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Conserved domains on  [gi|1057503232|ref|NP_001317167|]
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unconventional myosin-Ib isoform 5 [Homo sapiens]

Protein Classification

class I myosin( domain architecture ID 11544948)

class I myosin is an unconventional myosin; it contains a head/motor domain that has ATPase activity and functions as a molecular motor, utilizing ATP hydrolysis to generate directed movement toward the plus end along actin filaments

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 1057503232   29 ETFINNLKKRFDHSEIYTYIGSVVISVNPYRSLPIYSPEKVEEYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITG 108
Cdd:cd01378      1 EAINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  109 ESGAGKTEASKLVMSYVAAVCGKG-AEVNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGGVISN 187
Cdd:cd01378     81 ESGAGKTEASKRIMQYIAAVSGGSeSEVERVKDMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEPVGGHITN 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  188 YLLEKSRVVKQPRGERNFHVFYQLLSGASEELLNKLKLERDFSRYNYLSLDSAKVNGVDDAANFRTVRNAMQIVGFMDHE 267
Cdd:cd01378    161 YLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGCFDVDGIDDAADFKEVLNAMKVIGFTEEE 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  268 AESVLAVVAAVLKLGNIEFKPESRVNgldeSKIKDKNELKEICELTGIDQSVLERAFSFRTVEAKQEK---VSTTLNVAQ 344
Cdd:cd01378    241 QDSIFRILAAILHLGNIQFAEDEEGN----AAISDTSVLDFVAYLLGVDPDQLEKALTHRTIETGGGGrsvYEVPLNVEQ 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  345 AYYARDALAKNLYSRLFSWLVNRINESIKAQTKVRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKEEQ 424
Cdd:cd01378    317 AAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKKKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFIELTLKAEQ 396
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  425 EEYIREDIEWTHIDYFNNAIICDLIENNTNGILAMLDEECLRPGTVTDETFLEKLNQVCATHQHFESRmskcsrfLNDTS 504
Cdd:cd01378    397 EEYVREGIEWTPIKYFNNKIICDLIEEKPPGIFAILDDACLTAGDATDQTFLQKLNQLFSNHPHFECP-------SGHFE 469
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  505 LPHSCFRIQHYAGKVLYQVEGFVDKNNDLLYRDLSQAMWKASHALIKSLFPEGNPAKiNLKRPPTAGSQFKASVATLMKN 584
Cdd:cd01378    470 LRRGEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEGVDLD-SKKRPPTAGTKFKNSANALVET 548
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  585 LQTKNPNYIRCIKPNDKKAAHIFNEALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKMLCKQTWPHWKGPARSGV 664
Cdd:cd01378    549 LMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYKLLSPKTWPAWDGTWQGGV 628
                          650       660
                   ....*....|....*....|....
gi 1057503232  665 EVLFNELEIPVEEYSFGRSKIFIR 688
Cdd:cd01378    629 ESILKDLNIPPEEYQMGKTKIFIR 652
Myosin_TH1 pfam06017
Unconventional myosin tail, actin- and lipid-binding; Unconventional myosins, ie those that ...
912-1089 8.16e-37

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: 461801  Cd Length: 196  Bit Score: 137.34  E-value: 8.16e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  912 KLEASELFKDKKALYPSSVGQPFQGAYLEI--NKNPKYKKLKDAI----EEKIIIAEVVNKINRaNGKSTSRIFLLTNNN 985
Cdd:pfam06017    1 KDYASDLLKGRKERRRFSLLRRFMGDYLGLenNFSGPGPKLRKAVgiggDEKVLFSDRVSKFNR-SSKPSPRILILTDKA 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  986 LLLADQKSGQ------IKSEVPLVDVTKVSMSSQNDGFFAVHLKEGSeaasKGDFLFSSDHLIEMATKLYRTTLSQTKQK 1059
Cdd:pfam06017   80 VYLIDQKKLKnglqyvLKRRIPLSDITGVSVSPLQDDWVVLHLGSPQ----KGDLLLECDFKTELVTHLSKAYKKKTNRK 155
                          170       180       190
                   ....*....|....*....|....*....|.
gi 1057503232 1060 LNIEISDEFLVQFRQDK-VCVKFIQGNQKNG 1089
Cdd:pfam06017  156 LNVKIGDTIEYRKKKGKiRTVKFVKDEPKGK 186
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
749-771 4.59e-03

Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln residues.


:

Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 35.38  E-value: 4.59e-03
                            10        20
                    ....*....|....*....|...
gi 1057503232   749 QTKSSALVIQSYIRGWKARKILR 771
Cdd:smart00015    1 RLTRAAIIIQAAWRGYLARKRYK 23
 
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 1057503232   29 ETFINNLKKRFDHSEIYTYIGSVVISVNPYRSLPIYSPEKVEEYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITG 108
Cdd:cd01378      1 EAINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  109 ESGAGKTEASKLVMSYVAAVCGKG-AEVNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGGVISN 187
Cdd:cd01378     81 ESGAGKTEASKRIMQYIAAVSGGSeSEVERVKDMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEPVGGHITN 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  188 YLLEKSRVVKQPRGERNFHVFYQLLSGASEELLNKLKLERDFSRYNYLSLDSAKVNGVDDAANFRTVRNAMQIVGFMDHE 267
Cdd:cd01378    161 YLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGCFDVDGIDDAADFKEVLNAMKVIGFTEEE 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  268 AESVLAVVAAVLKLGNIEFKPESRVNgldeSKIKDKNELKEICELTGIDQSVLERAFSFRTVEAKQEK---VSTTLNVAQ 344
Cdd:cd01378    241 QDSIFRILAAILHLGNIQFAEDEEGN----AAISDTSVLDFVAYLLGVDPDQLEKALTHRTIETGGGGrsvYEVPLNVEQ 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  345 AYYARDALAKNLYSRLFSWLVNRINESIKAQTKVRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKEEQ 424
Cdd:cd01378    317 AAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKKKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFIELTLKAEQ 396
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  425 EEYIREDIEWTHIDYFNNAIICDLIENNTNGILAMLDEECLRPGTVTDETFLEKLNQVCATHQHFESRmskcsrfLNDTS 504
Cdd:cd01378    397 EEYVREGIEWTPIKYFNNKIICDLIEEKPPGIFAILDDACLTAGDATDQTFLQKLNQLFSNHPHFECP-------SGHFE 469
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  505 LPHSCFRIQHYAGKVLYQVEGFVDKNNDLLYRDLSQAMWKASHALIKSLFPEGNPAKiNLKRPPTAGSQFKASVATLMKN 584
Cdd:cd01378    470 LRRGEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEGVDLD-SKKRPPTAGTKFKNSANALVET 548
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  585 LQTKNPNYIRCIKPNDKKAAHIFNEALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKMLCKQTWPHWKGPARSGV 664
Cdd:cd01378    549 LMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYKLLSPKTWPAWDGTWQGGV 628
                          650       660
                   ....*....|....*....|....
gi 1057503232  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 [Multi-domain]  Cd Length: 677  Bit Score: 1036.35  E-value: 0e+00
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232    16 GVGDMVLLEPLNEETFINNLKKRFDHSEIYTYIGSVVISVNPYRSLPIYSPEKVEEYRNRNFYELSPHIFALSDEAYRSL 95
Cdd:smart00242    7 GVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIADNAYRNM 86
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232    96 RDQDKDQCILITGESGAGKTEASKLVMSYVAAVCGKGAEVNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFD 175
Cdd:smart00242   87 LNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNTEVGSVEDQILESNPILEAFGNAKTLRNNNSSRFGKFIEIHFD 166
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   176 FKGDPLGGVISNYLLEKSRVVKQPRGERNFHVFYQLLSGASEELLNKLKLERDfSRYNYLS-LDSAKVNGVDDAANFRTV 254
Cdd:smart00242  167 AKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSP-EDYRYLNqGGCLTVDGIDDAEEFKET 245
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   255 RNAMQIVGFMDHEAESVLAVVAAVLKLGNIEFKPESrvNGLDESKIKDKNELKEICELTGIDQSVLERAFSFRTVEAKQE 334
Cdd:smart00242  246 LNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGR--NDNAASTVKDKEELSNAAELLGVDPEELEKALTKRKIKTGGE 323
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   335 KVSTTLNVAQAYYARDALAKNLYSRLFSWLVNRINESIKAQTKvRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQI 414
Cdd:smart00242  324 VITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDG-STYFIGVLDIYGFEIFEVNSFEQLCINYANEKLQQF 402
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   415 FIELTLKEEQEEYIREDIEWTHIDYFNNAIICDLIENNTNGILAMLDEECLRPGtVTDETFLEKLNQVCATHQHFESRMS 494
Cdd:smart00242  403 FNQHVFKLEQEEYEREGIDWTFIDFFDNQDCIDLIEKKPPGILSLLDEECRFPK-GTDQTFLEKLNQHHKKHPHFSKPKK 481
                           490       500       510       520       530       540       550       560
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   495 KcsrflndtslPHSCFRIQHYAGKVLYQVEGFVDKNNDLLYRDLSQAMWKASHALIKSLFPEGNPAKINLKRPPTAGSQF 574
Cdd:smart00242  482 K----------GRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSGVSNAGSKKRFQTVGSQF 551
                           570       580       590       600       610       620       630       640
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   575 KASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNEALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKMLCKQTWP 654
Cdd:smart00242  552 KEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRLPFDEFLQRYRVLLPDTWP 631
                           650       660       670       680
                    ....*....|....*....|....*....|....*....|....*..
gi 1057503232   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: 395017 [Multi-domain]  Cd Length: 674  Bit Score: 945.17  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   17 VGDMVLLEPLNEETFINNLKKRFDHSEIYTYIGSVVISVNPYRSLPIYSPEKVEEYRNRNFYELSPHIFALSDEAYRSLR 96
Cdd:pfam00063    1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   97 DQDKDQCILITGESGAGKTEASKLVMSYVAAVCGKGAEVN--QVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEF 174
Cdd:pfam00063   81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAGNvgRLEEQILQSNPILEAFGNAKTVRNNNSSRFGKYIEIQF 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  175 DFKGDPLGGVISNYLLEKSRVVKQPRGERNFHVFYQLLSGASEELLNKLKLErDFSRYNYLSLD-SAKVNGVDDAANFRT 253
Cdd:pfam00063  161 DAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLT-NPKDYHYLSQSgCYTIDGIDDSEEFKI 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  254 VRNAMQIVGFMDHEAESVLAVVAAVLKLGNIEFKPESRVNGldeSKIKDKNELKEICELTGIDQSVLERAFSFRTVEAKQ 333
Cdd:pfam00063  240 TDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQ---AVPDDTENLQKAASLLGIDSTELEKALCKRRIKTGR 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  334 EKVSTTLNVAQAYYARDALAKNLYSRLFSWLVNRINESIKAQTKVRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQ 413
Cdd:pfam00063  317 ETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTIEKASFIGVLDIYGFEIFEKNSFEQLCINYVNEKLQQ 396
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  414 IFIELTLKEEQEEYIREDIEWTHIDYFNNAIICDLIENNTNGILAMLDEECLRPGtVTDETFLEKLNQVCATHQHFESrm 493
Cdd:pfam00063  397 FFNHHMFKLEQEEYVREGIEWTFIDFGDNQPCIDLIEKKPLGILSLLDEECLFPK-ATDQTFLDKLYSTFSKHPHFQK-- 473
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  494 skcSRFLNDTslphsCFRIQHYAGKVLYQVEGFVDKNNDLLYRDLSQAMWKASHALIKSLFPEGNPA------------- 560
Cdd:pfam00063  474 ---PRLQGET-----HFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAesaaanesgkstp 545
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  561 -KINLKRPPTAGSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNEALVCHQIRYLGLLENVRVRRAGYAFRQAYE 639
Cdd:pfam00063  546 kRTKKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQ 625
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*....
gi 1057503232  640 PCLERYKMLCKQTWPHWKGPARSGVEVLFNELEIPVEEYSFGRSKIFIR 688
Cdd:pfam00063  626 EFVQRYRILAPKTWPKWKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
COG5022 COG5022
Myosin heavy chain [General function prediction only];
16-806 0e+00

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 738.04  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   16 GVGDMVLLEPLNEETFINNLKKRFDHSEIYTYIGSVVISVNPYRSLPIYSPEKVEEYRNRNFYELSPHIFALSDEAYRSL 95
Cdd:COG5022     67 GVDDLTELSYLNEPAVLHNLEKRYNNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNL 146
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   96 RDQDKDQCILITGESGAGKTEASKLVMSYVAAVCG-KGAEVNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEF 174
Cdd:COG5022    147 LSEKENQTIIISGESGAGKTENAKRIMQYLASVTSsSTVEISSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEF 226
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  175 DFKGDPLGGVISNYLLEKSRVVKQPRGERNFHVFYQLLSGASEElLNKLKLERDFSRYNYLSlDSA--KVNGVDDAANFR 252
Cdd:COG5022    227 DENGEICGAKIETYLLEKSRVVHQNKNERNYHIFYQLLAGDPEE-LKKLLLLQNPKDYIYLS-QGGcdKIDGIDDAKEFK 304
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  253 TVRNAMQIVGFMDHEAESVLAVVAAVLKLGNIEFKpESRVnglDESKIKDKNELKEICELTGIDQSVLERAFSFRTVEAK 332
Cdd:COG5022    305 ITLDALKTIGIDEEEQDQIFKILAAILHIGNIEFK-EDRN---GAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTG 380
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  333 QEKVSTTLNVAQAYYARDALAKNLYSRLFSWLVNRINESIKAqTKVRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQ 412
Cdd:COG5022    381 GEWIVVPLNLEQALAIRDSLAKALYSNLFDWIVDRINKSLDH-SAAASNFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQ 459
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  413 QIFIELTLKEEQEEYIREDIEWTHIDYFNNAIICDLIEN-NTNGILAMLDEECLRPgTVTDETFLEKLNQV--CATHQHF 489
Cdd:COG5022    460 QFFNQHMFKLEQEEYVKEGIEWSFIDYFDNQPCIDLIEKkNPLGILSLLDEECVMP-HATDESFTSKLAQRlnKNSNPKF 538
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  490 ESrmskcSRFLNDTslphscFRIQHYAGKVLYQVEGFVDKNNDLLYRDLSQAMWKASHALIKSLFPEgnPAKINLK-RPP 568
Cdd:COG5022    539 KK-----SRFRDNK------FVVKHYAGDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDD--EENIESKgRFP 605
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  569 TAGSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNEALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKML 648
Cdd:COG5022    606 TLGSRFKESLNSLMSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRIL 685
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  649 CKQ----TWPHWKGPARSGVEVLFNELEIPVEEYSFGRSKIFIRNPrTLFKLEDLRKQRLEDLATLIQKIYRGWKCRTHF 724
Cdd:COG5022    686 SPSkswtGEYTWKEDTKNAVKSILEELVIDSSKYQIGNTKVFFKAG-VLAALEDMRDAKLDNIATRIQRAIRGRYLRRRY 764
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  725 LLMKKSQIVIAA---------------WYRRYAQQKRY-------QQTKSSALVIQSYIRGWKARKILRELKHQKRCKEA 782
Cdd:COG5022    765 LQALKRIKKIQViqhgfrlrrlvdyelKWRLFIKLQPLlsllgsrKEYRSYLACIIKLQKTIKREKKLRETEEVEFSLKA 844
                          810       820
                   ....*....|....*....|....
gi 1057503232  783 VTTIAAYWHGTQARRELRRLKEEA 806
Cdd:COG5022    845 EVLIQKFGRSLKAKKRFSLLKKET 868
PTZ00014 PTZ00014
myosin-A; Provisional
17-762 1.36e-154

myosin-A; Provisional


Pssm-ID: 240229 [Multi-domain]  Cd Length: 821  Bit Score: 480.68  E-value: 1.36e-154
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   17 VGDMVLLEPLNEETFINNLKKRFDHSEIYTYIGSVVISVNPYRSLPIYSPEKVEEYRN-RNFYELSPHIFALSDEAYRSL 95
Cdd:PTZ00014    98 YGDIGLLPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYRDaKDSDKLPPHVFTTARRALENL 177
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   96 RDQDKDQCILITGESGAGKTEASKLVMSYVAAvcGKGAEVNQ-VKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEF 174
Cdd:PTZ00014   178 HGVKKSQTIIVSGESGAGKTEATKQIMRYFAS--SKSGNMDLkIQNAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQL 255
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  175 DFKGDPLGGVISNYLLEKSRVVKQPRGERNFHVFYQLLSGASEELLNKLKLeRDFSRYNYLSLDSAKVNGVDDAANFRTV 254
Cdd:PTZ00014   256 GEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKL-KSLEEYKYINPKCLDVPGIDDVKDFEEV 334
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  255 RNAMQIVGFMDHEAESVLAVVAAVLKLGNIEFKPESRVNGLDESKIKDKNE--LKEICELTGIDQSVLERAFSFRTVEAK 332
Cdd:PTZ00014   335 MESFDSMGLSESQIEDIFSILSGVLLLGNVEIEGKEEGGLTDAAAISDESLevFNEACELLFLDYESLKKELTVKVTYAG 414
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  333 QEKVSTTLNVAQAYYARDALAKNLYSRLFSWLVNRINESIKAQTKVrKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQ 412
Cdd:PTZ00014   415 NQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGF-KVFIGMLDIFGFEVFKNNSLEQLFINITNEMLQ 493
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  413 QIFIELTLKEEQEEYIREDIEWTHIDYFNNAIICDLIENNTNGILAMLDEECLRPGTvTDETFLEKLNQVCATHQHFesr 492
Cdd:PTZ00014   494 KNFVDIVFERESKLYKDEGISTEELEYTSNESVIDLLCGKGKSVLSILEDQCLAPGG-TDEKFVSSCNTNLKNNPKY--- 569
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  493 mSKCSRFLNdtslphSCFRIQHYAGKVLYQVEGFVDKNNDLLYRDLSQAMWKASHALIKSLFP-----EGNPAKINLkrp 567
Cdd:PTZ00014   570 -KPAKVDSN------KNFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLFEgveveKGKLAKGQL--- 639
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  568 ptAGSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNEALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKM 647
Cdd:PTZ00014   640 --IGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKY 717
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  648 LCKQTWPHWKGPARSGVEVLFNELEIPVEEYSFGRSKIFIRnPRTLFKLEDLRKQRLEDLATLIQkiyrgwkcrthfllm 727
Cdd:PTZ00014   718 LDLAVSNDSSLDPKEKAEKLLERSGLPKDSYAIGKTMVFLK-KDAAKELTQIQREKLAAWEPLVS--------------- 781
                          730       740       750
                   ....*....|....*....|....*....|....*
gi 1057503232  728 kksqiVIAAWYRRYAQQKRYQQTKSSALVIQSYIR 762
Cdd:PTZ00014   782 -----VLEALILKIKKKRKVRKNIKSLVRIQAHLR 811
Myosin_TH1 pfam06017
Unconventional myosin tail, actin- and lipid-binding; Unconventional myosins, ie those that ...
912-1089 8.16e-37

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: 461801  Cd Length: 196  Bit Score: 137.34  E-value: 8.16e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  912 KLEASELFKDKKALYPSSVGQPFQGAYLEI--NKNPKYKKLKDAI----EEKIIIAEVVNKINRaNGKSTSRIFLLTNNN 985
Cdd:pfam06017    1 KDYASDLLKGRKERRRFSLLRRFMGDYLGLenNFSGPGPKLRKAVgiggDEKVLFSDRVSKFNR-SSKPSPRILILTDKA 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  986 LLLADQKSGQ------IKSEVPLVDVTKVSMSSQNDGFFAVHLKEGSeaasKGDFLFSSDHLIEMATKLYRTTLSQTKQK 1059
Cdd:pfam06017   80 VYLIDQKKLKnglqyvLKRRIPLSDITGVSVSPLQDDWVVLHLGSPQ----KGDLLLECDFKTELVTHLSKAYKKKTNRK 155
                          170       180       190
                   ....*....|....*....|....*....|.
gi 1057503232 1060 LNIEISDEFLVQFRQDK-VCVKFIQGNQKNG 1089
Cdd:pfam06017  156 LNVKIGDTIEYRKKKGKiRTVKFVKDEPKGK 186
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
749-771 4.59e-03

Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln residues.


Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 35.38  E-value: 4.59e-03
                            10        20
                    ....*....|....*....|...
gi 1057503232   749 QTKSSALVIQSYIRGWKARKILR 771
Cdd:smart00015    1 RLTRAAIIIQAAWRGYLARKRYK 23
 
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 1057503232   29 ETFINNLKKRFDHSEIYTYIGSVVISVNPYRSLPIYSPEKVEEYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITG 108
Cdd:cd01378      1 EAINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  109 ESGAGKTEASKLVMSYVAAVCGKG-AEVNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGGVISN 187
Cdd:cd01378     81 ESGAGKTEASKRIMQYIAAVSGGSeSEVERVKDMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEPVGGHITN 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  188 YLLEKSRVVKQPRGERNFHVFYQLLSGASEELLNKLKLERDFSRYNYLSLDSAKVNGVDDAANFRTVRNAMQIVGFMDHE 267
Cdd:cd01378    161 YLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGCFDVDGIDDAADFKEVLNAMKVIGFTEEE 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  268 AESVLAVVAAVLKLGNIEFKPESRVNgldeSKIKDKNELKEICELTGIDQSVLERAFSFRTVEAKQEK---VSTTLNVAQ 344
Cdd:cd01378    241 QDSIFRILAAILHLGNIQFAEDEEGN----AAISDTSVLDFVAYLLGVDPDQLEKALTHRTIETGGGGrsvYEVPLNVEQ 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  345 AYYARDALAKNLYSRLFSWLVNRINESIKAQTKVRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKEEQ 424
Cdd:cd01378    317 AAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKKKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFIELTLKAEQ 396
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  425 EEYIREDIEWTHIDYFNNAIICDLIENNTNGILAMLDEECLRPGTVTDETFLEKLNQVCATHQHFESRmskcsrfLNDTS 504
Cdd:cd01378    397 EEYVREGIEWTPIKYFNNKIICDLIEEKPPGIFAILDDACLTAGDATDQTFLQKLNQLFSNHPHFECP-------SGHFE 469
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  505 LPHSCFRIQHYAGKVLYQVEGFVDKNNDLLYRDLSQAMWKASHALIKSLFPEGNPAKiNLKRPPTAGSQFKASVATLMKN 584
Cdd:cd01378    470 LRRGEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEGVDLD-SKKRPPTAGTKFKNSANALVET 548
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  585 LQTKNPNYIRCIKPNDKKAAHIFNEALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKMLCKQTWPHWKGPARSGV 664
Cdd:cd01378    549 LMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYKLLSPKTWPAWDGTWQGGV 628
                          650       660
                   ....*....|....*....|....
gi 1057503232  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 [Multi-domain]  Cd Length: 677  Bit Score: 1036.35  E-value: 0e+00
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232    16 GVGDMVLLEPLNEETFINNLKKRFDHSEIYTYIGSVVISVNPYRSLPIYSPEKVEEYRNRNFYELSPHIFALSDEAYRSL 95
Cdd:smart00242    7 GVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIADNAYRNM 86
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232    96 RDQDKDQCILITGESGAGKTEASKLVMSYVAAVCGKGAEVNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFD 175
Cdd:smart00242   87 LNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNTEVGSVEDQILESNPILEAFGNAKTLRNNNSSRFGKFIEIHFD 166
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   176 FKGDPLGGVISNYLLEKSRVVKQPRGERNFHVFYQLLSGASEELLNKLKLERDfSRYNYLS-LDSAKVNGVDDAANFRTV 254
Cdd:smart00242  167 AKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSP-EDYRYLNqGGCLTVDGIDDAEEFKET 245
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   255 RNAMQIVGFMDHEAESVLAVVAAVLKLGNIEFKPESrvNGLDESKIKDKNELKEICELTGIDQSVLERAFSFRTVEAKQE 334
Cdd:smart00242  246 LNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGR--NDNAASTVKDKEELSNAAELLGVDPEELEKALTKRKIKTGGE 323
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   335 KVSTTLNVAQAYYARDALAKNLYSRLFSWLVNRINESIKAQTKvRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQI 414
Cdd:smart00242  324 VITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDG-STYFIGVLDIYGFEIFEVNSFEQLCINYANEKLQQF 402
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   415 FIELTLKEEQEEYIREDIEWTHIDYFNNAIICDLIENNTNGILAMLDEECLRPGtVTDETFLEKLNQVCATHQHFESRMS 494
Cdd:smart00242  403 FNQHVFKLEQEEYEREGIDWTFIDFFDNQDCIDLIEKKPPGILSLLDEECRFPK-GTDQTFLEKLNQHHKKHPHFSKPKK 481
                           490       500       510       520       530       540       550       560
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   495 KcsrflndtslPHSCFRIQHYAGKVLYQVEGFVDKNNDLLYRDLSQAMWKASHALIKSLFPEGNPAKINLKRPPTAGSQF 574
Cdd:smart00242  482 K----------GRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSGVSNAGSKKRFQTVGSQF 551
                           570       580       590       600       610       620       630       640
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   575 KASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNEALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKMLCKQTWP 654
Cdd:smart00242  552 KEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRLPFDEFLQRYRVLLPDTWP 631
                           650       660       670       680
                    ....*....|....*....|....*....|....*....|....*..
gi 1057503232   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: 395017 [Multi-domain]  Cd Length: 674  Bit Score: 945.17  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   17 VGDMVLLEPLNEETFINNLKKRFDHSEIYTYIGSVVISVNPYRSLPIYSPEKVEEYRNRNFYELSPHIFALSDEAYRSLR 96
Cdd:pfam00063    1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   97 DQDKDQCILITGESGAGKTEASKLVMSYVAAVCGKGAEVN--QVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEF 174
Cdd:pfam00063   81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAGNvgRLEEQILQSNPILEAFGNAKTVRNNNSSRFGKYIEIQF 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  175 DFKGDPLGGVISNYLLEKSRVVKQPRGERNFHVFYQLLSGASEELLNKLKLErDFSRYNYLSLD-SAKVNGVDDAANFRT 253
Cdd:pfam00063  161 DAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLT-NPKDYHYLSQSgCYTIDGIDDSEEFKI 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  254 VRNAMQIVGFMDHEAESVLAVVAAVLKLGNIEFKPESRVNGldeSKIKDKNELKEICELTGIDQSVLERAFSFRTVEAKQ 333
Cdd:pfam00063  240 TDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQ---AVPDDTENLQKAASLLGIDSTELEKALCKRRIKTGR 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  334 EKVSTTLNVAQAYYARDALAKNLYSRLFSWLVNRINESIKAQTKVRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQ 413
Cdd:pfam00063  317 ETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTIEKASFIGVLDIYGFEIFEKNSFEQLCINYVNEKLQQ 396
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  414 IFIELTLKEEQEEYIREDIEWTHIDYFNNAIICDLIENNTNGILAMLDEECLRPGtVTDETFLEKLNQVCATHQHFESrm 493
Cdd:pfam00063  397 FFNHHMFKLEQEEYVREGIEWTFIDFGDNQPCIDLIEKKPLGILSLLDEECLFPK-ATDQTFLDKLYSTFSKHPHFQK-- 473
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  494 skcSRFLNDTslphsCFRIQHYAGKVLYQVEGFVDKNNDLLYRDLSQAMWKASHALIKSLFPEGNPA------------- 560
Cdd:pfam00063  474 ---PRLQGET-----HFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAesaaanesgkstp 545
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  561 -KINLKRPPTAGSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNEALVCHQIRYLGLLENVRVRRAGYAFRQAYE 639
Cdd:pfam00063  546 kRTKKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQ 625
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*....
gi 1057503232  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 [Multi-domain]  Cd Length: 633  Bit Score: 784.86  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   29 ETFINNLKKRFDHSEIYTYIGSVVISVNPYRSLPIYSPEKVEEYRNRN-FYELSPHIFALSDEAYRSLRDQDKDQCILIT 107
Cdd:cd00124      1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGrSADLPPHVFAVADAAYRAMLRDGQNQSILIS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  108 GESGAGKTEASKLVMSYVAAVCGKGAEVNQVK-----EQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLG 182
Cdd:cd00124     81 GESGAGKTETTKLVLKYLAALSGSGSSKSSSSassieQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPTGRLVG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  183 GVISNYLLEKSRVVKQPRGERNFHVFYQLLSGASEELLNKLKLE---RDFSRYNYL-SLDSAKVNGVDDAANFRTVRNAM 258
Cdd:cd00124    161 ASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLElllSYYYLNDYLnSSGCDRIDGVDDAEEFQELLDAL 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  259 QIVGFMDHEAESVLAVVAAVLKLGNIEFKpESRVNGLDESKIKDKNELKEICELTGIDQSVLERAFSFRTVEAKQEKVST 338
Cdd:cd00124    241 DVLGFSDEEQDSIFRILAAILHLGNIEFE-EDEEDEDSSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGETITK 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  339 TLNVAQAYYARDALAKNLYSRLFSWLVNRINESIKAQTKVRKK-VMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIE 417
Cdd:cd00124    320 PLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAESTsFIGILDIFGFENFEVNSFEQLCINYANEKLQQFFNQ 399
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  418 LTLKEEQEEYIREDIEWTHIDYFNNAIICDLIENNTNGILAMLDEECLRPGTvTDETFLEKLNQVCATHqhfesrmskcS 497
Cdd:cd00124    400 HVFKLEQEEYEEEGIDWSFIDFPDNQDCLDLIEGKPLGILSLLDEECLFPKG-TDATFLEKLYSAHGSH----------P 468
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  498 RFLNDTSLPHSCFRIQHYAGKVLYQVEGFVDKNNDLLYRDLSQAMwkashalikslfpegnpakinlkrppTAGSQFKAS 577
Cdd:cd00124    469 RFFSKKRKAKLEFGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLL--------------------------RSGSQFRSQ 522
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  578 VATLMKNLQTKNPNYIRCIKPNDKKAAHIFNEALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKMLCKQTWPHWK 657
Cdd:cd00124    523 LDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYRILAPGATEKAS 602
                          650       660       670
                   ....*....|....*....|....*....|.
gi 1057503232  658 GPARSGVEVLFNELEIPVEEYSFGRSKIFIR 688
Cdd:cd00124    603 DSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
COG5022 COG5022
Myosin heavy chain [General function prediction only];
16-806 0e+00

