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Conserved domains on  [gi|291391928|ref|XP_002712394|]
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PREDICTED: unconventional myosin-Ib isoform X1 [Oryctolagus cuniculus]

Protein Classification

MYSc_Myo1 and Myosin_TH1 domain-containing protein (domain architecture ID 11544830)

MYSc_Myo1 and Myosin_TH1 domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MYSc_Myo1 cd01378
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ...
29-688 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: 1142.66  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928   29 ETFINNLKKRFDHNEIYTYIGSVVISVNPYRSLPIYSPEKVEDYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITG 108
Cdd:cd01378     1 EAINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  109 ESGAGKTEASKLVMSYVAAVCGKG-AEVNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGGVISN 187
Cdd:cd01378    81 ESGAGKTEASKRIMQYIAAVSGGSeSEVERVKDMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEPVGGHITN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  188 YLLEKSRVVKQPRGERNFHVFYQLLSGASEELLNKLKLERDFSRYNYLGLDSARVNGVDDAANFRTVRNAMQIVGFMDHE 267
Cdd:cd01378   161 YLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGCFDVDGIDDAADFKEVLNAMKVIGFTEEE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  268 VESVLEVVAAVLKLGNIEFKPESRVNgldeSKIKDKNELKEICELTSIDQSVLERAFSFRTVEAKQEK---VSTTLNVAQ 344
Cdd:cd01378   241 QDSIFRILAAILHLGNIQFAEDEEGN----AAISDTSVLDFVAYLLGVDPDQLEKALTHRTIETGGGGrsvYEVPLNVEQ 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  345 AYYARDALAKNLYSRLFSWLVNRINESIKAQTKVRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKEEQ 424
Cdd:cd01378   317 AAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKKKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFIELTLKAEQ 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  425 EEYIREDIEWTHIDYFNNAIICDLIENNTNGILAMLDEECLRPGTVTDETFLEKLNQVCATHQHFESRmskcsrfLNDTS 504
Cdd:cd01378   397 EEYVREGIEWTPIKYFNNKIICDLIEEKPPGIFAILDDACLTAGDATDQTFLQKLNQLFSNHPHFECP-------SGHFE 469
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  505 LPHSCFRIQHYAGKVLYQVEGFVDKNNDLLYRDLSQAMWKAGHALIKSLFPEGNPAKiNLKRPPTAGSQFKASVATLMKN 584
Cdd:cd01378   470 LRRGEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEGVDLD-SKKRPPTAGTKFKNSANALVET 548
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  585 LQTKNPNYIRCIKPNDKKAAHIFSEGLVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKMLCKQTWPHWKGPARSGV 664
Cdd:cd01378   549 LMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYKLLSPKTWPAWDGTWQGGV 628
                         650       660
                  ....*....|....*....|....
gi 291391928  665 EVLFNELEIPVEEYSFGRSKIFIR 688
Cdd:cd01378   629 ESILKDLNIPPEEYQMGKTKIFIR 652
Myosin_TH1 pfam06017
Unconventional myosin tail, actin- and lipid-binding; Unconventional myosins, ie those that ...
941-1116 8.40e-36

Unconventional myosin tail, actin- and lipid-binding; Unconventional myosins, ie those that are not found in muscle, have the common, classical-type head domain, sometimes a neck with the IQ calmodulin-binding motifs, and then non-standard tails. These tails determine the subcellular localization of the unconventional myosins and also help determine their individual functions. The family carries several different unconventional myosins, eg. Myo1f is expressed mainly in immune cells as well as in the inner ear where it can be associated with deafness, Myo1d has a lipid-binding module in their tail and is implicated in endosome vesicle recycling in epithelial cells. Myo1a, b, c and g from various eukaryotes are also found in this family.


:

Pssm-ID: 310539  Cd Length: 192  Bit Score: 136.94  E-value: 8.40e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928   941 KLEASELFKDKKALYPSSVGQPFQGAYLEI--NKNPKYKKLKDAI----EEKIIIAEVVNKINRaNGKSTSRIFLLTNNN 1014
Cdd:pfam06017    1 KDYASDLLKGKKERRRFSLLRRFMGDYLGLenNNSGVGPKLRKLAgiggDEKVLFSDRVSKFNR-SSKPSPRILILTDKA 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  1015 LLLADQKSGQ-----IKSEVPLVDVTKVSMSSQNDGFFAVHLKEgseaaSKGDFLFSSDHLIEMATKLYRTTLSQTKQKL 1089
Cdd:pfam06017   80 LYLIDPKKVKnlqyvLKRRIPLSDITSVSVSPLQDDWVVLHLGS-----SKGDLLLECDFKTELVTKLSKHYKKKTNKKL 154
                          170       180
                   ....*....|....*....|....*...
gi 291391928  1090 NIEISDEFLVQFRQDK-VCVKFIQGSQK 1116
Cdd:pfam06017  155 NVKISDTIEYRKKKGKkRTVKFVKGKGK 182
 
Name Accession Description Interval E-value
MYSc_Myo1 cd01378
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ...
29-688 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: 1142.66  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928   29 ETFINNLKKRFDHNEIYTYIGSVVISVNPYRSLPIYSPEKVEDYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITG 108
Cdd:cd01378     1 EAINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  109 ESGAGKTEASKLVMSYVAAVCGKG-AEVNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGGVISN 187
Cdd:cd01378    81 ESGAGKTEASKRIMQYIAAVSGGSeSEVERVKDMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEPVGGHITN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  188 YLLEKSRVVKQPRGERNFHVFYQLLSGASEELLNKLKLERDFSRYNYLGLDSARVNGVDDAANFRTVRNAMQIVGFMDHE 267
Cdd:cd01378   161 YLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGCFDVDGIDDAADFKEVLNAMKVIGFTEEE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  268 VESVLEVVAAVLKLGNIEFKPESRVNgldeSKIKDKNELKEICELTSIDQSVLERAFSFRTVEAKQEK---VSTTLNVAQ 344
Cdd:cd01378   241 QDSIFRILAAILHLGNIQFAEDEEGN----AAISDTSVLDFVAYLLGVDPDQLEKALTHRTIETGGGGrsvYEVPLNVEQ 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  345 AYYARDALAKNLYSRLFSWLVNRINESIKAQTKVRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKEEQ 424
Cdd:cd01378   317 AAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKKKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFIELTLKAEQ 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  425 EEYIREDIEWTHIDYFNNAIICDLIENNTNGILAMLDEECLRPGTVTDETFLEKLNQVCATHQHFESRmskcsrfLNDTS 504
Cdd:cd01378   397 EEYVREGIEWTPIKYFNNKIICDLIEEKPPGIFAILDDACLTAGDATDQTFLQKLNQLFSNHPHFECP-------SGHFE 469
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  505 LPHSCFRIQHYAGKVLYQVEGFVDKNNDLLYRDLSQAMWKAGHALIKSLFPEGNPAKiNLKRPPTAGSQFKASVATLMKN 584
Cdd:cd01378   470 LRRGEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEGVDLD-SKKRPPTAGTKFKNSANALVET 548
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  585 LQTKNPNYIRCIKPNDKKAAHIFSEGLVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKMLCKQTWPHWKGPARSGV 664
Cdd:cd01378   549 LMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYKLLSPKTWPAWDGTWQGGV 628
                         650       660
                  ....*....|....*....|....
gi 291391928  665 EVLFNELEIPVEEYSFGRSKIFIR 688
Cdd:cd01378   629 ESILKDLNIPPEEYQMGKTKIFIR 652
MYSc smart00242
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ...
16-701 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  Cd Length: 677  Bit Score: 1035.96  E-value: 0e+00
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928     16 GVGDMVLLEPLNEETFINNLKKRFDHNEIYTYIGSVVISVNPYRSLPIYSPEKVEDYRNRNFYELSPHIFALSDEAYRSL 95
Cdd:smart00242    7 GVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIADNAYRNM 86
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928     96 RDQDKDQCILITGESGAGKTEASKLVMSYVAAVCGKGAEVNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFD 175
Cdd:smart00242   87 LNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNTEVGSVEDQILESNPILEAFGNAKTLRNNNSSRFGKFIEIHFD 166
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928    176 FKGDPLGGVISNYLLEKSRVVKQPRGERNFHVFYQLLSGASEELLNKLKLERDfSRYNYL-GLDSARVNGVDDAANFRTV 254
Cdd:smart00242  167 AKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSP-EDYRYLnQGGCLTVDGIDDAEEFKET 245
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928    255 RNAMQIVGFMDHEVESVLEVVAAVLKLGNIEFKPESrvNGLDESKIKDKNELKEICELTSIDQSVLERAFSFRTVEAKQE 334
Cdd:smart00242  246 LNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGR--NDNAASTVKDKEELSNAAELLGVDPEELEKALTKRKIKTGGE 323
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928    335 KVSTTLNVAQAYYARDALAKNLYSRLFSWLVNRINESIKAQTKvRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQI 414
Cdd:smart00242  324 VITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDG-STYFIGVLDIYGFEIFEVNSFEQLCINYANEKLQQF 402
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928    415 FIELTLKEEQEEYIREDIEWTHIDYFNNAIICDLIENNTNGILAMLDEECLRPGtVTDETFLEKLNQVCATHQHFESRMS 494
Cdd:smart00242  403 FNQHVFKLEQEEYEREGIDWTFIDFFDNQDCIDLIEKKPPGILSLLDEECRFPK-GTDQTFLEKLNQHHKKHPHFSKPKK 481
                           490       500       510       520       530       540       550       560
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928    495 KcsrflndtslPHSCFRIQHYAGKVLYQVEGFVDKNNDLLYRDLSQAMWKAGHALIKSLFPEGNPAKINLKRPPTAGSQF 574
Cdd:smart00242  482 K----------GRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSGVSNAGSKKRFQTVGSQF 551
                           570       580       590       600       610       620       630       640
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928    575 KASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFSEGLVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKMLCKQTWP 654
Cdd:smart00242  552 KEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRLPFDEFLQRYRVLLPDTWP 631
                           650       660       670       680
                    ....*....|....*....|....*....|....*....|....*..
gi 291391928    655 HWKGPARSGVEVLFNELEIPVEEYSFGRSKIFIRnPRTLFKLEDLRK 701
Cdd:smart00242  632 PWGGDAKKACEALLQSLGLDEDEYQLGKTKVFLR-PGQLAELEELRE 677
Myosin_head pfam00063
Myosin head (motor domain);
17-688 0e+00

Myosin head (motor domain);


Pssm-ID: 306553  Cd Length: 674  Bit Score: 937.86  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928    17 VGDMVLLEPLNEETFINNLKKRFDHNEIYTYIGSVVISVNPYRSLPIYSPEKVEDYRNRNFYELSPHIFALSDEAYRSLR 96
Cdd:pfam00063    1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928    97 DQDKDQCILITGESGAGKTEASKLVMSYVAAVCGKGAEVN--QVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEF 174
Cdd:pfam00063   81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAGNvgRLEEQILQSNPILEAFGNAKTVRNNNSSRFGKYIEIQF 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928   175 DFKGDPLGGVISNYLLEKSRVVKQPRGERNFHVFYQLLSGASEELLNKLKLErDFSRYNYL-GLDSARVNGVDDAANFRT 253
Cdd:pfam00063  161 DAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLT-NPKDYHYLsQSGCYTIDGIDDVEEFKI 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928   254 VRNAMQIVGFMDHEVESVLEVVAAVLKLGNIEFKPESRVNGldeSKIKDKNELKEICELTSIDQSVLERAFSFRTVEAKQ 333
Cdd:pfam00063  240 TDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQ---AVPDDTENLQKAASLLGIDSTELEKALCKRRIKTGR 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928   334 EKVSTTLNVAQAYYARDALAKNLYSRLFSWLVNRINESIKAQTKVRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQ 413
Cdd:pfam00063  317 ETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTIERASFIGVLDIYGFEIFEKNSFEQLCINYVNEKLQQ 396
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928   414 IFIELTLKEEQEEYIREDIEWTHIDYFNNAIICDLIENNTNGILAMLDEECLRPGtVTDETFLEKLNQVCATHQHFESrm 493
Cdd:pfam00063  397 FFNHHMFKLEQEEYVREGIEWTFIDFGDNQPCIDLIEKKPLGILSLLDEECLFPK-ATDQTFLDKLYSTFSKHPHFQK-- 473
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928   494 skcSRFLNDTslphsCFRIQHYAGKVLYQVEGFVDKNNDLLYRDLSQAMWKAGHALIKSLFPEGNPA------------- 560
Cdd:pfam00063  474 ---PRLQGET-----HFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAesaaanesgkstp 545
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928   561 -KINLKRPPTAGSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFSEGLVCHQIRYLGLLENVRVRRAGYAFRQAYE 639
Cdd:pfam00063  546 kRTKKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQ 625
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*....
gi 291391928   640 PCLERYKMLCKQTWPHWKGPARSGVEVLFNELEIPVEEYSFGRSKIFIR 688
Cdd:pfam00063  626 EFVQRYRILAPKTWPKWKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
COG5022 COG5022
Myosin heavy chain [General function prediction only];
16-837 0e+00

