKLKQlkadaksv 933
Cdd:TIGR00618 400 KELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAI-----TCTAQCEKLEKIHLQESAQ-------- 466
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 934 nHLKEVSYKLENKvieltQNLASKVKENKemTERIKELQVQVEESAKLQETLENMKkEHLIDIDNQKSKDMELQKtIENN 1013
Cdd:TIGR00618 467 -SLKEREQQLQTK-----EQIHLQETRKK--AVVLARLLELQEEPCPLCGSCIHPN-PARQDIDNPGPLTRRMQR-GEQT 536
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768464868 1014 LQSTEQTLKDAQLELEDMVKQHDELKEESKKQLEELEQTKKTLVEYQTLNGDLQNEVKSLKEEI 1077
Cdd:TIGR00618 537 YAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLT 600
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
942-1052 |
4.35e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 41.60 E-value: 4.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 942 KLENKVIELTQNLASKvkenkemtERIKELQVQVEESAKLQETLENMKKEHLIDIDNQKSKDMELQKTIENNLQSTEQ-- 1019
Cdd:pfam05622 288 QHENKMLRLGQEGSYR--------ERLTELQQLLEDANRRKNELETQNRLANQRILELQQQVEELQKALQEQGSKAEDss 359
|
90 100 110
....*....|....*....|....*....|...
gi 768464868 1020 TLKDAQLELEDMVKQHDELKEESKKQLEELEQT 1052
Cdd:pfam05622 360 LLKQKLEEHLEKLHEAQSELQKKKEQIEELEPK 392
|
|
| DUF4200 |
pfam13863 |
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ... |
977-1081 |
5.04e-03 |
|
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil domain of unknwon function.
Pssm-ID: 464003 [Multi-domain] Cd Length: 119 Bit Score: 38.70 E-value: 5.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 977 ESAKLQETLENMKKEHLididnqksKDMELQKTIENNLQSTEQTLKDAQLELEDMVKQHDELKEESKKQLEELEQTKKTL 1056
Cdd:pfam13863 7 EMFLVQLALDAKREEIE--------RLEELLKQREEELEKKEQELKEDLIKFDKFLKENDAKRRRALKKAEEETKLKKEK 78
|
90 100
....*....|....*....|....*
gi 768464868 1057 VEYQTlngDLQNEVKSLKEEIARLQ 1081
Cdd:pfam13863 79 EKEIK---KLTAQIEELKSEISKLE 100
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
864-1082 |
5.43e-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: 41.59 E-value: 5.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 864 KKIRKELkqRQLKQEHEYNAAVT--IQSKVRTFEPRSRFLRTKKDTVVVQSL---IRRRAAQRKLKQLKADAKSvnhLKE 938
Cdd:TIGR02169 794 PEIQAEL--SKLEEEVSRIEARLreIEQKLNRLTLEKEYLEKEIQELQEQRIdlkEQIKSIEKEIENLNGKKEE---LEE 868
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 939 VSYKLENKVIELTQNLASKVKENKEMTERIKELQVQVEEsaklQETLENMKKEHLIDIDNQKSKDMELQKTIENNLQStE 1018
Cdd:TIGR02169 869 ELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEE----LEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGE-D 943
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 1019 QTLKDAQLELEDMVKQHDELK-----------------EESKKQLEELEQTKKTLVEyqtlngdlqnEVKSLKEEIARLQ 1081
Cdd:TIGR02169 944 EEIPEEELSLEDVQAELQRVEeeiralepvnmlaiqeyEEVLKRLDELKEKRAKLEE----------ERKAILERIEEYE 1013
|
.