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 738.04  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   16 GVGDMVLLEPLNEETFINNLKKRFDHSEIYTYIGSVVISVNPYRSLPIYSPEKVEEYRNRNFYELSPHIFALSDEAYRSL 95
Cdd:COG5022     67 GVDDLTELSYLNEPAVLHNLEKRYNNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNL 146
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   96 RDQDKDQCILITGESGAGKTEASKLVMSYVAAVCG-KGAEVNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEF 174
Cdd:COG5022    147 LSEKENQTIIISGESGAGKTENAKRIMQYLASVTSsSTVEISSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEF 226
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  175 DFKGDPLGGVISNYLLEKSRVVKQPRGERNFHVFYQLLSGASEElLNKLKLERDFSRYNYLSlDSA--KVNGVDDAANFR 252
Cdd:COG5022    227 DENGEICGAKIETYLLEKSRVVHQNKNERNYHIFYQLLAGDPEE-LKKLLLLQNPKDYIYLS-QGGcdKIDGIDDAKEFK 304
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  253 TVRNAMQIVGFMDHEAESVLAVVAAVLKLGNIEFKpESRVnglDESKIKDKNELKEICELTGIDQSVLERAFSFRTVEAK 332
Cdd:COG5022    305 ITLDALKTIGIDEEEQDQIFKILAAILHIGNIEFK-EDRN---GAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTG 380
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  333 QEKVSTTLNVAQAYYARDALAKNLYSRLFSWLVNRINESIKAqTKVRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQ 412
Cdd:COG5022    381 GEWIVVPLNLEQALAIRDSLAKALYSNLFDWIVDRINKSLDH-SAAASNFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQ 459
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  413 QIFIELTLKEEQEEYIREDIEWTHIDYFNNAIICDLIEN-NTNGILAMLDEECLRPgTVTDETFLEKLNQV--CATHQHF 489
Cdd:COG5022    460 QFFNQHMFKLEQEEYVKEGIEWSFIDYFDNQPCIDLIEKkNPLGILSLLDEECVMP-HATDESFTSKLAQRlnKNSNPKF 538
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  490 ESrmskcSRFLNDTslphscFRIQHYAGKVLYQVEGFVDKNNDLLYRDLSQAMWKASHALIKSLFPEgnPAKINLK-RPP 568
Cdd:COG5022    539 KK-----SRFRDNK------FVVKHYAGDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDD--EENIESKgRFP 605
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  569 TAGSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNEALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKML 648
Cdd:COG5022    606 TLGSRFKESLNSLMSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRIL 685
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  649 CKQ----TWPHWKGPARSGVEVLFNELEIPVEEYSFGRSKIFIRNPrTLFKLEDLRKQRLEDLATLIQKIYRGWKCRTHF 724
Cdd:COG5022    686 SPSkswtGEYTWKEDTKNAVKSILEELVIDSSKYQIGNTKVFFKAG-VLAALEDMRDAKLDNIATRIQRAIRGRYLRRRY 764
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  725 LLMKKSQIVIAA---------------WYRRYAQQKRY-------QQTKSSALVIQSYIRGWKARKILRELKHQKRCKEA 782
Cdd:COG5022    765 LQALKRIKKIQViqhgfrlrrlvdyelKWRLFIKLQPLlsllgsrKEYRSYLACIIKLQKTIKREKKLRETEEVEFSLKA 844
                          810       820
                   ....*....|....*....|....
gi 1057503232  783 VTTIAAYWHGTQARRELRRLKEEA 806
Cdd:COG5022    845 EVLIQKFGRSLKAKKRFSLLKKET 868
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 [Multi-domain]  Cd Length: 662  Bit Score: 677.26  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   32 INNLKKRFDHSEIYTYIGSVVISVNPYRSLPIYSPEKVEEYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITGESG 111
Cdd:cd01377      4 LHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITGESG 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  112 AGKTEASKLVMSYVAAVCG-------KGAEVNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGGV 184
Cdd:cd01377     84 AGKTENTKKVIQYLASVAAsskkkkeSGKKKGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTGKIAGAD 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  185 ISNYLLEKSRVVKQPRGERNFHVFYQLLSGASEELLNKLKLERDFSRYNYLSLDSAKVNGVDDAANFRTVRNAMQIVGFM 264
Cdd:cd01377    164 IETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYFFLSQGELTIDGVDDAEEFKLTDEAFDILGFS 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  265 DHEAESVLAVVAAVLKLGNIEFKPESRvngLDESKIKDKNELKEICELTGIDQSVLERAFSFRTVEAKQEKVSTTLNVAQ 344
Cdd:cd01377    244 EEEKMSIFKIVAAILHLGNIKFKQRRR---EEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKGQNKEQ 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  345 AYYARDALAKNLYSRLFSWLVNRINESIKaQTKVRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIF----IELtl 420
Cdd:cd01377    321 VVFSVGALAKALYERLFLWLVKRINKTLD-TKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFnhhmFVL-- 397
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  421 keEQEEYIREDIEWTHIDYFNNAIIC-DLIENNTNGILAMLDEECLRPGTvTDETFLEKLNQVCATHQHFESRMSKCSrf 499
Cdd:cd01377    398 --EQEEYKKEGIEWTFIDFGLDLQPTiDLIEKPNMGILSILDEECVFPKA-TDKTFVEKLYSNHLGKSKNFKKPKPKK-- 472
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  500 lndtslPHSCFRIQHYAGKVLYQVEGFVDKNNDLLYRDLSQAMWKASHALIKSLFPE-----GNPAKINLKRPP--TAGS 572
Cdd:cd01377    473 ------SEAHFILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDyeesgGGGGKKKKKGGSfrTVSQ 546
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  573 QFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNEALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKMLCKQT 652
Cdd:cd01377    547 LHKEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNA 626
                          650       660       670
                   ....*....|....*....|....*....|....*.
gi 1057503232  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 [Multi-domain]  Cd Length: 629  Bit Score: 670.40  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   33 NNLKKRF-DHSEIYTYIGSVVISVNPYRSLPIYSPEKVEEYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITGESG 111
Cdd:cd01380      5 HNLKVRFcQRNAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVSGESG 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  112 AGKTEASKLVMSYVAAVCGKGAEVNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGGVISNYLLE 191
Cdd:cd01380     85 AGKTVSAKYAMRYFATVGGSSSGETQVEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYRIIGANMRTYLLE 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  192 KSRVVKQPRGERNFHVFYQLLSGASEELLNKLKLErDFSRYNYLSL-DSAKVNGVDDAANFRTVRNAMQIVGFMDHEAES 270
Cdd:cd01380    165 KSRVVFQAEEERNYHIFYQLCAAASLPELKELHLG-SAEDFFYTNQgGSPVIDGVDDAAEFEETRKALTLLGISEEEQME 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  271 VLAVVAAVLKLGNIEFKPESRvnglDESKIKDKNE-LKEICELTGIDQSVLERAFSFRTVEAKQEKVSTTLNVAQAYYAR 349
Cdd:cd01380    244 IFRILAAILHLGNVEIKATRN----DSASISPDDEhLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPLTLQQAIVAR 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  350 DALAKNLYSRLFSWLVNRINESIKAQTKVR-KKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKEEQEEYI 428
Cdd:cd01380    320 DALAKHIYAQLFDWIVDRINKALASPVKEKqHSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHVFKLEQEEYV 399
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  429 REDIEWTHIDYFNNAIICDLIENNTnGILAMLDEECLRPGTvTDETFLEKLNQVCATH--QHFESrmskcSRFLNDTslp 506
Cdd:cd01380    400 KEEIEWSFIDFYDNQPCIDLIEGKL-GILDLLDEECRLPKG-SDENWAQKLYNQHLKKpnKHFKK-----PRFSNTA--- 469
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  507 hscFRIQHYAGKVLYQVEGFVDKNNDLLYRDLSQAMwKASHalikslfpegnpakinlKRPPTAGSQFKASVATLMKNLQ 586
Cdd:cd01380    470 ---FIVKHFADDVEYQVEGFLEKNRDTVSEEHLNVL-KASK-----------------NRKKTVGSQFRDSLILLMETLN 528
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  587 TKNPNYIRCIKPNDKKAAHIFNEALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKMLCKQTWPHWKGPARSGVEV 666
Cdd:cd01380    529 STTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLPSKEWLRDDKKKTCENI 608
                          650       660
                   ....*....|....*....|..
gi 1057503232  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: 658.56  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   34 NLKKRFDHSEIYTYIGSVVISVNPYRSLPIYSPEKVEEYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITGESGAG 113
Cdd:cd01381      6 NLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISGESGAG 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  114 KTEASKLVMSYVAAVCGKGAEVNQvkeQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGGVISNYLLEKS 193
Cdd:cd01381     86 KTESTKLILQYLAAISGQHSWIEQ---QILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIEGAKIEQYLLEKS 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  194 RVVKQPRGERNFHVFYQLLSGASEELLNKLKLErDFSRYNYLSL-DSAKVNGVDDAANFRTVRNAMQIVGFMDHEAESVL 272
Cdd:cd01381    163 RIVSQAPDERNYHIFYCMLAGLSAEEKKKLELG-DASDYYYLTQgNCLTCEGRDDAAEFADIRSAMKVLMFTDEEIWDIF 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  273 AVVAAVLKLGNIEFKpESRVNGLDESKIKDKNELKEICELTGIDQSVLERAFSFRTVEAKQEKVSTTLNVAQAYYARDAL 352
Cdd:cd01381    242 KLLAAILHLGNIKFE-ATVVDNLDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSPLSAEQALDVRDAF 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  353 AKNLYSRLFSWLVNRINESI---KAQTKVRKKVmGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKEEQEEYIR 429
Cdd:cd01381    321 VKGIYGRLFIWIVNKINSAIykpRGTDSSRTSI-GVLDIFGFENFEVNSFEQLCINFANENLQQFFVRHIFKLEQEEYDK 399
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  430 EDIEWTHIDYFNNAIICDLIENNTNGILAMLDEECLRP-GtvTDETFLEKLNQVCATHQHFESRMSKcsrflNDTSlphs 508
Cdd:cd01381    400 EGINWQHIEFVDNQDVLDLIALKPMNIMSLIDEESKFPkG--TDQTMLEKLHSTHGNNKNYLKPKSD-----LNTS---- 468
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  509 cFRIQHYAGKVLYQVEGFVDKNNDLLYRDLSQAMWKASHALIKSLF-PEGNPAKINLKRPPTAGSQFKASVATLMKNLQT 587
Cdd:cd01381    469 -FGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFnEDISMGSETRKKSPTLSSQFRKSLDQLMKTLSA 547
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  588 KNPNYIRCIKPNDKKAAHIFNEALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKMLCKQTWPHWKGPARSGVEVL 667
Cdd:cd01381    548 CQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVLVPGIPPAHKTDCRAATRKI 627
                          650       660
                   ....*....|....*....|.
gi 1057503232  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: 642.42  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   34 NLKKRFDHSEIYTYIGSVVISVNPYRSLP-IYSPEKVEEYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITGESGA 112
Cdd:cd01384      6 NLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVSGESGA 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  113 GKTEASKLVMSYVAAVCGKGA-EVNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGGVISNYLLE 191
Cdd:cd01384     86 GKTETTKMLMQYLAYMGGRAVtEGRSVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAGRISGAAIRTYLLE 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  192 KSRVVKQPRGERNFHVFYQLLSGASEELLNKLKLErDFSRYNYLSL-DSAKVNGVDDAANFRTVRNAMQIVGFMDHEAES 270
Cdd:cd01384    166 RSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLK-DPKQFHYLNQsKCFELDGVDDAEEYRATRRAMDVVGISEEEQDA 244
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  271 VLAVVAAVLKLGNIEFKPESRVnglDESKIKD---KNELKEICELTGIDQSVLERAFSFRTVEAKQEKVSTTLNVAQAYY 347
Cdd:cd01384    245 IFRVVAAILHLGNIEFSKGEED---DSSVPKDeksEFHLKAAAELLMCDEKALEDALCKRVIVTPDGIITKPLDPDAATL 321
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  348 ARDALAKNLYSRLFSWLVNRINESIkAQTKVRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKEEQEEY 427
Cdd:cd01384    322 SRDALAKTIYSRLFDWLVDKINRSI-GQDPNSKRLIGVLDIYGFESFKTNSFEQFCINLANEKLQQHFNQHVFKMEQEEY 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  428 IREDIEWTHIDYFNNAIICDLIENNTNGILAMLDEECLRPgTVTDETFLEKLNQVCATHQHFESrmSKCSRflndtslph 507
Cdd:cd01384    401 TKEEIDWSYIEFVDNQDVLDLIEKKPGGIIALLDEACMFP-RSTHETFAQKLYQTLKDHKRFSK--PKLSR--------- 468
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  508 SCFRIQHYAGKVLYQVEGFVDKNNDLLYRDlSQAMWKAS-HALIKSLFPEGNPAKINLKRPPTA-GSQFKASVATLMKNL 585
Cdd:cd01384    469 TDFTIDHYAGDVTYQTDLFLDKNKDYVVAE-HQALLNASkCPFVAGLFPPLPREGTSSSSKFSSiGSRFKQQLQELMETL 547
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  586 QTKNPNYIRCIKPNDKKAAHIFNEALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKMLCKQTwPHWKGPARSGVE 665
Cdd:cd01384    548 NTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGLLAPEV-LKGSDDEKAACK 626
                          650       660
                   ....*....|....*....|...
gi 1057503232  666 VLFNELEipVEEYSFGRSKIFIR 688
Cdd:cd01384    627 KILEKAG--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 [Multi-domain]  Cd Length: 661  Bit Score: 634.36  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   29 ETFINNLKKRFDHSEIYTYIGSVVISVNPYRSLPIYSPEKVEEYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITG 108
Cdd:cd14883      1 EGINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  109 ESGAGKTEASKLVMSYVAAVCGKGAEVNQvkeQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGGVISNY 188
Cdd:cd14883     81 ESGAGKTETTKLILQYLCAVTNNHSWVEQ---QILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGHIKGAIIQDY 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  189 LLEKSRVVKQPRGERNFHVFYQLLSGA--SEELLNKLKLeRDFSRYNYLSLD-SAKVNGVDDAANFRTVRNAMQIVGFMD 265
Cdd:cd14883    158 LLEQSRITFQAPGERNYHVFYQLLAGAkhSKELKEKLKL-GEPEDYHYLNQSgCIRIDNINDKKDFDHLRLAMNVLGIPE 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  266 HEAESVLAVVAAVLKLGNIEFKpesrvnGLDESKI----KDKNELKEICELTGIDQSVLERAFSFRTVEAKQEKVSTTLN 341
Cdd:cd14883    237 EMQEGIFSVLSAILHLGNLTFE------DIDGETGaltvEDKEILKIVAKLLGVDPDKLKKALTIRQINVRGNVTEIPLK 310
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  342 VAQAYYARDALAKNLYSRLFSWLVNRINESIKAQTKvRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLK 421
Cdd:cd14883    311 VQEARDNRDAMAKALYSRTFAWLVNHINSCTNPGQK-NSRFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHYVFK 389
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  422 EEQEEYIREDIEWTHIDYFNNAIICDLIENNTNGILAMLDEECLRPgTVTDETFLEKLNQVCATHQHFEsrmsKCSRFLN 501
Cdd:cd14883    390 LEQEEYEKEGINWSHIVFTDNQECLDLIEKPPLGILKLLDEECRFP-KGTDLTYLEKLHAAHEKHPYYE----KPDRRRW 464
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  502 DTSlphscFRIQHYAGKVLYQVEGFVDKNNDLLYRDLSQAMWKASHALIKSLF-PEGNPAKINL--------------KR 566
Cdd:cd14883    465 KTE-----FGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFtYPDLLALTGLsislggdttsrgtsKG 539
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  567 PPTAGSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNEALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYK 646
Cdd:cd14883    540 KPTVGDTFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYL 619
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|..
gi 1057503232  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: 621.41  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   32 INNLKKRFDHSEIYTYIGSVVISVNPYRSLPIYSPEKVEEYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITGESG 111
Cdd:cd14872      4 VHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISGESG 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  112 AGKTEASKLVMSYVAAVCGkgaEVNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGGVISNYLLE 191
Cdd:cd14872     84 AGKTEATKQCLSFFAEVAG---STNGVEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRICGASTENYLLE 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  192 KSRVVKQPRGERNFHVFYQLLSGASEELLNKLKLERDfsrYNYLSLDSA-KVNGVDDAANFRTVRNAMQIVGFMDHEAES 270
Cdd:cd14872    161 KSRVVYQIKGERNFHIFYQLLASPDPASRGGWGSSAA---YGYLSLSGCiEVEGVDDVADFEEVVLAMEQLGFDDADINN 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  271 VLAVVAAVLKLGNIEFKPESRVNGLDESKIKDKNELKEICELTGIDQSVLERAFSFRTVEAK-QEKVSTTLNVAQAYYAR 349
Cdd:cd14872    238 VMSLIAAILKLGNIEFASGGGKSLVSGSTVANRDVLKEVATLLGVDAATLEEALTSRLMEIKgCDPTRIPLTPAQATDAC 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  350 DALAKNLYSRLFSWLVNRINESIKAQTKVRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKEEQEEYIR 429
Cdd:cd14872    318 DALAKAAYSRLFDWLVKKINESMRPQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEKLQQHFNQYTFKLEEALYQS 397
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  430 EDIEWTHIDYFNNAIICDLIENNTNGILAMLDEECLRPGTvTDETFLEKLNQVCATHQHFESRMSKCSRFLndtslphsc 509
Cdd:cd14872    398 EGVKFEHIDFIDNQPVLDLIEKKQPGLMLALDDQVKIPKG-SDATFMIAANQTHAAKSTFVYAEVRTSRTE--------- 467
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  510 FRIQHYAGKVLYQVEGFVDKNNDLLYRDLSQAMWKASHALIKSLFPEGNPAKINLKrpPTAGSQFKASVATLMKNLQTKN 589
Cdd:cd14872    468 FIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLFPPSEGDQKTSK--VTLGGQFRKQLSALMTALNATE 545
                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1057503232  590 PNYIRCIKPNDKKAAHIFNEALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKMLCK 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: 613.94  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   34 NLKKRFDHSEIYTYIGSVVISVNPYRSLPIYSPEKVEEYRNRNfyELSPHIFALSDEAYRSLRDQDKDQCILITGESGAG 113
Cdd:cd01383      6 NLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYRQKL--LDSPHVYAVADTAYREMMRDEINQSIIISGESGAG 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  114 KTEASKLVMSYVAAVCGKGaevNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGGVISNYLLEKS 193
Cdd:cd01383     84 KTETAKIAMQYLAALGGGS---SGIENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKICGAKIQTYLLEKS 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  194 RVVKQPRGERNFHVFYQLLSGASEELLNKLKLeRDFSRYNYLS-LDSAKVNGVDDAANFRTVRNAMQIVGFMDHEAESVL 272
Cdd:cd01383    161 RVVQLANGERSYHIFYQLCAGASPALREKLNL-KSASEYKYLNqSNCLTIDGVDDAKKFHELKEALDTVGISKEDQEHIF 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  273 AVVAAVLKLGNIEFkpeSRVNGLDESKIKDKNELKEICELTGIDQSVLERAFSFRTVEAKQEKVSTTLNVAQAYYARDAL 352
Cdd:cd01383    240 QMLAAVLWLGNISF---QVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKLTLQQAIDARDAL 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  353 AKNLYSRLFSWLVNRINESIKAQTKVRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKEEQEEYIREDI 432
Cdd:cd01383    317 AKAIYASLFDWLVEQINKSLEVGKRRTGRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLFKLEQEEYELDGI 396
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  433 EWTHIDYFNNAIICDLIENNTNGILAMLDEECLRPGTvTDETFLEKLNQVCATHQHFESRmskcsrflNDTSlphscFRI 512
Cdd:cd01383    397 DWTKVDFEDNQECLDLIEKKPLGLISLLDEESNFPKA-TDLTFANKLKQHLKSNSCFKGE--------RGGA-----FTI 462
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  513 QHYAGKVLYQVEGFVDKNNDLLYRDLSQAMWKASHALIK---SLFPEGNPAKINLKRPPTAGSQfKASVAT--------L 581
Cdd:cd01383    463 RHYAGEVTYDTSGFLEKNRDLLHSDLIQLLSSCSCQLPQlfaSKMLDASRKALPLTKASGSDSQ-KQSVATkfkgqlfkL 541
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  582 MKNLQTKNPNYIRCIKPNDKKAAHIFNEALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKMLCKQTWPHWKGPAR 661
Cdd:cd01383    542 MQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLPEDVSASQDPLS 621
                          650       660
                   ....*....|....*....|....*....
gi 1057503232  662 SGVEVL--FNeleIPVEEYSFGRSKIFIR 688
Cdd:cd01383    622 TSVAILqqFN---ILPEMYQVGYTKLFFR 647
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 [Multi-domain]  Cd Length: 662  Bit Score: 557.08  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   29 ETFINNLKKRFDHSEIYTYIGSVVISVNPYRSLP-IYSPEKVEEYRNRNFYELSPHIFALSDEAYRSLRDQD----KDQC 103
Cdd:cd14890      1 ASLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQSGvldpSNQS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  104 ILITGESGAGKTEASKLVMSYVAAVCGK----------------GAEVNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFG 167
Cdd:cd14890     81 IIISGESGAGKTEATKIIMQYLARITSGfaqgasgegeaaseaiEQTLGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  168 KYMDIEFDFKGDPLGGVISNYLLEKSRVVKQPRGERNFHVFYQLLSGASEELLNKLKLERDfSRYNYLSLDSAKVNGVDD 247
Cdd:cd14890    161 KFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTP-VEYFYLRGECSSIPSCDD 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  248 AANFRTVRNAMQIVGFMDHEAESVLAVVAAVLKLGNIEFKPESRVNGLdeSKIKDKNELKEICELTGIDQSVLERAFSFR 327
Cdd:cd14890    240 AKAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTVL--EDATTLQSLKLAAELLGVNEDALEKALLTR 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  328 TVEAKQEKVSTTLNVAQAYYARDALAKNLYSRLFSWLVNRINESIkAQTKVRKKVMGVLDIYGFEIFEDNSFEQFIINYC 407
Cdd:cd14890    318 QLFVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTI-SSPDDKWGFIGVLDIYGFEKFEWNTFEQLCINYA 396
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  408 NEKLQQIFIELTLKEEQEEYIREDIEWTHIDYFNNAIICDLIENNTN---GILAMLDEECLRPGTVTDETFLEKLNQV-- 482
Cdd:cd14890    397 NEKLQRHFNQHMFEVEQVEYSNEGIDWQYITFNDNQACLELIEGKVNgkpGIFITLDDCWRFKGEEANKKFVSQLHASfg 476
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  483 -----------CATHQHFESrmskcSRFLNDTSlphscFRIQHYAGKVLYQVEGFVDKNNDLLYRDLSQAMWKASHALik 551
Cdd:cd14890    477 rksgsggtrrgSSQHPHFVH-----PKFDADKQ-----FGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSRRSI-- 544
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  552 slfpegnpakinlkRPPTAGSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNEALVCHQIRYLGLLENVRVRRAG 631
Cdd:cd14890    545 --------------REVSVGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGMMEAIQIRQQG 610
                          650       660       670       680       690       700
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  632 YAFRQAYEPCLERYKMLCKQtwphwkgpARSG---VEVLFNELEIPVEEYSFGRSKIFIR 688
Cdd:cd14890    611 FALREEHDSFFYDFQVLLPT--------AENIeqlVAVLSKMLGLGKADWQIGSSKIFLK 662
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 [Multi-domain]  Cd Length: 657  Bit Score: 555.13  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   34 NLKKRFDHSEIYTYIGSVVISVNPYRSLPIYSPEKVEEYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITGESGAG 113
Cdd:cd01387      6 NLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISGESGSG 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  114 KTEASKLVMSYVAAVCGKGAevNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDfKGDPLGGVISNYLLEKS 193
Cdd:cd01387     86 KTEATKLIMQYLAAVNQRRN--NLVTEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFFE-GGVIVGAITSQYLLEKS 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  194 RVVKQPRGERNFHVFYQLLSGASEELLNKLKLErDFSRYNYLSLD-SAKVNGVDDAANFRTVRNAMQIVGFMDHEAESVL 272
Cdd:cd01387    163 RIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQ-EAEKYFYLNQGgNCEIAGKSDADDFRRLLAAMQVLGFSSEEQDSIF 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  273 AVVAAVLKLGNIEFKPESRVNGLDESKIKDKNELKEICELTGIDQSVLERAFSFRTVEAKQEKVSTTLNVAQAYYARDAL 352
Cdd:cd01387    242 RILASVLHLGNVYFHKRQLRHGQEGVSVGSDAEIQWVAHLLQISPEGLQKALTFKVTETRRERIFTPLTIDQALDARDAI 321
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  353 AKNLYSRLFSWLVNRINESIKAQTKvRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKEEQEEYIREDI 432
Cdd:cd01387    322 AKALYALLFSWLVTRVNAIVYSGTQ-DTLSIAILDIFGFEDLSENSFEQLCINYANENLQYYFNKHVFKLEQEEYIREQI 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  433 EWTHIDYFNNAIICDLIENNTNGILAMLDEECLRPgTVTDETFLEKlnqvCATHQHFESRMSKcsrflndTSLPHSCFRI 512
Cdd:cd01387    401 DWTEIAFADNQPVINLISKKPVGILHILDDECNFP-QATDHSFLEK----CHYHHALNELYSK-------PRMPLPEFTI 468
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  513 QHYAGKVLYQVEGFVDKNNDLLYRDLSQAMWKASHALIKSLFPE------------GNPAKINLK-RPPTAGSQFKASVA 579
Cdd:cd01387    469 KHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSShraqtdkapprlGKGRFVTMKpRTPTVAARFQDSLL 548
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  580 TLMKNLQTKNPNYIRCIKPNDKKAAHIFNEALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKMLCKQTWPHwKGP 659
Cdd:cd01387    549 QLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYRCLVALKLPR-PAP 627
                          650       660       670
                   ....*....|....*....|....*....|
gi 1057503232  660 ARSGVEVLFNELE-IPVEEYSFGRSKIFIR 688
Cdd:cd01387    628 GDMCVSLLSRLCTvTPKDMYRLGATKVFLR 657
MYSc_Myo6 cd01382
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ...
30-688 0e+00

class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the minus-end of actin filaments, in contrast to most other myosins which moves towards the plus-end of actin filaments. It is thought that myosin VI, unlike plus-end directed myosins, does not use a pure lever arm mechanism, but instead steps with a mechanism analogous to the kinesin neck-linker uncoupling model. It has been implicated in a myriad of functions including: the transport of cytoplasmic organelles, maintenance of normal Golgi morphology, endocytosis, secretion, cell migration, border cell migration during development, and in cancer metastasis playing roles in deafness and retinal development among others. While how this is accomplished is largely unknown there are several interacting proteins that have been identified such as disabled homolog 2 (DAB2), GIPC1, synapse-associated protein 97 (SAP97; also known as DLG1) and optineurin, which have been found to target myosin VI to different cellular compartments. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the minus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276833  Cd Length: 649  Bit Score: 548.77  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   30 TFINNLKKRFDHSEIYTYIGSVVISVNPYRSLP-IYSPEKVEEYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITG 108
Cdd:cd01382      2 TLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVSG 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  109 ESGAGKTEASKLVMSYVAAVCGKGAevNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGGVISNY 188
Cdd:cd01382     82 ESGAGKTESTKYILRYLTESWGSGA--GPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVGGFVSHY 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  189 LLEKSRVVKQPRGERNFHVFYQLLSGASEELLNKLklerdfsrynylsldsAKVNGVDDAANFRTVRNAMQIVGFMDHEA 268
Cdd:cd01382    160 LLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKL----------------LKDPLLDDVGDFIRMDKAMKKIGLSDEEK 223
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  269 ESVLAVVAAVLKLGNIEFKpESRVNGLDESKIKDKNE--LKEICELTGIDQSVLERAFSFRTVEAKQEKVSTT-----LN 341
Cdd:cd01382    224 LDIFRVVAAVLHLGNIEFE-ENGSDSGGGCNVKPKSEqsLEYAAELLGLDQDELRVSLTTRVMQTTRGGAKGTvikvpLK 302
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  342 VAQAYYARDALAKNLYSRLFSWLVNRINESIKAQTKVrkKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLK 421
Cdd:cd01382    303 VEEANNARDALAKAIYSKLFDHIVNRINQCIPFETSS--YFIGVLDIAGFEYFEVNSFEQFCINYCNEKLQQFFNERILK 380
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  422 EEQEEYIREDIEWTHIDYFNNAIICDLIENNTNGILAMLDEECLRPgTVTDETFLEKLNQVCATHQHFES-RMSKCS--R 498
Cdd:cd01382    381 EEQELYEKEGLGVKEVEYVDNQDCIDLIEAKLVGILDLLDEESKLP-KPSDQHFTSAVHQKHKNHFRLSIpRKSKLKihR 459
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  499 FLNDtslpHSCFRIQHYAGKVLYQVEGFVDKNNDLLYRDLSQAMWKASHALIKSLFPEGNPA---------KINLKrppT 569
Cdd:cd01382    460 NLRD----DEGFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFESSTNNnkdskqkagKLSFI---S 532
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  570 AGSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNEALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYK--- 646
Cdd:cd01382    533 VGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRTSFHDLYNMYKkyl 612
                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1057503232  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 0e+00