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355  Cd Length: 1463  Bit Score: 744.21  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928   16 GVGDMVLLEPLNEETFINNLKKRFDHNEIYTYIGSVVISVNPYRSLPIYSPEKVEDYRNRNFYELSPHIFALSDEAYRSL 95
Cdd:COG5022    67 GVDDLTELSYLNEPAVLHNLEKRYNNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNL 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928   96 RDQDKDQCILITGESGAGKTEASKLVMSYVAAVCG-KGAEVNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEF 174
Cdd:COG5022   147 LSEKENQTIIISGESGAGKTENAKRIMQYLASVTSsSTVEISSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEF 226
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  175 DFKGDPLGGVISNYLLEKSRVVKQPRGERNFHVFYQLLSGASEElLNKLKLERDFSRYNYL---GLDSarVNGVDDAANF 251
Cdd:COG5022   227 DENGEICGAKIETYLLEKSRVVHQNKNERNYHIFYQLLAGDPEE-LKKLLLLQNPKDYIYLsqgGCDK--IDGIDDAKEF 303
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  252 RTVRNAMQIVGFMDHEVESVLEVVAAVLKLGNIEFKpESRVnglDESKIKDKNELKEICELTSIDQSVLERAFSFRTVEA 331
Cdd:COG5022   304 KITLDALKTIGIDEEEQDQIFKILAAILHIGNIEFK-EDRN---GAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKT 379
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  332 KQEKVSTTLNVAQAYYARDALAKNLYSRLFSWLVNRINESIKAqTKVRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKL 411
Cdd:COG5022   380 GGEWIVVPLNLEQALAIRDSLAKALYSNLFDWIVDRINKSLDH-SAAASNFIGVLDIYGFEIFEKNSFEQLCINYTNEKL 458
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  412 QQIFIELTLKEEQEEYIREDIEWTHIDYFNNAIICDLIEN-NTNGILAMLDEECLRPgTVTDETFLEKLNQV--CATHQH 488
Cdd:COG5022   459 QQFFNQHMFKLEQEEYVKEGIEWSFIDYFDNQPCIDLIEKkNPLGILSLLDEECVMP-HATDESFTSKLAQRlnKNSNPK 537
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  489 FESrmskcSRFLNDTslphscFRIQHYAGKVLYQVEGFVDKNNDLLYRDLSQAMWKAGHALIKSLFPEgnPAKINLK-RP 567
Cdd:COG5022   538 FKK-----SRFRDNK------FVVKHYAGDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDD--EENIESKgRF 604
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  568 PTAGSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFSEGLVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKM 647
Cdd:COG5022   605 PTLGSRFKESLNSLMSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRI 684
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  648 LCKQ----TWPHWKGPARSGVEVLFNELEIPVEEYSFGRSKIFIRNPrTLFKLEDLRKQRLEDLATLIQKIYRGWKCRTH 723
Cdd:COG5022   685 LSPSkswtGEYTWKEDTKNAVKSILEELVIDSSKYQIGNTKVFFKAG-VLAALEDMRDAKLDNIATRIQRAIRGRYLRRR 763
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  724 FLLMKRSQIVIAA---------------WYRRYAQQKRY-------QQIKSSALVIQSYIRGWKARKILRELKHQKRCQE 781
Cdd:COG5022   764 YLQALKRIKKIQViqhgfrlrrlvdyelKWRLFIKLQPLlsllgsrKEYRSYLACIIKLQKTIKREKKLRETEEVEFSLK 843
                         810       820       830       840       850
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 291391928  782 AATTIAAYWHGTQARRELRRLKeearnKHAIAVIWAcWLGSKARRELKRLKEEARR 837
Cdd:COG5022   844 AEVLIQKFGRSLKAKKRFSLLK-----KETIYLQSA-QRVELAERQLQELKIDVKS 893
PTZ00014 PTZ00014
myosin-A; Provisional
17-762 1.36e-151

myosin-A; Provisional


Pssm-ID: 240229  Cd Length: 821  Bit Score: 477.60  E-value: 1.36e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928   17 VGDMVLLEPLNEETFINNLKKRFDHNEIYTYIGSVVISVNPYRSLPIYSPEKVEDYRN-RNFYELSPHIFALSDEAYRSL 95
Cdd:PTZ00014   98 YGDIGLLPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYRDaKDSDKLPPHVFTTARRALENL 177
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928   96 RDQDKDQCILITGESGAGKTEASKLVMSYVAAvcGKGAEVNQ-VKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEF 174
Cdd:PTZ00014  178 HGVKKSQTIIVSGESGAGKTEATKQIMRYFAS--SKSGNMDLkIQNAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQL 255
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  175 DFKGDPLGGVISNYLLEKSRVVKQPRGERNFHVFYQLLSGASEELLNKLKLeRDFSRYNYLGLDSARVNGVDDAANFRTV 254
Cdd:PTZ00014  256 GEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKL-KSLEEYKYINPKCLDVPGIDDVKDFEEV 334
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  255 RNAMQIVGFMDHEVESVLEVVAAVLKLGNIEFKPESRVNGLDESKIKDKNE--LKEICELTSIDQSVLERAFSFRTVEAK 332
Cdd:PTZ00014  335 MESFDSMGLSESQIEDIFSILSGVLLLGNVEIEGKEEGGLTDAAAISDESLevFNEACELLFLDYESLKKELTVKVTYAG 414
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  333 QEKVSTTLNVAQAYYARDALAKNLYSRLFSWLVNRINESIKAQTKVrKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQ 412
Cdd:PTZ00014  415 NQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGF-KVFIGMLDIFGFEVFKNNSLEQLFINITNEMLQ 493
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  413 QIFIELTLKEEQEEYIREDIEWTHIDYFNNAIICDLIENNTNGILAMLDEECLRPGTvTDETFLEKLNQVCATHQHFesr 492
Cdd:PTZ00014  494 KNFVDIVFERESKLYKDEGISTEELEYTSNESVIDLLCGKGKSVLSILEDQCLAPGG-TDEKFVSSCNTNLKNNPKY--- 569
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  493 mSKCSRFLNdtslphSCFRIQHYAGKVLYQVEGFVDKNNDLLYRDLSQAMWKAGHALIKSLFP-----EGNPAKINLkrp 567
Cdd:PTZ00014  570 -KPAKVDSN------KNFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLFEgveveKGKLAKGQL--- 639
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  568 ptAGSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFSEGLVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKM 647
Cdd:PTZ00014  640 --IGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKY 717
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  648 LCKQTWPHWKGPARSGVEVLFNELEIPVEEYSFGRSKIFIRnPRTLFKLEDLRKQRLEDLATLIQkiyrgwkcrthfllm 727
Cdd:PTZ00014  718 LDLAVSNDSSLDPKEKAEKLLERSGLPKDSYAIGKTMVFLK-KDAAKELTQIQREKLAAWEPLVS--------------- 781
                         730       740       750
                  ....*....|....*....|....*....|....*
gi 291391928  728 krsqiVIAAWYRRYAQQKRYQQIKSSALVIQSYIR 762
Cdd:PTZ00014  782 -----VLEALILKIKKKRKVRKNIKSLVRIQAHLR 811
Myosin_TH1 pfam06017
Unconventional myosin tail, actin- and lipid-binding; Unconventional myosins, ie those that ...
941-1116 8.40e-36

Unconventional myosin tail, actin- and lipid-binding; Unconventional myosins, ie those that are not found in muscle, have the common, classical-type head domain, sometimes a neck with the IQ calmodulin-binding motifs, and then non-standard tails. These tails determine the subcellular localization of the unconventional myosins and also help determine their individual functions. The family carries several different unconventional myosins, eg. Myo1f is expressed mainly in immune cells as well as in the inner ear where it can be associated with deafness, Myo1d has a lipid-binding module in their tail and is implicated in endosome vesicle recycling in epithelial cells. Myo1a, b, c and g from various eukaryotes are also found in this family.


Pssm-ID: 310539  Cd Length: 192  Bit Score: 136.94  E-value: 8.40e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928   941 KLEASELFKDKKALYPSSVGQPFQGAYLEI--NKNPKYKKLKDAI----EEKIIIAEVVNKINRaNGKSTSRIFLLTNNN 1014
Cdd:pfam06017    1 KDYASDLLKGKKERRRFSLLRRFMGDYLGLenNNSGVGPKLRKLAgiggDEKVLFSDRVSKFNR-SSKPSPRILILTDKA 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  1015 LLLADQKSGQ-----IKSEVPLVDVTKVSMSSQNDGFFAVHLKEgseaaSKGDFLFSSDHLIEMATKLYRTTLSQTKQKL 1089
Cdd:pfam06017   80 LYLIDPKKVKnlqyvLKRRIPLSDITSVSVSPLQDDWVVLHLGS-----SKGDLLLECDFKTELVTKLSKHYKKKTNKKL 154
                          170       180
                   ....*....|....*....|....*...
gi 291391928  1090 NIEISDEFLVQFRQDK-VCVKFIQGSQK 1116
Cdd:pfam06017  155 NVKISDTIEYRKKKGKkRTVKFVKGKGK 182
 
Name Accession Description Interval E-value
MYSc_Myo1 cd01378
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ...
29-688 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: 1142.66  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928   29 ETFINNLKKRFDHNEIYTYIGSVVISVNPYRSLPIYSPEKVEDYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITG 108
Cdd:cd01378     1 EAINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  109 ESGAGKTEASKLVMSYVAAVCGKG-AEVNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGGVISN 187
Cdd:cd01378    81 ESGAGKTEASKRIMQYIAAVSGGSeSEVERVKDMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEPVGGHITN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  188 YLLEKSRVVKQPRGERNFHVFYQLLSGASEELLNKLKLERDFSRYNYLGLDSARVNGVDDAANFRTVRNAMQIVGFMDHE 267
Cdd:cd01378   161 YLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGCFDVDGIDDAADFKEVLNAMKVIGFTEEE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  268 VESVLEVVAAVLKLGNIEFKPESRVNgldeSKIKDKNELKEICELTSIDQSVLERAFSFRTVEAKQEK---VSTTLNVAQ 344
Cdd:cd01378   241 QDSIFRILAAILHLGNIQFAEDEEGN----AAISDTSVLDFVAYLLGVDPDQLEKALTHRTIETGGGGrsvYEVPLNVEQ 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  345 AYYARDALAKNLYSRLFSWLVNRINESIKAQTKVRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKEEQ 424
Cdd:cd01378   317 AAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKKKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFIELTLKAEQ 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  425 EEYIREDIEWTHIDYFNNAIICDLIENNTNGILAMLDEECLRPGTVTDETFLEKLNQVCATHQHFESRmskcsrfLNDTS 504
Cdd:cd01378   397 EEYVREGIEWTPIKYFNNKIICDLIEEKPPGIFAILDDACLTAGDATDQTFLQKLNQLFSNHPHFECP-------SGHFE 469
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  505 LPHSCFRIQHYAGKVLYQVEGFVDKNNDLLYRDLSQAMWKAGHALIKSLFPEGNPAKiNLKRPPTAGSQFKASVATLMKN 584
Cdd:cd01378   470 LRRGEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEGVDLD-SKKRPPTAGTKFKNSANALVET 548
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  585 LQTKNPNYIRCIKPNDKKAAHIFSEGLVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKMLCKQTWPHWKGPARSGV 664
Cdd:cd01378   549 LMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYKLLSPKTWPAWDGTWQGGV 628
                         650       660
                  ....*....|....*....|....
gi 291391928  665 EVLFNELEIPVEEYSFGRSKIFIR 688
Cdd:cd01378   629 ESILKDLNIPPEEYQMGKTKIFIR 652
MYSc smart00242
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ...
16-701 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  Cd Length: 677  Bit Score: 1035.96  E-value: 0e+00
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928     16 GVGDMVLLEPLNEETFINNLKKRFDHNEIYTYIGSVVISVNPYRSLPIYSPEKVEDYRNRNFYELSPHIFALSDEAYRSL 95
Cdd:smart00242    7 GVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIADNAYRNM 86
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928     96 RDQDKDQCILITGESGAGKTEASKLVMSYVAAVCGKGAEVNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFD 175
Cdd:smart00242   87 LNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNTEVGSVEDQILESNPILEAFGNAKTLRNNNSSRFGKFIEIHFD 166
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928    176 FKGDPLGGVISNYLLEKSRVVKQPRGERNFHVFYQLLSGASEELLNKLKLERDfSRYNYL-GLDSARVNGVDDAANFRTV 254
Cdd:smart00242  167 AKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSP-EDYRYLnQGGCLTVDGIDDAEEFKET 245
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928    255 RNAMQIVGFMDHEVESVLEVVAAVLKLGNIEFKPESrvNGLDESKIKDKNELKEICELTSIDQSVLERAFSFRTVEAKQE 334
Cdd:smart00242  246 LNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGR--NDNAASTVKDKEELSNAAELLGVDPEELEKALTKRKIKTGGE 323
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928    335 KVSTTLNVAQAYYARDALAKNLYSRLFSWLVNRINESIKAQTKvRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQI 414
Cdd:smart00242  324 VITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDG-STYFIGVLDIYGFEIFEVNSFEQLCINYANEKLQQF 402
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928    415 FIELTLKEEQEEYIREDIEWTHIDYFNNAIICDLIENNTNGILAMLDEECLRPGtVTDETFLEKLNQVCATHQHFESRMS 494
Cdd:smart00242  403 FNQHVFKLEQEEYEREGIDWTFIDFFDNQDCIDLIEKKPPGILSLLDEECRFPK-GTDQTFLEKLNQHHKKHPHFSKPKK 481
                           490       500       510       520       530       540       550       560
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928    495 KcsrflndtslPHSCFRIQHYAGKVLYQVEGFVDKNNDLLYRDLSQAMWKAGHALIKSLFPEGNPAKINLKRPPTAGSQF 574
Cdd:smart00242  482 K----------GRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSGVSNAGSKKRFQTVGSQF 551
                           570       580       590       600       610       620       630       640
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928    575 KASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFSEGLVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKMLCKQTWP 654
Cdd:smart00242  552 KEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRLPFDEFLQRYRVLLPDTWP 631
                           650       660       670       680
                    ....*....|....*....|....*....|....*....|....*..
gi 291391928    655 HWKGPARSGVEVLFNELEIPVEEYSFGRSKIFIRnPRTLFKLEDLRK 701
Cdd:smart00242  632 PWGGDAKKACEALLQSLGLDEDEYQLGKTKVFLR-PGQLAELEELRE 677
Myosin_head pfam00063
Myosin head (motor domain);
17-688 0e+00