gi 768464868 1082 T 1082
Cdd:TIGR02169 1014 K 1014
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
959-1082 |
6.35e-03 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 38.36 E-value: 6.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 959 KENKEMTERIKELQvqvEESAKLQETLENMkkEHLIDIDNQKSKDMELQKtiennlQSTEQtlkdAQLELEDMVKqhdEL 1038
Cdd:pfam20492 6 REKQELEERLKQYE---EETKKAQEELEES--EETAEELEEERRQAEEEA------ERLEQ----KRQEAEEEKE---RL 67
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 768464868 1039 KEESKKQLEELEQTKKTLVEYQTLNGDLQNEVKSLKEEIARLQT 1082
Cdd:pfam20492 68 EESAEMEAEEKEQLEAELAEAQEEIARLEEEVERKEEEARRLQE 111
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
941-1081 |
6.82e-03 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 40.35 E-value: 6.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 941 YKLE-NKVIELTQNLASKVKENKEMTERIKELQVQVEESAKLQETlENMKKEHL-IDIDNQKSKDMELQKTIENNLQSTE 1018
Cdd:pfam02841 164 YNQVpRKGVKAEEVLQEFLQSKEAVEEAILQTDQALTAKEKAIEA-ERAKAEAAeAEQELLREKQKEEEQMMEAQERSYQ 242
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768464868 1019 QTLKdaQLElEDMVKQHDELKEESKKQLEELEQTKKTLveyqtLNGDLQNEVKSLKEEIARLQ 1081
Cdd:pfam02841 243 EHVK--QLI-EKMEAEREQLLAEQERMLEHKLQEQEEL-----LKEGFKTEAESLQKEIQDLK 297
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
853-1079 |
7.44e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 7.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 853 FSVLRTITNLQKKIRKELKQRQLKQ-EHEYNAAVTIQSKVRTFEprSRFLRTKKDTVVVQSLIRRRAA-QRKLKQLKADA 930
Cdd:PRK03918 495 LIKLKELAEQLKELEEKLKKYNLEElEKKAEEYEKLKEKLIKLK--GEIKSLKKELEKLEELKKKLAElEKKLDELEEEL 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 931 KSVNH-LKEVSYKLENKVIELTQNLASKVKENKEMTERIKELQVQVEESAKLQETLEnMKKEHLIDIDN----------- 998
Cdd:PRK03918 573 AELLKeLEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELD-KAFEELAETEKrleelrkelee 651
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 999 -QKSKDMELQKTIENNLQSTEQTLKDAQLELEDMVKQHDELK----------EESKKQLEELEQTKKTLVEYQtlngDLQ 1067
Cdd:PRK03918 652 lEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKktleklkeelEEREKAKKELEKLEKALERVE----ELR 727
|
250
....*....|..
gi 768464868 1068 NEVKSLKEEIAR 1079
Cdd:PRK03918 728 EKVKKYKALLKE 739
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
901-1078 |
7.69e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.79 E-value: 7.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 901 LRTKKDTVvvQSLIRRRAAQR-KLKQLKADAKSV-----NHLKEVSyKLENKVIELTQNLASKVKENKEMTERIKELQVQ 974
Cdd:PRK02224 211 LESELAEL--DEEIERYEEQReQARETRDEADEVleeheERREELE-TLEAEIEDLRETIAETEREREELAEEVRDLRER 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 975 VEE-----SAKLQET-LENMKKEHLID-IDNQKSKDMELQKTIENNLQSTEQTLKDAQLELE---DMVKQHDELKEESKK 1044
Cdd:PRK02224 288 LEEleeerDDLLAEAgLDDADAEAVEArREELEDRDEELRDRLEECRVAAQAHNEEAESLREdadDLEERAEELREEAAE 367
|
170 180 190
....*....|....*....|....*....|....