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


Pssm-ID: 276866 [Multi-domain]  Cd Length: 655  Bit Score: 544.38  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   30 TFINNLKKRFDHSEIYTYIGSVVISVNPYRSLPIYSPEKVEEY------RNRNFYELSPHIFALSDEAYRSL----RDQD 99
Cdd:cd14901      2 SILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMlfasRGQK 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  100 KDQCILITGESGAGKTEASKLVMSYVAAVC------GKGAEVNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIE 173
Cdd:cd14901     82 CDQSILVSGESGAGKTETTKIIMNYLASVSsatthgQNATERENVRDRVLESNPILEAFGNARTNRNNNSSRFGKFIRLG 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  174 FDFKGDPLGGVISNYLLEKSRVVKQPRGERNFHVFYQLLSGASEELLNKLKLErDFSRYNYLSLDSA--KVNGVDDAANF 251
Cdd:cd14901    162 FASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLT-HVEEYKYLNSSQCydRRDGVDDSVQY 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  252 RTVRNAMQIVGFMDHEAESVLAVVAAVLKLGNIEFKPESRVNGldESKIKDKNELKEICELTGIDQSVLERAFSFRTVEA 331
Cdd:cd14901    241 AKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFVKKDGEGG--TFSMSSLANVRAACDLLGLDMDVLEKTLCTREIRA 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  332 KQEKVSTTLNVAQAYYARDALAKNLYSRLFSWLVNRINESIK-AQTKVRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEK 410
Cdd:cd14901    319 GGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAySESTGASRFIGIVDIFGFEIFATNSLEQLCINFANEK 398
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  411 LQQIFIELTLKEEQEEYIREDIEWTHIDYFNNAIICDLIENNTNGILAMLDEECLRPGTvTDETFLEKLNQVCATHQHFE 490
Cdd:cd14901    399 LQQLFGKFVFEMEQDEYVAEAIPWTFVEYPNNDACVAMFEARPTGLFSLLDEQCLLPRG-NDEKLANKYYDLLAKHASFS 477
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  491 SrmSKCSRFLNdtslphsCFRIQHYAGKVLYQVEGFVDKNNDLLYRDLSQAMWKASHALIkslfpegnpakinlkrPPTA 570
Cdd:cd14901    478 V--SKLQQGKR-------QFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFL----------------SSTV 532
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  571 GSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNEALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKMLCK 650
Cdd:cd14901    533 VAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFPHDAFVHTYSCLAP 612
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|...
gi 1057503232  651 QTwPHWKGPARSGVEVLFNELEIPV------EEYSFGRSKIFI 687
Cdd:cd14901    613 DG-ASDTWKVNELAERLMSQLQHSElniehlPPFQVGKTKVFL 654
MYSc_Myo36 cd14897
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ...
29-688 2.11e-179

class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain followed by a GlcAT-I (Beta1,3-glucuronyltransferase I) domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276862 [Multi-domain]  Cd Length: 635  Bit Score: 538.89  E-value: 2.11e-179
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   29 ETFINNLKKRFDHSEIYTYIGSVVISVNPYRSLPIYSPEKVEEYRNRNF-YELSPHIFALSDEAYRSLRDQDKDQCILIT 107
Cdd:cd14897      1 NTIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSVrSQRPPHLFWIADQAYRRLLETGRNQCILVS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  108 GESGAGKTEASKLVMSYVAAVCGKgaEVNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGGVISN 187
Cdd:cd14897     81 GESGAGKTESTKYMIKHLMKLSPS--DDSDLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQLLGAKIDD 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  188 YLLEKSRVVKQPRGERNFHVFYQLLSGASEELLNKLKLErDFSRYNYLSLDSAKVNGVDDA-------ANFRTVRNAMQI 260
Cdd:cd14897    159 YLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLE-DPDCHRILRDDNRNRPVFNDSeeleyyrQMFHDLTNIMKL 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  261 VGFMDHEAESVLAVVAAVLKLGNIEFKPESRVNGLdesKIKDKNELKEICELTGIDQSVLERAFSFRTVEAKQEKVSTTL 340
Cdd:cd14897    238 IGFSEEDISVIFTILAAILHLTNIVFIPDEDTDGV---TVADEYPLHAVAKLLGIDEVELTEALISNVNTIRGERIQSWK 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  341 NVAQAYYARDALAKNLYSRLFSWLVNRINESIKAQTKVRKKV----MGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFI 416
Cdd:cd14897    315 SLRQANDSRDALAKDLYSRLFGWIVGQINRNLWPDKDFQIMTrgpsIGILDMSGFENFKINSFDQLCINLSNERLQQYFN 394
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  417 ELTLKEEQEEYIREDIEWTHIDYFNNAIICDLIENNTNGILAMLDEECLRPGTvTDETFLEKLNQVCATHQHFESRMSKc 496
Cdd:cd14897    395 DYVFPRERSEYEIEGIEWRDIEYHDNDDVLELFFKKPLGILPLLDEESTFPQS-TDSSLVQKLNKYCGESPRYVASPGN- 472
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  497 srflndtslpHSCFRIQHYAGKVLYQVEGFVDKNNDLLYRDLSQAMWKASHALIKSLFPegnpakinlkrpptagSQFKA 576
Cdd:cd14897    473 ----------RVAFGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLFT----------------SYFKR 526
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  577 SVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNEALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKMLCKQTWPHW 656
Cdd:cd14897    527 SLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYEDFVKRYKEICDFSNKVR 606
                          650       660       670
                   ....*....|....*....|....*....|..
gi 1057503232  657 KGPARSGVEVLFNELeipVEEYSFGRSKIFIR 688
Cdd:cd14897    607 SDDLGKCQKILKTAG---IKGYQFGKTKVFLK 635
MYSc_Myo9 cd01385
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ...
29-688 2.33e-179

class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play a role in signalling. It has a N-terminal RA domain, an IQ domain, a C1_1 domain, and a RhoGAP domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276836 [Multi-domain]  Cd Length: 690  Bit Score: 540.81  E-value: 2.33e-179
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   29 ETFINNLKKRFDHSEIYTYIGSVVISVNPYRSLPIYSPEKVEEYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITG 108
Cdd:cd01385      1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  109 ESGAGKTEASKLVMSYVAAVCGKGAEVNqVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGGVISNY 188
Cdd:cd01385     81 ESGSGKTESTNFLLHHLTALSQKGYGSG-VEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRGAVVEKY 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  189 LLEKSRVVKQPRGERNFHVFYQLLSGASEELLNKLKLERDfSRYNYLS-LDSAKVNGVDDAANFRTVRNAMQIVGFMDHE 267
Cdd:cd01385    160 LLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQP-EDYHYLNqSDCYTLEGEDEKYEFERLKQAMEMVGFLPET 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  268 AESVLAVVAAVLKLGNIEFKPEsRVNGLDESKIKDKNELKEICELTGIDQSVLERAFSFRTVEAKQEKVSTTLNVAQAYY 347
Cdd:cd01385    239 QRQIFSVLSAVLHLGNIEYKKK-AYHRDESVTVGNPEVLDIISELLRVKEETLLEALTTKKTVTVGETLILPYKLPEAIA 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  348 ARDALAKNLYSRLFSWLVNRINE---SIKAQTKVRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKEEQ 424
Cdd:cd01385    318 TRDAMAKCLYSALFDWIVLRINHallNKKDLEEAKGLSIGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQHIFKLEQ 397
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  425 EEYIREDIEWTHIDYFNNAIICDLIENNTNGILAMLDEECLRPGTvTDETFLEKLNQVCATHQHFESrmskcsrflndTS 504
Cdd:cd01385    398 EEYKKEGISWHNIEYTDNTGCLQLISKKPTGLLCLLDEESNFPGA-TNQTLLAKFKQQHKDNKYYEK-----------PQ 465
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  505 LPHSCFRIQHYAGKVLYQVEGFVDKNNDLLYRDLSQAMWKASHALIKSL-----------------------FPE----- 556
Cdd:cd01385    466 VMEPAFIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVRELigidpvavfrwavlrafframaaFREagrrr 545
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  557 ----GNPAKINL-------------KRPPTAGSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNEALVCHQIRYL 619
Cdd:cd01385    546 aqrtAGHSLTLHdrttksllhlhkkKKPPSVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVLRQLRYT 625
                          650       660       670       680       690       700
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1057503232  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 3.38e-175

class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a monomer. In mammalian cells, the motor is found to localize to filopodia. Myosin X walks towards the barbed ends of filaments and is thought to walk on bundles of actin, rather than single filaments, a unique behavior. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to the head domain are a variable number of IQ domains, 2 PH domains, a MyTH4 domain, and a FERM domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276840 [Multi-domain]  Cd Length: 651  Bit Score: 528.60  E-value: 3.38e-175
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   34 NLKKRFDHSEIYTYIGSVVISVNPYRSLP-IYSPEKVEEYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITGESGA 112
Cdd:cd14873      6 NLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILISGESGA 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  113 GKTEASKL------VMSYVAAVCGKGAEVNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGGVIS 186
Cdd:cd14873     86 GKTESTKLilkflsVISQQSLELSLKEKTSCVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNIQGGRIV 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  187 NYLLEKSRVVKQPRGERNFHVFYQLLSGASEELLNKLKLErDFSRYNYLSlDSAKVN--GVDDAANFRTVRNAMQIVGFM 264
Cdd:cd14873    166 DYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLS-TPENYHYLN-QSGCVEdkTISDQESFREVITAMEVMQFS 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  265 DHEAESVLAVVAAVLKLGNIEFKPESrvngldESKIKDKNELKEICELTGIDQSVLERAFSFRTVEAKQEKVSTTLNVAQ 344
Cdd:cd14873    244 KEEVREVSRLLAGILHLGNIEFITAG------GAQVSFKTALGRSAELLGLDPTQLTDALTQRSMFLRGEEILTPLNVQQ 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  345 AYYARDALAKNLYSRLFSWLVNRINESIKAQTKVrkKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKEEQ 424
Cdd:cd14873    318 AVDSRDSLAMALYARCFEWVIKKINSRIKGKEDF--KSIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKHIFSLEQ 395
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  425 EEYIREDIEWTHIDYFNNAIICDLIENNTnGILAMLDEECLRPgTVTDETFLEKLNQVCATHQHF-ESRMSKcsrflndt 503
Cdd:cd14873    396 LEYSREGLVWEDIDWIDNGECLDLIEKKL-GLLALINEESHFP-QATDSTLLEKLHSQHANNHFYvKPRVAV-------- 465
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  504 slphSCFRIQHYAGKVLYQVEGFVDKNNDLLYRDLSQAMWKASHALIKSLFP-------EGNPAKINLKRPPTAGSQFKA 576
Cdd:cd14873    466 ----NNFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEhvssrnnQDTLKCGSKHRRPTVSSQFKD 541
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  577 SVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNEALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKMLCKQTwpHW 656
Cdd:cd14873    542 SLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMRNL--AL 619
                          650       660       670
                   ....*....|....*....|....*....|..
gi 1057503232  657 KGPARSGVEVLFNELEIPVEEYSFGRSKIFIR 688
Cdd:cd14873    620 PEDVRGKCTSLLQLYDASNSEWQLGKTKVFLR 651
MYSc_Myo42 cd14903
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ...
34-688 3.69e-173

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


Pssm-ID: 276868 [Multi-domain]  Cd Length: 658  Bit Score: 523.57  E-value: 3.69e-173
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   34 NLKKRFDHSEIYTYIGSVVISVNPYRSLP-IYSPEKVEEYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITGESGA 112
Cdd:cd14903      6 NVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVSGESGA 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  113 GKTEASKLVMSYVAAVCGkGAEvNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGGVISNYLLEK 192
Cdd:cd14903     86 GKTETTKILMNHLATIAG-GLN-DSTIKKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKNGTLVGAKCRTYLLEK 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  193 SRVVKQPRGERNFHVFYQLLSGASEEllNKLKLERDFSRYNYLSLDSAKVNGVDDAANFRTVRNAMQIVGFMDHEAESVL 272
Cdd:cd14903    164 TRVISHERPERNYHIFYQLLASPDVE--ERLFLDSANECAYTGANKTIKIEGMSDRKHFARTKEALSLIGVSEEKQEVLF 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  273 AVVAAVLKLGNIEFKPEsrvNGLDESKI--KDKNELKEICELTGIDQSVLERAFSFRTVEAKQEKVSTTLNVAQAYYARD 350
Cdd:cd14903    242 EVLAGILHLGQLQIQSK---PNDDEKSAiaPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDVYTVPLKKDQAEDCRD 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  351 ALAKNLYSRLFSWLVNRINESIKAQTKVRKKVmGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKEEQEEYIRE 430
Cdd:cd14903    319 ALAKAIYSNVFDWLVATINASLGNDAKMANHI-GVLDIFGFEHFKHNSFEQFCINYANEKLQQKFTQDVFKTVQIEYEEE 397
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  431 DIEWTHIDYFNNAIICDLIENNTnGILAMLDEECLRPGTvTDETFLEKLNQVCATHQHFeSRMSKCSRFLndtslphscF 510
Cdd:cd14903    398 GIRWAHIDFADNQDVLAVIEDRL-GIISLLNDEVMRPKG-NEESFVSKLSSIHKDEQDV-IEFPRTSRTQ---------F 465
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  511 RIQHYAGKVLYQVEGFVDKNNDLLYRDLSQAMWKASHALIKSLFPEG----NPAKINLKRP-----------PTAGSQFK 575
Cdd:cd14903    466 TIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKEKvespAAASTSLARGarrrrggalttTTVGTQFK 545
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  576 ASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNEALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKMLCKQTwPH 655
Cdd:cd14903    546 DSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWLFLPEG-RN 624
                          650       660       670
                   ....*....|....*....|....*....|....*
gi 1057503232  656 WKGPARSGVEVLFN--ELEIPvEEYSFGRSKIFIR 688
Cdd:cd14903    625 TDVPVAERCEALMKklKLESP-EQYQMGLTRIYFQ 658
MYSc_Myh10 cd14920
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ...
30-688 3.89e-173

class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy chain 10 (also called NMMHCB). Mutations in this gene have been associated with May-Hegglin anomaly and developmental defects in brain and heart. Multiple transcript variants encoding different isoforms have been found for this gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276952 [Multi-domain]  Cd Length: 673  Bit Score: 524.19  E-value: 3.89e-173
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   30 TFINNLKKRFDHSEIYTYIGSVVISVNPYRSLPIYSPEKVEEYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITGE 109
Cdd:cd14920      2 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  110 SGAGKTEASKLVMSYVAAVCGK------GAEVNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGG 183
Cdd:cd14920     82 SGAGKTENTKKVIQYLAHVASShkgrkdHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGA 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  184 VISNYLLEKSRVVKQPRGERNFHVFYQLLSGASEELLNKLKLErDFSRYNYLSLDSAKVNGVDDAANFRTVRNAMQIVGF 263
Cdd:cd14920    162 NIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLE-GFNNYRFLSNGYIPIPGQQDKDNFQETMEAMHIMGF 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  264 MDHEAESVLAVVAAVLKLGNIEFKPESRVnglDESKIKDKNELKEICELTGIDQSVLERAFSFRTVEAKQEKVSTTLNVA 343
Cdd:cd14920    241 SHEEILSMLKVVSSVLQFGNISFKKERNT---DQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKE 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  344 QAYYARDALAKNLYSRLFSWLVNRINESIKAQTKVRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKEE 423
Cdd:cd14920    318 QADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILE 397
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  424 QEEYIREDIEWTHIDYFNNAIIC-DLIENNTN--GILAMLDEECLRPgTVTDETFLEKLNQVCATHQHFESrmskcSRFL 500
Cdd:cd14920    398 QEEYQREGIEWNFIDFGLDLQPCiDLIERPANppGVLALLDEECWFP-KATDKTFVEKLVQEQGSHSKFQK-----PRQL 471
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  501 NDtslpHSCFRIQHYAGKVLYQVEGFVDKNNDLLYRDLSQAMWKASHALIKSLFPE------------------GNPAKI 562
Cdd:cd14920    472 KD----KADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDvdrivgldqvtgmtetafGSAYKT 547
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  563 NLKRPPTAGSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNEALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCL 642
Cdd:cd14920    548 KKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFR 627
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*.
gi 1057503232  643 ERYKMLCKQTWPHWKGPARSGVEVLFNELEIPVEEYSFGRSKIFIR 688
Cdd:cd14920    628 QRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
MYSc_Myo3 cd01379
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ...
29-688 4.72e-170

class III myosin, motor domain; Myosin III has been shown to play a role in the vision process in insects and in hearing in mammals. Myosin III, an unconventional myosin, does not form dimers. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. They are characterized by an N-terminal protein kinase domain and several IQ domains. Some members also contain WW, SH2, PH, and Y-phosphatase domains. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276830 [Multi-domain]  Cd Length: 633  Bit Score: 514.52  E-value: 4.72e-170
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   29 ETFINNLKKRFDHSEIYTYIGSVVISVNPYRSLPIYSPEKVEEYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITG 108
Cdd:cd01379      1 DTIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  109 ESGAGKTEASKLVMSYVAAVcGKGAEVNqVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGGVISNY 188
Cdd:cd01379     81 ESGAGKTESANLLVQQLTVL-GKANNRT-LEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAVTGARISEY 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  189 LLEKSRVVKQPRGERNFHVFYQLLSG-ASEELLNKLKLErDFSRYNYLSLDSAKV-NGVDDAAN---FRTVRNAMQIVGF 263
Cdd:cd01379    159 LLEKSRVVHQAIGERNFHIFYYIYAGlAEDKKLAKYKLP-ENKPPRYLQNDGLTVqDIVNNSGNrekFEEIEQCFKVIGF 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  264 MDHEAESVLAVVAAVLKLGNIEFKP-ESRVNGLDESKIKDKNELKEICELTGIDQSVLERAFSFRTVEAKQEKVSTTLNV 342
Cdd:cd01379    238 TKEEVDSVYSILAAILHIGDIEFTEvESNHQTDKSSRISNPEALNNVAKLLGIEADELQEALTSHSVVTRGETIIRNNTV 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  343 AQAYYARDALAKNLYSRLFSWLVNRINESIKAQTKVRKKVM--GVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTL 420
Cdd:cd01379    318 EEATDARDAMAKALYGRLFSWIVNRINSLLKPDRSASDEPLsiGILDIFGFENFQKNSFEQLCINIANEQIQYYFNQHIF 397
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  421 KEEQEEYIREDIEWTHIDYFNNAIICDLIENNTNGILAMLDEECLRPGTvTDETFLEKLnqvcatHQHFesrmsKCSRFl 500
Cdd:cd01379    398 AWEQQEYLNEGIDVDLIEYEDNRPLLDMFLQKPMGLLALLDEESRFPKA-TDQTLVEKF------HNNI-----KSKYY- 464
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  501 ndtSLPHS---CFRIQHYAGKVLYQVEGFVDKNNDLLYRDLSQAMWKASHALIKSlfpegnpakinlkrppTAGSQFKAS 577
Cdd:cd01379    465 ---WRPKSnalSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVRQ----------------TVATYFRYS 525
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  578 VATLMKNLQTKNPNYIRCIKPNDKKAAHIFNEALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKMLCkQTWPHWK 657
Cdd:cd01379    526 LMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRILFADFLKRYYFLA-FKWNEEV 604
                          650       660       670
                   ....*....|....*....|....*....|.
gi 1057503232  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 3.45e-166

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


Pssm-ID: 276872 [Multi-domain]  Cd Length: 669  Bit Score: 506.11  E-value: 3.45e-166
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   32 INNLKKRFDHSEIYTYIGSVVISVNPYRSLP-IYSPEKVEEYRNR--------NFYELSPHIFALSDEAYRSLRDQDKDQ 102
Cdd:cd14907      4 LINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEQiiqngeyfDIKKEPPHIYAIAALAFKQLFENNKKQ 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  103 CILITGESGAGKTEASKLVMSYVAAVCGK-----------------GAEVNQVKEQLLQSNPVLEAFGNAKTVRNDNSSR 165
Cdd:cd14907     84 AIVISGESGAGKTENAKYAMKFLTQLSQQeqnseevltltssiratSKSTKSIEQKILSCNPILEAFGNAKTVRNDNSSR 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  166 FGKYMDIEFDFK-GDPLGGVISNYLLEKSRVVKQPRGERNFHVFYQLLSGASEELLNKLKLERDFSRYNYLSL---DSAK 241
Cdd:cd14907    164 FGKYVSILVDKKkRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLKNQLSGDRYDYLkksNCYE 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  242 VNGVDDAANFRTVRNAMQIVGFMDHEAESVLAVVAAVLKLGNIEFKpESRVNGLDESKIKDKNELKEICELTGIDQSVLE 321
Cdd:cd14907    244 VDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFD-DSTLDDNSPCCVKNKETLQIIAKLLGIDEEELK 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  322 RAFSFRTVEAKQEKVSTTLNVAQAYYARDALAKNLYSRLFSWLVNRINESI-------KAQTKVRKKVMGVLDIYGFEIF 394
Cdd:cd14907    323 EALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpkdekdQQLFQNKYLSIGLLDIFGFEVF 402
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  395 EDNSFEQFIINYCNEKLQQIFIELTLKEEQEEYIREDIE--WTHIDYFNNAIICDLIENNTNGILAMLDEECLRpGTVTD 472
Cdd:cd14907    403 QNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEdyLNQLSYTDNQDVIDLLDKPPIGIFNLLDDSCKL-ATGTD 481
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  473 ETFLEKLnqvCATHQHFesrmskcSRFLNDTSLPHSCFRIQHYAGKVLYQVEGFVDKNNDLLYRDLSQAMWKASHALIKS 552
Cdd:cd14907    482 EKLLNKI---KKQHKNN-------SKLIFPNKINKDTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISS 551
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  553 LF--------PEGNPAKINLKRPPTAGSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNEALVCHQIRYLGLLEN 624
Cdd:cd14907    552 IFsgedgsqqQNQSKQKKSQKKDKFLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYLGVLES 631
                          650       660       670       680       690       700
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1057503232  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 3.80e-166