Myosin head (motor domain);


Pssm-ID: 306553  Cd Length: 674  Bit Score: 937.86  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928    17 VGDMVLLEPLNEETFINNLKKRFDHNEIYTYIGSVVISVNPYRSLPIYSPEKVEDYRNRNFYELSPHIFALSDEAYRSLR 96
Cdd:pfam00063    1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928    97 DQDKDQCILITGESGAGKTEASKLVMSYVAAVCGKGAEVN--QVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEF 174
Cdd:pfam00063   81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAGNvgRLEEQILQSNPILEAFGNAKTVRNNNSSRFGKYIEIQF 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928   175 DFKGDPLGGVISNYLLEKSRVVKQPRGERNFHVFYQLLSGASEELLNKLKLErDFSRYNYL-GLDSARVNGVDDAANFRT 253
Cdd:pfam00063  161 DAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLT-NPKDYHYLsQSGCYTIDGIDDVEEFKI 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928   254 VRNAMQIVGFMDHEVESVLEVVAAVLKLGNIEFKPESRVNGldeSKIKDKNELKEICELTSIDQSVLERAFSFRTVEAKQ 333
Cdd:pfam00063  240 TDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQ---AVPDDTENLQKAASLLGIDSTELEKALCKRRIKTGR 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928   334 EKVSTTLNVAQAYYARDALAKNLYSRLFSWLVNRINESIKAQTKVRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQ 413
Cdd:pfam00063  317 ETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTIERASFIGVLDIYGFEIFEKNSFEQLCINYVNEKLQQ 396
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928   414 IFIELTLKEEQEEYIREDIEWTHIDYFNNAIICDLIENNTNGILAMLDEECLRPGtVTDETFLEKLNQVCATHQHFESrm 493
Cdd:pfam00063  397 FFNHHMFKLEQEEYVREGIEWTFIDFGDNQPCIDLIEKKPLGILSLLDEECLFPK-ATDQTFLDKLYSTFSKHPHFQK-- 473
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928   494 skcSRFLNDTslphsCFRIQHYAGKVLYQVEGFVDKNNDLLYRDLSQAMWKAGHALIKSLFPEGNPA------------- 560
Cdd:pfam00063  474 ---PRLQGET-----HFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAesaaanesgkstp 545
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928   561 -KINLKRPPTAGSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFSEGLVCHQIRYLGLLENVRVRRAGYAFRQAYE 639
Cdd:pfam00063  546 kRTKKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQ 625
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*....
gi 291391928   640 PCLERYKMLCKQTWPHWKGPARSGVEVLFNELEIPVEEYSFGRSKIFIR 688
Cdd:pfam00063  626 EFVQRYRILAPKTWPKWKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
MYSc cd00124
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ...
29-688 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  Cd Length: 633  Bit Score: 784.09  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928   29 ETFINNLKKRFDHNEIYTYIGSVVISVNPYRSLPIYSPEKVEDYRNRN-FYELSPHIFALSDEAYRSLRDQDKDQCILIT 107
Cdd:cd00124     1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGrSADLPPHVFAVADAAYRAMLRDGQNQSILIS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  108 GESGAGKTEASKLVMSYVAAVCGKGAEVNQVK-----EQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLG 182
Cdd:cd00124    81 GESGAGKTETTKLVLKYLAALSGSGSSKSSSSassieQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPTGRLVG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  183 GVISNYLLEKSRVVKQPRGERNFHVFYQLLSGASEELLNKLKLE---RDFSRYNYLGL-DSARVNGVDDAANFRTVRNAM 258
Cdd:cd00124   161 ASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLElllSYYYLNDYLNSsGCDRIDGVDDAEEFQELLDAL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  259 QIVGFMDHEVESVLEVVAAVLKLGNIEFKpESRVNGLDESKIKDKNELKEICELTSIDQSVLERAFSFRTVEAKQEKVST 338
Cdd:cd00124   241 DVLGFSDEEQDSIFRILAAILHLGNIEFE-EDEEDEDSSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGETITK 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  339 TLNVAQAYYARDALAKNLYSRLFSWLVNRINESIKAQTKVRKK-VMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIE 417
Cdd:cd00124   320 PLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAESTsFIGILDIFGFENFEVNSFEQLCINYANEKLQQFFNQ 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  418 LTLKEEQEEYIREDIEWTHIDYFNNAIICDLIENNTNGILAMLDEECLRPGTvTDETFLEKLNQVCATHqhfesrmskcS 497
Cdd:cd00124   400 HVFKLEQEEYEEEGIDWSFIDFPDNQDCLDLIEGKPLGILSLLDEECLFPKG-TDATFLEKLYSAHGSH----------P 468
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  498 RFLNDTSLPHSCFRIQHYAGKVLYQVEGFVDKNNDLLYRDLSQAMwkaghalikslfpegnpakinlkrppTAGSQFKAS 577
Cdd:cd00124   469 RFFSKKRKAKLEFGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLL--------------------------RSGSQFRSQ 522
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  578 VATLMKNLQTKNPNYIRCIKPNDKKAAHIFSEGLVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKMLCKQTWPHWK 657
Cdd:cd00124   523 LDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYRILAPGATEKAS 602
                         650       660       670
                  ....*....|....*....|....*....|.
gi 291391928  658 GPARSGVEVLFNELEIPVEEYSFGRSKIFIR 688
Cdd:cd00124   603 DSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
COG5022 COG5022
Myosin heavy chain [General function prediction only];
16-837 0e+00