gi 768464868 1045 QLEELEQTKKTLVEYQTLNGDLQNEVKSLKEEIA 1078
Cdd:PRK02224 368 LESELEEAREAVEDRREEIEELEEEIEELRERFG 401
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
835-1058 |
8.29e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.52 E-value: 8.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 835 CATLLQAAYRGHSIRANVFSVLRTITNLQKKIRKELKQRQ--LKQEHEYNAAV-TIQSKVRTFEPRSRFLRTKkdtvvVQ 911
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKalLKQLAALERRIaALARRIRALEQELAALEAE-----LA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 912 SLIRRRAAQRKlkQLKADAKSVNHLKEVSYKLEN----KVIELTQNLASKVKE-------NKEMTERIKELQVQVEESAK 980
Cdd:COG4942 87 ELEKEIAELRA--ELEAQKEELAELLRALYRLGRqpplALLLSPEDFLDAVRRlqylkylAPARREQAEELRADLAELAA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768464868 981 LQETLENMKKEHLIDIDNQKskdmELQKTIENNLQSTEQTLKDAQLELEDMVKQHDELKEESkkqlEELEQTKKTLVE 1058
Cdd:COG4942 165 LRAELEAERAELEALLAELE----EERAALEALKAERQKLLARLEKELAELAAELAELQQEA----EELEALIARLEA 234
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
931-1063 |
9.21e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 40.81 E-value: 9.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 931 KSVNHLKEVSYKLENKVIELT--------------------------QNLASKVKENKEMTERIKELQVQVEESAKLQET 984
Cdd:TIGR01612 1129 HHIKALEEIKKKSENYIDEIKaqindledvadkaisnddpeeiekkiENIVTKIDKKKNIYDEIKKLLNEIAEIEKDKTS 1208
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768464868 985 LENMKKehlIDIDNQKSKDMELQKTIENNLQSTEQTLKDAQLELEDMvkqhDELKEESKKQLEELEQTKKTLVEYQTLN 1063
Cdd:TIGR01612 1209 LEEVKG---INLSYGKNLGKLFLEKIDEEKKKSEHMIKAMEAYIEDL----DEIKEKSPEIENEMGIEMDIKAEMETFN 1280
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1005-1079 |
9.21e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.58 E-value: 9.21e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768464868 1005 ELQKTIENnLQSTEQTLKDAQLELEDMVKQHDELKEESKKQLEELEQTKKTLVEYQTLngDLQNEVKSLKEEIAR 1079
Cdd:PRK00409 517 KLNELIAS-LEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEK--EAQQAIKEAKKEADE 588
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
901-1081 |
9.23e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 39.89 E-value: 9.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 901 LRTKKDTVVVQSLIRRRAAQRKLKQLKADAKSVNHLKEVSYKLENKVIELTQNLASKVKENKEMTER---IKELQVQVEE 977
Cdd:COG1340 41 LAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELAELNKAggsIDKLRKEIER 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 978 SAKLQETlENMKKEHLIDIDNQ------KSKDMELQKTIENNLQSTEQTLKDAQLELEDMVKQHDELKEESKK------- 1044
Cdd:COG1340 121 LEWRQQT-EVLSPEEEKELVEKikelekELEKAKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQElheemie 199
|
170 180 190
....*....|....*....|....*....|....*..
gi 768464868 1045 QLEELEQTKKTLVEYQTLNGDLQNEVKSLKEEIARLQ 1081
Cdd:COG1340 200 LYKEADELRKEADELHKEIVEAQEKADELHEEIIELQ 236
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
900-1085 |
9.69e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 9.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 900 FLRTKKDTVVVQSLIRRRAAQRKLKQLkaDAKSVNHLKEVSYKLENKVIELTQNLASKVKENKEMTERIKELQVQVEESA 979
Cdd:COG4717 290 FLLLAREKASLGKEAEELQALPALEEL--EEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEE 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768464868 980 KLQETLENMKKEHLIDID--NQKSKDMELQKTIENNLQSTEQTLKDAQLELEDMVKQHDElkEESKKQLEELEQTKKtlv 1057
Cdd:COG4717 368 LEQEIAALLAEAGVEDEEelRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDE--EELEEELEELEEELE--- 442
|
170 180
....*....|....*....|....*...
gi 768464868 1058 eyqtlngDLQNEVKSLKEEIARLQTAMS 1085
Cdd:COG4717 443 -------ELEEELEELREELAELEAELE 463
|
|
| |