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


Pssm-ID: 276853 [Multi-domain]  Cd Length: 667  Bit Score: 505.77  E-value: 3.80e-166
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   32 INNLKKRFDHSEIYTYIGSVVISVNPYRSLP-IYSPEKVEEYRNRNfYELSPHIFALSDEAYRSLRDQDKDQCILITGES 110
Cdd:cd14888      4 LHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFIQPS-ISKSPHVFSTASSAYQGMCNNKKSQTILISGES 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  111 GAGKTEASKLVMSYVAAVcGKGAEVN--QVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDF---------KGD 179
Cdd:cd14888     83 GAGKTESTKYVMKFLACA-GSEDIKKrsLVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFSKlkskrmsgdRGR 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  180 PLGGVISNYLLEKSRVVKQPRGERNFHVFYQLLSGASE------------------------ELLNKLKLERDFSRYNYL 235
Cdd:cd14888    162 LCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAREakntglsyeendeklakgadakpiSIDMSSFEPHLKFRYLTK 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  236 SLdSAKVNGVDDAANFRTVRNAMQIVGFMDHEAESVLAVVAAVLKLGNIEFK-PESRVNGLDESKIKDKNeLKEICELTG 314
Cdd:cd14888    242 SS-CHELPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFEnNEACSEGAVVSASCTDD-LEKVASLLG 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  315 IDQSVLERAFSFRTVEAKQEKVSTTLNVAQAYYARDALAKNLYSRLFSWLVNRINESIKAQTKVRKKVMGVLDIYGFEIF 394
Cdd:cd14888    320 VDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGYSKDNSLLFCGVLDIFGFECF 399
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  395 EDNSFEQFIINYCNEKLQQIFIELTLKEEQEEYIREDIEWTHIDYFNNAIICDLIENNTNGILAMLDEECLRPGTvTDET 474
Cdd:cd14888    400 QLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFPDNQDCVDLLQEKPLGIFCMLDEECFVPGG-KDQG 478
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  475 FLEKLNQVCATHQHFESRMSKcsrflndtslpHSCFRIQHYAGKVLYQVEGFVDKNNDLLYRDlSQAMWKAS-----HAL 549
Cdd:cd14888    479 LCNKLCQKHKGHKRFDVVKTD-----------PNSFVIVHFAGPVKYCSDGFLEKNKDQLSVD-AQEVIKNSknpfiSNL 546
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  550 IKSLFPEGNPAKINLKRPPTAGSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNEALVCHQIRYLGLLENVRVRR 629
Cdd:cd14888    547 FSAYLRRGTDGNTKKKKFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQLKYGGVLQAVQVSR 626
                          650
                   ....*....|....*....
gi 1057503232  630 AGYAFRQAYEPCLERYKML 648
Cdd:cd14888    627 AGYPVRLSHAEFYNDYRIL 645
MYSc_Myo31 cd14892
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ...
32-688 9.88e-164

class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of 17 IQ motifs and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276857 [Multi-domain]  Cd Length: 656  Bit Score: 499.29  E-value: 9.88e-164
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   32 INNLKKRFDHSEIYTYIGSVVISVNPYRSLP-IYS-PEKVEEYRNRNFYELS-PHIFALSDEAYRSLR----DQDKDQCI 104
Cdd:cd14892      4 LDVLRRRYERDAIYTFTADILISINPYKSIPlLYDvPGFDSQRKEEATASSPpPHVFSIAERAYRAMKgvgkGQGTPQSI 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  105 LITGESGAGKTEASKLVMSYVA--------AVCGKGAEV--NQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEF 174
Cdd:cd14892     84 VVSGESGAGKTEASKYIMKYLAtasklakgASTSKGAANahESIEECVLLSNLILEAFGNAKTIRNDNSSRFGKYIQIHY 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  175 DFKGDPLGGVISNYLLEKSRVVKQPRGERNFHVFYQLLSGASEELLNKLKLErDFSRYNYLSLDSA-KVNGVDDAANFRT 253
Cdd:cd14892    164 NSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELT-PAESFLFLNQGNCvEVDGVDDATEFKQ 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  254 VRNAMQIVGFMDHEAESVLAVVAAVLKLGNIEFKPESRVNGLDeSKIKDKNELKEICELTGIDQSVLERAFSFRT-VEAK 332
Cdd:cd14892    243 LRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEENADDEDVF-AQSADGVNVAKAAGLLGVDAAELMFKLVTQTtSTAR 321
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  333 QEKVSTTLNVAQAYYARDALAKNLYSRLFSWLVNRINESIKAQTKV---------RKKVMGVLDIYGFEIFEDNSFEQFI 403
Cdd:cd14892    322 GSVLEIKLTAREAKNALDALCKYLYGELFDWLISRINACHKQQTSGvtggaasptFSPFIGILDIFGFEIMPTNSFEQLC 401
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  404 INYCNEKLQQIFIELTLKEEQEEYIREDIEWTHIDYFNNAIICDLIENNTNGILAMLDEECLRPGTVTDETFLEKLNQV- 482
Cdd:cd14892    402 INFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQDNQDCLDLIQKKPLGLLPLLEEQMLLKRKTTDKQLLTIYHQTh 481
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  483 CATHQHFESRmskcsRFLNDTslphscFRIQHYAGKVLYQVEGFVDKNNDLLYRDLsqamwkashalikslfpegnpakI 562
Cdd:cd14892    482 LDKHPHYAKP-----RFECDE------FVLRHYAGDVTYDVHGFLAKNNDNLHDDL-----------------------R 527
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  563 NLKRpptAGSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNEALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCL 642
Cdd:cd14892    528 DLLR---SSSKFRTQLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVRIRREGFPIRRQFEEFY 604
                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1057503232  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 6.65e-159

class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle myosin heavy chain 2 (also called MYH2A, MYHSA2, MyHC-IIa, MYHas8, MyHC-2A) in insects and mollusks. This gene encodes a member of the class II or conventional myosin heavy chains, and functions in skeletal muscle contraction. Mutations in this gene results in inclusion body myopathy-3 and familial congenital myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276876 [Multi-domain]  Cd Length: 674  Bit Score: 487.18  E-value: 6.65e-159
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   32 INNLKKRFDHSEIYTYIGSVVISVNPYRSLPIYSPEKVEEYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITGESG 111
Cdd:cd14911      4 LHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTGESG 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  112 AGKTEASKLV---MSYVAAVCGKGA------------EVNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDF 176
Cdd:cd14911     84 AGKTENTKKViqfLAYVAASKPKGSgavphpavnpavLIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDA 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  177 KGDPLGGVISNYLLEKSRVVKQPRGERNFHVFYQLLSGASEELLNKLKLErDFSRYNYLSLDSAKVNGVDDAANFRTVRN 256
Cdd:cd14911    164 SGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILD-DVKSYAFLSNGSLPVPGVDDYAEFQATVK 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  257 AMQIVGFMDHEAESVLAVVAAVLKLGNIEFKPEsRVNglDESKIKDKNELKEICELTGIDQSVLERAFSFRTVEAKQEKV 336
Cdd:cd14911    243 SMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQE-RNN--DQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFV 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  337 STTLNVAQAYYARDALAKNLYSRLFSWLVNRINESIKAQTKVRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFI 416
Cdd:cd14911    320 TKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFN 399
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  417 ELTLKEEQEEYIREDIEWTHIDY-FNNAIICDLIENNTnGILAMLDEECLRPgTVTDETFLEKLNQVCATHQHFesrMSK 495
Cdd:cd14911    400 HTMFILEQEEYQREGIEWKFIDFgLDLQPTIDLIDKPG-GIMALLDEECWFP-KATDKTFVDKLVSAHSMHPKF---MKT 474
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  496 CSRFLNDtslphscFRIQHYAGKVLYQVEGFVDKNNDLLYRDLSQAM-----------WK-------ASHALIKSLFpeG 557
Cdd:cd14911    475 DFRGVAD-------FAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLqgsqdpfvvniWKdaeivgmAQQALTDTQF--G 545
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  558 NPAKINLKRppTAGSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNEALVCHQIRYLGLLENVRVRRAGYAFRQA 637
Cdd:cd14911    546 ARTRKGMFR--TVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIP 623
                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1057503232  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 5.03e-156

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: 479.05  E-value: 5.03e-156
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   34 NLKKRFDHSEIYTYIGSVVISVNPYRSLP-IYSPEKVEEYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITGESGA 112
Cdd:cd14904      6 NLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVSGESGA 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  113 GKTEASKLVMSYVAAVCG--KGAEVNQVkeqlLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGGVISNYLL 190
Cdd:cd14904     86 GKTETTKIVMNHLASVAGgrKDKTIAKV----IDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRGKLIGAKCETYLL 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  191 EKSRVVKQPRGERNFHVFYQLLSGASEELLNKLKLERDFSrYNYL--SLDSAKVNGVDDAANFRTVRNAMQIVGFMDHEA 268
Cdd:cd14904    162 EKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQ-YQYLgdSLAQMQIPGLDDAKLFASTQKSLSLIGLDNDAQ 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  269 ESVLAVVAAVLKLGNIEFKpESRVNGldeSKIKDKNELKEICELTGIDQSVLERAFSFRTVEAKQEKVSTTLNVAQAYYA 348
Cdd:cd14904    241 RTLFKILSGVLHLGEVMFD-KSDENG---SRISNGSQLSQVAKMLGLPTTRIEEALCNRSVVTRNESVTVPLAPVEAEEN 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  349 RDALAKNLYSRLFSWLVNRINESIKAQTKVRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKEEQEEYI 428
Cdd:cd14904    317 RDALAKAIYSKLFDWMVVKINAAISTDDDRIKGQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDVFKTVEEEYI 396
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  429 REDIEWTHIDYFNNAIICDLIENNTnGILAMLDEEcLRPGTVTDETFlekLNQVCATHQhfESRMSKCSRFlndTSLPHS 508
Cdd:cd14904    397 REGLQWDHIEYQDNQGIVEVIDGKM-GIIALMNDH-LRQPRGTEEAL---VNKIRTNHQ--TKKDNESIDF---PKVKRT 466
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  509 CFRIQHYAGKVLYQVEGFVDKNNDLLYRDLSQAMWKASHALIKSLF--------PEGNPAKINLKRPPTAGSQFKASVAT 580
Cdd:cd14904    467 QFIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFgsseapseTKEGKSGKGTKAPKSLGSQFKTSLSQ 546
                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1057503232  581 LMKNLQTKNPNYIRCIKPNDKKAAHIFNEALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKML 648
Cdd:cd14904    547 LMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAIM 614
PTZ00014 PTZ00014
myosin-A; Provisional
17-762 1.36e-154

myosin-A; Provisional


Pssm-ID: 240229 [Multi-domain]  Cd Length: 821  Bit Score: 480.68  E-value: 1.36e-154
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   17 VGDMVLLEPLNEETFINNLKKRFDHSEIYTYIGSVVISVNPYRSLPIYSPEKVEEYRN-RNFYELSPHIFALSDEAYRSL 95
Cdd:PTZ00014    98 YGDIGLLPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYRDaKDSDKLPPHVFTTARRALENL 177
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   96 RDQDKDQCILITGESGAGKTEASKLVMSYVAAvcGKGAEVNQ-VKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEF 174
Cdd:PTZ00014   178 HGVKKSQTIIVSGESGAGKTEATKQIMRYFAS--SKSGNMDLkIQNAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQL 255
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  175 DFKGDPLGGVISNYLLEKSRVVKQPRGERNFHVFYQLLSGASEELLNKLKLeRDFSRYNYLSLDSAKVNGVDDAANFRTV 254
Cdd:PTZ00014   256 GEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKL-KSLEEYKYINPKCLDVPGIDDVKDFEEV 334
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  255 RNAMQIVGFMDHEAESVLAVVAAVLKLGNIEFKPESRVNGLDESKIKDKNE--LKEICELTGIDQSVLERAFSFRTVEAK 332
Cdd:PTZ00014   335 MESFDSMGLSESQIEDIFSILSGVLLLGNVEIEGKEEGGLTDAAAISDESLevFNEACELLFLDYESLKKELTVKVTYAG 414
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  333 QEKVSTTLNVAQAYYARDALAKNLYSRLFSWLVNRINESIKAQTKVrKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQ 412
Cdd:PTZ00014   415 NQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGF-KVFIGMLDIFGFEVFKNNSLEQLFINITNEMLQ 493
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  413 QIFIELTLKEEQEEYIREDIEWTHIDYFNNAIICDLIENNTNGILAMLDEECLRPGTvTDETFLEKLNQVCATHQHFesr 492
Cdd:PTZ00014   494 KNFVDIVFERESKLYKDEGISTEELEYTSNESVIDLLCGKGKSVLSILEDQCLAPGG-TDEKFVSSCNTNLKNNPKY--- 569
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  493 mSKCSRFLNdtslphSCFRIQHYAGKVLYQVEGFVDKNNDLLYRDLSQAMWKASHALIKSLFP-----EGNPAKINLkrp 567
Cdd:PTZ00014   570 -KPAKVDSN------KNFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLFEgveveKGKLAKGQL--- 639
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  568 ptAGSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNEALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKM 647
Cdd:PTZ00014   640 --IGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKY 717
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  648 LCKQTWPHWKGPARSGVEVLFNELEIPVEEYSFGRSKIFIRnPRTLFKLEDLRKQRLEDLATLIQkiyrgwkcrthfllm 727
Cdd:PTZ00014   718 LDLAVSNDSSLDPKEKAEKLLERSGLPKDSYAIGKTMVFLK-KDAAKELTQIQREKLAAWEPLVS--------------- 781
                          730       740       750
                   ....*....|....*....|....*....|....*
gi 1057503232  728 kksqiVIAAWYRRYAQQKRYQQTKSSALVIQSYIR 762
Cdd:PTZ00014   782 -----VLEALILKIKKKRKVRKNIKSLVRIQAHLR 811
MYSc_Myo47 cd14908
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ...
32-688 8.90e-153

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


Pssm-ID: 276873 [Multi-domain]  Cd Length: 682  Bit Score: 471.31  E-value: 8.90e-153
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   32 INNLKKRFDHSEIYTYIGSVVISVNPYRSLPIYSPEKVEEYRNRNFY---------ELSPHIFALSDEAYRSL-RDQDKD 101
Cdd:cd14908      4 LHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRQEGLLrsqgiespqALGPHVFAIADRSYRQMmSEIRAS 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  102 QCILITGESGAGKTEASKLVMSYVAAVCGKGAEVNQ---------VKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDI 172
Cdd:cd14908     84 QSILISGESGAGKTESTKIVMLYLTTLGNGEEGAPNegeelgklsIMDRVLQSNPILEAFGNARTLRNDNSSRFGKFIEL 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  173 EFDFKGDPLGGVISNYLLEKSRVVKQPRGERNFHVFYQLLSGASEELLNKLKLERDFSR-------YNYLSL-DSAKVNG 244
Cdd:cd14908    164 GFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEEEHEKYEFHDGITGglqlpneFHYTGQgGAPDLRE 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  245 VDDAANFRTVRNAMQIVGFMDHEAESVLAVVAAVLKLGNIEFKPESRVNGLDESKIKDKNELKEICELTGIDQSVLERAF 324
Cdd:cd14908    244 FTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDGAAEIAEEGNEKCLARVAKLLGVDVDKLLRAL 323
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  325 SFRTVEAKQEKVSTTLNVAQAYYARDALAKNLYSRLFSWLVNRINESIKAQT-KVRKKVMGVLDIYGFEIFEDNSFEQFI 403
Cdd:cd14908    324 TSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSINWENdKDIRSSVGVLDIFGFECFAHNSFEQLC 403
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  404 INYCNEKLQQIFIELTLKEEQEEYIREDIEWTHIDYFNNAIICDLIENNTNGILAMLDEECLRPGTVTDETFLEKLNQVC 483
Cdd:cd14908    404 INFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFPDNQDCLDTIQAKKKGILTMLDDECRLGIRGSDANYASRLYETY 483
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  484 ATHQHFEsrMSKCSRFLNDTSL-PHSCFRIQHYAGKVLYQVE-GFVDKNNDLLYRDlsqamwkashalIKSLFPEgnpak 561
Cdd:cd14908    484 LPEKNQT--HSENTRFEATSIQkTKLIFAVRHFAGQVQYTVEtTFCEKNKDEIPLT------------ADSLFES----- 544
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  562 inlkrpptaGSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNEALVCHQIRYLGLLENVRVRRAGYAFRQAYEPC 641
Cdd:cd14908    545 ---------GQQFKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRYGGVLEAVRVARSGYPVRLPHKDF 615
                          650       660       670       680       690       700
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1057503232  642 LERYKMLC------KQTW-PHWKGPARSGVEVLFNEL-------------EIPVEEYSFGRSKIFIR 688
Cdd:cd14908    616 FKRYRMLLplipevVLSWsMERLDPQKLCVKKMCKDLvkgvlspamvsmkNIPEDTMQLGKSKVFMR 682
MYSc_Myh18 cd14932
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ...
30-688 1.51e-152

class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain 18. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276895 [Multi-domain]  Cd Length: 676  Bit Score: 470.66  E-value: 1.51e-152
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   30 TFINNLKKRFDHSEIYTYIGSVVISVNPYRSLPIYSPEKVEEYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITGE 109
Cdd:cd14932      2 SVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  110 SGAGKTEASKLVMSYVAAVCG-------KGAEV---NQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGD 179
Cdd:cd14932     82 SGAGKTENTKKVIQYLAYVASsfktkkdQSSIAlshGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  180 PLGGVISNYLLEKSRVVKQPRGERNFHVFYQLLSGASEELLNKLKLErDFSRYNYLSLDSAKVNGVDDAANFRTVRNAMQ 259
Cdd:cd14932    162 IVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLE-DYSKYRFLSNGNVTIPGQQDKELFAETMEAFR 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  260 IVGFMDHEAESVLAVVAAVLKLGNIEFKPESRVnglDESKIKDKNELKEICELTGIDQSVLERAFSFRTVEAKQEKVSTT 339
Cdd:cd14932    241 IMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNS---DQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQKA 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  340 LNVAQAYYARDALAKNLYSRLFSWLVNRINESIKAQTKVRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELT 419
Cdd:cd14932    318 QTQEQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTM 397
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  420 LKEEQEEYIREDIEWTHIDYFNNAIIC-DLIE--NNTNGILAMLDEECLRPgTVTDETFLEKLNQVCATHQHFEsrmsKC 496
Cdd:cd14932    398 FILEQEEYQREGIEWSFIDFGLDLQPCiELIEkpNGPPGILALLDEECWFP-KATDKSFVEKVVQEQGNNPKFQ----KP 472
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  497 SRFLNDTSlphscFRIQHYAGKVLYQVEGFVDKNNDLLYRDLSQAMWKASHALIKSLFPEGN-----------------P 559
Cdd:cd14932    473 KKLKDDAD-----FCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVDrivgldkvagmgeslhgA 547
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  560 AKINLKRPPTAGSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNEALVCHQIRYLGLLENVRVRRAGYAFRQAYE 639
Cdd:cd14932    548 FKTRKGMFRTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQ 627
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*....
gi 1057503232  640 PCLERYKMLCKQTWPHWKGPARSGVEVLFNELEIPVEEYSFGRSKIFIR 688
Cdd:cd14932    628 EFRQRYEILTPNAIPKGFMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
MYSc_Myh11 cd14921
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ...
30-688 1.25e-151

class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin heavy chain 11 (also called SMMHC, SMHC). The gene product is a subunit of a hexameric protein that consists of two heavy chain subunits and two pairs of non-identical light chain subunits. It functions as a major contractile protein, converting chemical energy into mechanical energy through the hydrolysis of ATP. The gene encoding a human ortholog of rat NUDE1 is transcribed from the reverse strand of this gene, and its 3' end overlaps with that of the latter. Inversion of the MYH11 locus is one of the most frequent chromosomal aberrations found in acute myeloid leukemia. Alternative splicing generates isoforms that are differentially expressed, with ratios changing during muscle cell maturation. Mutations in MYH11 have been described in individuals with thoracic aortic aneurysms leading to acute aortic dissections with patent ductus arteriosus. MYH11 mutations are also thought to contribute to human colorectal cancer and are also associated with Peutz-Jeghers syndrome. The mutations found in human intestinal neoplasia result in unregulated proteins with constitutive motor activity, similar to the mutant myh11 zebrafish. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276885 [Multi-domain]  Cd Length: 673  Bit Score: 468.34  E-value: 1.25e-151
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   30 TFINNLKKRFDHSEIYTYIGSVVISVNPYRSLPIYSPEKVEEYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITGE 109
Cdd:cd14921      2 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  110 SGAGKTEASKLVMSYVAAVCG--KGAE----VNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGG 183
Cdd:cd14921     82 SGAGKTENTKKVIQYLAVVASshKGKKdtsiTGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGA 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  184 VISNYLLEKSRVVKQPRGERNFHVFYQLLSGASEELLNKLKLErDFSRYNYLSLDSAKVNGVDDAANFRTVRNAMQIVGF 263
Cdd:cd14921    162 NIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLE-GFNNYTFLSNGFVPIPAAQDDEMFQETLEAMSIMGF 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  264 MDHEAESVLAVVAAVLKLGNIEFKPESRVnglDESKIKDKNELKEICELTGIDQSVLERAFSFRTVEAKQEKVSTTLNVA 343
Cdd:cd14921    241 SEEEQLSILKVVSSVLQLGNIVFKKERNT---DQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKE 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  344 QAYYARDALAKNLYSRLFSWLVNRINESIKAQTKVRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKEE 423
Cdd:cd14921    318 QADFAIEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILE 397
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  424 QEEYIREDIEWTHIDYFNNAIIC-DLIE--NNTNGILAMLDEECLRPgTVTDETFLEKLNQVCATHQHFESrmskcSRFL 500
Cdd:cd14921    398 QEEYQREGIEWNFIDFGLDLQPCiELIErpNNPPGVLALLDEECWFP-KATDKSFVEKLCTEQGNHPKFQK-----PKQL 471
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  501 NDTSLphscFRIQHYAGKVLYQVEGFVDKNNDLLYRDLSQAMWKASHALIKSLF--------------------PEGNPA 560
Cdd:cd14921    472 KDKTE----FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWkdvdrivgldqmakmtesslPSASKT 547
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  561 KINLKRppTAGSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNEALVCHQIRYLGLLENVRVRRAGYAFRQAYEP 640
Cdd:cd14921    548 KKGMFR--TVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQE 625
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*...
gi 1057503232  641 CLERYKMLCKQTWPHWKGPARSGVEVLFNELEIPVEEYSFGRSKIFIR 688
Cdd:cd14921    626 FRQRYEILAANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
MYSc_Myo34 cd14895
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ...
30-688 1.84e-150

class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short coiled-coil region, 5 tandem ANK repeats, and a carboxy-terminal FYVE domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276860 [Multi-domain]  Cd Length: 704  Bit Score: 466.35  E-value: 1.84e-150
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   30 TFINNLKKRFDHSEIYTYIGSVVISVNPYRSLP-IYSpekVEEYRNR--NFYELSPHIFALSDEAYRSLR-------DQD 99
Cdd:cd14895      2 AFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIPgLYD---LHKYREEmpGWTALPPHVFSIAEGAYRSLRrrlhepgASK 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  100 KDQCILITGESGAGKTEASKLVMSYVAAVCGKGAEVNQVK-------EQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDI 172
Cdd:cd14895     79 KNQTILVSGESGAGKTETTKFIMNYLAESSKHTTATSSSKrrraisgSELLSANPILESFGNARTLRNDNSSRFGKFVRM 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  173 -----EFDFKGDPLGGVISNYLLEKSRVVKQPRGERNFHVFYQLLSGASEELLNKLKLERDFSR-YNYLSLDSAKV--NG 244
Cdd:cd14895    159 ffeghELDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQLELLSAQeFQYISGGQCYQrnDG 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  245 VDDAANFRTVRNAMQIVGFMDHEAESVLAVVAAVLKLGNIEFKPESRVNGLDE---------------SKIKDKNELKEI 309
Cdd:cd14895    239 VRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEGEEDngaasapcrlasaspSSLTVQQHLDIV 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  310 CELTGIDQSVLERAFSFRTVEAKQEKVSTTLNVAQAYYARDALAKNLYSRLFSWLVNRINESI----------KAQTKVR 379
Cdd:cd14895    319 SKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASpqrqfalnpnKAANKDT 398
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  380 KKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKEEQEEYIREDIEWTHIDYFNNAIICDLIENNTNGILAM 459
Cdd:cd14895    399 TPCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDNSVCLEMLEQRPSGIFSL 478
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  460 LDEECLRPGTvTDETFLEKLNQVCATHQHFESrmskcSRflndTSLPHSCFRIQHYAGKVLYQVEGFVDKNNDLLYRDLS 539
Cdd:cd14895    479 LDEECVVPKG-SDAGFARKLYQRLQEHSNFSA-----SR----TDQADVAFQIHHYAGAVRYQAEGFCEKNKDQPNAELF 548
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  540 QAMWKASHALIKSL---FPEGNPAKINLKRPPT-----------AGSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAH 605
Cdd:cd14895    549 SVLGKTSDAHLRELfefFKASESAELSLGQPKLrrrssvlssvgIGSQFKQQLASLLDVVQQTQTHYIRCIKPNDESASD 628
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  606 IFNEALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKML-CKQTWPHWKgpARSGVEVLFneleipVEEYSFGRSK 684
Cdd:cd14895    629 QFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLvAAKNASDAT--ASALIETLK------VDHAELGKTR 700

                   ....
gi 1057503232  685 IFIR 688
Cdd:cd14895    701 VFLR 704
MYSc_Myo35 cd14896
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ...
34-688 3.83e-150

class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 domains, a single FERM domain, and an SH3 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276861 [Multi-domain]  Cd Length: 644  Bit Score: 463.10  E-value: 3.83e-150
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   34 NLKKRFDHSEIYTYIGSVVISVNPYRSLPIYSPEKVEEYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITGESGAG 113
Cdd:cd14896      6 CLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSGHSGSG 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  114 KTEASKLVMSYVAAVCGKGAEVN--QVKEQLlqsnPVLEAFGNAKTVRNDNSSRFGKYMDIEFDfKGDPLGGVISNYLLE 191
Cdd:cd14896     86 KTEAAKKIVQFLSSLYQDQTEDRlrQPEDVL----PILESFGHAKTILNANASRFGQVLRLHLQ-HGVIVGASVSHYLLE 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  192 KSRVVKQPRGERNFHVFYQLLSGASEELLNKLKLERDFSrYNYLSLDSA-KVNGVDDAANFRTVRNAMQIVGFMDHEAES 270
Cdd:cd14896    161 TSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQGPET-YYYLNQGGAcRLQGKEDAQDFEGLLKALQGLGLCAEELTA 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  271 VLAVVAAVLKLGNIEFKPESRvNGLDESKIKDKNELKEICELTGIDQSVLERAFSFRTVEAKQEKVSTTLNVAQAYYARD 350
Cdd:cd14896    240 IWAVLAAILQLGNICFSSSER-ESQEVAAVSSWAEIHTAARLLQVPPERLEGAVTHRVTETPYGRVSRPLPVEGAIDARD 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  351 ALAKNLYSRLFSWLVNRINESIKAQTKVRK-KVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKEEQEEYIR 429
Cdd:cd14896    319 ALAKTLYSRLFTWLLKRINAWLAPPGEAESdATIGVVDAYGFEALRVNGLEQLCINLASERLQLFSSQTLLAQEEEECQR 398
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  430 EDIEWTHIDYFNNAIICDLIENNTNGILAMLDEECLRPgTVTDETFLEKlnqvCATHQHFESRMSKcsrflndTSLPHSC 509
Cdd:cd14896    399 ELLPWVPIPQPPRESCLDLLVDQPHSLLSILDDQTWLS-QATDHTFLQK----CHYHHGDHPSYAK-------PQLPLPV 466
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  510 FRIQHYAGKVLYQVEGFVDKNNDLLYRDLSQAMWKASHALIKSLFPEGNPAKINLKRPPTAGSQFKASVATLMKNLQTKN 589
Cdd:cd14896    467 FTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQEAEPQYGLGQGKPTLASRFQQSLGDLTARLGRSH 546
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  590 PNYIRCIKPNDKKAAHIFNEALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKMLCKQTWPHWKGPARSGVeVLFN 669
Cdd:cd14896    547 VYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGALGSERQEALSDRERCGA-ILSQ 625
                          650
                   ....*....|....*....
gi 1057503232  670 ELEIPVEEYSFGRSKIFIR 688
Cdd:cd14896    626 VLGAESPLYHLGATKVLLK 644
MYSc_Myo30 cd14891
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ...
34-688 5.19e-150