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355  Cd Length: 1463  Bit Score: 744.21  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928   16 GVGDMVLLEPLNEETFINNLKKRFDHNEIYTYIGSVVISVNPYRSLPIYSPEKVEDYRNRNFYELSPHIFALSDEAYRSL 95
Cdd:COG5022    67 GVDDLTELSYLNEPAVLHNLEKRYNNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNL 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928   96 RDQDKDQCILITGESGAGKTEASKLVMSYVAAVCG-KGAEVNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEF 174
Cdd:COG5022   147 LSEKENQTIIISGESGAGKTENAKRIMQYLASVTSsSTVEISSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEF 226
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  175 DFKGDPLGGVISNYLLEKSRVVKQPRGERNFHVFYQLLSGASEElLNKLKLERDFSRYNYL---GLDSarVNGVDDAANF 251
Cdd:COG5022   227 DENGEICGAKIETYLLEKSRVVHQNKNERNYHIFYQLLAGDPEE-LKKLLLLQNPKDYIYLsqgGCDK--IDGIDDAKEF 303
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  252 RTVRNAMQIVGFMDHEVESVLEVVAAVLKLGNIEFKpESRVnglDESKIKDKNELKEICELTSIDQSVLERAFSFRTVEA 331
Cdd:COG5022   304 KITLDALKTIGIDEEEQDQIFKILAAILHIGNIEFK-EDRN---GAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKT 379
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  332 KQEKVSTTLNVAQAYYARDALAKNLYSRLFSWLVNRINESIKAqTKVRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKL 411
Cdd:COG5022   380 GGEWIVVPLNLEQALAIRDSLAKALYSNLFDWIVDRINKSLDH-SAAASNFIGVLDIYGFEIFEKNSFEQLCINYTNEKL 458
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  412 QQIFIELTLKEEQEEYIREDIEWTHIDYFNNAIICDLIEN-NTNGILAMLDEECLRPgTVTDETFLEKLNQV--CATHQH 488
Cdd:COG5022   459 QQFFNQHMFKLEQEEYVKEGIEWSFIDYFDNQPCIDLIEKkNPLGILSLLDEECVMP-HATDESFTSKLAQRlnKNSNPK 537
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  489 FESrmskcSRFLNDTslphscFRIQHYAGKVLYQVEGFVDKNNDLLYRDLSQAMWKAGHALIKSLFPEgnPAKINLK-RP 567
Cdd:COG5022   538 FKK-----SRFRDNK------FVVKHYAGDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDD--EENIESKgRF 604
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  568 PTAGSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFSEGLVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKM 647
Cdd:COG5022   605 PTLGSRFKESLNSLMSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRI 684
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  648 LCKQ----TWPHWKGPARSGVEVLFNELEIPVEEYSFGRSKIFIRNPrTLFKLEDLRKQRLEDLATLIQKIYRGWKCRTH 723
Cdd:COG5022   685 LSPSkswtGEYTWKEDTKNAVKSILEELVIDSSKYQIGNTKVFFKAG-VLAALEDMRDAKLDNIATRIQRAIRGRYLRRR 763
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  724 FLLMKRSQIVIAA---------------WYRRYAQQKRY-------QQIKSSALVIQSYIRGWKARKILRELKHQKRCQE 781
Cdd:COG5022   764 YLQALKRIKKIQViqhgfrlrrlvdyelKWRLFIKLQPLlsllgsrKEYRSYLACIIKLQKTIKREKKLRETEEVEFSLK 843
                         810       820       830       840       850
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 291391928  782 AATTIAAYWHGTQARRELRRLKeearnKHAIAVIWAcWLGSKARRELKRLKEEARR 837
Cdd:COG5022   844 AEVLIQKFGRSLKAKKRFSLLK-----KETIYLQSA-QRVELAERQLQELKIDVKS 893
MYSc_class_II cd01377
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ...
32-688 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  Cd Length: 662  Bit Score: 671.48  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928   32 INNLKKRFDHNEIYTYIGSVVISVNPYRSLPIYSPEKVEDYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITGESG 111
Cdd:cd01377     4 LHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITGESG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  112 AGKTEASKLVMSYVAAVCG-------KGAEVNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGGV 184
Cdd:cd01377    84 AGKTENTKKVIQYLASVAAsskkkkeSGKKKGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTGKIAGAD 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  185 ISNYLLEKSRVVKQPRGERNFHVFYQLLSGASEELLNKLKLERDFSRYNYLGLDSARVNGVDDAANFRTVRNAMQIVGFM 264
Cdd:cd01377   164 IETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYFFLSQGELTIDGVDDAEEFKLTDEAFDILGFS 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  265 DHEVESVLEVVAAVLKLGNIEFKPESRvngLDESKIKDKNELKEICELTSIDQSVLERAFSFRTVEAKQEKVSTTLNVAQ 344
Cdd:cd01377   244 EEEKMSIFKIVAAILHLGNIKFKQRRR---EEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKGQNKEQ 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  345 AYYARDALAKNLYSRLFSWLVNRINESIKaQTKVRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIF----IELtl 420
Cdd:cd01377   321 VVFSVGALAKALYERLFLWLVKRINKTLD-TKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFnhhmFVL-- 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  421 keEQEEYIREDIEWTHIDYFNNAIIC-DLIENNTNGILAMLDEECLRPGTvTDETFLEKLNQVCATHQHFESRMSKCSrf 499
Cdd:cd01377   398 --EQEEYKKEGIEWTFIDFGLDLQPTiDLIEKPNMGILSILDEECVFPKA-TDKTFVEKLYSNHLGKSKNFKKPKPKK-- 472
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  500 lndtslPHSCFRIQHYAGKVLYQVEGFVDKNNDLLYRDLSQAMWKAGHALIKSLFPE-----GNPAKINLKRPP--TAGS 572
Cdd:cd01377   473 ------SEAHFILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDyeesgGGGGKKKKKGGSfrTVSQ 546
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  573 QFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFSEGLVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKMLCKQT 652
Cdd:cd01377   547 LHKEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNA 626
                         650       660       670
                  ....*....|....*....|....*....|....*.
gi 291391928  653 WPHWKGPARSGVEVLFNELEIPVEEYSFGRSKIFIR 688
Cdd:cd01377   627 IPKGFDDGKAACEKILKALQLDPELYRIGNTKVFFK 662
MYSc_Myo5 cd01380
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ...
33-688 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  Cd Length: 629  Bit Score: 663.85  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928   33 NNLKKRF-DHNEIYTYIGSVVISVNPYRSLPIYSPEKVEDYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITGESG 111
Cdd:cd01380     5 HNLKVRFcQRNAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVSGESG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  112 AGKTEASKLVMSYVAAVCGKGAEVNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGGVISNYLLE 191
Cdd:cd01380    85 AGKTVSAKYAMRYFATVGGSSSGETQVEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYRIIGANMRTYLLE 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  192 KSRVVKQPRGERNFHVFYQLLSGASEELLNKLKLErDFSRYNYLGL-DSARVNGVDDAANFRTVRNAMQIVGFMDHEVES 270
Cdd:cd01380   165 KSRVVFQAEEERNYHIFYQLCAAASLPELKELHLG-SAEDFFYTNQgGSPVIDGVDDAAEFEETRKALTLLGISEEEQME 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  271 VLEVVAAVLKLGNIEFKPESRvnglDESKIKDKNE-LKEICELTSIDQSVLERAFSFRTVEAKQEKVSTTLNVAQAYYAR 349
Cdd:cd01380   244 IFRILAAILHLGNVEIKATRN----DSASISPDDEhLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPLTLQQAIVAR 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  350 DALAKNLYSRLFSWLVNRINESIKAQTKVR-KKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKEEQEEYI 428
Cdd:cd01380   320 DALAKHIYAQLFDWIVDRINKALASPVKEKqHSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHVFKLEQEEYV 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  429 REDIEWTHIDYFNNAIICDLIENNTnGILAMLDEECLRPGTvTDETFLEKLNQVCATH--QHFESrmskcSRFLNDTslp 506
Cdd:cd01380   400 KEEIEWSFIDFYDNQPCIDLIEGKL-GILDLLDEECRLPKG-SDENWAQKLYNQHLKKpnKHFKK-----PRFSNTA--- 469
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  507 hscFRIQHYAGKVLYQVEGFVDKNNDLLYRDLSQAMwkaghalikslfpegnpaKINLKRPPTAGSQFKASVATLMKNLQ 586
Cdd:cd01380   470 ---FIVKHFADDVEYQVEGFLEKNRDTVSEEHLNVL------------------KASKNRKKTVGSQFRDSLILLMETLN 528
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  587 TKNPNYIRCIKPNDKKAAHIFSEGLVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKMLCKQTWPHWKGPARSGVEV 666
Cdd:cd01380   529 STTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLPSKEWLRDDKKKTCENI 608
                         650       660
                  ....*....|....*....|..
gi 291391928  667 LFNELEIPvEEYSFGRSKIFIR 688
Cdd:cd01380   609 LENLILDP-DKYQFGKTKIFFR 629
MYSc_Myo7 cd01381
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ...
34-688 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: 656.63  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928   34 NLKKRFDHNEIYTYIGSVVISVNPYRSLPIYSPEKVEDYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITGESGAG 113
Cdd:cd01381     6 NLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISGESGAG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  114 KTEASKLVMSYVAAVCGKGAEVNQvkeQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGGVISNYLLEKS 193
Cdd:cd01381    86 KTESTKLILQYLAAISGQHSWIEQ---QILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIEGAKIEQYLLEKS 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  194 RVVKQPRGERNFHVFYQLLSGASEELLNKLKLErDFSRYNYL-GLDSARVNGVDDAANFRTVRNAMQIVGFMDHEVESVL 272
Cdd:cd01381   163 RIVSQAPDERNYHIFYCMLAGLSAEEKKKLELG-DASDYYYLtQGNCLTCEGRDDAAEFADIRSAMKVLMFTDEEIWDIF 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  273 EVVAAVLKLGNIEFKpESRVNGLDESKIKDKNELKEICELTSIDQSVLERAFSFRTVEAKQEKVSTTLNVAQAYYARDAL 352
Cdd:cd01381   242 KLLAAILHLGNIKFE-ATVVDNLDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSPLSAEQALDVRDAF 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  353 AKNLYSRLFSWLVNRINESI---KAQTKVRKKVmGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKEEQEEYIR 429
Cdd:cd01381   321 VKGIYGRLFIWIVNKINSAIykpRGTDSSRTSI-GVLDIFGFENFEVNSFEQLCINFANENLQQFFVRHIFKLEQEEYDK 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  430 EDIEWTHIDYFNNAIICDLIENNTNGILAMLDEECLRP-GtvTDETFLEKLNQVCATHQHFESRMSKcsrflNDTSlphs 508
Cdd:cd01381   400 EGINWQHIEFVDNQDVLDLIALKPMNIMSLIDEESKFPkG--TDQTMLEKLHSTHGNNKNYLKPKSD-----LNTS---- 468
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  509 cFRIQHYAGKVLYQVEGFVDKNNDLLYRDLSQAMWKAGHALIKSLF-PEGNPAKINLKRPPTAGSQFKASVATLMKNLQT 587
Cdd:cd01381   469 -FGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFnEDISMGSETRKKSPTLSSQFRKSLDQLMKTLSA 547
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  588 KNPNYIRCIKPNDKKAAHIFSEGLVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKMLCKQTWPHWKGPARSGVEVL 667
Cdd:cd01381   548 CQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVLVPGIPPAHKTDCRAATRKI 627
                         650       660
                  ....*....|....*....|.
gi 291391928  668 FNELEIPVEEYSFGRSKIFIR 688
Cdd:cd01381   628 CCAVLGGDADYQLGKTKIFLK 648
MYSc_Myo11 cd01384
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ...
34-688 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: 638.18  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928   34 NLKKRFDHNEIYTYIGSVVISVNPYRSLP-IYSPEKVEDYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITGESGA 112
Cdd:cd01384     6 NLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVSGESGA 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  113 GKTEASKLVMSYVAAVCGKGA-EVNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGGVISNYLLE 191
Cdd:cd01384    86 GKTETTKMLMQYLAYMGGRAVtEGRSVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAGRISGAAIRTYLLE 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  192 KSRVVKQPRGERNFHVFYQLLSGASEELLNKLKLErDFSRYNYLGL-DSARVNGVDDAANFRTVRNAMQIVGFMDHEVES 270
Cdd:cd01384   166 RSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLK-DPKQFHYLNQsKCFELDGVDDAEEYRATRRAMDVVGISEEEQDA 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  271 VLEVVAAVLKLGNIEFKPESRVnglDESKIKD---KNELKEICELTSIDQSVLERAFSFRTVEAKQEKVSTTLNVAQAYY 347
Cdd:cd01384   245 IFRVVAAILHLGNIEFSKGEED---DSSVPKDeksEFHLKAAAELLMCDEKALEDALCKRVIVTPDGIITKPLDPDAATL 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  348 ARDALAKNLYSRLFSWLVNRINESIkAQTKVRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKEEQEEY 427
Cdd:cd01384   322 SRDALAKTIYSRLFDWLVDKINRSI-GQDPNSKRLIGVLDIYGFESFKTNSFEQFCINLANEKLQQHFNQHVFKMEQEEY 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  428 IREDIEWTHIDYFNNAIICDLIENNTNGILAMLDEECLRPgTVTDETFLEKLNQVCATHQHFESrmSKCSRflndtslph 507
Cdd:cd01384   401 TKEEIDWSYIEFVDNQDVLDLIEKKPGGIIALLDEACMFP-RSTHETFAQKLYQTLKDHKRFSK--PKLSR--------- 468
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  508 SCFRIQHYAGKVLYQVEGFVDKNNDLLYRDLSQAMWKAGHALIKSLFPEGNPAKINLKRPPTA-GSQFKASVATLMKNLQ 586
Cdd:cd01384   469 TDFTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLFPPLPREGTSSSSKFSSiGSRFKQQLQELMETLN 548
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  587 TKNPNYIRCIKPNDKKAAHIFSEGLVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKMLCKQTwPHWKGPARSGVEV 666
Cdd:cd01384   549 TTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGLLAPEV-LKGSDDEKAACKK 627
                         650       660
                  ....*....|....*....|..
gi 291391928  667 LFNELEipVEEYSFGRSKIFIR 688
Cdd:cd01384   628 ILEKAG--LKGYQIGKTKVFLR 647
MYSc_Myo22 cd14883
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ...
29-688 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  Cd Length: 661  Bit Score: 632.44  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928   29 ETFINNLKKRFDHNEIYTYIGSVVISVNPYRSLPIYSPEKVEDYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITG 108
Cdd:cd14883     1 EGINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  109 ESGAGKTEASKLVMSYVAAVCGKGAEVNQvkeQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGGVISNY 188
Cdd:cd14883    81 ESGAGKTETTKLILQYLCAVTNNHSWVEQ---QILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGHIKGAIIQDY 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  189 LLEKSRVVKQPRGERNFHVFYQLLSGA--SEELLNKLKLeRDFSRYNYLGLD-SARVNGVDDAANFRTVRNAMQIVGFMD 265
Cdd:cd14883   158 LLEQSRITFQAPGERNYHVFYQLLAGAkhSKELKEKLKL-GEPEDYHYLNQSgCIRIDNINDKKDFDHLRLAMNVLGIPE 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  266 HEVESVLEVVAAVLKLGNIEFKpesrvnGLDESKI----KDKNELKEICELTSIDQSVLERAFSFRTVEAKQEKVSTTLN 341
Cdd:cd14883   237 EMQEGIFSVLSAILHLGNLTFE------DIDGETGaltvEDKEILKIVAKLLGVDPDKLKKALTIRQINVRGNVTEIPLK 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  342 VAQAYYARDALAKNLYSRLFSWLVNRINESIKAQTKvRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLK 421
Cdd:cd14883   311 VQEARDNRDAMAKALYSRTFAWLVNHINSCTNPGQK-NSRFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHYVFK 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  422 EEQEEYIREDIEWTHIDYFNNAIICDLIENNTNGILAMLDEECLRPgTVTDETFLEKLNQVCATHQHFEsrmsKCSRFLN 501
Cdd:cd14883   390 LEQEEYEKEGINWSHIVFTDNQECLDLIEKPPLGILKLLDEECRFP-KGTDLTYLEKLHAAHEKHPYYE----KPDRRRW 464
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  502 DTSlphscFRIQHYAGKVLYQVEGFVDKNNDLLYRDLSQAMWKAGHALIKSLF-PEGNPAKINL--------------KR 566
Cdd:cd14883   465 KTE-----FGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFtYPDLLALTGLsislggdttsrgtsKG 539
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  567 PPTAGSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFSEGLVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYK 646
Cdd:cd14883   540 KPTVGDTFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYL 619
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|..
gi 291391928  647 MLCKQTWPHWKGPARSGVEVLFNELEIPVEEYSFGRSKIFIR 688
Cdd:cd14883   620 CLDPRARSADHKETCGAVRALMGLGGLPEDEWQVGKTKVFLR 661
MYSc_Myo4 cd14872
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ...
32-650 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: 616.79  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928   32 INNLKKRFDHNEIYTYIGSVVISVNPYRSLPIYSPEKVEDYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITGESG 111
Cdd:cd14872     4 VHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISGESG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  112 AGKTEASKLVMSYVAAVCGkgaEVNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGGVISNYLLE 191
Cdd:cd14872    84 AGKTEATKQCLSFFAEVAG---STNGVEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRICGASTENYLLE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  192 KSRVVKQPRGERNFHVFYQLLSGASEELLNKLKLERDfsrYNYLGLDSA-RVNGVDDAANFRTVRNAMQIVGFMDHEVES 270
Cdd:cd14872   161 KSRVVYQIKGERNFHIFYQLLASPDPASRGGWGSSAA---YGYLSLSGCiEVEGVDDVADFEEVVLAMEQLGFDDADINN 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  271 VLEVVAAVLKLGNIEFKPESRVNGLDESKIKDKNELKEICELTSIDQSVLERAFSFRTVEAK-QEKVSTTLNVAQAYYAR 349
Cdd:cd14872   238 VMSLIAAILKLGNIEFASGGGKSLVSGSTVANRDVLKEVATLLGVDAATLEEALTSRLMEIKgCDPTRIPLTPAQATDAC 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  350 DALAKNLYSRLFSWLVNRINESIKAQTKVRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKEEQEEYIR 429
Cdd:cd14872   318 DALAKAAYSRLFDWLVKKINESMRPQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEKLQQHFNQYTFKLEEALYQS 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  430 EDIEWTHIDYFNNAIICDLIENNTNGILAMLDEECLRPGTvTDETFLEKLNQVCATHQHFESRMSKCSRFLndtslphsc 509
Cdd:cd14872   398 EGVKFEHIDFIDNQPVLDLIEKKQPGLMLALDDQVKIPKG-SDATFMIAANQTHAAKSTFVYAEVRTSRTE--------- 467
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  510 FRIQHYAGKVLYQVEGFVDKNNDLLYRDLSQAMWKAGHALIKSLFPEGNPAKINLKrpPTAGSQFKASVATLMKNLQTKN 589
Cdd:cd14872   468 FIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLFPPSEGDQKTSK--VTLGGQFRKQLSALMTALNATE 545
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 291391928  590 PNYIRCIKPNDKKAAHIFSEGLVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKMLCK 650
Cdd:cd14872   546 PHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKRYRFLVK 606
MYSc_Myo8 cd01383
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ...
34-688 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: 607.78  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928   34 NLKKRFDHNEIYTYIGSVVISVNPYRSLPIYSPEKVEDYRNRNfyELSPHIFALSDEAYRSLRDQDKDQCILITGESGAG 113
Cdd:cd01383     6 NLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYRQKL--LDSPHVYAVADTAYREMMRDEINQSIIISGESGAG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  114 KTEASKLVMSYVAAVCGKGaevNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGGVISNYLLEKS 193
Cdd:cd01383    84 KTETAKIAMQYLAALGGGS---SGIENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKICGAKIQTYLLEKS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  194 RVVKQPRGERNFHVFYQLLSGASEELLNKLKLeRDFSRYNYL-GLDSARVNGVDDAANFRTVRNAMQIVGFMDHEVESVL 272
Cdd:cd01383   161 RVVQLANGERSYHIFYQLCAGASPALREKLNL-KSASEYKYLnQSNCLTIDGVDDAKKFHELKEALDTVGISKEDQEHIF 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  273 EVVAAVLKLGNIEFkpeSRVNGLDESKIKDKNELKEICELTSIDQSVLERAFSFRTVEAKQEKVSTTLNVAQAYYARDAL 352
Cdd:cd01383   240 QMLAAVLWLGNISF---QVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKLTLQQAIDARDAL 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  353 AKNLYSRLFSWLVNRINESIKAQTKVRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKEEQEEYIREDI 432
Cdd:cd01383   317 AKAIYASLFDWLVEQINKSLEVGKRRTGRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLFKLEQEEYELDGI 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  433 EWTHIDYFNNAIICDLIENNTNGILAMLDEECLRPGTvTDETFLEKLNQVCATHQHFESRmskcsrflNDTSlphscFRI 512
Cdd:cd01383   397 DWTKVDFEDNQECLDLIEKKPLGLISLLDEESNFPKA-TDLTFANKLKQHLKSNSCFKGE--------RGGA-----FTI 462
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  513 QHYAGKVLYQVEGFVDKNNDLLYRDLSQAMWKAGHALIK---SLFPEGNPAKINLKRPPTAGSQfKASVAT--------L 581
Cdd:cd01383   463 RHYAGEVTYDTSGFLEKNRDLLHSDLIQLLSSCSCQLPQlfaSKMLDASRKALPLTKASGSDSQ-KQSVATkfkgqlfkL 541
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  582 MKNLQTKNPNYIRCIKPNDKKAAHIFSEGLVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKMLCKQTWPHWKGPAR 661
Cdd:cd01383   542 MQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLPEDVSASQDPLS 621
                         650       660
                  ....*....|....*....|....*....
gi 291391928  662 SGVEVL--FNeleIPVEEYSFGRSKIFIR 688
Cdd:cd01383   622 TSVAILqqFN---ILPEMYQVGYTKLFFR 647
MYSc_Myo15 cd01387
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ...
34-688 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  Cd Length: 657  Bit Score: 554.36  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928   34 NLKKRFDHNEIYTYIGSVVISVNPYRSLPIYSPEKVEDYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITGESGAG 113
Cdd:cd01387     6 NLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISGESGSG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  114 KTEASKLVMSYVAAVCGKGAevNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDfKGDPLGGVISNYLLEKS 193
Cdd:cd01387    86 KTEATKLIMQYLAAVNQRRN--NLVTEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFFE-GGVIVGAITSQYLLEKS 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  194 RVVKQPRGERNFHVFYQLLSGASEELLNKLKLErDFSRYNYLGLD-SARVNGVDDAANFRTVRNAMQIVGFMDHEVESVL 272
Cdd:cd01387   163 RIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQ-EAEKYFYLNQGgNCEIAGKSDADDFRRLLAAMQVLGFSSEEQDSIF 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  273 EVVAAVLKLGNIEFKPESRVNGLDESKIKDKNELKEICELTSIDQSVLERAFSFRTVEAKQEKVSTTLNVAQAYYARDAL 352
Cdd:cd01387   242 RILASVLHLGNVYFHKRQLRHGQEGVSVGSDAEIQWVAHLLQISPEGLQKALTFKVTETRRERIFTPLTIDQALDARDAI 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  353 AKNLYSRLFSWLVNRINESIKAQTKvRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKEEQEEYIREDI 432
Cdd:cd01387   322 AKALYALLFSWLVTRVNAIVYSGTQ-DTLSIAILDIFGFEDLSENSFEQLCINYANENLQYYFNKHVFKLEQEEYIREQI 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  433 EWTHIDYFNNAIICDLIENNTNGILAMLDEECLRPgTVTDETFLEKlnqvCATHQHFESRMSKcsrflndTSLPHSCFRI 512
Cdd:cd01387   401 DWTEIAFADNQPVINLISKKPVGILHILDDECNFP-QATDHSFLEK----CHYHHALNELYSK-------PRMPLPEFTI 468
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  513 QHYAGKVLYQVEGFVDKNNDLLYRDLSQAMWKAGHALIKSLFPE------------GNPAKINLK-RPPTAGSQFKASVA 579
Cdd:cd01387   469 KHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSShraqtdkapprlGKGRFVTMKpRTPTVAARFQDSLL 548
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  580 TLMKNLQTKNPNYIRCIKPNDKKAAHIFSEGLVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKMLCKQTWPHwKGP 659
Cdd:cd01387   549 QLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYRCLVALKLPR-PAP 627
                         650       660       670
                  ....*....|....*....|....*....|
gi 291391928  660 ARSGVEVLFNELE-IPVEEYSFGRSKIFIR 688
Cdd:cd01387   628 GDMCVSLLSRLCTvTPKDMYRLGATKVFLR 657
MYSc_Myo29 cd14890
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ...
29-688 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  Cd Length: 662  Bit Score: 552.46  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928   29 ETFINNLKKRFDHNEIYTYIGSVVISVNPYRSLP-IYSPEKVEDYRNRNFYELSPHIFALSDEAYRSLRDQD----KDQC 103
Cdd:cd14890     1 ASLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQSGvldpSNQS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  104 ILITGESGAGKTEASKLVMSYVAAVCGK----------------GAEVNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFG 167
Cdd:cd14890    81 IIISGESGAGKTEATKIIMQYLARITSGfaqgasgegeaaseaiEQTLGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  168 KYMDIEFDFKGDPLGGVISNYLLEKSRVVKQPRGERNFHVFYQLLSGASEELLNKLKLERDfSRYNYLGLDSARVNGVDD 247
Cdd:cd14890   161 KFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTP-VEYFYLRGECSSIPSCDD 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  248 AANFRTVRNAMQIVGFMDHEVESVLEVVAAVLKLGNIEFKPESRVNGLdeSKIKDKNELKEICELTSIDQSVLERAFSFR 327
Cdd:cd14890   240 AKAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTVL--EDATTLQSLKLAAELLGVNEDALEKALLTR 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  328 TVEAKQEKVSTTLNVAQAYYARDALAKNLYSRLFSWLVNRINESIkAQTKVRKKVMGVLDIYGFEIFEDNSFEQFIINYC 407
Cdd:cd14890   318 QLFVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTI-SSPDDKWGFIGVLDIYGFEKFEWNTFEQLCINYA 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  408 NEKLQQIFIELTLKEEQEEYIREDIEWTHIDYFNNAIICDLIENNTN---GILAMLDEECLRPGTVTDETFLEKLNQV-- 482
Cdd:cd14890   397 NEKLQRHFNQHMFEVEQVEYSNEGIDWQYITFNDNQACLELIEGKVNgkpGIFITLDDCWRFKGEEANKKFVSQLHASfg 476
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  483 -----------CATHQHFESrmskcSRFLNDTSlphscFRIQHYAGKVLYQVEGFVDKNNDLLYRDLSQAMWKAGHALik 551
Cdd:cd14890   477 rksgsggtrrgSSQHPHFVH-----PKFDADKQ-----FGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSRRSI-- 544
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  552 slfpegnpakinlkRPPTAGSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFSEGLVCHQIRYLGLLENVRVRRAG 631
Cdd:cd14890   545 --------------REVSVGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGMMEAIQIRQQG 610
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  632 YAFRQAYEPCLERYKMLCKQtwphwkgpARSG---VEVLFNELEIPVEEYSFGRSKIFIR 688
Cdd:cd14890   611 FALREEHDSFFYDFQVLLPT--------AENIeqlVAVLSKMLGLGKADWQIGSSKIFLK 662
MYSc_Myo6 cd01382
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ...
30-688 9.30e-180