class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal SH3-like domain, two IQ motifs, a coiled-coil region and a PX domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276856  Cd Length: 645  Bit Score: 462.98  E-value: 5.19e-150
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   34 NLKKRF--DHSEIYTYIGSVVISVNPYRSLPiySPeKVEEYRNRNFYELSPHIFALSDEAYRSLRDQ---DKDQCILITG 108
Cdd:cd14891      6 NLEERSklDNQRPYTFMANVLIAVNPLRRLP--EP-DKSDYINTPLDPCPPHPYAIAEMAYQQMCLGsgrMQNQSIVISG 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  109 ESGAGKTEASKLVMSYV----------------AAVCGKGAEVNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDI 172
Cdd:cd14891     83 ESGAGKTETSKIILRFLttravggkkasgqdieQSSKKRKLSVTSLDERLMDTNPILESFGNAKTLRNHNSSRFGKFMKL 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  173 EFDFKGDPL-GGVISNYLLEKSRVVKQPRGERNFHVFYQLLSGASEELLNKLKLERDFSRYNYLSLDSAKVNGVDDAANF 251
Cdd:cd14891    163 QFTKDKFKLaGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSPEDFIYLNQSGCVSDDNIDDAANF 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  252 RTVRNAMQIVGFMDHEAESVLAVVAAVLKLGNIEFKPESRVNGL-DESKIKDKNELKEICELTGIDQSVLERAFSFRTVE 330
Cdd:cd14891    243 DNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEEDTSEGEaEIASESDKEALATAAELLGVDEEALEKVITQREIV 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  331 AKQEKVSTTLNVAQAYYARDALAKNLYSRLFSWLVNRINESIKAQTKVRKKVmGVLDIYGFEIFE-DNSFEQFIINYCNE 409
Cdd:cd14891    323 TRGETFTIKRNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGHDPDPLPYI-GVLDIFGFESFEtKNDFEQLLINYANE 401
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  410 KLQQIFIELTLKEEQEEYIREDIEWTHIDYFNNAIICDLIENNTNGILAMLDEECLRPGTvTDETFLEKLNQVCATHQHF 489
Cdd:cd14891    402 ALQATFNQQVFIAEQELYKSEGIDVGVITWPDNRECLDLIASKPNGILPLLDNEARNPNP-SDAKLNETLHKTHKRHPCF 480
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  490 ESRMSKCSRFlndtslphsCFRIQHYAGKVLYQVEGFVDKNNDLLYRDLSqamwkashalikSLFpegnpakinlkrppT 569
Cdd:cd14891    481 PRPHPKDMRE---------MFIVKHYAGTVSYTIGSFIDKNNDIIPEDFE------------DLL--------------A 525
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  570 AGSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNEALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYK-ML 648
Cdd:cd14891    526 SSAKFSDQMQELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVLKVGLPTRVTYAELVDVYKpVL 605
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|
gi 1057503232  649 CKQTWPHWKGPARSGVEVLFNELEIPVEEYSFGRSKIFIR 688
Cdd:cd14891    606 PPSVTRLFAENDRTLTQAILWAFRVPSDAYRLGRTRVFFR 645
MYSc_Myo28 cd14889
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ...
31-688 1.28e-148

class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The tail regions of these class-XXVIII myosins consist of an IQ motif, a short coiled-coil region, and an SH2 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276854  Cd Length: 659  Bit Score: 459.76  E-value: 1.28e-148
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   31 FINNLKKRFDHSEIYTYIGSVVISVNPYRSLPIYSPEKVEEYRNRNFYELSPHIFALSDEAYRSLRDQ----DKDQCILI 106
Cdd:cd14889      3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLGRlargPKNQCIVI 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  107 TGESGAGKTEASKLVMSYVAAVCgKGAevNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFdFKGDPLGGVIS 186
Cdd:cd14889     83 SGESGAGKTESTKLLLRQIMELC-RGN--SQLEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRF-RNGHVKGAKIN 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  187 NYLLEKSRVVKQPRGERNFHVFYQLLSGASEELLNKLKLeRDFSRYNYLSldsAKVNGVDDAANFRT----VRNAMQIVG 262
Cdd:cd14889    159 EYLLEKSRVVHQDGGEENFHIFYYMFAGISAEDRENYGL-LDPGKYRYLN---NGAGCKREVQYWKKkydeVCNAMDMVG 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  263 FMDHEAESVLAVVAAVLKLGNIEFKPESrvNGLDESKIKDKNELKEICELTGIDQSVLERAFSFRTVEAKQEKVSTTLNV 342
Cdd:cd14889    235 FTEQEEVDMFTILAGILSLGNITFEMDD--DEALKVENDSNGWLKAAAGQFGVSEEDLLKTLTCTVTFTRGEQIQRHHTK 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  343 AQAYYARDALAKNLYSRLFSWLVNRINESI--KAQTKVRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTL 420
Cdd:cd14889    313 QQAEDARDSIAKVAYGRVFGWIVSKINQLLapKDDSSVELREIGILDIFGFENFAVNRFEQACINLANEQLQYFFNHHIF 392
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  421 KEEQEEYIREDIEWTHIDYFNNAIICDLIENNTNGILAMLDEECLRPgTVTDETFLEKLNQVCATHQHFESRMSKCSRfl 500
Cdd:cd14889    393 LMEQKEYKKEGIDWKEITYKDNKPILDLFLNKPIGILSLLDEQSHFP-QATDESFVDKLNIHFKGNSYYGKSRSKSPK-- 469
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  501 ndtslphscFRIQHYAGKVLYQVEGFVDKNNDLLYRDLSQAMWKASHALIKSLF----------------PEGNPAKINL 564
Cdd:cd14889    470 ---------FTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFtatrsrtgtlmpraklPQAGSDNFNS 540
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  565 KRPPTAGSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNEALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLER 644
Cdd:cd14889    541 TRKQSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFSWRPSFAEFAER 620
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*
gi 1057503232  645 YK-MLCKQTWPHWKGPARSgvevLFNELEIpvEEYSFGRSKIFIR 688
Cdd:cd14889    621 YKiLLCEPALPGTKQSCLR----ILKATKL--VGWKCGKTRLFFK 659
MYSc_Myh3 cd14913
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ...
34-688 4.99e-148

class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle myosin heavy chain 3 (MYHC-EMB, MYHSE1, HEMHC, SMHCE) in tetrapods including mammals, lizards, and frogs. This gene is a member of the MYH family and encodes a protein with an IQ domain and a myosin head-like domain. Mutations in this gene have been associated with two congenital contracture (arthrogryposis) syndromes, Freeman-Sheldon syndrome and Sheldon-Hall syndrome. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276878 [Multi-domain]  Cd Length: 668  Bit Score: 458.75  E-value: 4.99e-148
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   34 NLKKRFDHSEIYTYIGSVVISVNPYRSLPIYSPEKVEEYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITGESGAG 113
Cdd:cd14913      6 NLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESGAG 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  114 KTEASKLVMSYVAAVCGKGAEVNQ--------VKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGGVI 185
Cdd:cd14913     86 KTVNTKRVIQYFATIAATGDLAKKkdskmkgtLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLASADI 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  186 SNYLLEKSRVVKQPRGERNFHVFYQLLSGASEELLNKLKLERDFSRYNYLSLDSAKVNGVDDAANFRTVRNAMQIVGFMD 265
Cdd:cd14913    166 ETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPYDYPFISQGEILVASIDDAEELLATDSAIDILGFTP 245
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  266 HEAESVLAVVAAVLKLGNIEFKPESRvnglDESKIKDKNELKE-ICELTGIDQSVLERAFSFRTVEAKQEKVSTTLNVAQ 344
Cdd:cd14913    246 EEKSGLYKLTGAVMHYGNMKFKQKQR----EEQAEPDGTEVADkTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTVDQ 321
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  345 AYYARDALAKNLYSRLFSWLVNRINESIkaQTKV-RKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKEE 423
Cdd:cd14913    322 VHHAVNALSKSVYEKLFLWMVTRINQQL--DTKLpRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVLE 399
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  424 QEEYIREDIEWTHIDYFNNAIIC-DLIENNTnGILAMLDEECLRPgTVTDETFLEKLnqvcathqhFESRMSKCSRFLND 502
Cdd:cd14913    400 QEEYKKEGIEWTFIDFGMDLAACiELIEKPM-GIFSILEEECMFP-KATDTSFKNKL---------YDQHLGKSNNFQKP 468
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  503 TSL---PHSCFRIQHYAGKVLYQVEGFVDKNNDLLYRDLSQAMWKASHALIKSLFP--EGNPAKINLKRPP--------T 569
Cdd:cd14913    469 KVVkgrAEAHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYAtfATADADSGKKKVAkkkgssfqT 548
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  570 AGSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNEALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKMLC 649
Cdd:cd14913    549 VSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLN 628
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|
gi 1057503232  650 KQTWPHWKG-PARSGVEVLFNELEIPVEEYSFGRSKIFIR 688
Cdd:cd14913    629 ASAIPEGQFiDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
MYSc_Myh9 cd14919
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ...
30-688 4.15e-147

class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy chain 9 (also called NMMHCA, NMHC-II-A, MHA, FTNS, EPSTS, and DFNA17). Myosin is a hexameric protein composed of a pair of myosin heavy chains (MYH) and two pairs of nonidentical light chains. The encoded protein is a myosin IIA heavy chain that contains an IQ domain and a myosin head-like domain which is involved in several important functions, including cytokinesis, cell motility and maintenance of cell shape. Defects in this gene have been associated with non-syndromic sensorineural deafness autosomal dominant type 17, Epstein syndrome, Alport syndrome with macrothrombocytopenia, Sebastian syndrome, Fechtner syndrome and macrothrombocytopenia with progressive sensorineural deafness. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276883 [Multi-domain]  Cd Length: 670  Bit Score: 456.09  E-value: 4.15e-147
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   30 TFINNLKKRFDHSEIYTYIGSVVISVNPYRSLPIYSPEKVEEYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITGE 109
Cdd:cd14919      2 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  110 SGAGKTEASKLVMSYVAAVCGK---GAEVNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGGVIS 186
Cdd:cd14919     82 SGAGKTENTKKVIQYLAHVASShksKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIE 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  187 NYLLEKSRVVKQPRGERNFHVFYQLLSGASEELLNKLKLErDFSRYNYLSLDSAKVNGVDDAANFRTVRNAMQIVGFMDH 266
Cdd:cd14919    162 TYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLE-PYNKYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGIPEE 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  267 EAESVLAVVAAVLKLGNIEFKPESRVnglDESKIKDKNELKEICELTGIDQSVLERAFSFRTVEAKQEKVSTTLNVAQAY 346
Cdd:cd14919    241 EQMGLLRVISGVLQLGNIVFKKERNT---DQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQAD 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  347 YARDALAKNLYSRLFSWLVNRINESIKAQTKVRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKEEQEE 426
Cdd:cd14919    318 FAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEE 397
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  427 YIREDIEWTHIDYFNNAIIC-DLIENNTN--GILAMLDEECLRPgTVTDETFLEKLNQVCATHQHFESrmskcSRFLNDT 503
Cdd:cd14919    398 YQREGIEWNFIDFGLDLQPCiDLIEKPAGppGILALLDEECWFP-KATDKSFVEKVVQEQGTHPKFQK-----PKQLKDK 471
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  504 slphSCFRIQHYAGKVLYQVEGFVDKNNDLLYRDLSQAMWKASHALIKSLFPEGN----------------PAKINLKRP 567
Cdd:cd14919    472 ----ADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDriigldqvagmsetalPGAFKTRKG 547
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  568 --PTAGSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNEALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERY 645
Cdd:cd14919    548 mfRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRY 627
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|...
gi 1057503232  646 KMLCKQTWPHWKGPARSGVEVLFNELEIPVEEYSFGRSKIFIR 688
Cdd:cd14919    628 EILTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
MYSc_Myh15_mammals cd14929
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ...
30-688 4.22e-147

class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy chain 15 in mammals (also called KIAA1000) . MYH15 is a slow-twitch myosin. Myh15 is a ventricular myosin heavy chain. Myh15 is absent in embryonic and fetal muscles and is found in orbital layer of extraocular muscles at birth. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276892 [Multi-domain]  Cd Length: 662  Bit Score: 455.97  E-value: 4.22e-147
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   30 TFINNLKKRFDHSEIYTYIGSVVISVNPYRSLPIYSPEKVEEYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITGE 109
Cdd:cd14929      2 SVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTGE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  110 SGAGKTEASKLVMSY---VAAVCGKGAEVNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGGVIS 186
Cdd:cd14929     82 SGAGKTVNTKHIIQYfatIAAMIESKKKLGALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSADID 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  187 NYLLEKSRVVKQPRGERNFHVFYQLLSGaSEELLNKLKLERDFSRYNYLSLDSAKVNGVDDAANFRTVRNAMQIVGFMDH 266
Cdd:cd14929    162 IYLLEKSRVIFQQPGERNYHIFYQILSG-KKELRDLLLVSANPSDFHFCSCGAVAVESLDDAEELLATEQAMDILGFLPD 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  267 EAESVLAVVAAVLKLGNIEFKPESRVNGL--DESKIKDKNELkeiceLTGIDQSVLERAFSFRTVEAKQEKVSTTLNVAQ 344
Cdd:cd14929    241 EKYGCYKLTGAIMHFGNMKFKQKPREEQLeaDGTENADKAAF-----LMGINSSELVKGLIHPRIKVGNEYVTRSQNIEQ 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  345 AYYARDALAKNLYSRLFSWLVNRINESIKAQTKvRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKEEQ 424
Cdd:cd14929    316 VTYAVGALSKSIYERMFKWLVARINRVLDAKLS-RQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMFVLEQ 394
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  425 EEYIREDIEWTHIDYFNNAIIC-DLIENNTnGILAMLDEECLRPgTVTDETFLEKLnqvcathqhFESRMSKCSRFLNDT 503
Cdd:cd14929    395 EEYRKEGIDWVSIDFGLDLQACiDLIEKPM-GIFSILEEECMFP-KATDLTFKTKL---------FDNHFGKSVHFQKPK 463
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  504 SLPHSC---FRIQHYAGKVLYQVEGFVDKNNDLLYRDLSQAMWKASHALIKSLFPE---GNPAKINLKRPPTAGSQF--- 574
Cdd:cd14929    464 PDKKKFeahFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENyisTDSAIQFGEKKRKKGASFqtv 543
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  575 ----KASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNEALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKMLCK 650
Cdd:cd14929    544 aslhKENLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNP 623
                          650       660       670
                   ....*....|....*....|....*....|....*....
gi 1057503232  651 QTWPHWK-GPARSGVEVLFNELEIPVEEYSFGRSKIFIR 688
Cdd:cd14929    624 RTFPKSKfVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
MYSc_Myo39 cd14900
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ...
30-655 5.00e-144

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


Pssm-ID: 276865  Cd Length: 627  Bit Score: 446.68  E-value: 5.00e-144
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   30 TFINNLKKRFDHSEIYTYIGSVVISVNPYRSLP-IYSPEKVEEY-----------RNRNFYELSPHIFALSDEAYRSLRD 97
Cdd:cd14900      2 TILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssstRNKGSDPMPPHIYQVAGEAYKAMML 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   98 ----QDKDQCILITGESGAGKTEASKLVMSYVAAV--------CGKGAEVNQVKEQLLQSNPVLEAFGNAKTVRNDNSSR 165
Cdd:cd14900     82 glngVMSDQSILVSGESGSGKTESTKFLMEYLAQAgdnnlaasVSMGKSTSGIAAKVLQTNILLESFGNARTLRNDNSSR 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  166 FGKYMDIEFDFKGDPLGGVISNYLLEKSRVVKQPRGERNFHVFYQLLSGASEEllnklKLERDfsrynylsldsakvngv 245
Cdd:cd14900    162 FGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASEA-----ARKRD----------------- 219
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  246 ddaaNFRTVRNAMQIVGFMDHEAESVLAVVAAVLKLGNIEFK--PESRVNGLDESKIKDKNE--LKEICELTGIDQSVLE 321
Cdd:cd14900    220 ----MYRRVMDAMDIIGFTPHERAGIFDLLAALLHIGNLTFEhdENSDRLGQLKSDLAPSSIwsRDAAATLLSVDATKLE 295
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  322 RAFSFRTVEAKQEKVSTTLNVAQAYYARDALAKNLYSRLFSWLVNRINESIK----AQTKVRKKVMGVLDIYGFEIFEDN 397
Cdd:cd14900    296 KALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLKmddsSKSHGGLHFIGILDIFGFEVFPKN 375
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  398 SFEQFIINYCNEKLQQIFIELTLKEEQEEYIREDIEWTHIDYFNNAIICDLIENNTNGILAMLDEECLRPGTvTDETFLE 477
Cdd:cd14900    376 SFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFCDNQDCVNLISQRPTGILSLIDEECVMPKG-SDTTLAS 454
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  478 KLNQVCATHQHFESRMSKCSRFLndtslphscFRIQHYAGKVLYQVEGFVDKNNDLLYRDlsqamwkashalIKSLFpeg 557
Cdd:cd14900    455 KLYRACGSHPRFSASRIQRARGL---------FTIVHYAGHVEYSTDGFLEKNKDVLHQE------------AVDLF--- 510
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  558 npakinlkrppTAGSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNEALVCHQIRYLGLLENVRVRRAGYAFRQA 637
Cdd:cd14900    511 -----------VYGLQFKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVMEAVRVARAGFPIRLL 579
                          650
                   ....*....|....*...
gi 1057503232  638 YEPCLERYKMLCKQTWPH 655
Cdd:cd14900    580 HDEFVARYFSLARAKNRL 597
MYSc_Myh7b cd14927
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ...
34-688 3.53e-143

class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta myosin heavy chain 7b (also called KIAA1512, dJ756N5.1, MYH14, MHC14). MYH7B is a slow-twitch myosin. Mutations in this gene result in one form of autosomal dominant hearing impairment. Multiple transcript variants encoding different isoforms have been found for this gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276953 [Multi-domain]  Cd Length: 676  Bit Score: 446.32  E-value: 3.53e-143
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   34 NLKKRFDHSEIYTYIGSVVISVNPYRSLPIYSPEKVEEYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITGESGAG 113
Cdd:cd14927      6 NLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITGESGAG 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  114 KTEASKLVMSYVAAVCGKGAEVNQ------------VKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPL 181
Cdd:cd14927     86 KTVNTKRVIQYFAIVAALGDGPGKkaqflatktggtLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPTGKLA 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  182 GGVISNYLLEKSRVVKQPRGERNFHVFYQLLSGASEELLNKLKLERDFSRYNYLSLDSAKVNGVDDAANFRTVRNAMQIV 261
Cdd:cd14927    166 SADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLVSMNPYDYHFCSQGVTTVDNMDDGEELMATDHAMDIL 245
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  262 GFMDHEAESVLAVVAAVLKLGNIEFKPESRvnglDESKIKDKNE-LKEICELTGIDQSVLERAFSFRTVEAKQEKVSTTL 340
Cdd:cd14927    246 GFSPDEKYGCYKIVGAIMHFGNMKFKQKQR----EEQAEADGTEsADKAAYLMGVSSADLLKGLLHPRVKVGNEYVTKGQ 321
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  341 NVAQAYYARDALAKNLYSRLFSWLVNRINESIKAQTKvRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTL 420
Cdd:cd14927    322 SVEQVVYAVGALAKATYDRMFKWLVSRINQTLDTKLP-RQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMF 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  421 KEEQEEYIREDIEWTHIDYFNNAIIC-DLIENNTnGILAMLDEECLRPgTVTDETFLEKL--NQVCATHQHFESRMSKCS 497
Cdd:cd14927    401 ILEQEEYKREGIEWVFIDFGLDLQACiDLIEKPL-GILSILEEECMFP-KASDASFKAKLydNHLGKSPNFQKPRPDKKR 478
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  498 RFlndtslpHSCFRIQHYAGKVLYQVEGFVDKNNDLLYRDLSQAMWKASHALIKSLF-------PEGNP-AKINLKRPPT 569
Cdd:cd14927    479 KY-------EAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYenyvgsdSTEDPkSGVKEKRKKA 551
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  570 AGSQ-----FKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNEALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLER 644
Cdd:cd14927    552 ASFQtvsqlHKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQR 631
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*
gi 1057503232  645 YKMLCKQTWPHWK-GPARSGVEVLFNELEIPVEEYSFGRSKIFIR 688
Cdd:cd14927    632 YRILNPSAIPDDKfVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
MYSc_Myh14_mammals cd14930
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ...
30-688 2.01e-142

class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy chain 14 (also called FLJ13881, KIAA2034, MHC16, MYH17). Its members include mammals, chickens, and turtles. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Some of the data used for this classification were produced by the CyMoBase team at the Max-Planck-Institute for Biophysical Chemistry. The sequence names are composed of the species abbreviation followed by the protein abbreviation and optional protein classifier and variant designations.


Pssm-ID: 276893 [Multi-domain]  Cd Length: 670  Bit Score: 444.15  E-value: 2.01e-142
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   30 TFINNLKKRFDHSEIYTYIGSVVISVNPYRSLPIYSPEKVEEYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITGE 109
Cdd:cd14930      2 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  110 SGAGKTEASKLVMSYVAAVCG--KGAE----VNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGG 183
Cdd:cd14930     82 SGAGKTENTKKVIQYLAHVASspKGRKepgvPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVGA 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  184 VISNYLLEKSRVVKQPRGERNFHVFYQLLSGASEELLNKLKLErDFSRYNYLSLDSAKVNGvDDAANFRTVRNAMQIVGF 263
Cdd:cd14930    162 NIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLE-PCSHYRFLTNGPSSSPG-QERELFQETLESLRVLGF 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  264 MDHEAESVLAVVAAVLKLGNIEFKPESRVnglDESKIKDKNELKEICELTGIDQSVLERAFSFRTVEAKQEKVSTTLNVA 343
Cdd:cd14930    240 SHEEITSMLRMVSAVLQFGNIVLKRERNT---DQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKE 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  344 QAYYARDALAKNLYSRLFSWLVNRINESIKAQTKVRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKEE 423
Cdd:cd14930    317 QADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLE 396
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  424 QEEYIREDIEWTHIDYFNNAIIC-DLIENNTN--GILAMLDEECLRPgTVTDETFLEKLNQVCATHQHFESrmskcSRFL 500
Cdd:cd14930    397 QEEYQREGIPWTFLDFGLDLQPCiDLIERPANppGLLALLDEECWFP-KATDKSFVEKVAQEQGGHPKFQR-----PRHL 470
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  501 NDtslpHSCFRIQHYAGKVLYQVEGFVDKNND--------LLYRD---LSQAMWKASHAL-----IKSLF---PEGNPAK 561
Cdd:cd14930    471 RD----QADFSVLHYAGKVDYKANEWLMKNMDplndnvaaLLHQStdrLTAEIWKDVEGIvgleqVSSLGdgpPGGRPRR 546
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  562 INLKrppTAGSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNEALVCHQIRYLGLLENVRVRRAGYAFRQAYEPC 641
Cdd:cd14930    547 GMFR---TVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEF 623
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*..
gi 1057503232  642 LERYKMLCKQTWPHWKGPARSGVEVLFNELEIPVEEYSFGRSKIFIR 688
Cdd:cd14930    624 RQRYEILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
MYSc_Myh19 cd15896
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ...
30-688 2.05e-142

class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain 19. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276899 [Multi-domain]  Cd Length: 675  Bit Score: 444.12  E-value: 2.05e-142
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   30 TFINNLKKRFDHSEIYTYIGSVVISVNPYRSLPIYSPEKVEEYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITGE 109
Cdd:cd15896      2 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  110 SGAGKTEASKLVMSYVAAVCGK----------GAEVNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGD 179
Cdd:cd15896     82 SGAGKTENTKKVIQYLAHVASShktkkdqnslALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  180 PLGGVISNYLLEKSRVVKQPRGERNFHVFYQLLSGASEELLNKLKLErDFSRYNYLSLDSAKVNGVDDAANFRTVRNAMQ 259
Cdd:cd15896    162 IVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLE-NYNNYRFLSNGNVTIPGQQDKDLFTETMEAFR 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  260 IVGFMDHEAESVLAVVAAVLKLGNIEFKPESRVnglDESKIKDKNELKEICELTGIDQSVLERAFSFRTVEAKQEKVSTT 339
Cdd:cd15896    241 IMGIPEDEQIGMLKVVASVLQLGNMSFKKERHT---DQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQKA 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  340 LNVAQAYYARDALAKNLYSRLFSWLVNRINESIKAQTKVRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELT 419
Cdd:cd15896    318 QTQEQAEFAVEALAKATYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTM 397
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  420 LKEEQEEYIREDIEWTHIDYFNNAIIC-DLIENNTN--GILAMLDEECLRPgTVTDETFLEKLNQVCATHQHFESrmskc 496
Cdd:cd15896    398 FILEQEEYQREGIEWSFIDFGLDLQPCiDLIEKPASppGILALLDEECWFP-KATDKSFVEKVLQEQGTHPKFFK----- 471
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  497 SRFLNDtslpHSCFRIQHYAGKVLYQVEGFVDKNNDLLYRDLSQAMWKASHALIKSLFPEGN--------------PAKI 562
Cdd:cd15896    472 PKKLKD----EADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVDrivgldkvsgmsemPGAF 547
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  563 NLKRP--PTAGSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNEALVCHQIRYLGLLENVRVRRAGYAFRQAYEP 640
Cdd:cd15896    548 KTRKGmfRTVGQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQE 627
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*...
gi 1057503232  641 CLERYKMLCKQTWPHWKGPARSGVEVLFNELEIPVEEYSFGRSKIFIR 688
Cdd:cd15896    628 FRQRYEILTPNAIPKGFMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
MYSc_Myh7 cd14917
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ...
34-688 2.90e-142

class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I cardiac muscle myosin heavy chain 7 (also called CMH1, MPD1, and CMD1S). Muscle myosin is a hexameric protein containing 2 heavy chain subunits, 2 alkali light chain subunits, and 2 regulatory light chain subunits. It is expressed predominantly in normal human ventrical and in skeletal muscle tissues rich in slow-twitch type I muscle fibers. Changes in the relative abundance of this protein and the alpha (or fast) heavy subunit of cardiac myosin correlate with the contractile velocity of cardiac muscle. Its expression is also altered during thyroid hormone depletion and hemodynamic overloading. Mutations in this gene are associated with familial hypertrophic cardiomyopathy, myosin storage myopathy, dilated cardiomyopathy, and Laing early-onset distal myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276881 [Multi-domain]  Cd Length: 668  Bit Score: 443.39  E-value: 2.90e-142
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   34 NLKKRFDHSEIYTYIGSVVISVNPYRSLPIYSPEKVEEYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITGESGAG 113
Cdd:cd14917      6 NLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGESGAG 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  114 KTEASKLVMSYVAAVCGKGAEVNQ--------VKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGGVI 185
Cdd:cd14917     86 KTVNTKRVIQYFAVIAAIGDRSKKdqtpgkgtLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASADI 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  186 SNYLLEKSRVVKQPRGERNFHVFYQLLSGASEELLNKLKLERDFSRYNYLSLDSAKVNGVDDAANFRTVRNAMQIVGFMD 265
Cdd:cd14917    166 ETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNAFDVLGFTS 245
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  266 HEAESVLAVVAAVLKLGNIEFKPESRVnglDESKIKDKNELKEICELTGIDQSVLERAFSFRTVEAKQEKVSTTLNVAQA 345
Cdd:cd14917    246 EEKNSMYKLTGAIMHFGNMKFKQKQRE---EQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQQV 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  346 YYARDALAKNLYSRLFSWLVNRINESIKAQtKVRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKEEQE 425
Cdd:cd14917    323 IYATGALAKAVYEKMFNWMVTRINATLETK-QPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQE 401
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  426 EYIREDIEWTHIDYFNNAIIC-DLIENNTnGILAMLDEECLRPgTVTDETFLEKLnqvcathqhFESRMSKCSRFLNDTS 504
Cdd:cd14917    402 EYKKEGIEWTFIDFGMDLQACiDLIEKPM-GIMSILEEECMFP-KATDMTFKAKL---------FDNHLGKSNNFQKPRN 470
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  505 L---PHSCFRIQHYAGKVLYQVEGFVDKNNDLLYRDLSQAMWKASHALIKSLFPE--GNPAKINL-KRPPTAGSQFKASV 578
Cdd:cd14917    471 IkgkPEAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFANyaGADAPIEKgKGKAKKGSSFQTVS 550
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  579 A-------TLMKNLQTKNPNYIRCIKPNDKKAAHIFNEALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKMLCKQ 651
Cdd:cd14917    551 AlhrenlnKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPA 630
                          650       660       670
                   ....*....|....*....|....*....|....*...
gi 1057503232  652 TWPHWKG-PARSGVEVLFNELEIPVEEYSFGRSKIFIR 688
Cdd:cd14917    631 AIPEGQFiDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
MYSc_Myo14 cd14876
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ...
35-688 5.20e-141

class XIV myosin, motor domain; These myosins localize to plasma membranes of the intracellular parasites and may be involved in the cell invasion process. Their known functions include: transporting phagosomes to the nucleus and perturbing the developmentally regulated elimination of the macronucleus during conjugation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to their motor domain these myosins have a MyTH4-FERM protein domain combination. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276843  Cd Length: 649  Bit Score: 439.42  E-value: 5.20e-141
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   35 LKKRFDHSEIYTYIGSVVISVNPYRSLPIYSPEKVEEYRN-RNFYELSPHIFALSDEAYRSLRDQDKDQCILITGESGAG 113
Cdd:cd14876      7 LKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDaPDLTKLPPHVFYTARRALENLHGVNKSQTIIVSGESGAG 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  114 KTEASKLVMSYVAAVcGKGAEVNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGGVISNYLLEKS 193
Cdd:cd14876     87 KTEATKQIMRYFASA-KSGNMDLRIQTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVASEGGIRYGSVVAFLLEKS 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  194 RVVKQPRGERNFHVFYQLLSGASEELLNKLKLeRDFSRYNYLSLDSAKVNGVDDAANFRTVRNAMQIVGFMDHEAESVLA 273
Cdd:cd14876    166 RIVTQDDNERSYHIFYQLLKGADSEMKSKYHL-LGLKEYKFLNPKCLDVPGIDDVADFEEVLESLKSMGLTEEQIDTVFS 244
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  274 VVAAVLKLGNIEFKPESRvNGLDES-KI--KDKNELKEICELTGIDQSVLERAFSFRTVEAKQEKVSTTLNVAQAYYARD 350
Cdd:cd14876    245 IVSGVLLLGNVKITGKTE-QGVDDAaAIsnESLEVFKEACSLLFLDPEALKRELTVKVTKAGGQEIEGRWTKDDAEMLKL 323
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  351 ALAKNLYSRLFSWLVNRINESIKAQTKVrKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKEEQEEYIRE 430
Cdd:cd14876    324 SLAKAMYDKLFLWIIRNLNSTIEPPGGF-KNFMGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFIDIVFERESKLYKDE 402
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  431 DIEWTHIDYFNNAIICDLIENNTNGILAMLDEECLRPGTvTDETFLEKLNQVCATHQHFESrmSKCSRFLNdtslphscF 510
Cdd:cd14876    403 GIPTAELEYTSNAEVIDVLCGKGKSVLSILEDQCLAPGG-SDEKFVSACVSKLKSNGKFKP--AKVDSNIN--------F 471
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  511 RIQHYAGKVLYQVEGFVDKNNDLLYRDLSQAMWKASHALIKSLFP-----EGNPAKINLkrpptAGSQFKASVATLMKNL 585
Cdd:cd14876    472 IVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEgvvveKGKIAKGSL-----IGSQFLKQLESLMGLI 546
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  586 QTKNPNYIRCIKPNDKKAAHIFNEALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKMLCKQTWPHWKGPARSGVE 665
Cdd:cd14876    547 NSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEFLYQFKFLDLGIANDKSLDPKVAAL 626
                          650       660
                   ....*....|....*....|...
gi 1057503232  666 VLFNELEIPVEEYSFGRSKIFIR 688
Cdd:cd14876    627 KLLESSGLSEDEYAIGKTMVFLK 649
MYSc_Myh1_insects_crustaceans cd14909
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ...
32-688 7.58e-140

class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle myosin heavy chain 1 (also called MYHSA1, MYHa, MyHC-2X/D, MGC133384) in insects and crustaceans. Myh1 is a type I skeletal muscle myosin that in Humans is encoded by the MYH1 gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276874  Cd Length: 666  Bit Score: 436.96  E-value: 7.58e-140
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   32 INNLKKRFDHSEIYTYIGSVVISVNPYRSLPIYSPEKVEEYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITGESG 111
Cdd:cd14909      4 LHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITGESG 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  112 AGKTEASKLVMSYVAAVCG------KGAEVNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGGVI 185
Cdd:cd14909     84 AGKTENTKKVIAYFATVGAskktdeAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLAGADI 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  186 SNYLLEKSRVVKQPRGERNFHVFYQLLSGASEELLNKLKLERDFSRYNYLSLDSAKVNGVDDAANFRTVRNAMQIVGFMD 265
Cdd:cd14909    164 ETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLSDNIYDYYIVSQGKVTVPNVDDGEEFSLTDQAFDILGFTK 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  266 HEAESVLAVVAAVLKLGNIEFKPESRvnglDESKIKDKNELKE-ICELTGIDQSVLERAFSFRTVEAKQEKVSTTLNVAQ 344
Cdd:cd14909    244 QEKEDVYRITAAVMHMGGMKFKQRGR----EEQAEQDGEEEGGrVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNVQQ 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  345 AYYARDALAKNLYSRLFSWLVNRINESIKAQTKvRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKEEQ 424
Cdd:cd14909    320 VTNSIGALCKGVFDRLFKWLVKKCNETLDTQQK-RQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLEQ 398
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  425 EEYIREDIEWTHIDYFNNAIIC-DLIENNTnGILAMLDEECLRPgTVTDETFLEKLNqvcATHqhfesrMSKCSRFLNDT 503
Cdd:cd14909    399 EEYKREGIDWAFIDFGMDLLACiDLIEKPM-GILSILEEESMFP-KATDQTFSEKLT---NTH------LGKSAPFQKPK 467
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  504 SLPHSC----FRIQHYAGKVLYQVEGFVDKNNDLLYRDLSQAMWKASHALIKSLFPE-----GNPAKINLKRP------P 568
Cdd:cd14909    468 PPKPGQqaahFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADhagqsGGGEQAKGGRGkkgggfA 547
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  569 TAGSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNEALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKML 648
Cdd:cd14909    548 TVSSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKIL 627
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|
gi 1057503232  649 CKQTWPHWKGPaRSGVEVLFNELEIPVEEYSFGRSKIFIR 688
Cdd:cd14909    628 NPAGIQGEEDP-KKAAEIILESIALDPDQYRLGHTKVFFR 666
MYSc_Myo41 cd14902
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ...
35-654 2.23e-139

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


Pssm-ID: 276867 [Multi-domain]  Cd Length: 716  Bit Score: 437.40  E-value: 2.23e-139
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   35 LKKRFDHSEIYTYIGSVVISVNPYRSLP-IYSPEKVEEYR--------NRNFYELSPHIFALSDEAYRSLRDQDK-DQCI 104
Cdd:cd14902      7 LSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLKPERrNQSI 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  105 LITGESGAGKTEASKLVMSYVAAV-----CGKGAEVNQVK--EQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFK 177
Cdd:cd14902     87 LVSGESGSGKTESTKFLMQFLTSVgrdqsSTEQEGSDAVEigKRILQTNPILESFGNAQTIRNDNSSRFGKFIKIQFGAN 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  178 GDPLGGVISNYLLEKSRVVKQPRGERNFHVFYQLLSGASEELLNKLKLERDFsryNYLSLDS-------AKVNGVDDAAN 250
Cdd:cd14902    167 NEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKGG---KYELLNSygpsfarKRAVADKYAQL 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  251 FRTVRNAMQIVGFMDHEAESVLAVVAAVLKLGNIEFKPESrvNGLDESKIKDKNE--LKEICELTGIDQSVLERAFSFRT 328
Cdd:cd14902    244 YVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAEN--GQEDATAVTAASRfhLAKCAELMGVDVDKLETLLSSRE 321
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  329 VEAKQEKVSTTLNVAQAYYARDALAKNLYSRLFSWLVNRINESIKA--------QTKVRKKVMGVLDIYGFEIFEDNSFE 400
Cdd:cd14902    322 IKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINYfdsavsisDEDEELATIGILDIFGFESLNRNGFE 401
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  401 QFIINYCNEKLQQIFIELTLKEEQEEYIREDIEWTHIDYFNNAIICDLIENNTNGILAMLDEECLRPGTvTDETFLEKLN 480
Cdd:cd14902    402 QLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYPSNAACLALFDDKSNGLFSLLDQECLMPKG-SNQALSTKFY 480
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  481 QvcathqhfesrmskcsrflndTSLPHSCFRIQHYAGKVLYQVEGFVDKNNDLLYRDLSQAMWKASHALIKSLFPEGN-- 558
Cdd:cd14902    481 R---------------------YHGGLGQFVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVVVAIGADENrd 539
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  559 -PAKINLK---------RPPTAGSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNEALVCHQIRYLGLLENVRVR 628
Cdd:cd14902    540 sPGADNGAagrrrysmlRAPSVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLEAVRIA 619
                          650       660
                   ....*....|....*....|....*..
gi 1057503232  629 RAGYAFRQAYEPCLERYK-MLCKQTWP 654
Cdd:cd14902    620 RHGYSVRLAHASFIELFSgFKCFLSTR 646
MYSc_Myh16 cd14934
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ...
30-688 6.92e-139

class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 pseudogene (also called MHC20, MYH16, and myh5), encoding a sarcomeric myosin heavy chain expressed in nonhuman primate masticatory muscles, is inactivated in humans. This cd contains Myh16 in mammals. MYH16 has intermediate fibres between that of slow type 1 and fast 2B fibres, but exert more force than any other fibre type examined. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Some of the data used for this classification were produced by the CyMoBase team at the Max-Planck-Institute for Biophysical Chemistry. The sequence names are composed of the species abbreviation followed by the protein abbreviation and optional protein classifier and variant designations.


Pssm-ID: 276896 [Multi-domain]  Cd Length: 659  Bit Score: 434.46  E-value: 6.92e-139
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   30 TFINNLKKRFDHSEIYTYIGSVVISVNPYRSLPIYSPEKVEEYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITGE 109
Cdd:cd14934      2 SVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITGE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  110 SGAGKTEASKLVMSYVAAVCGKGAEV----NQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGGVI 185
Cdd:cd14934     82 SGAGKTENTKKVIQYFANIGGTGKQSsdgkGSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKLAGADI 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  186 SNYLLEKSRVVKQPRGERNFHVFYQLLSGASEELLNKLKLERDFSRYNYLSLDSAKVNGVDDAANFRTVRNAMQIVGFMD 265
Cdd:cd14934    162 ESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLLVPNPKEYHWVSQGVTVVDNMDDGEELQITDVAFDVLGFSA 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  266 HEAESVLAVVAAVLKLGNIEF--KPESRVNGLDESKIKDKnelkeICELTGIDQSVLERAFSFRTVEAKQEKVSTTLNVA 343
Cdd:cd14934    242 EEKIGVYKLTGGIMHFGNMKFkqKPREEQAEVDTTEVADK-----VAHLMGLNSGELQKGITRPRVKVGNEFVQKGQNME 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  344 QAYYARDALAKNLYSRLFSWLVNRINESIKAQTKvRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKEE 423
Cdd:cd14934    317 QCNNSIGALGKAVYDKMFKWLVVRINKTLDTKMQ-RQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFVLE 395
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  424 QEEYIREDIEWTHIDYFNNAIIC-DLIENNTnGILAMLDEECLRPgTVTDETFLEKLnqvcathqhFESRMSKCSRFLND 502
Cdd:cd14934    396 QEEYKREGIEWVFIDFGLDLQACiDLLEKPM-GIFSILEEQCVFP-KATDATFKAAL---------YDNHLGKSSNFLKP 464
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  503 T----SLPHSCFRIQHYAGKVLYQVEGFVDKNNDLLyRDLSQAMWKASHALIKSLFPEGNPAKINLKRPP------TAGS 572
Cdd:cd14934    465 KggkgKGPEAHFELVHYAGTVGYNITGWLEKNKDPL-NETVVGLFQKSSLGLLALLFKEEEAPAGSKKQKrgssfmTVSN 543
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  573 QFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNEALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKMLCKQT 652
Cdd:cd14934    544 FYREQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLNPNV 623
                          650       660       670
                   ....*....|....*....|....*....|....*.
gi 1057503232  653 WPHWKGPARSGVEVLFNELEIPVEEYSFGRSKIFIR 688
Cdd:cd14934    624 IPQGFVDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
MYSc_Myo45 cd14906
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ...
32-650 1.11e-135

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


Pssm-ID: 276871 [Multi-domain]  Cd Length: 715  Bit Score: 427.86  E-value: 1.11e-135
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   32 INNLKKRFDHSEIYTYIGSVVISVNPYRSLP-IYSPEKVEEYRNRNFY-ELSPHIFALSDEAYRSLRDQDKDQCILITGE 109
Cdd:cd14906      4 LNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQNkSPIPHIYAVALRAYQSMVSEKKNQSIIISGE 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  110 SGAGKTEASKLVMSYVAAVCGKGAEV--------NQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEF---DFKG 178
Cdd:cd14906     84 SGSGKTEASKTILQYLINTSSSNQQQnnnnnnnnNSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFrssDGKI 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  179 DplGGVISNYLLEKSRVVKQP-RGERNFHVFYQLLSGASEELLNKLKLERDFSRYNYLS-----LDSAK----------V 242
Cdd:cd14906    164 D--GASIETYLLEKSRISHRPdNINLSYHIFYYLVYGASKDERSKWGLNNDPSKYRYLDarddvISSFKsqssnknsnhN 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  243 NGVDDAANFRTVRNAMQIVGFMDHEAESVLAVVAAVLKLGNIEFKPESRVNGLDESKIKDKNELKEICELTGIDQSVLER 322
Cdd:cd14906    242 NKTESIESFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSDFSKYAYQKDKVTASLESVSKLLGYIESVFKQ 321
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  323 AFSFRTVEA--KQEKVSTTLNVAQAYYARDALAKNLYSRLFSWLVNRINESIKAQT----------KVRKKVMGVLDIYG 390
Cdd:cd14906    322 ALLNRNLKAggRGSVYCRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRKFNQNTqsndlaggsnKKNNLFIGVLDIFG 401
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  391 FEIFEDNSFEQFIINYCNEKLQQIFIELTLKEEQEEYIREDIEWTHIDYFNNAIICDLIENNTNGILAMLDEECLRPGTv 470
Cdd:cd14906    402 FENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNFIDNKECIELIEKKSDGILSLLDDECIMPKG- 480
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  471 TDETFLEKLN-QVCATHQHFESRMSKCSrflndtslphscFRIQHYAGKVLYQVEGFVDKNNDLLYRDLSQAMWKASHAL 549
Cdd:cd14906    481 SEQSLLEKYNkQYHNTNQYYQRTLAKGT------------LGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFL 548
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  550 IKSLFPEGNPAKINLKRPPTAG----SQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNEALVCHQIRYLGLLENV 625
Cdd:cd14906    549 KKSLFQQQITSTTNTTKKQTQSntvsGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLSQLRNVGVLNTI 628
                          650       660
                   ....*....|....*....|....*
gi 1057503232  626 RVRRAGYAFRQAYEPCLERYKMLCK 650
Cdd:cd14906    629 KVRKMGYSYRRDFNQFFSRYKCIVD 653
MYSc_Myh6 cd14916
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ...
34-688 4.69e-134

class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac muscle myosin heavy chain 6. Cardiac muscle myosin is a hexamer consisting of two heavy chain subunits, two light chain subunits, and two regulatory subunits. This gene encodes the alpha heavy chain subunit of cardiac myosin. Mutations in this gene cause familial hypertrophic cardiomyopathy and atrial septal defect. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276880 [Multi-domain]  Cd Length: 670  Bit Score: 421.77  E-value: 4.69e-134
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   34 NLKKRFDHSEIYTYIGSVVISVNPYRSLPIYSPEKVEEYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITGESGAG 113
Cdd:cd14916      6 NLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGESGAG 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  114 KTEASKLVMSYVAAVCGKG---------AEVNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGGV 184
Cdd:cd14916     86 KTVNTKRVIQYFASIAAIGdrskkenpnANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASAD 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  185 ISNYLLEKSRVVKQPRGERNFHVFYQLLSGASEELLNKLKLERDFSRYNYLSLDSAKVNGVDDAANFRTVRNAMQIVGFM 264
Cdd:cd14916    166 IETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELLATDSAFDVLGFT 245
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  265 DHEAESVLAVVAAVLKLGNIEFKPESRVNGLDESKIKDKNelkEICELTGIDQSVLERAFSFRTVEAKQEKVSTTLNVAQ 344
Cdd:cd14916    246 AEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDAD---KSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSVQQ 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  345 AYYARDALAKNLYSRLFSWLVNRINESIKAQtKVRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKEEQ 424
Cdd:cd14916    323 VYYSIGALAKSVYEKMFNWMVTRINATLETK-QPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQ 401
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  425 EEYIREDIEWTHIDYFNNAIIC-DLIENNTnGILAMLDEECLRPgTVTDETFLEKLnqvcathqhFESRMSKCSRF---L 500
Cdd:cd14916    402 EEYKKEGIEWEFIDFGMDLQACiDLIEKPM-GIMSILEEECMFP-KASDMTFKAKL---------YDNHLGKSNNFqkpR 470
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  501 NDTSLPHSCFRIQHYAGKVLYQVEGFVDKNNDLLYRDLSQAMWKASHALIKSLFP-----------EGNPAKINLKRPPT 569
Cdd:cd14916    471 NVKGKQEAHFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFStyasadtgdsgKGKGGKKKGSSFQT 550
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  570 AGSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNEALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKMLC 649
Cdd:cd14916    551 VSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILN 630
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|
gi 1057503232  650 KQTWPHWKG-PARSGVEVLFNELEIPVEEYSFGRSKIFIR 688
Cdd:cd14916    631 PAAIPEGQFiDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
MYSc_Myh8 cd14918
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ...
34-688 2.76e-129

class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle myosin heavy chain 8 (also called MyHC-peri, MyHC-pn). Myosin is a hexameric protein composed of a pair of myosin heavy chains (MYH) and two pairs of nonidentical light chains. A mutation in this gene results in trismus-pseudocamptodactyly syndrome. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276882 [Multi-domain]  Cd Length: 668  Bit Score: 409.12  E-value: 2.76e-129
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   34 NLKKRFDHSEIYTYIGSVVISVNPYRSLPIYSPEKVEEYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITGESGAG 113
Cdd:cd14918      6 NLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESGAG 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  114 KTEASKLVMSYVA--AVCGK------GAEVNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGGVI 185
Cdd:cd14918     86 KTVNTKRVIQYFAtiAVTGEkkkeesGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLASADI 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  186 SNYLLEKSRVVKQPRGERNFHVFYQLLSGASEELLNKLKLERDFSRYNYLSLDSAKVNGVDDAANFRTVRNAMQIVGFMD 265
Cdd:cd14918    166 ETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAIDILGFTP 245
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  266 HEAESVLAVVAAVLKLGNIEFKPESRvnglDESKIKDKNELKE-ICELTGIDQSVLERAFSFRTVEAKQEKVSTTLNVAQ 344
Cdd:cd14918    246 EEKVSIYKLTGAVMHYGNMKFKQKQR----EEQAEPDGTEVADkAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVQQ 321
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  345 AYYARDALAKNLYSRLFSWLVNRINESIKAQtKVRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKEEQ 424
Cdd:cd14918    322 VYNAVGALAKAVYEKMFLWMVTRINQQLDTK-QPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQ 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  425 EEYIREDIEWTHIDYFNNAIIC-DLIENNTnGILAMLDEECLRPgTVTDETFLEKLnqvcathqhFESRMSKCSRFLNDT 503
Cdd:cd14918    401 EEYKKEGIEWTFIDFGMDLAACiELIEKPL-GIFSILEEECMFP-KATDTSFKNKL---------YDQHLGKSANFQKPK 469
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  504 SL---PHSCFRIQHYAGKVLYQVEGFVDKNNDLLYRDLSQAMWKASHALIKSLFP------EGNPAKINLKRP----PTA 570
Cdd:cd14918    470 VVkgkAEAHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFStyasaeADSGAKKGAKKKgssfQTV 549
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  571 GSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNEALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKMLCK 650
Cdd:cd14918    550 SALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNA 629
                          650       660       670
                   ....*....|....*....|....*....|....*....
gi 1057503232  651 QTWPHWKG-PARSGVEVLFNELEIPVEEYSFGRSKIFIR 688
Cdd:cd14918    630 SAIPEGQFiDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
MYSc_Myh13 cd14923
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ...
34-688 1.48e-128

class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin heavy chain 13 (also called MyHC-eo) in mammals, chicken, and green anole. Myh13 is a myosin whose expression is restricted primarily to the extrinsic eye muscles which are specialized for function in eye movement. Class II myosins, also called conventional myosins, are the myosin type responsible for producing muscle contraction in muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276887 [Multi-domain]  Cd Length: 671  Bit Score: 407.53  E-value: 1.48e-128
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   34 NLKKRFDHSEIYTYIGSVVISVNPYRSLPIYSPEKVEEYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITGESGAG 113
Cdd:cd14923      6 NLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGESGAG 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  114 KTEASKLVMSYVA--AVCGKGAEVNQ-------VKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGGV 184
Cdd:cd14923     86 KTVNTKRVIQYFAtiAVTGDKKKEQQpgkmqgtLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASAD 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  185 ISNYLLEKSRVVKQPRGERNFHVFYQLLSGASEELLNKLKLERDFSRYNYLSLDSAKVNGVDDAANFRTVRNAMQIVGFM 264
Cdd:cd14923    166 IETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLISTNPFDFPFVSQGEVTVASIDDSEELLATDNAIDILGFS 245
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  265 DHEAESVLAVVAAVLKLGNIEFKPESRvnglDESKIKDKNELKEIC-ELTGIDQSVLERAFSFRTVEAKQEKVSTTLNVA 343
Cdd:cd14923    246 SEEKVGIYKLTGAVMHYGNMKFKQKQR----EEQAEPDGTEVADKAgYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQNVQ 321
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  344 QAYYARDALAKNLYSRLFSWLVNRINESIKAQtKVRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKEE 423
Cdd:cd14923    322 QVTNSVGALAKAVYEKMFLWMVTRINQQLDTK-QPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLE 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  424 QEEYIREDIEWTHIDYFNNAIIC-DLIENNTnGILAMLDEECLRPgTVTDETFLEKLnqvcathqhFESRMSKCSRFLND 502
Cdd:cd14923    401 QEEYKKEGIEWEFIDFGMDLAACiELIEKPM-GIFSILEEECMFP-KATDTSFKNKL---------YDQHLGKSNNFQKP 469
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  503 TSL---PHSCFRIQHYAGKVLYQVEGFVDKNNDLLYRDLSQAMWKASHALIKSLFP--------EGNPAKINLKRP---- 567
Cdd:cd14923    470 KPAkgkAEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSnyagaeagDSGGSKKGGKKKgssf 549
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  568 PTAGSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNEALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKM 647
Cdd:cd14923    550 QTVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRI 629
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|..
gi 1057503232  648 LCKQTWPHWKG-PARSGVEVLFNELEIPVEEYSFGRSKIFIR 688
Cdd:cd14923    630 LNASAIPEGQFiDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
MYSc_Myh4 cd14915
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ...
34-688 5.06e-128

class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin heavy chain 4 (also called MYH2B, MyHC-2B, MyHC-IIb). Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276879 [Multi-domain]  Cd Length: 671  Bit Score: 406.04  E-value: 5.06e-128
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   34 NLKKRFDHSEIYTYIGSVVISVNPYRSLPIYSPEKVEEYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITGESGAG 113
Cdd:cd14915      6 NLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESGAG 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  114 KTEASKLVMSYVAAVCGKGAEVNQ----------VKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGG 183
Cdd:cd14915     86 KTVNTKRVIQYFATIAVTGEKKKEeaasgkmqgtLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASA 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  184 VISNYLLEKSRVVKQPRGERNFHVFYQLLSGASEELLNKLKLERDFSRYNYLSLDSAKVNGVDDAANFRTVRNAMQIVGF 263
Cdd:cd14915    166 DIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITTNPYDFAFVSQGEITVPSIDDQEELMATDSAVDILGF 245
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  264 MDHEAESVLAVVAAVLKLGNIEFKPESRvnglDESKIKDKNELKE-ICELTGIDQSVLERAFSFRTVEAKQEKVSTTLNV 342
Cdd:cd14915    246 SADEKVAIYKLTGAVMHYGNMKFKQKQR----EEQAEPDGTEVADkAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQTV 321
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  343 AQAYYARDALAKNLYSRLFSWLVNRINESIKAQtKVRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKE 422
Cdd:cd14915    322 QQVYNSVGALAKAIYEKMFLWMVTRINQQLDTK-QPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  423 EQEEYIREDIEWTHIDYFNNAIIC-DLIENNTnGILAMLDEECLRPgTVTDETFLEKLnqvcathqhFESRMSKCSRFLN 501
Cdd:cd14915    401 EQEEYKKEGIEWEFIDFGMDLAACiELIEKPM-GIFSILEEECMFP-KATDTSFKNKL---------YEQHLGKSNNFQK 469
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  502 DTSL---PHSCFRIQHYAGKVLYQVEGFVDKNNDLLYRDLSQAMWKASHALIKSLF-------PEGNPAKINLKRP---- 567
Cdd:cd14915    470 PKPAkgkAEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFsggqtaeAEGGGGKKGGKKKgssf 549
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  568 PTAGSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNEALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKM 647
Cdd:cd14915    550 QTVSALFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKV 629
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|..
gi 1057503232  648 LCKQTWPHWKG-PARSGVEVLFNELEIPVEEYSFGRSKIFIR 688
Cdd:cd14915    630 LNASAIPEGQFiDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
MYSc_Myh2_mammals cd14912
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ...
34-688 5.94e-128

class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle myosin heavy chain 2 (also called MYH2A, MYHSA2, MyHC-IIa, MYHas8, MyHC-2A) in mammals. Mutations in this gene results in inclusion body myopathy-3 and familial congenital myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276877 [Multi-domain]  Cd Length: 673  Bit Score: 406.04  E-value: 5.94e-128
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   34 NLKKRFDHSEIYTYIGSVVISVNPYRSLPIYSPEKVEEYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITGESGAG 113
Cdd:cd14912      6 NLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESGAG 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  114 KTEASKLVMSYVAAVCGKGAEVNQ----------VKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGG 183
Cdd:cd14912     86 KTVNTKRVIQYFATIAVTGEKKKEeitsgkmqgtLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLASA 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  184 VISNYLLEKSRVVKQPRGERNFHVFYQLLSGASEELLNKLKLERDFSRYNYLSLDSAKVNGVDDAANFRTVRNAMQIVGF 263
Cdd:cd14912    166 DIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSAIDILGF 245
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  264 MDHEAESVLAVVAAVLKLGNIEFKPESRvnglDESKIKDKNELKE-ICELTGIDQSVLERAFSFRTVEAKQEKVSTTLNV 342
Cdd:cd14912    246 TNEEKVSIYKLTGAVMHYGNLKFKQKQR----EEQAEPDGTEVADkAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTV 321
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  343 AQAYYARDALAKNLYSRLFSWLVNRINESIKAQtKVRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKE 422
Cdd:cd14912    322 EQVTNAVGALAKAVYEKMFLWMVARINQQLDTK-QPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  423 EQEEYIREDIEWTHIDYFNNAIIC-DLIENNTnGILAMLDEECLRPgTVTDETFLEKLnqvcathqhFESRMSKCSRFLN 501
Cdd:cd14912    401 EQEEYKKEGIEWTFIDFGMDLAACiELIEKPM-GIFSILEEECMFP-KATDTSFKNKL---------YEQHLGKSANFQK 469
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  502 DTSL---PHSCFRIQHYAGKVLYQVEGFVDKNNDLLYRDLSQAMWKASHALIKSLFP---------EGNPAKINLKRP-- 567
Cdd:cd14912    470 PKVVkgkAEAHFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSgaqtaegasAGGGAKKGGKKKgs 549
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  568 --PTAGSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNEALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERY 645
Cdd:cd14912    550 sfQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRY 629
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....
gi 1057503232  646 KMLCKQTWPHWKG-PARSGVEVLFNELEIPVEEYSFGRSKIFIR 688
Cdd:cd14912    630 KVLNASAIPEGQFiDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
MYSc_Myo19 cd14880
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ...
29-687 1.11e-127