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: 545.69  E-value: 9.30e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928   30 TFINNLKKRFDHNEIYTYIGSVVISVNPYRSLP-IYSPEKVEDYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITG 108
Cdd:cd01382     2 TLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVSG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  109 ESGAGKTEASKLVMSYVAAVCGKGAevNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGGVISNY 188
Cdd:cd01382    82 ESGAGKTESTKYILRYLTESWGSGA--GPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVGGFVSHY 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  189 LLEKSRVVKQPRGERNFHVFYQLLSGASEELLNKLklerdfsrynylgldsARVNGVDDAANFRTVRNAMQIVGFMDHEV 268
Cdd:cd01382   160 LLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKL----------------LKDPLLDDVGDFIRMDKAMKKIGLSDEEK 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  269 ESVLEVVAAVLKLGNIEFKpESRVNGLDESKIKDKNE--LKEICELTSIDQSVLERAFSFRTVEAKQEKVSTT-----LN 341
Cdd:cd01382   224 LDIFRVVAAVLHLGNIEFE-ENGSDSGGGCNVKPKSEqsLEYAAELLGLDQDELRVSLTTRVMQTTRGGAKGTvikvpLK 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  342 VAQAYYARDALAKNLYSRLFSWLVNRINESIKAQTKVrkKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLK 421
Cdd:cd01382   303 VEEANNARDALAKAIYSKLFDHIVNRINQCIPFETSS--YFIGVLDIAGFEYFEVNSFEQFCINYCNEKLQQFFNERILK 380
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  422 EEQEEYIREDIEWTHIDYFNNAIICDLIENNTNGILAMLDEECLRPgTVTDETFLEKLNQVCATHQHFES-RMSKCS--R 498
Cdd:cd01382   381 EEQELYEKEGLGVKEVEYVDNQDCIDLIEAKLVGILDLLDEESKLP-KPSDQHFTSAVHQKHKNHFRLSIpRKSKLKihR 459
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  499 FLNDtslpHSCFRIQHYAGKVLYQVEGFVDKNNDLLYRDLSQAMWKAGHALIKSLFPEGNPA---------KINLKrppT 569
Cdd:cd01382   460 NLRD----DEGFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFESSTNNnkdskqkagKLSFI---S 532
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  570 AGSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFSEGLVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYK--- 646
Cdd:cd01382   533 VGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRTSFHDLYNMYKkyl 612
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|..
gi 291391928  647 ----------MLCKqtwphwkgparsgveVLFNELEIPVEEYSFGRSKIFIR 688
Cdd:cd01382   613 ppklarldprLFCK---------------ALFKALGLNENDFKFGLTKVFFR 649
MYSc_Myo40 cd14901
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ...
30-687 3.11e-177