class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor for mitochondrial movement in vertebrate cells. It contains a variable number of IQ domains. Human myo19 contains a motor domain, three IQ motifs, and a short tail. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276846 [Multi-domain]  Cd Length: 658  Bit Score: 404.62  E-value: 1.11e-127
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   29 ETFINNLKKRFDHSEIYTYIGSVVISVNPYRSLP-IYSPEKVEEYRNR-NFYELSPHIFALSDEAYRSLRDQDK--DQCI 104
Cdd:cd14880      1 ETVLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAApQPQKLKPHIFTVGEQTYRNVKSLIEpvNQSI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  105 LITGESGAGKTEASKLVMSYVAAV------CGKGAEVNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKG 178
Cdd:cd14880     81 VVSGESGAGKTWTSRCLMKFYAVVaasptsWESHKIAERIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQLNRAQ 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  179 DPLGGVISNYLLEKSRVVKQPRGERNFHVFYQLLSGASEELLNKLKLERdfsRYNYLSLDSAKVNGVDDAanFRTVRNAM 258
Cdd:cd14880    161 QMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPE---GAAFSWLPNPERNLEEDC--FEVTREAM 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  259 QIVGFMDHEAESVLAVVAAVLKLGNIEFkpesrVNGLDESKI-----KDKNELKEICELTGIDQSVLERAFSFRTVEA-K 332
Cdd:cd14880    236 LHLGIDTPTQNNIFKVLAGLLHLGNIQF-----ADSEDEAQPcqpmdDTKESVRTSALLLKLPEDHLLETLQIRTIRAgK 310
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  333 QEKV-STTLNVAQAYYARDALAKNLYSRLFSWLVNRINESIKAQTKVRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKL 411
Cdd:cd14880    311 QQQVfKKPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSICADTDSWTTFIGLLDVYGFESFPENSLEQLCINYANEKL 390
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  412 QQIFIELTLKEEQEEYIREDIEWTHIDYFNNAIICDLIENNTNGILAMLDEEClrpgtvtdetfleKLNQVCATHQ---H 488
Cdd:cd14880    391 QQHFVAHYLRAQQEEYAVEGLEWSFINYQDNQTCLDLIEGSPISICSLINEEC-------------RLNRPSSAAQlqtR 457
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  489 FESRMSKCSRFLNDTSLPHSCFRIQHYAGKVLYQVEGFVDKNNDLLYRDLSQAMWKASHALIKSLFP--EGNPAKINLK- 565
Cdd:cd14880    458 IESALAGNPCLGHNKLSREPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPanPEEKTQEEPSg 537
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  566 --RPP--TAGSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNEALVCHQIRYLGLLENVRVRRAGYAFRQAYEPC 641
Cdd:cd14880    538 qsRAPvlTVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQNF 617
                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1057503232  642 LERYKMLCK-----QTWPHWKGPARSGVEVLFneleipveeysFGRSKIFI 687
Cdd:cd14880    618 VERYKLLRRlrphtSSGPHSPYPAKGLSEPVH-----------CGRTKVFM 657
MYSc_Myh1_mammals cd14910
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ...
34-688 7.37e-127

class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle myosin heavy chain 1 (also called MYHSA1, MYHa, MyHC-2X/D, MGC133384) in mammals. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276875 [Multi-domain]  Cd Length: 671  Bit Score: 402.96  E-value: 7.37e-127
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   34 NLKKRFDHSEIYTYIGSVVISVNPYRSLPIYSPEKVEEYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITGESGAG 113
Cdd:cd14910      6 NLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESGAG 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  114 KTEASKLVMSYVA--AVCG--KGAEVNQ------VKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGG 183
Cdd:cd14910     86 KTVNTKRVIQYFAtiAVTGekKKEEATSgkmqgtLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLASA 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  184 VISNYLLEKSRVVKQPRGERNFHVFYQLLSGASEELLNKLKLERDFSRYNYLSLDSAKVNGVDDAANFRTVRNAMQIVGF 263
Cdd:cd14910    166 DIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAIEILGF 245
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  264 MDHEAESVLAVVAAVLKLGNIEFKPESRvnglDESKIKDKNELKE-ICELTGIDQSVLERAFSFRTVEAKQEKVSTTLNV 342
Cdd:cd14910    246 TSDERVSIYKLTGAVMHYGNMKFKQKQR----EEQAEPDGTEVADkAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQTV 321
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  343 AQAYYARDALAKNLYSRLFSWLVNRINESIKAQtKVRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKE 422
Cdd:cd14910    322 QQVYNAVGALAKAVYDKMFLWMVTRINQQLDTK-QPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  423 EQEEYIREDIEWTHIDYFNNAIIC-DLIENNTnGILAMLDEECLRPgTVTDETFLEKLnqvcathqhFESRMSKCSRFLN 501
Cdd:cd14910    401 EQEEYKKEGIEWEFIDFGMDLAACiELIEKPM-GIFSILEEECMFP-KATDTSFKNKL---------YEQHLGKSNNFQK 469
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  502 DTSLP---HSCFRIQHYAGKVLYQVEGFVDKNNDLLYRDLSQAMWKASHALIKSLFPEGNPAKINLKRPPTAGSQ----- 573
Cdd:cd14910    470 PKPAKgkvEAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGAAAAEAEEGGGKKGGKKkgssf 549
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  574 ------FKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNEALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKM 647
Cdd:cd14910    550 qtvsalFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKV 629
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|..
gi 1057503232  648 LCKQTWPHWKG-PARSGVEVLFNELEIPVEEYSFGRSKIFIR 688
Cdd:cd14910    630 LNASAIPEGQFiDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
MYSc_Myo25 cd14886
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ...
32-688 5.17e-125

class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell adhesion and filopodia formation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276851  Cd Length: 650  Bit Score: 397.33  E-value: 5.17e-125
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   32 INNLKKRFDHSEIYTYIGSVVISVNPYRSLP-IYSPEKVEEYR----NRNF-YELSPHIFALSDEAYRSLRDQDKDQCIL 105
Cdd:cd14886      4 IDILRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRqadtSRGFpSDLPPHSYAVAQSALNGLISDGISQSCI 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  106 ITGESGAGKTEASKLVMSYVAAvcGKGAEVNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGGVI 185
Cdd:cd14886     84 VSGESGAGKTETAKQLMNFFAY--GHSTSSTDVQSLILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGPDGGLKGGKI 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  186 SNYLLEKSRVVKQPRGERNFHVFYQLLSGASEELLNKLKLeRDFSRYNYLSLDSA-KVNGVDDAANFRTVRNAMQIVgFM 264
Cdd:cd14886    162 TSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGF-KSLESYNFLNASKCyDAPGIDDQKEFAPVRSQLEKL-FS 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  265 DHEAESVLAVVAAVLKLGNIEFKPESRVNGLDESKIKDKNELKEICELTGIDQSVLERAFSFRTVEAKQEKVSTTLNVAQ 344
Cdd:cd14886    240 KNEIDSFYKCISGILLAGNIEFSEEGDMGVINAAKISNDEDFGKMCELLGIESSKAAQAIITKVVVINNETIISPVTQAQ 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  345 AYYARDALAKNLYSRLFSWLVNRINESIKAQTkVRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKEEQ 424
Cdd:cd14886    320 AEVNIRAVAKDLYGALFELCVDTLNEIIQFDA-DARPWIGILDIYGFEFFERNTYEQLLINYANERLQQYFINQVFKSEI 398
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  425 EEYIREDIEWTHIDYFNNAIICDLIENNTNGILAMLDEECLRPgTVTDETFLEKLNQVCATHQHFESRMSKCSrflndts 504
Cdd:cd14886    399 QEYEIEGIDHSMITFTDNSNVLAVFDKPNLSIFSFLEEQCLIQ-TGSSEKFTSSCKSKIKNNSFIPGKGSQCN------- 470
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  505 lphscFRIQHYAGKVLYQVEGFVDKNNDLLYRDLSQAMWKASHALIKSLFpEGNPAKINLKRPPTAGSQFKASVATLMKN 584
Cdd:cd14886    471 -----FTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNKAF-SDIPNEDGNMKGKFLGSTFQLSIDQLMKT 544
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  585 LQTKNPNYIRCIKPNDKKAAHIFNEALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKMLCKQTWPHWKGPA--RS 662
Cdd:cd14886    545 LSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFFHRNKILISHNSSSQNAGEdlVE 624
                          650       660
                   ....*....|....*....|....*.
gi 1057503232  663 GVEVLFNELEIPVEEYSFGRSKIFIR 688
Cdd:cd14886    625 AVKSILENLGIPCSDYRIGKTKVFLR 650
MYSc_Myo38 cd14899
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ...
30-664 1.16e-119

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


Pssm-ID: 276864 [Multi-domain]  Cd Length: 717  Bit Score: 385.22  E-value: 1.16e-119
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   30 TFINNLKKRFDHSEIYTYIGSVVISVNPYRSLP-IYSPEKVEEY---RNRNFYE-------LSPHIFALSDEAYRSLRDQ 98
Cdd:cd14899      2 SILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYaydHNSQFGDrvtstdpREPHLFAVARAAYIDIVQN 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   99 DKDQCILITGESGAGKTEASKLVMSYVAAVCGKGAEVNQ---------------VKEQLLQSNPVLEAFGNAKTVRNDNS 163
Cdd:cd14899     82 GRSQSILISGESGAGKTEATKIIMTYFAVHCGTGNNNLTnsesisppaspsrttIEEQVLQSNPILEAFGNARTVRNDNS 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  164 SRFGKYMDIEF-DFKGDPLGGVISNYLLEKSRVVKQPRGERNFHVFYQLLSG----ASEELLNKLKLERDFSRYNYL--S 236
Cdd:cd14899    162 SRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSAdnncVSKEQKQVLALSGGPQSFRLLnqS 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  237 LDSAKVNGVDDAANFRTVRNAMQIVGFMDHEAESVLAVVAAVLKLGNIEFK--PESRVNGL--DESKIKDK-----NELK 307
Cdd:cd14899    242 LCSKRRDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEqiPHKGDDTVfaDEARVMSSttgafDHFT 321
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  308 EICELTGIDQSVLERAFSFRTVEAKQEKVSTTLNVAQAYYARDALAKNLYSRLFSWLVNRINESIKAQTKV--------- 378
Cdd:cd14899    322 KAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLQRQASApwgadesdv 401
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  379 -----RKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKEEQEEYIREDIEWTHIDYFNNAIICDLIENNT 453
Cdd:cd14899    402 ddeedATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFPNNRACLELFEHRP 481
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  454 NGILAMLDEECLRPGTvTDETFLEKLN---QVCATHQHFESR--MSKCSRFLndtslphscfrIQHYAGKVLYQVEGFVD 528
Cdd:cd14899    482 IGIFSLTDQECVFPQG-TDRALVAKYYlefEKKNSHPHFRSAplIQRTTQFV-----------VAHYAGCVTYTIDGFLA 549
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  529 KNNDLLYRDLSQAMWKASHALIKSLFPEGNPAKINLKRPP------------------TAGSQFKASVATLMKNLQTKNP 590
Cdd:cd14899    550 KNKDSFCESAAQLLAGSSNPLIQALAAGSNDEDANGDSELdgfggrtrrraksaiaavSVGTQFKIQLNELLSTVRATTP 629
                          650       660       670       680       690       700       710
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1057503232  591 NYIRCIKPNDKKAAHIFNEALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKM----LCKQTWPHWKGPARSGV 664
Cdd:cd14899    630 RYVRCIKPNDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRYRRvllsLYKWGDNDFERQMRCGV 707
MYSc_Myo17 cd14879
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ...
26-706 2.33e-119

class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase uses its motor domain to tether its vesicular cargo to peripheral actin. It works in opposition to dynein, contributing to the retention of Mcs1 vesicles at the site of cell growth and increasing vesicle fusion necessary for polarized growth. Class 17 myosins consist of a N-terminal myosin motor domain with Cyt-b5, chitin synthase 2, and a DEK_C domains at it C-terminus. The chitin synthase region contains several transmembrane domains by which myosin 17 is thought to bind secretory vesicles. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276845 [Multi-domain]  Cd Length: 647  Bit Score: 382.28  E-value: 2.33e-119
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   26 LNEETFINNLKKRFDHSEIYTYIGS-VVISVNPYRSLPIYSPEKVEEYRNRNFYELS-------PHIFALSDEAYRSLRD 97
Cdd:cd14879      1 PSDDAITSHLASRFRSDLPYTRLGSsALVAVNPYKYLSSNSDASLGEYGSEYYDTTSgskeplpPHAYDLAARAYLRMRR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   98 QDKDQCILITGESGAGKTEASKLVMSYV---AAVCGKGAevnQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEF 174
Cdd:cd14879     81 RSEDQAVVFLGETGSGKSESRRLLLRQLlrlSSHSKKGT---KLSSQISAAEFVLDSFGNAKTLTNPNASRFGRYTELQF 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  175 DFKGDPLGGVISNYLLEKSRVVKQPRGERNFHVFYQLLSGASEELLNKLKLE-----RDFSRYNYLSLDSAKvnGVDDAA 249
Cdd:cd14879    158 NERGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDdpsdyALLASYGCHPLPLGP--GSDDAE 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  250 NFRTVRNAMQIVGFMDHEAESVLAVVAAVLKLGNIEFKpESRVNGLDESKIKDKNELKEICELTGIDQSVLERAFSFRTV 329
Cdd:cd14879    236 GFQELKTALKTLGFKRKHVAQICQLLAAILHLGNLEFT-YDHEGGEESAVVKNTDVLDIVAAFLGVSPEDLETSLTYKTK 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  330 EAKQEKVSTTLNVAQAYYARDALAKNLYSRLFSWLVNRINESIKAQTKVRKKVMGVLDIYGFEIF---EDNSFEQFIINY 406
Cdd:cd14879    315 LVRKELCTVFLDPEGAAAQRDELARTLYSLLFAWVVETINQKLCAPEDDFATFISLLDFPGFQNRsstGGNSLDQFCVNF 394
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  407 CNEKLQQIFIELTLKEEQEEYIREDIEWTHIDYFNNAIICDLIENNTNGILAMLDEECLRPGTVTDETFLEKLNQVCATH 486
Cdd:cd14879    395 ANERLHNYVLRSFFERKAEELEAEGVSVPATSYFDNSDCVRLLRGKPGGLLGILDDQTRRMPKKTDEQMLEALRKRFGNH 474
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  487 QHFESRMSKCSRflNDTSLphscFRIQHYAGKVLYQVEGFVDKNNDLLyrdlsqamwkashalikslfpegNPAKINLKR 566
Cdd:cd14879    475 SSFIAVGNFATR--SGSAS----FTVNHYAGEVTYSVEGFLERNGDVL-----------------------SPDFVNLLR 525
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  567 PPTagsQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNEALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYK 646
Cdd:cd14879    526 GAT---QLNAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQIRSLGLPELAARLRVEYVVSLEHAEFCERYK 602
                          650       660       670       680       690       700
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  647 MlckqtWPHWKGPARSGVEVLFNELEIPVeEYSFGRSKIFirnprtlfkLEDLRKQRLED 706
Cdd:cd14879    603 S-----TLRGSAAERIRQCARANGWWEGR-DYVLGNTKVF---------LSYAAWRMLED 647
MYSc_Myo13 cd14875
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ...
30-688 4.15e-114

class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain binding domain, and a C-terminal GPA/Q-rich domain. There is little known about the function of this myosin class. Two of the earliest members identified in this class are green alga Acetabularia cliftonii, Aclmyo1 and Aclmyo2. They are striking with their short tail of Aclmyo1 of 18 residues and the maximum of 7 IQ motifs in Aclmyo2. It is thought that these myosins are involved in organelle transport and tip growth. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276842 [Multi-domain]  Cd Length: 664  Bit Score: 368.75  E-value: 4.15e-114
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   30 TFINNLKKRFD--HSEiYTYIGSVVISVNPYRSLPIYSPEKVEEYRNR-NFYELSPHIFALSDEAYRSLRDQDKD-QCIL 105
Cdd:cd14875      2 TLLHCIKERFEklHQQ-YSLMGEMVLSVNPFRLMPFNSEEERKKYLALpDPRLLPPHIWQVAHKAFNAIFVQGLGnQSVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  106 ITGESGAGKTEASKLVMSYVAAV-CGKGAEVNQ------VKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFD-FK 177
Cdd:cd14875     81 ISGESGSGKTENAKMLIAYLGQLsYMHSSNTSQrsiadkIDENLKWSNPVMESFGNARTVRNDNSSRFGKYIKLYFDpTS 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  178 GDPLGGVISNYLLEKSRVVKQPRGERNFHVFYQLLSGASEE---LLNKLKLERDFSRYNY-LSLDSAKVNG--VDDAANF 251
Cdd:cd14875    161 GVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEekkELGGLKTAQDYKCLNGgNTFVRRGVDGktLDDAHEF 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  252 RTVRNAMQIVGFMDHEAESVLAVVAAVLKLGNIEFKPESRvnglDESKIKDKNELKEICELTGIDQSVLERAFsfrTVEA 331
Cdd:cd14875    241 QNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQN----DKAQIADETPFLTACRLLQLDPAKLRECF---LVKS 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  332 KQEKVSTTLNVAQAYYARDALAKNLYSRLFSWLVNRINESIKAQTKV-RKKVMGVLDIYGFEIFEDNSFEQFIINYCNEK 410
Cdd:cd14875    314 KTSLVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNASITPQGDCsGCKYIGLLDIFGFENFTRNSFEQLCINYANES 393
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  411 LQQIFIELTLKEEQEEYIREDIEWTHIDYFNNAIICDLIENNTNGILAMLDEEC-LRPGTVtdETFleklnqvcaTHQHF 489
Cdd:cd14875    394 LQNHYNKYTFINDEEECRREGIQIPKIEFPDNSECVNMFDQKRTGIFSMLDEECnFKGGTT--ERF---------TTNLW 462
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  490 ESRMSKCSRFLNDTSLPHSCFRIQHYAGKVLYQVEGFVDKNNDLLYRDLSQAMWKASHALIKSLFPEGnpaKINLKRPPT 569
Cdd:cd14875    463 DQWANKSPYFVLPKSTIPNQFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTLLSTE---KGLARRKQT 539
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  570 AGSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNEALVCHQIRYLGLLENVRVRRAGYAFRQAYEP-CLERYKML 648
Cdd:cd14875    540 VAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRRPIEQfCRYFYLIM 619
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*
gi 1057503232  649 CKQTWPHWKGPARSGVEVLFNEL-----EIPVEEYSFGRSKIFIR 688
Cdd:cd14875    620 PRSTASLFKQEKYSEAAKDFLAYyqrlyGWAKPNYAVGKTKVFLR 664
MYSc_Myo16 cd14878
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ...
35-648 2.30e-106

class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal tyrosine-phosphorylated phosphoinositide-3-kinase adapter 3/NYAP3. Myo16 is thought to play a regulatory role in cell cycle progression and has been recently implicated in Schizophrenia. Class XVI myosins are characterized by an N-terminal ankyrin repeat domain and some with chitin synthase domains that arose independently from the ones in the class XVII fungal myosins. They bind protein phosphatase 1 catalytic subunits 1alpha/PPP1CA and 1gamma/PPP1CC. Human Myo16 interacts with ACOT9, ARHGAP26 and PIK3R2 and with components of the WAVE1 complex, CYFIP1 and NCKAP1. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276844 [Multi-domain]  Cd Length: 656  Bit Score: 347.57  E-value: 2.30e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   35 LKKRFDHSEIYTYIGSVVISVNPYRSLPIYSPEKVEEYRN---RNFYELSPHIFALSDEAYRSLRDQDKDQCILITGESG 111
Cdd:cd14878      7 IQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYLSssgQLCSSLPPHLFSCAERAFHQLFQERRPQCFILSGERG 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  112 AGKTEASKLVMSYVAavCGKGAEVNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEF-DFKGDPLGGVISNYLL 190
Cdd:cd14878     87 SGKTEASKQIMKHLT--CRASSSRTTFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFcERKKHLTGARIYTYML 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  191 EKSRVVKQPRGERNFHVFYQLLSGASEELLNKLKLeRDFSRYNYLSL----DSAKVNGVDDAANFRTVRNAMQIVGFMDH 266
Cdd:cd14878    165 EKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHL-NNLCAHRYLNQtmreDVSTAERSLNREKLAVLKQALNVVGFSSL 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  267 EAESVLAVVAAVLKLGNIEFkpeSRVNGLDESKIKDKNELKEICELTGIDQSVLERAFSFRTVEAKQEKVSTTLNVAQAY 346
Cdd:cd14878    244 EVENLFVILSAILHLGDIRF---TALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHTIQIAE 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  347 YARDALAKNLYSRLFSWLVNRINESIKAQ---TKVRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKEE 423
Cdd:cd14878    321 FYRDLLAKSLYSRLFSFLVNTVNCCLQSQdeqKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVLFLQE 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  424 QEEYIREDIEW-THIDYFNNAIICDLIENNTNGILAMLDEEC--LRPGTVTDETFLEKLNQVCATHQ-HFESRMSKCSRF 499
Cdd:cd14878    401 QTECVQEGVTMeTAYSPGNQTGVLDFFFQKPSGFLSLLDEESqmIWSVEPNLPKKLQSLLESSNTNAvYSPMKDGNGNVA 480
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  500 LNDTSlphSCFRIQHYAGKVLYQVEGFVDKNNDLLYRDLSQAMWKASHALIKSLFPEgnpakinlkRPPTAGSQFKASVA 579
Cdd:cd14878    481 LKDQG---TAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQS---------KLVTIASQLRKSLA 548
                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1057503232  580 TLMKNLQTKNPNYIRCIKPNDKKAAHIFNEALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKML 648
Cdd:cd14878    549 DIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPL 617
MYSc_Myo24A cd14937
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ...
32-688 2.25e-100

class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a coiled-coil region in their C-terminal tail. The function of the class XXIV myosins remain elusive. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276897  Cd Length: 637  Bit Score: 331.21  E-value: 2.25e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   32 INNLKKRFDHSEIYTYIGSVVISVNPYRSLPIyspeKVEEYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITGESG 111
Cdd:cd14937      4 LNMLALRYKKNYIYTIAEPMLISINPYQVIDV----DINEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISGESG 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  112 AGKTEASKLVMS-YVAAVcgkgAEVNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGGVISNYLL 190
Cdd:cd14937     80 SGKTEASKLVIKyYLSGV----KEDNEISNTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIVSSSIEIFLL 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  191 EKSRVVKQPRGERNFHVFYQLLSGASEELLNKLKLeRDFSRYNYLSLDSAKVNGVDDAANFRTVRNAMQIVGFMDHEaES 270
Cdd:cd14937    156 ENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKI-RSENEYKYIVNKNVVIPEIDDAKDFGNLMISFDKMNMHDMK-DD 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  271 VLAVVAAVLKLGNIEFKPESRVNGLDESKIKDKN--ELKEICELTGIDQSVLERAFSFRTVEAKQEKVSTTLNVAQAYYA 348
Cdd:cd14937    234 LFLTLSGLLLLGNVEYQEIEKGGKTNCSELDKNNleLVNEISNLLGINYENLKDCLVFTEKTIANQKIEIPLSVEESVSI 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  349 RDALAKNLYSRLFSWLVNRINESIKaQTKVRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKEEQEEYI 428
Cdd:cd14937    314 CKSISKDLYNKIFSYITKRINNFLN-NNKELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIHSIYLYIVYEKETELYK 392
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  429 REDIEWTHIDYFNNAIICDLIENNTNgILAMLDEECLRPGTvTDETFLEKLNQVCATHQHFesrmSKCSRFLNDTslphs 508
Cdd:cd14937    393 AEDILIESVKYTTNESIIDLLRGKTS-IISILEDSCLGPVK-NDESIVSVYTNKFSKHEKY----ASTKKDINKN----- 461
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  509 cFRIQHYAGKVLYQVEGFVDKNNDLLYRDLSQAMWKASHALIKSLFPEGNPAKiNLKRPPTAGSQFKASVATLMKNLQTK 588
Cdd:cd14937    462 -FVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDVEVSE-SLGRKNLITFKYLKNLNNIISYLKST 539
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  589 NPNYIRCIKPNDKKAAHIFNEALVCHQIRYLGLLENVRVRRAgYAFRQAYEPCLERYKMLCKQTWPHWKGPARSGVEVLF 668
Cdd:cd14937    540 NIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNISFF-FQYKYTFDVFLSYFEYLDYSTSKDSSLTDKEKVSMIL 618
                          650       660
                   ....*....|....*....|
gi 1057503232  669 NELEIPvEEYSFGRSKIFIR 688
Cdd:cd14937    619 QNTVDP-DLYKVGKTMVFLK 637
MYSc_Myo26 cd14887
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ...
32-688 1.16e-97

class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the other myosins that have a MyTH4 domain such as class III, VII, IX, X , XV, XVI, XVII, XX, XXII, XXV, and XXXIV. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276852  Cd Length: 725  Bit Score: 326.22  E-value: 1.16e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   32 INNLKKRF--------DHSEIYTYIGSVVISVNPYRSLPIYSPEKVEEYRNRNFYELSPHIFALSDEAYRSLRDQDKDQC 103
Cdd:cd14887      4 LENLYQRYnkayinkeNRNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRRSQS 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  104 ILITGESGAGKTEASKLVMSYVAAVCG--KGAEVNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPL 181
Cdd:cd14887     84 ILISGESGAGKTETSKHVLTYLAAVSDrrHGADSQGLEARLLQSGPVLEAFGNAHTVLNANSSRFGKMLLLHFTGRGKLT 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  182 GGVISNYLLEKSRVVKQPRGERNFHVFYQLLSGAseellnklKLERDFsrynylslDSAKVNGVDDAANFRTVRNAMQIV 261
Cdd:cd14887    164 RASVATYLLANERVVRIPSDEFSFHIFYALCNAA--------VAAATQ--------KSSAGEGDPESTDLRRITAAMKTV 227
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  262 GFMDHEAESVLAVVAAVLKLGNIEF-----KPESRVNGLDESKI------KDKNELKEI-CELTGIDQS--------VLE 321
Cdd:cd14887    228 GIGGGEQADIFKLLAAILHLGNVEFttdqePETSKKRKLTSVSVgceetaADRSHSSEVkCLSSGLKVTeasrkhlkTVA 307
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  322 RAFSFRTVEAKQEKVSTTL------------NVAQAYYARDALAKNLYSRLFSWLVNRINESIK-----------AQTKV 378
Cdd:cd14887    308 RLLGLPPGVEGEEMLRLALvsrsvretrsffDLDGAAAARDAACKNLYSRAFDAVVARINAGLQrsakpsesdsdEDTPS 387
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  379 RKKV--MGVLDIYGFEIFED---NSFEQFIINYCNEKLQQIFIELTLKEEQEEYIREDIEWTHIDY---FNNAIICDLIE 450
Cdd:cd14887    388 TTGTqtIGILDLFGFEDLRNhskNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGVFQNQDCSafpFSFPLASTLTS 467
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  451 NNTN-----------------------GILAMLDEECL-----RPGTVTDETFLEKLNQVCAThqhfESRMSKCSRFLND 502
Cdd:cd14887    468 SPSStspfsptpsfrsssafatspslpSSLSSLSSSLSssppvWEGRDNSDLFYEKLNKNIIN----SAKYKNITPALSR 543
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  503 TSLPhscFRIQHYAGKVLYQVEGFVDKNNDLLYRDLSQAMWKASHALIKSLFPEGNPAKINLKRPPTAGSQFKASVATLM 582
Cdd:cd14887    544 ENLE---FTVSHFACDVTYDARDFCRANREATSDELERLFLACSTYTRLVGSKKNSGVRAISSRRSTLSAQFASQLQQVL 620
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  583 KNLQTKNPNYIRCIKPNDKKAAHIFNEALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKMLCKQTWPHWKGPARS 662
Cdd:cd14887    621 KALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVELWRRYETKLPMALREALTPKMF 700
                          730       740
                   ....*....|....*....|....*.
gi 1057503232  663 GVEVLFnELEIPVEEYSFGRSKIFIR 688
Cdd:cd14887    701 CKIVLM-FLEINSNSYTFGKTKIFFR 725
MYSc_Myo20 cd14881
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ...
29-649 4.02e-94

class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such members as Drosophila, Daphnia, and mosquitoes. These myosins contain a single IQ motif in the neck region. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276847 [Multi-domain]  Cd Length: 633  Bit Score: 313.97  E-value: 4.02e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   29 ETFINNLKKRFDHSEIYTYIGSVVISVNPYRSLPiySPEKVEEYRNRnfyELSPHIFALSDEAYRSLRDQDKDQCILITG 108
Cdd:cd14881      1 DAVMKCLQARFYAKEFFTNVGPILLSVNPYRDVG--NPLTLTSTRSS---PLAPQLLKVVQEAVRQQSETGYPQAIILSG 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  109 ESGAGKTEASKLVMSYVAAVCGKGAEVNQVKeQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDfKGDPLGGVISNY 188
Cdd:cd14881     76 TSGSGKTYASMLLLRQLFDVAGGGPETDAFK-HLAAAFTVLRSLGSAKTATNSESSRIGHFIEVQVT-DGALYRTKIHCY 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  189 LLEKSRVVKQPRGERNFHVFYQLLSGASEELLNKLKLErDFSRYN--YLSLDSAKVNGVDDAANFRTVRNAMQIVG--FM 264
Cdd:cd14881    154 FLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLD-GYSPANlrYLSHGDTRQNEAEDAARFQAWKACLGILGipFL 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  265 DheaesVLAVVAAVLKLGNIEFkpeSRVNGLDESkIKDKNELKEICELTGIDQSVLERAFSFRTVEAKQEKVSTTLNVAQ 344
Cdd:cd14881    233 D-----VVRVLAAVLLLGNVQF---IDGGGLEVD-VKGETELKSVAALLGVSGAALFRGLTTRTHNARGQLVKSVCDANM 303
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  345 AYYARDALAKNLYSRLFSWLVNRINeSIK-----AQTKVRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIF---- 415
Cdd:cd14881    304 SNMTRDALAKALYCRTVATIVRRAN-SLKrlgstLGTHATDGFIGILDMFGFEDPKPSQLEHLCINLCAETMQHFYnthi 382
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  416 IELTLKEEQEEYIREDIEwthIDYFNNAIICDLIENNTNGILAMLDEECLRPGTVtdETFLEKLNqvcATHQH----FES 491
Cdd:cd14881    383 FKSSIESCRDEGIQCEVE---VDYVDNVPCIDLISSLRTGLLSMLDVECSPRGTA--ESYVAKIK---VQHRQnprlFEA 454
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  492 RMSKCSRFLndtslphscfrIQHYAGKVLYQVEGFVDKNNDLLYRDLSQAMWK-------ASHAlikslfpegnpakinl 564
Cdd:cd14881    455 KPQDDRMFG-----------IRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYKqncnfgfATHT---------------- 507
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  565 krpptagSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNEALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLER 644
Cdd:cd14881    508 -------QDFHTRLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAGGYPHRMRFKAFNAR 580