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  Cd Length: 655  Bit Score: 539.38  E-value: 3.11e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928   30 TFINNLKKRFDHNEIYTYIGSVVISVNPYRSLPIYSPEKVEDY------RNRNFYELSPHIFALSDEAYRSL----RDQD 99
Cdd:cd14901     2 SILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMlfasRGQK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  100 KDQCILITGESGAGKTEASKLVMSYVAAVC------GKGAEVNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIE 173
Cdd:cd14901    82 CDQSILVSGESGAGKTETTKIIMNYLASVSsatthgQNATERENVRDRVLESNPILEAFGNARTNRNNNSSRFGKFIRLG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  174 FDFKGDPLGGVISNYLLEKSRVVKQPRGERNFHVFYQLLSGASEELLNKLKLErDFSRYNYL----GLDsaRVNGVDDAA 249
Cdd:cd14901   162 FASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLT-HVEEYKYLnssqCYD--RRDGVDDSV 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  250 NFRTVRNAMQIVGFMDHEVESVLEVVAAVLKLGNIEFKPESRVNGldESKIKDKNELKEICELTSIDQSVLERAFSFRTV 329
Cdd:cd14901   239 QYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFVKKDGEGG--TFSMSSLANVRAACDLLGLDMDVLEKTLCTREI 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  330 EAKQEKVSTTLNVAQAYYARDALAKNLYSRLFSWLVNRINESIK-AQTKVRKKVMGVLDIYGFEIFEDNSFEQFIINYCN 408
Cdd:cd14901   317 RAGGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAySESTGASRFIGIVDIFGFEIFATNSLEQLCINFAN 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  409 EKLQQIFIELTLKEEQEEYIREDIEWTHIDYFNNAIICDLIENNTNGILAMLDEECLRPGTvTDETFLEKLNQVCATHQH 488
Cdd:cd14901   397 EKLQQLFGKFVFEMEQDEYVAEAIPWTFVEYPNNDACVAMFEARPTGLFSLLDEQCLLPRG-NDEKLANKYYDLLAKHAS 475
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  489 FESrmSKCSRFLNdtslphsCFRIQHYAGKVLYQVEGFVDKNNDLLYRDLSQAMWKAGHALIkslfpegnpakinlkrPP 568
Cdd:cd14901   476 FSV--SKLQQGKR-------QFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFL----------------SS 530
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  569 TAGSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFSEGLVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKML 648
Cdd:cd14901   531 TVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFPHDAFVHTYSCL 610
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*
gi 291391928  649 CKQTwPHWKGPARSGVEVLFNELEIPV------EEYSFGRSKIFI 687
Cdd:cd14901   611 APDG-ASDTWKVNELAERLMSQLQHSElniehlPPFQVGKTKVFL 654
MYSc_Myo36 cd14897
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ...
29-688 1.11e-176

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  Cd Length: 635  Bit Score: 536.97  E-value: 1.11e-176
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928   29 ETFINNLKKRFDHNEIYTYIGSVVISVNPYRSLPIYSPEKVEDYRNRNF-YELSPHIFALSDEAYRSLRDQDKDQCILIT 107
Cdd:cd14897     1 NTIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSVrSQRPPHLFWIADQAYRRLLETGRNQCILVS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  108 GESGAGKTEASKLVMSYVAAVCGKgaEVNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGGVISN 187
Cdd:cd14897    81 GESGAGKTESTKYMIKHLMKLSPS--DDSDLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQLLGAKIDD 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  188 YLLEKSRVVKQPRGERNFHVFYQLLSGASEELLNKLKLErDFSRYNYLGlDSARVNGVDDAAN--------FRTVRNAMQ 259
Cdd:cd14897   159 YLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLE-DPDCHRILR-DDNRNRPVFNDSEeleyyrqmFHDLTNIMK 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  260 IVGFMDHEVESVLEVVAAVLKLGNIEFKPESRVNGLdesKIKDKNELKEICELTSIDQSVLERAFSFRTVEAKQEKVSTT 339
Cdd:cd14897   237 LIGFSEEDISVIFTILAAILHLTNIVFIPDEDTDGV---TVADEYPLHAVAKLLGIDEVELTEALISNVNTIRGERIQSW 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  340 LNVAQAYYARDALAKNLYSRLFSWLVNRINESIKAQTKVRKKV----MGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIF 415
Cdd:cd14897   314 KSLRQANDSRDALAKDLYSRLFGWIVGQINRNLWPDKDFQIMTrgpsIGILDMSGFENFKINSFDQLCINLSNERLQQYF 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  416 IELTLKEEQEEYIREDIEWTHIDYFNNAIICDLIENNTNGILAMLDEECLRPGTvTDETFLEKLNQVCATHQHFESRMSK 495
Cdd:cd14897   394 NDYVFPRERSEYEIEGIEWRDIEYHDNDDVLELFFKKPLGILPLLDEESTFPQS-TDSSLVQKLNKYCGESPRYVASPGN 472
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  496 csrflndtslpHSCFRIQHYAGKVLYQVEGFVDKNNDLLYRDLSQAMWKAGHALIKSLFPegnpakinlkrpptagSQFK 575
Cdd:cd14897   473 -----------RVAFGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLFT----------------SYFK 525
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  576 ASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFSEGLVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKMLCKQTWPH 655
Cdd:cd14897   526 RSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYEDFVKRYKEICDFSNKV 605
                         650       660       670
                  ....*....|....*....|....*....|...
gi 291391928  656 WKGPARSGVEVLFNELeipVEEYSFGRSKIFIR 688
Cdd:cd14897   606 RSDDLGKCQKILKTAG---IKGYQFGKTKVFLK 635
MYSc_Myo9 cd01385
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ...
29-688 1.69e-175

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  Cd Length: 690  Bit Score: 535.80  E-value: 1.69e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928   29 ETFINNLKKRFDHNEIYTYIGSVVISVNPYRSLPIYSPEKVEDYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITG 108
Cdd:cd01385     1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  109 ESGAGKTEASKLVMSYVAAVCGKGAEVNqVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGGVISNY 188
Cdd:cd01385    81 ESGSGKTESTNFLLHHLTALSQKGYGSG-VEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRGAVVEKY 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  189 LLEKSRVVKQPRGERNFHVFYQLLSGASEELLNKLKLERDfSRYNYLG-LDSARVNGVDDAANFRTVRNAMQIVGFMDHE 267
Cdd:cd01385   160 LLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQP-EDYHYLNqSDCYTLEGEDEKYEFERLKQAMEMVGFLPET 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  268 VESVLEVVAAVLKLGNIEFKPEsRVNGLDESKIKDKNELKEICELTSIDQSVLERAFSFRTVEAKQEKVSTTLNVAQAYY 347
Cdd:cd01385   239 QRQIFSVLSAVLHLGNIEYKKK-AYHRDESVTVGNPEVLDIISELLRVKEETLLEALTTKKTVTVGETLILPYKLPEAIA 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  348 ARDALAKNLYSRLFSWLVNRINE---SIKAQTKVRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKEEQ 424
Cdd:cd01385   318 TRDAMAKCLYSALFDWIVLRINHallNKKDLEEAKGLSIGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQHIFKLEQ 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  425 EEYIREDIEWTHIDYFNNAIICDLIENNTNGILAMLDEECLRPGTvTDETFLEKLNQVCATHQHFESrmskcsrflndTS 504
Cdd:cd01385   398 EEYKKEGISWHNIEYTDNTGCLQLISKKPTGLLCLLDEESNFPGA-TNQTLLAKFKQQHKDNKYYEK-----------PQ 465
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  505 LPHSCFRIQHYAGKVLYQVEGFVDKNNDLLYRDLSQAM---------------------WKAGHALIKSLFP-------- 555
Cdd:cd01385   466 VMEPAFIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLrssssafvreligidpvavfrWAVLRAFFRAMAAfreagrrr 545
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  556 ---EGNPAKINL-------------KRPPTAGSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFSEGLVCHQIRYL 619
Cdd:cd01385   546 aqrTAGHSLTLHdrttksllhlhkkKKPPSVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVLRQLRYT 625
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 291391928  620 GLLENVRVRRAGYAFRQAYEPCLERYKMLCkqtwPHWKGPARSGVEVLFNELEIPVEEYSFGRSKIFIR 688
Cdd:cd01385   626 GMLETVRIRRSGYSVRYTFQEFITQFQVLL----PKGLISSKEDIKDFLEKLNLDRDNYQIGKTKVFLK 690
MYSc_Myo10 cd14873
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ...
34-688 1.24e-171

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  Cd Length: 651  Bit Score: 524.36  E-value: 1.24e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928   34 NLKKRFDHNEIYTYIGSVVISVNPYRSLP-IYSPEKVEDYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITGESGA 112
Cdd:cd14873     6 NLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILISGESGA 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  113 GKTEASKL------VMSYVAAVCGKGAEVNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGGVIS 186
Cdd:cd14873    86 GKTESTKLilkflsVISQQSLELSLKEKTSCVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNIQGGRIV 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  187 NYLLEKSRVVKQPRGERNFHVFYQLLSGASEELLNKLKLErDFSRYNYLGlDSARVN--GVDDAANFRTVRNAMQIVGFM 264
Cdd:cd14873   166 DYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLS-TPENYHYLN-QSGCVEdkTISDQESFREVITAMEVMQFS 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  265 DHEVESVLEVVAAVLKLGNIEFKPESrvngldESKIKDKNELKEICELTSIDQSVLERAFSFRTVEAKQEKVSTTLNVAQ 344
Cdd:cd14873   244 KEEVREVSRLLAGILHLGNIEFITAG------GAQVSFKTALGRSAELLGLDPTQLTDALTQRSMFLRGEEILTPLNVQQ 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  345 AYYARDALAKNLYSRLFSWLVNRINESIKAQTKVrkKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKEEQ 424
Cdd:cd14873   318 AVDSRDSLAMALYARCFEWVIKKINSRIKGKEDF--KSIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKHIFSLEQ 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  425 EEYIREDIEWTHIDYFNNAIICDLIENNTnGILAMLDEECLRPgTVTDETFLEKLNQVCATHQHF-ESRMSKcsrflndt 503
Cdd:cd14873   396 LEYSREGLVWEDIDWIDNGECLDLIEKKL-GLLALINEESHFP-QATDSTLLEKLHSQHANNHFYvKPRVAV-------- 465
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  504 slphSCFRIQHYAGKVLYQVEGFVDKNNDLLYRDLSQAMWKAGHALIKSLFP-------EGNPAKINLKRPPTAGSQFKA 576
Cdd:cd14873   466 ----NNFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEhvssrnnQDTLKCGSKHRRPTVSSQFKD 541
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  577 SVATLMKNLQTKNPNYIRCIKPNDKKAAHIFSEGLVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKMLCKQTwpHW 656
Cdd:cd14873   542 SLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMRNL--AL 619
                         650       660       670
                  ....*....|....*....|....*....|..
gi 291391928  657 KGPARSGVEVLFNELEIPVEEYSFGRSKIFIR 688
Cdd:cd14873   620 PEDVRGKCTSLLQLYDASNSEWQLGKTKVFLR 651
MYSc_Myh10 cd14920
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ...
30-688 1.66e-169

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  Cd Length: 673  Bit Score: 519.57  E-value: 1.66e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928   30 TFINNLKKRFDHNEIYTYIGSVVISVNPYRSLPIYSPEKVEDYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITGE 109
Cdd:cd14920     2 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  110 SGAGKTEASKLVMSYVAAVCGK------GAEVNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGG 183
Cdd:cd14920    82 SGAGKTENTKKVIQYLAHVASShkgrkdHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  184 VISNYLLEKSRVVKQPRGERNFHVFYQLLSGASEELLNKLKLErDFSRYNYLGLDSARVNGVDDAANFRTVRNAMQIVGF 263
Cdd:cd14920   162 NIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLE-GFNNYRFLSNGYIPIPGQQDKDNFQETMEAMHIMGF 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  264 MDHEVESVLEVVAAVLKLGNIEFKPESRVnglDESKIKDKNELKEICELTSIDQSVLERAFSFRTVEAKQEKVSTTLNVA 343
Cdd:cd14920   241 SHEEILSMLKVVSSVLQFGNISFKKERNT---DQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKE 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  344 QAYYARDALAKNLYSRLFSWLVNRINESIKAQTKVRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKEE 423
Cdd:cd14920   318 QADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILE 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  424 QEEYIREDIEWTHIDYFNNAIIC-DLIENNTN--GILAMLDEECLRPgTVTDETFLEKLNQVCATHQHFESrmskcSRFL 500
Cdd:cd14920   398 QEEYQREGIEWNFIDFGLDLQPCiDLIERPANppGVLALLDEECWFP-KATDKTFVEKLVQEQGSHSKFQK-----PRQL 471
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  501 NDtslpHSCFRIQHYAGKVLYQVEGFVDKN----NDLLYRDLSQA-------MWKAGHALIKS---------LFPEGNPA 560
Cdd:cd14920   472 KD----KADFCIIHYAGKVDYKADEWLMKNmdplNDNVATLLHQSsdrfvaeLWKDVDRIVGLdqvtgmtetAFGSAYKT 547
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  561 KINLKRppTAGSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFSEGLVCHQIRYLGLLENVRVRRAGYAFRQAYEP 640
Cdd:cd14920   548 KKGMFR--TVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQE 625
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*...
gi 291391928  641 CLERYKMLCKQTWPHWKGPARSGVEVLFNELEIPVEEYSFGRSKIFIR 688
Cdd:cd14920   626 FRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
MYSc_Myo42 cd14903
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ...
34-688 1.14e-168

class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276868  Cd Length: 658  Bit Score: 517.02  E-value: 1.14e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928   34 NLKKRFDHNEIYTYIGSVVISVNPYRSLP-IYSPEKVEDYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITGESGA 112
Cdd:cd14903     6 NVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVSGESGA 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  113 GKTEASKLVMSYVAAVCGkGAEvNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGGVISNYLLEK 192
Cdd:cd14903    86 GKTETTKILMNHLATIAG-GLN-DSTIKKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKNGTLVGAKCRTYLLEK 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  193 SRVVKQPRGERNFHVFYQLLSGASEEllNKLKLERDfSRYNYLGLDSAR-VNGVDDAANFRTVRNAMQIVGFMDHEVESV 271
Cdd:cd14903   164 TRVISHERPERNYHIFYQLLASPDVE--ERLFLDSA-NECAYTGANKTIkIEGMSDRKHFARTKEALSLIGVSEEKQEVL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  272 LEVVAAVLKLGNIEFKPEsrvNGLDESKI--KDKNELKEICELTSIDQSVLERAFSFRTVEAKQEKVSTTLNVAQAYYAR 349
Cdd:cd14903   241 FEVLAGILHLGQLQIQSK---PNDDEKSAiaPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDVYTVPLKKDQAEDCR 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  350 DALAKNLYSRLFSWLVNRINESIKAQTKVRKKVmGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKEEQEEYIR 429
Cdd:cd14903   318 DALAKAIYSNVFDWLVATINASLGNDAKMANHI-GVLDIFGFEHFKHNSFEQFCINYANEKLQQKFTQDVFKTVQIEYEE 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  430 EDIEWTHIDYFNNAIICDLIENNTnGILAMLDEECLRPGTvTDETFLEKLNQVCATHQHFeSRMSKCSRFLndtslphsc 509
Cdd:cd14903   397 EGIRWAHIDFADNQDVLAVIEDRL-GIISLLNDEVMRPKG-NEESFVSKLSSIHKDEQDV-IEFPRTSRTQ--------- 464
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  510 FRIQHYAGKVLYQVEGFVDKNNDLLYRDLSQAMWKAGHALIKSLFPEG----NPAKINLKRP-----------PTAGSQF 574
Cdd:cd14903   465 FTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKEKvespAAASTSLARGarrrrggalttTTVGTQF 544
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  575 KASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFSEGLVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKMLCKQTwP 654
Cdd:cd14903   545 KDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWLFLPEG-R 623
                         650       660       670
                  ....*....|....*....|....*....|....*.
gi 291391928  655 HWKGPARSGVEVLFN--ELEIPvEEYSFGRSKIFIR 688
Cdd:cd14903   624 NTDVPVAERCEALMKklKLESP-EQYQMGLTRIYFQ 658
MYSc_Myo3 cd01379
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ...
29-688 8.94e-168

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  Cd Length: 633  Bit Score: 513.75  E-value: 8.94e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928   29 ETFINNLKKRFDHNEIYTYIGSVVISVNPYRSLPIYSPEKVEDYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITG 108
Cdd:cd01379     1 DTIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  109 ESGAGKTEASKLVMSYVAAVcGKGAEVNqVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGGVISNY 188
Cdd:cd01379    81 ESGAGKTESANLLVQQLTVL-GKANNRT-LEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAVTGARISEY 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  189 LLEKSRVVKQPRGERNFHVFYQLLSG-ASEELLNKLKLErDFSRYNYLGLDSARV-NGVDDAAN---FRTVRNAMQIVGF 263
Cdd:cd01379   159 LLEKSRVVHQAIGERNFHIFYYIYAGlAEDKKLAKYKLP-ENKPPRYLQNDGLTVqDIVNNSGNrekFEEIEQCFKVIGF 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  264 MDHEVESVLEVVAAVLKLGNIEFKP-ESRVNGLDESKIKDKNELKEICELTSIDQSVLERAFSFRTVEAKQEKVSTTLNV 342
Cdd:cd01379   238 TKEEVDSVYSILAAILHIGDIEFTEvESNHQTDKSSRISNPEALNNVAKLLGIEADELQEALTSHSVVTRGETIIRNNTV 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  343 AQAYYARDALAKNLYSRLFSWLVNRINESIKAQTKVRKKVM--GVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTL 420
Cdd:cd01379   318 EEATDARDAMAKALYGRLFSWIVNRINSLLKPDRSASDEPLsiGILDIFGFENFQKNSFEQLCINIANEQIQYYFNQHIF 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  421 KEEQEEYIREDIEWTHIDYFNNAIICDLIENNTNGILAMLDEECLRPGTvTDETFLEKLnqvcatHQHFesrmsKCSRFl 500
Cdd:cd01379   398 AWEQQEYLNEGIDVDLIEYEDNRPLLDMFLQKPMGLLALLDEESRFPKA-TDQTLVEKF------HNNI-----KSKYY- 464
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  501 ndtSLPHS---CFRIQHYAGKVLYQVEGFVDKNNDLLYRDLSQAMWKAGHALIKSlfpegnpakinlkrppTAGSQFKAS 577
Cdd:cd01379   465 ---WRPKSnalSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVRQ----------------TVATYFRYS 525
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  578 VATLMKNLQTKNPNYIRCIKPNDKKAAHIFSEGLVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKMLCkQTWPHWK 657
Cdd:cd01379   526 LMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRILFADFLKRYYFLA-FKWNEEV 604
                         650       660       670
                  ....*....|....*....|....*....|.
gi 291391928  658 GPARSGVEVLFNELEIpvEEYSFGRSKIFIR 688
Cdd:cd01379   605 VANRENCRLILERLKL--DNWALGKTKVFLK 633
MYSc_Myo46 cd14907
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ...
32-688 1.22e-164

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  Cd Length: 669  Bit Score: 506.88  E-value: 1.22e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928   32 INNLKKRFDHNEIYTYIGSVVISVNPYRSLP-IYSPEKVEDYRNR--------NFYELSPHIFALSDEAYRSLRDQDKDQ 102
Cdd:cd14907     4 LINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEQiiqngeyfDIKKEPPHIYAIAALAFKQLFENNKKQ 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  103 CILITGESGAGKTEASKLVMSYVAAVCGK-----------------GAEVNQVKEQLLQSNPVLEAFGNAKTVRNDNSSR 165
Cdd:cd14907    84 AIVISGESGAGKTENAKYAMKFLTQLSQQeqnseevltltssiratSKSTKSIEQKILSCNPILEAFGNAKTVRNDNSSR 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  166 FGKYMDIEFDFK-GDPLGGVISNYLLEKSRVVKQPRGERNFHVFYQLLSGASEELLNKLKLERDFSRYNYLGL---DSAR 241
Cdd:cd14907   164 FGKYVSILVDKKkRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLKNQLSGDRYDYLkksNCYE 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  242 VNGVDDAANFRTVRNAMQIVGFMDHEVESVLEVVAAVLKLGNIEFKpESRVNGLDESKIKDKNELKEICELTSIDQSVLE 321
Cdd:cd14907   244 VDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFD-DSTLDDNSPCCVKNKETLQIIAKLLGIDEEELK 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  322 RAFSFRTVEAKQEKVSTTLNVAQAYYARDALAKNLYSRLFSWLVNRINESI-------KAQTKVRKKVMGVLDIYGFEIF 394
Cdd:cd14907   323 EALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpkdekdQQLFQNKYLSIGLLDIFGFEVF 402
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  395 EDNSFEQFIINYCNEKLQQIFIELTLKEEQEEYIREDIE--WTHIDYFNNAIICDLIENNTNGILAMLDEECLRpGTVTD 472
Cdd:cd14907   403 QNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEdyLNQLSYTDNQDVIDLLDKPPIGIFNLLDDSCKL-ATGTD 481
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  473 ETFLEKLnqvCATHQHFesrmskcSRFLNDTSLPHSCFRIQHYAGKVLYQVEGFVDKNNDLLYRDLSQAMWKAGHALIKS 552
Cdd:cd14907   482 EKLLNKI---KKQHKNN-------SKLIFPNKINKDTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISS 551
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  553 LF--------PEGNPAKINLKRPPTAGSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFSEGLVCHQIRYLGLLEN 624
Cdd:cd14907   552 IFsgedgsqqQNQSKQKKSQKKDKFLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYLGVLES 631
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 291391928  625 VRVRRAGYAFRQAYEPCLERYKMLCKQtwphwkgparsgvevlfneleipveeYSFGRSKIFIR 688
Cdd:cd14907   632 IRVRKQGYPYRKSYEDFYKQYSLLKKN--------------------------VLFGKTKIFMK 669
MYSc_Myo27 cd14888
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ...
32-648 2.07e-164

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  Cd Length: 667  Bit Score: 506.15  E-value: 2.07e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928   32 INNLKKRFDHNEIYTYIGSVVISVNPYRSLP-IYSPEKVEDYRNRNfYELSPHIFALSDEAYRSLRDQDKDQCILITGES 110
Cdd:cd14888     4 LHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFIQPS-ISKSPHVFSTASSAYQGMCNNKKSQTILISGES 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  111 GAGKTEASKLVMSYVAAVcGKGAEVN--QVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDF---------KGD 179
Cdd:cd14888    83 GAGKTESTKYVMKFLACA-GSEDIKKrsLVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFSKlkskrmsgdRGR 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  180 PLGGVISNYLLEKSRVVKQPRGERNFHVFYQLLSGASE--------------------ELLNKLKLERDFSRYNYLGLDS 239
Cdd:cd14888   162 LCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAREakntglsyeendeklakgadAKPISIDMSSFEPHLKFRYLTK 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  240 ARV---NGVDDAANFRTVRNAMQIVGFMDHEVESVLEVVAAVLKLGNIEFK-PESRVNGLDESKIKDKNeLKEICELTSI 315
Cdd:cd14888   242 SSChelPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFEnNEACSEGAVVSASCTDD-LEKVASLLGV 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  316 DQSVLERAFSFRTVEAKQEKVSTTLNVAQAYYARDALAKNLYSRLFSWLVNRINESIKAQTKVRKKVMGVLDIYGFEIFE 395
Cdd:cd14888   321 DAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGYSKDNSLLFCGVLDIFGFECFQ 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  396 DNSFEQFIINYCNEKLQQIFIELTLKEEQEEYIREDIEWTHIDYFNNAIICDLIENNTNGILAMLDEECLRPGTvTDETF 475
Cdd:cd14888   401 LNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFPDNQDCVDLLQEKPLGIFCMLDEECFVPGG-KDQGL 479
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  476 LEKLNQVCATHQHFESRMSKcsrflndtslpHSCFRIQHYAGKVLYQVEGFVDKNNDLLYRDLSQAMWKAG----HALIK 551
Cdd:cd14888   480 CNKLCQKHKGHKRFDVVKTD-----------PNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKnpfiSNLFS 548
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  552 SLFPEGNPAKINLKRPPTAGSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFSEGLVCHQIRYLGLLENVRVRRAG 631
Cdd:cd14888   549 AYLRRGTDGNTKKKKFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQLKYGGVLQAVQVSRAG 628
                         650
                  ....*....|....*..
gi 291391928  632 YAFRQAYEPCLERYKML 648
Cdd:cd14888   629 YPVRLSHAEFYNDYRIL 645
MYSc_Myo31 cd14892
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ...
32-688 9.09e-161

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  Cd Length: 656  Bit Score: 496.20  E-value: 9.09e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928   32 INNLKKRFDHNEIYTYIGSVVISVNPYRSLP-IYS-PEKVEDYRNRNFYELS-PHIFALSDEAYRSLR----DQDKDQCI 104
Cdd:cd14892     4 LDVLRRRYERDAIYTFTADILISINPYKSIPlLYDvPGFDSQRKEEATASSPpPHVFSIAERAYRAMKgvgkGQGTPQSI 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  105 LITGESGAGKTEASKLVMSYVA--------AVCGKGAEV--NQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEF 174
Cdd:cd14892    84 VVSGESGAGKTEASKYIMKYLAtasklakgASTSKGAANahESIEECVLLSNLILEAFGNAKTIRNDNSSRFGKYIQIHY 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  175 DFKGDPLGGVISNYLLEKSRVVKQPRGERNFHVFYQLLSGASEELLNKLKLErDFSRYNYLGLDSA-RVNGVDDAANFRT 253
Cdd:cd14892   164 NSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELT-PAESFLFLNQGNCvEVDGVDDATEFKQ 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  254 VRNAMQIVGFMDHEVESVLEVVAAVLKLGNIEFKPESRVNGLDeSKIKDKNELKEICELTSIDQSVLERAFSFRT-VEAK 332
Cdd:cd14892   243 LRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEENADDEDVF-AQSADGVNVAKAAGLLGVDAAELMFKLVTQTtSTAR 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  333 QEKVSTTLNVAQAYYARDALAKNLYSRLFSWLVNRINESIKAQTKV---------RKKVMGVLDIYGFEIFEDNSFEQFI 403
Cdd:cd14892   322 GSVLEIKLTAREAKNALDALCKYLYGELFDWLISRINACHKQQTSGvtggaasptFSPFIGILDIFGFEIMPTNSFEQLC 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  404 INYCNEKLQQIFIELTLKEEQEEYIREDIEWTHIDYFNNAIICDLIENNTNGILAMLDEECLRPGTVTDETFLEKLNQV- 482
Cdd:cd14892   402 INFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQDNQDCLDLIQKKPLGLLPLLEEQMLLKRKTTDKQLLTIYHQTh 481
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  483 CATHQHFESRmskcsRFLNDTslphscFRIQHYAGKVLYQVEGFVDKNNDLLYRDLsqamwkaghalikslfpegnpakI 562
Cdd:cd14892   482 LDKHPHYAKP-----RFECDE------FVLRHYAGDVTYDVHGFLAKNNDNLHDDL-----------------------R 527
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  563 NLKRpptAGSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFSEGLVCHQIRYLGLLENVRVRRAGYAFRQAYEPCL 642
Cdd:cd14892   528 DLLR---SSSKFRTQLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVRIRREGFPIRRQFEEFY 604
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|..
gi 291391928  643 ERYKMLCKQTWPHWKGPARSGVEVLFNELE------IPVEEYSFGRSKIFIR 688
Cdd:cd14892   605 EKFWPLARNKAGVAASPDACDATTARKKCEeivaraLERENFQLGRTKVFLR 656
MYSc_Myh2_insects_mollusks cd14911
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ...
32-688 3.48e-155

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  Cd Length: 674  Bit Score: 482.17  E-value: 3.48e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928   32 INNLKKRFDHNEIYTYIGSVVISVNPYRSLPIYSPEKVEDYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITGESG 111
Cdd:cd14911     4 LHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTGESG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  112 AGKTEASKLV---MSYVAAVCGKGA------------EVNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDF 176
Cdd:cd14911    84 AGKTENTKKViqfLAYVAASKPKGSgavphpavnpavLIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDA 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  177 KGDPLGGVISNYLLEKSRVVKQPRGERNFHVFYQLLSGASEELLNKLKLErDFSRYNYLGLDSARVNGVDDAANFRTVRN 256
Cdd:cd14911   164 SGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILD-DVKSYAFLSNGSLPVPGVDDYAEFQATVK 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  257 AMQIVGFMDHEVESVLEVVAAVLKLGNIEFKPEsRVNglDESKIKDKNELKEICELTSIDQSVLERAFSFRTVEAKQEKV 336
Cdd:cd14911   243 SMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQE-RNN--DQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFV 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  337 STTLNVAQAYYARDALAKNLYSRLFSWLVNRINESIKAQTKVRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFI 416
Cdd:cd14911   320 TKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFN 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  417 ELTLKEEQEEYIREDIEWTHIDY-FNNAIICDLIENNTnGILAMLDEECLRPgTVTDETFLEKLNQVCATHQHFesrMSK 495
Cdd:cd14911   400 HTMFILEQEEYQREGIEWKFIDFgLDLQPTIDLIDKPG-GIMALLDEECWFP-KATDKTFVDKLVSAHSMHPKF---MKT 474
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  496 CSRFLNDtslphscFRIQHYAGKVLYQVEGFVDKNNDLLYRDLSQAM-----------WK-------AGHALIKSLFpeG 557
Cdd:cd14911   475 DFRGVAD-------FAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLqgsqdpfvvniWKdaeivgmAQQALTDTQF--G 545
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  558 NPAKINLKRppTAGSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFSEGLVCHQIRYLGLLENVRVRRAGYAFRQA 637
Cdd:cd14911   546 ARTRKGMFR--TVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIP 623
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|.
gi 291391928  638 YEPCLERYKMLCKQTWPHWKGPARSGVEVLFNELEIPVEEYSFGRSKIFIR 688
Cdd:cd14911   624 FQEFRQRYELLTPNVIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
MYSc_Myo43 cd14904
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ...
34-648 4.06e-152

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: 473.28  E-value: 4.06e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928   34 NLKKRFDHNEIYTYIGSVVISVNPYRSLP-IYSPEKVEDYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITGESGA 112
Cdd:cd14904     6 NLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVSGESGA 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  113 GKTEASKLVMSYVAAVCG--KGAEVNQVkeqlLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGGVISNYLL 190
Cdd:cd14904    86 GKTETTKIVMNHLASVAGgrKDKTIAKV----IDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRGKLIGAKCETYLL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  191 EKSRVVKQPRGERNFHVFYQLLSGASEELLNKLKLERDFSrYNYLG--LDSARVNGVDDAANFRTVRNAMQIVGFMDHEV 268
Cdd:cd14904   162 EKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQ-YQYLGdsLAQMQIPGLDDAKLFASTQKSLSLIGLDNDAQ 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  269 ESVLEVVAAVLKLGNIEFKpESRVNGldeSKIKDKNELKEICELTSIDQSVLERAFSFRTVEAKQEKVSTTLNVAQAYYA 348
Cdd:cd14904   241 RTLFKILSGVLHLGEVMFD-KSDENG---SRISNGSQLSQVAKMLGLPTTRIEEALCNRSVVTRNESVTVPLAPVEAEEN 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  349 RDALAKNLYSRLFSWLVNRINESIKAQTKVRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKEEQEEYI 428
Cdd:cd14904   317 RDALAKAIYSKLFDWMVVKINAAISTDDDRIKGQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDVFKTVEEEYI 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  429 REDIEWTHIDYFNNAIICDLIENNTnGILAMLDEEcLRPGTVTDETFlekLNQVCATHQhfESRMSKCSRFlndTSLPHS 508
Cdd:cd14904   397 REGLQWDHIEYQDNQGIVEVIDGKM-GIIALMNDH-LRQPRGTEEAL---VNKIRTNHQ--TKKDNESIDF---PKVKRT 466
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  509 CFRIQHYAGKVLYQVEGFVDKNNDLLYRDLSQAMWKAGHALIKSLF--------PEGNPAKINLKRPPTAGSQFKASVAT 580
Cdd:cd14904   467 QFIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFgsseapseTKEGKSGKGTKAPKSLGSQFKTSLSQ 546
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 291391928  581 LMKNLQTKNPNYIRCIKPNDKKAAHIFSEGLVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKML 648
Cdd:cd14904   547 LMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAIM 614
MYSc_Myo47 cd14908
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ...
32-688 1.36e-151

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  Cd Length: 682  Bit Score: 473.24  E-value: 1.36e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928   32 INNLKKRFDHNEIYTYIGSVVISVNPYRSLPIYSPEKVEDYRNRNFY---------ELSPHIFALSDEAYRSL-RDQDKD 101
Cdd:cd14908     4 LHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRQEGLLrsqgiespqALGPHVFAIADRSYRQMmSEIRAS 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  102 QCILITGESGAGKTEASKLVMSYVAAVCGKGAEVNQ---------VKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDI 172
Cdd:cd14908    84 QSILISGESGAGKTESTKIVMLYLTTLGNGEEGAPNegeelgklsIMDRVLQSNPILEAFGNARTLRNDNSSRFGKFIEL 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  173 EFDFKGDPLGGVISNYLLEKSRVVKQPRGERNFHVFYQLLSGASEELLNKLKLERDFSR-------YNYLGL-DSARVNG 244
Cdd:cd14908   164 GFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEEEHEKYEFHDGITGglqlpneFHYTGQgGAPDLRE 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  245 VDDAANFRTVRNAMQIVGFMDHEVESVLEVVAAVLKLGNIEFKPESRVNGLDESKIKDKNELKEICELTSIDQSVLERAF 324
Cdd:cd14908   244 FTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDGAAEIAEEGNEKCLARVAKLLGVDVDKLLRAL 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  325 SFRTVEAKQEKVSTTLNVAQAYYARDALAKNLYSRLFSWLVNRINESIKAQT-KVRKKVMGVLDIYGFEIFEDNSFEQFI 403
Cdd:cd14908   324 TSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSINWENdKDIRSSVGVLDIFGFECFAHNSFEQLC 403
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  404 INYCNEKLQQIFIELTLKEEQEEYIREDIEWTHIDYFNNAIICDLIENNTNGILAMLDEECLRPGTVTDETFLEKLNQVC 483
Cdd:cd14908   404 INFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFPDNQDCLDTIQAKKKGILTMLDDECRLGIRGSDANYASRLYETY 483
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  484 ATHQHFEsrMSKCSRFLNDTSL-PHSCFRIQHYAGKVLYQVE-GFVDKNNDLLYRDlsqamwkaghalIKSLFPEgnpak 561
Cdd:cd14908   484 LPEKNQT--HSENTRFEATSIQkTKLIFAVRHFAGQVQYTVEtTFCEKNKDEIPLT------------ADSLFES----- 544
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  562 inlkrpptaGSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFSEGLVCHQIRYLGLLENVRVRRAGYAFRQAYEPC 641
Cdd:cd14908   545 ---------GQQFKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRYGGVLEAVRVARSGYPVRLPHKDF 615
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 291391928  642 LERYKMLC------KQTW-PHWKGPARSGVEVLFNEL-------------EIPVEEYSFGRSKIFIR 688
Cdd:cd14908   616 FKRYRMLLplipevVLSWsMERLDPQKLCVKKMCKDLvkgvlspamvsmkNIPEDTMQLGKSKVFMR 682
PTZ00014 PTZ00014
myosin-A; Provisional
17-762 1.36e-151

myosin-A; Provisional


Pssm-ID: 240229  Cd Length: 821  Bit Score: 477.60  E-value: 1.36e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928   17 VGDMVLLEPLNEETFINNLKKRFDHNEIYTYIGSVVISVNPYRSLPIYSPEKVEDYRN-RNFYELSPHIFALSDEAYRSL 95
Cdd:PTZ00014   98 YGDIGLLPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYRDaKDSDKLPPHVFTTARRALENL 177
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928   96 RDQDKDQCILITGESGAGKTEASKLVMSYVAAvcGKGAEVNQ-VKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEF 174
Cdd:PTZ00014  178 HGVKKSQTIIVSGESGAGKTEATKQIMRYFAS--SKSGNMDLkIQNAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQL 255
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  175 DFKGDPLGGVISNYLLEKSRVVKQPRGERNFHVFYQLLSGASEELLNKLKLeRDFSRYNYLGLDSARVNGVDDAANFRTV 254
Cdd:PTZ00014  256 GEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKL-KSLEEYKYINPKCLDVPGIDDVKDFEEV 334
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  255 RNAMQIVGFMDHEVESVLEVVAAVLKLGNIEFKPESRVNGLDESKIKDKNE--LKEICELTSIDQSVLERAFSFRTVEAK 332
Cdd:PTZ00014  335 MESFDSMGLSESQIEDIFSILSGVLLLGNVEIEGKEEGGLTDAAAISDESLevFNEACELLFLDYESLKKELTVKVTYAG 414
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  333 QEKVSTTLNVAQAYYARDALAKNLYSRLFSWLVNRINESIKAQTKVrKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQ 412
Cdd:PTZ00014  415 NQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGF-KVFIGMLDIFGFEVFKNNSLEQLFINITNEMLQ 493
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  413 QIFIELTLKEEQEEYIREDIEWTHIDYFNNAIICDLIENNTNGILAMLDEECLRPGTvTDETFLEKLNQVCATHQHFesr 492
Cdd:PTZ00014  494 KNFVDIVFERESKLYKDEGISTEELEYTSNESVIDLLCGKGKSVLSILEDQCLAPGG-TDEKFVSSCNTNLKNNPKY--- 569
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  493 mSKCSRFLNdtslphSCFRIQHYAGKVLYQVEGFVDKNNDLLYRDLSQAMWKAGHALIKSLFP-----EGNPAKINLkrp 567
Cdd:PTZ00014  570 -KPAKVDSN------KNFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLFEgveveKGKLAKGQL--- 639
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  568 ptAGSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFSEGLVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKM 647
Cdd:PTZ00014  640 --IGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKY 717
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  648 LCKQTWPHWKGPARSGVEVLFNELEIPVEEYSFGRSKIFIRnPRTLFKLEDLRKQRLEDLATLIQkiyrgwkcrthfllm 727
Cdd:PTZ00014  718 LDLAVSNDSSLDPKEKAEKLLERSGLPKDSYAIGKTMVFLK-KDAAKELTQIQREKLAAWEPLVS--------------- 781
                         730       740       750
                  ....*....|....*....|....*....|....*
gi 291391928  728 krsqiVIAAWYRRYAQQKRYQQIKSSALVIQSYIR 762
Cdd:PTZ00014  782 -----VLEALILKIKKKRKVRKNIKSLVRIQAHLR 811
MYSc_Myh18 cd14932
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ...
30-688 6.26e-150

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  Cd Length: 676  Bit Score: 468.35  E-value: 6.26e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928   30 TFINNLKKRFDHNEIYTYIGSVVISVNPYRSLPIYSPEKVEDYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITGE 109
Cdd:cd14932     2 SVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391928  110 SGAGKTEASKLVMSYVAAVCG-------KGAEV---NQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGD 179
Cdd:cd14932    82 SGAGKTENTKKVIQY