                   ....*
gi 1057503232  645 YKMLC 649
Cdd:cd14881    581 YRLLA 585
MYSc_Myo37 cd14898
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ...
32-648 1.29e-91

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


Pssm-ID: 276863  Cd Length: 578  Bit Score: 305.28  E-value: 1.29e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   32 INNLKKRFDHSEIYTYIGSVVISVNPYRSlpIYSPEKVEEYRnRNFYELSPHIFALSDEAYRSLRDQDkDQCILITGESG 111
Cdd:cd14898      4 LEILEKRYASGKIYTKSGLVFLALNPYET--IYGAGAMKAYL-KNYSHVEPHVYDVAEASVQDLLVHG-NQTIVISGESG 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  112 AGKTEASKLVMSYVAAvcgKGAEVNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDfkGDPLGGVISNYLLE 191
Cdd:cd14898     80 SGKTENAKLVIKYLVE---RTASTTSIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKFD--GKITGAKFETYLLE 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  192 KSRVVKQPRGERNFHVFYQLLsgASEellnKLKLERDFsrYNYLSLDSAKVNGVDDAANFRTVRNAMQIVGFMDheAESV 271
Cdd:cd14898    155 KSRVTHHEKGERNFHIFYQFC--ASK----RLNIKNDF--IDTSSTAGNKESIVQLSEKYKMTCSAMKSLGIAN--FKSI 224
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  272 LAVVAAVLKLGNIEFKPESRVngldesKIKDKNELKEICELTGIDQSVLERAFSFRTVEAKQEKVSTTLNVAQAYYARDA 351
Cdd:cd14898    225 EDCLLGILYLGSIQFVNDGIL------KLQRNESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIEVFNTLKQARTIRNS 298
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  352 LAKNLYSRLFSWLVNRINESIKAQTKvrkKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKEEQEEYIRED 431
Cdd:cd14898    299 MARLLYSNVFNYITASINNCLEGSGE---RSISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMFRAKQGMYKEEG 375
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  432 IEWTHIDYFNNAIICDLIENNTnGILAMLDEECLRPgtvtdetfleklnqvCATHQHFESRMSKCSRFLNDTSLPHScFR 511
Cdd:cd14898    376 IEWPDVEFFDNNQCIRDFEKPC-GLMDLISEESFNA---------------WGNVKNLLVKIKKYLNGFINTKARDK-IK 438
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  512 IQHYAGKVLYQVEGFVDKNNDllyrdlsqamwKASHALIKSLFPEGNPAKINLKRpptagsQFKASVATLMKNLQTKNPN 591
Cdd:cd14898    439 VSHYAGDVEYDLRDFLDKNRE-----------KGQLLIFKNLLINDEGSKEDLVK------YFKDSMNKLLNSINETQAK 501
                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1057503232  592 YIRCIKPNDKKAAHIFNEALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKML 648
Cdd:cd14898    502 YIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRIL 558
MYSc_Myo44 cd14905
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ...
29-648 1.33e-87

class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV class. Members here include cellular slime mold Polysphondylium and soil-living amoeba Dictyostelium. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276870  Cd Length: 673  Bit Score: 297.39  E-value: 1.33e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   29 ETFINNLKKRFDHSEIYTYIGSVVISVNPYRSLP-IYSPEKVEEYRNRNfyELSPHIFALSDEAYRSLRDQDKDQCILIT 107
Cdd:cd14905      1 DTLINIIQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNYNQRR--GLPPHLFALAAKAISDMQDFRRDQLIFIG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  108 GESGAGKTEASKLVMSYVAAVcgKGAEVNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGGVISN 187
Cdd:cd14905     79 GESGSGKSENTKIIIQYLLTT--DLSRSKYLRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQGAKLYS 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  188 YLLEKSRVVKQPRGERNFHVFYQLLSGASEELLNKLKLErDFSRYNYLSL-DSAKVNGVDDAANFRTVRNAMQIVGFMDH 266
Cdd:cd14905    157 YFLDENRVTYQNKGERNFHIFYQFLKGITDEEKAAYQLG-DINSYHYLNQgGSISVESIDDNRVFDRLKMSFVFFDFPSE 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  267 EAESVLAVVAAVLKLGNIEFKPEsrvNGldESKIKDKNELKEICELTGIDQSVLERAFSfrtveakqekVSTTLNVAQAY 346
Cdd:cd14905    236 KIDLIFKTLSFIIILGNVTFFQK---NG--KTEVKDRTLIESLSHNITFDSTKLENILI----------SDRSMPVNEAV 300
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  347 YARDALAKNLYSRLFSWLVNRINESIKAQTkvRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKEEQEE 426
Cdd:cd14905    301 ENRDSLARSLYSALFHWIIDFLNSKLKPTQ--YSHTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVLKQEQRE 378
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  427 YIREDIEW-THIDYFNNAIICDLIENntngILAMLDEECLRPGTvTDETFLEKLNQVCATHQHFESRMSKcsrflndtsl 505
Cdd:cd14905    379 YQTERIPWmTPISFKDNEESVEMMEK----IINLLDQESKNINS-SDQIFLEKLQNFLSRHHLFGKKPNK---------- 443
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  506 phscFRIQHYAGKVLYQVEGFVDKNND-LLYR---------------------------------DLSQAMWKASHALIK 551
Cdd:cd14905    444 ----FGIEHYFGQFYYDVRGFIIKNRDeILQRtnvlhknsitkylfsrdgvfninatvaelnqmfDAKNTAKKSPLSIVK 519
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  552 SLFPEGNPAKINLKRPP-----------------TAGSQFKASVATlmkNLQTKNPN----YIRCIKPNDKKAAHIFNEA 610
Cdd:cd14905    520 VLLSCGSNNPNNVNNPNnnsgggggggnsgggsgSGGSTYTTYSST---NKAINNSNcdfhFIRCIKPNSKKTHLTFDVK 596
                          650       660       670
                   ....*....|....*....|....*....|....*...
gi 1057503232  611 LVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKML 648
Cdd:cd14905    597 SVNEQIKSLCLLETTRIQRFGYTIHYNNKIFFDRFSFF 634
MYSc_Myo23 cd14884
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ...
29-646 1.42e-77

class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 IQ motifs and a single MyTH4 domain in its C-terminal tail. The lack of a FERM domain here is odd since MyTH4 domains are usually found alongside FERM domains where they bind to microtubules. At any rate these Class XXIII myosins are still proposed to function in the apicomplexan microtubule cytoskeleton. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276850 [Multi-domain]  Cd Length: 685  Bit Score: 269.47  E-value: 1.42e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   29 ETFINNLKKRFDHSEIYTYIGSVVISVNPYRSLP-IYSPEKVEEY----RNRNFYE---LSPHIFALSDEAYRSLRDQDK 100
Cdd:cd14884      1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYlhkkSNSAASAapfPKAHIYDIANMAYKNMRGKLK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  101 DQCILITGESGAGKTEASKLVMSYVAAVCGKgAEVNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFD----- 175
Cdd:cd14884     81 RQTIVVSGHSGSGKTENCKFLFKYFHYIQTD-SQMTERIDKLIYINNILESMSNATTIKNNNSSRCGRINLLIFEevent 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  176 ----FKGDPLGGVISNYLLEKSRVVKQPRGERNFHVFYQLLSGASEELLNKLKLERDFSRYNYL---------------- 235
Cdd:cd14884    160 qknmFNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGLSDEDLARRNLVRNCGVYGLLnpdeshqkrsvkgtlr 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  236 ----SLDSAKVNGVDDAANFRTVRNAMQIVGFMDHEAESVLAVVAAVLKLGNiefkpesrvngldeskikdkNELKEICE 311
Cdd:cd14884    240 lgsdSLDPSEEEKAKDEKNFVALLHGLHYIKYDERQINEFFDIIAGILHLGN--------------------RAYKAAAE 299
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  312 LTGIDQSVLERAFSFRTVEAKQEKVSTTLNVAQAYYARDALAKNLYSRLFSWLVNRIN----------ESIKAQT-KVRK 380
Cdd:cd14884    300 CLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINrnvlkckekdESDNEDIySINE 379
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  381 KVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKEEQEEYIREDIEWTHI---DYFNNAIICDLIENNTNGIL 457
Cdd:cd14884    380 AIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDvapSYSDTLIFIAKIFRRLDDIT 459
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  458 AMLDEECLRpgtvTDETFLEKLNQVCATHQHFESRMS-KCSRFLNDTS-----LPHSCFRIQHYAGKVLYQVEGFVDKNN 531
Cdd:cd14884    460 KLKNQGQKK----TDDHFFRYLLNNERQQQLEGKVSYgFVLNHDADGTakkqnIKKNIFFIRHYAGLVTYRINNWIDKNS 535
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  532 DLLYRDLSQAMWKASHALIKSLFPEGNPAKINlkrppTAGSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNEAL 611
Cdd:cd14884    536 DKIETSIETLISCSSNRFLREANNGGNKGNFL-----SVSKKYIKELDNLFTQLQSTDMYYIRCFLPNAKMLPNTFKRLL 610
                          650       660       670
                   ....*....|....*....|....*....|....*
gi 1057503232  612 VCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYK 646
Cdd:cd14884    611 VYRQLKQCGSNEMIKILNRGLSHKIPKKETAAALK 645
MYSc_Myo32 cd14893
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ...
35-687 3.35e-77

class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but possess tandem MyTH4 and FERM domains. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276858  Cd Length: 741  Bit Score: 269.92  E-value: 3.35e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   35 LKKRFDHSEIYTYIGSVVISVNPYRSLPIYSPEKVEEYRNRN----FYELS------PHIFALSDEAYRSLRDQDKDQCI 104
Cdd:cd14893      7 LRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSReqtpLYEKDtvndapPHVFALAQNALRCMQDAGEDQAV 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  105 LITGESGAGKTEASKLVMSYVAAVcGKGAE-----------VNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIE 173
Cdd:cd14893     87 ILLGGMGAGKSEAAKLIVQYLCEI-GDETEprpdsegasgvLHPIGQQILHAFTILEAFGNAATRQNRNSSRFAKMISVE 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  174 FDFKGDPLGGVISNYLLEKSRVVKQPRGERNFHVFYQLLSGASEE--LLNKLKLERDFSRYNYL-SLDSAKVNGVDDAAN 250
Cdd:cd14893    166 FSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQHDptLRDSLEMNKCVNEFVMLkQADPLATNFALDARD 245
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  251 FRTVRNAMQIVGFMDHEAESVLAVVAAVLKLGNIEFKPE----SRVNGLDESKI--------KDKNELKEICELTGIDQS 318
Cdd:cd14893    246 YRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFVPDpeggKSVGGANSTTVsdaqscalKDPAQILLAAKLLEVEPV 325
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  319 VLERAFSFRTVEAKQ--EKVST--TLNVAQAYYARDALAKNLYSRLFSWLVNRINESI--------KAQTKVRKKVMGVL 386
Cdd:cd14893    326 VLDNYFRTRQFFSKDgnKTVSSlkVVTVHQARKARDTFVRSLYESLFNFLVETLNGILggifdryeKSNIVINSQGVHVL 405
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  387 DIYGFEIFED--NSFEQFIINYCNEKLQQIFIELTL-------KEEQEEYIREDIEWTHIDYFNNAIIC-DLIENNTNGI 456
Cdd:cd14893    406 DMVGFENLTPsqNSFDQLCFNYWSEKVHHFYVQNTLainfsflEDESQQVENRLTVNSNVDITSEQEKClQLFEDKPFGI 485
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  457 LAMLDEEClRPGTVTDETFLEKLNQVCATHQHFeSRMSKCSRFLNDTSLPHS----CFRIQHYAGKVLYQVEGFVDKN-- 530
Cdd:cd14893    486 FDLLTENC-KVRLPNDEDFVNKLFSGNEAVGGL-SRPNMGADTTNEYLAPSKdwrlLFIVQHHCGKVTYNGKGLSSKNml 563
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  531 --------------NDLLYRDLSQAMWKASHALIKSLFPEGNPAKINLKRPPTAGSQFKA---SVATLMKN-----LQTK 588
Cdd:cd14893    564 sisstcaaimqsskNAVLHAVGAAQMAAASSEKAAKQTEERGSTSSKFRKSASSARESKNitdSAATDVYNqadalLHAL 643
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  589 N---PNYIRCIKPNDKKAAHIFNEALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKMLCKQtwphwkgpaRSGVE 665
Cdd:cd14893    644 NhtgKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRYKNVCGH---------RGTLE 714
                          730       740
                   ....*....|....*....|....*.
gi 1057503232  666 VLFNELE-IPV---EEYSFGRSKIFI 687
Cdd:cd14893    715 SLLRSLSaIGVleeEKFVVGKTKVYL 740
MYSc_Myo18 cd01386
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ...
35-688 5.05e-77

class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain which is commonly found in proteins establishing molecular complexes. The motor domain itself does not exhibit ATPase activity, suggesting that it functions as an actin tether protein. It also has two IQ domains that probably bind light chains or related calmodulins and a C-terminal tail with two sections of coiled-coil domains, which are thought to mediate homodimerization. The function of these myosins are largely unknown. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276837 [Multi-domain]  Cd Length: 689  Bit Score: 268.02  E-value: 5.05e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   35 LKKRFDHSEIYTYIGSVVISVNPYRSLPIYSPEKVEEYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITGESGAGK 114
Cdd:cd01386      7 LRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLGRSGSGK 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  115 TEASKLVMSYVAAVcgKGAEVNQVKEQLLQS-NPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGGVISNYLLEKS 193
Cdd:cd01386     87 TTNCRHILEYLVTA--AGSVGGVLSVEKLNAaLTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQLASASIQTLLLERS 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  194 RVVKQPRGERNFHVFYQLLSGASEELLNKLKLERDFSRYNYLSLDSAKVNGV-DDAANFRTVRNAMQIVGFMDHEAESVL 272
Cdd:cd01386    165 RVARRPEGESNFNVFYYLLAGADAALRTELHLNQLAESNSFGIVPLQKPEDKqKAAAAFSKLQAAMKTLGISEEEQRAIW 244
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  273 AVVAAVLKLGNIEFKPESRVNgldESKIKDKNELKEICELTGIDQSVLERA--------------FSFRTVEAKQEKVST 338
Cdd:cd01386    245 SILAAIYHLGAAGATKAASAG---RKQFARPEWAQRAAYLLGCTLEELSSAifkhhlsggpqqstTSSGQESPARSSSGG 321
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  339 TLNVAQAyyARDALAKNLYSRLFSWLVNRINESIKAQTKVRKKVMgVLDIYGFeifeDN----------SFEQFIINYCN 408
Cdd:cd01386    322 PKLTGVE--ALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSSIT-IVDTPGF----QNpahsgsqrgaTFEDLCHNYAQ 394
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  409 EKLQQIFIELTLKEEQEEYIREDIEwthIDY----FNNAIICDLIENNTN--------------GILAMLDEECLRPGTv 470
Cdd:cd01386    395 ERLQLLFHERTFVAPLERYKQENVE---VDFdlpeLSPGALVALIDQAPQqalvrsdlrdedrrGLLWLLDEEALYPGS- 470
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  471 TDETFLEKLnqvCAthQHFESRMSKCSRFLNDTSLPHScFRIQHYAGK--VLYQVEGFVDK-NNDLLYRDLSQAMWKASH 547
Cdd:cd01386    471 SDDTFLERL---FS--HYGDKEGGKGHSLLRRSEGPLQ-FVLGHLLGTnpVEYDVSGWLKAaKENPSAQNATQLLQESQK 544
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  548 AL----IKSLFpegnpakinlkrpptagSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAH------------IFNEAL 611
Cdd:cd01386    545 ETaavkRKSPC-----------------LQIKFQVDALIDTLRRTGLHFVHCLLPQHNAGKDerstsspaagdeLLDVPL 607
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  612 VCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKMLCKQ--TWPHWKGPA---RSGVEVLFNELEIPVEEYSFGRSKIF 686
Cdd:cd01386    608 LRSQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPltKKLGLNSEVadeRKAVEELLEELDLEKSSYRIGLSQVF 687

                   ..
gi 1057503232  687 IR 688
Cdd:cd01386    688 FR 689
MYSc_Myo12 cd14874
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ...
34-648 1.06e-74

class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They are found predominately in nematodes. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276841 [Multi-domain]  Cd Length: 628  Bit Score: 259.80  E-value: 1.06e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   34 NLKKRFDHSEIYTYIGSVVISVNPYRSLPIYSPEKVEEYrnrnfyelspHIFALSDEAYRSL-RDQDKDQCILITGESGA 112
Cdd:cd14874      6 NLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIkSMSSNAESIVFGGESGS 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  113 GKTEASKLVMSYVAAvcGKGAEVNQVKEQLLQSnpVLEAFGNAKTVRNDNSSRFGKYMDIEFdfKGDPLGGVISNYL--L 190
Cdd:cd14874     76 GKSYNAFQVFKYLTS--QPKSKVTTKHSSAIES--VFKSFGCAKTLKNDEATRFGCSIDLLY--KRNVLTGLNLKYTvpL 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  191 EKSRVVKQPRGERNFHVFYQLLSGASEELLNKLKLeRDFSRYNYLSLDSAKVNGVDDAANFRTVRNAMQIVGFMDHEAES 270
Cdd:cd14874    150 EVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGI-KGLQKFFYINQGNSTENIQSDVNHFKHLEDALHVLGFSDDHCIS 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  271 VLAVVAAVLKLGNIEFKPESRVNG-LDESKIKDKNELKEICELTGIDQSVLERAFSFRTveakqeKVSTTLNVAQAYYAR 349
Cdd:cd14874    229 IYKIISTILHIGNIYFRTKRNPNVeQDVVEIGNMSEVKWVAFLLEVDFDQLVNFLLPKS------EDGTTIDLNAALDNR 302
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  350 DALAKNLYSRLFSWLVNRIneSIKAQTKVRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKEEQEEYIR 429
Cdd:cd14874    303 DSFAMLIYEELFKWVLNRI--GLHLKCPLHTGVISILDHYGFEKYNNNGVEEFLINSVNERIENLFVKHSFHDQLVDYAK 380
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  430 EDIEwthIDY-----FNNAIICDLIENNTNGILAMLDEECLRPgTVTDETFLEKLNQvcathQHFESrmskcSRFLNDTS 504
Cdd:cd14874    381 DGIS---VDYkvpnsIENGKTVELLFKKPYGLLPLLTDECKFP-KGSHESYLEHCNL-----NHTDR-----SSYGKARN 446
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  505 LPHSCFRIQHYAGKVLYQVEGFVDKNNDLLYRDLSQAMWKASHALIKSLFPE--GNPAKINLkrppTAGSQFKASVATLM 582
Cdd:cd14874    447 KERLEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFESysSNTSDMIV----SQAQFILRGAQEIA 522
                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1057503232  583 KNLQTKNPNYIRCIKPNDKKAAHIFNEALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKML 648
Cdd:cd14874    523 DKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYRCL 588
MYSc_Myo21 cd14882
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ...
29-648 6.94e-70

class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class XXI myosins do not group with them. Myo21, unlike other myosin proteins, contains UBA-like protein domains and has no structural or functional relationship with the myosins present in other organisms possessing cilia or flagella. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. They have diverse tails with IQ, WW, PX, and Tub domains. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276848  Cd Length: 642  Bit Score: 246.58  E-value: 6.94e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   29 ETFINNLKKRFDHSEIYTYIGSVVISVNPYRSLPIYSPEKVEEYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITG 108
Cdd:cd14882      1 ENILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  109 ESGAGKTEASKLVMSYVAaVCGKGaeVNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGGVISNY 188
Cdd:cd14882     81 ESYSGKTTNARLLIKHLC-YLGDG--NRGATGRVESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMSGAIFWMY 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  189 LLEKSRVVKQPRGERNFHVFYQLLSG-ASEELLNKLKLERDfSRYNYLSLD------SAKVNGVDDAANFRTVRNAMQIV 261
Cdd:cd14882    158 QLEKLRVSTTDGNQSNFHIFYYFYDFiEAQNRLKEYNLKAG-RNYRYLRIPpevppsKLKYRRDDPEGNVERYKEFEEIL 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  262 GFMDHE---AESVLAVVAAVLKLGNIEFkpesrVNGLDESKIKDKNELKEICELTGIDQSVLERAFSFRTVEAKQEKVST 338
Cdd:cd14882    237 KDLDFNeeqLETVRKVLAAILNLGEIRF-----RQNGGYAELENTEIASRVAELLRLDEKKFMWALTNYCLIKGGSAERR 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  339 TLNVAQAYYARDALAKNLYSRLFSWLVNRINESIKAQTKV--RKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFI 416
Cdd:cd14882    312 KHTTEEARDARDVLASTLYSRLVDWIINRINMKMSFPRAVfgDKYSISIHDMFGFECFHRNRLEQLMVNTLNEQMQYHYN 391
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  417 ELTLKEEQEEYIREDIEWTHIDYFNNAIICDLIENNTNGILAMLDEEclrpgtvtdetfleklNQVCATHQH-FESRMSK 495
Cdd:cd14882    392 QRIFISEMLEMEEEDIPTINLRFYDNKTAVDQLMTKPDGLFYIIDDA----------------SRSCQDQNYiMDRIKEK 455
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  496 CSRFLNdtslPHSC--FRIQHYAGKVLYQVEGFVDKNNDLLYRDLSQAMWKASHALIKSLFPEGNPAKINlkrppTAGSQ 573
Cdd:cd14882    456 HSQFVK----KHSAheFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTNSQVRNMR-----TLAAT 526
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  574 FKASVATLMKNLqTKNPN-----YIRCIKPNDKKAAHIFNEALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKML 648
Cdd:cd14882    527 FRATSLELLKML-SIGANsggthFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRIPFQEFLRRYQFL 605
MYSc_Myo24B cd14938
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ...
30-687 3.39e-42

class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a coiled-coil region in their C-terminal tail. The functions of these myosins remain elusive. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276898 [Multi-domain]  Cd Length: 713  Bit Score: 165.78  E-value: 3.39e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   30 TFINNLKKRFDHSEIYTYIGSVVISVNPYRSLPIYSPEKVEEYR-NRNFYELSPHIFALSDEAYRSLRDQDKDQCILITG 108
Cdd:cd14938      2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKcIDCIEDLSLNEYHVVHNALKNLNELKRNQSIIISG 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  109 ESGAGKTEASKLVMSYVA-AVCGKGAEVNQVKEQ--------------------LLQSNPVLEAFGNAKTVRNDNSSRFG 167
Cdd:cd14938     82 ESGSGKSEIAKNIINFIAyQVKGSRRLPTNLNDQeednihneentdyqfnmsemLKHVNVVMEAFGNAKTVKNNNSSRFS 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  168 KYMDIEFDfKGDPLGGVISNYLLEKSRVVKQPRGERNFHVFYQLLSGASEELlNKLKLERDFSRYNYLSLDSAKVNGVDD 247
Cdd:cd14938    162 KFCTIHIE-NEEIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKF-KKMYFLKNIENYSMLNNEKGFEKFSDY 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  248 AANFRTVRNAMQIVGFMDHEAESVLAVVAAVLKLGNIE----FKPESRVNGLDESKIKDKNELK----EICELTGIDQSV 319
Cdd:cd14938    240 SGKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNTEivkaFRKKSLLMGKNQCGQNINYETIlselENSEDIGLDENV 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  320 LERAFSFRTVEAKQE---KVSTT------------LNVAQAYYARDALAKNLYSRLFSWLVNRINESIKAQTK--VRKKV 382
Cdd:cd14938    320 KNLLLACKLLSFDIEtfvKYFTTnyifndsilikvHNETKIQKKLENFIKTCYEELFNWIIYKINEKCTQLQNinINTNY 399
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  383 MGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKEEQEEYIREDIEWTH-IDYFNNAIICDLIENNTNGILAMLD 461
Cdd:cd14938    400 INVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYnSENIDNEPLYNLLVGPTEGSLFSLL 479
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  462 EEcLRPGTVTDETFLeklnqvcatHQHFESRMSKCSRFL--NDTSLPHSCFRIQHYAGKVLYQVEGFVDKNNDLLYRDLS 539
Cdd:cd14938    480 EN-VSTKTIFDKSNL---------HSSIIRKFSRNSKYIkkDDITGNKKTFVITHSCGDIIYNAENFVEKNIDILTNRFI 549
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  540 QAMWKASHALIKSL---FPEGNPAKI-----------NLK--------RPPTAGSQFKASVATLMKNLQTKNPNYIRCIK 597
Cdd:cd14938    550 DMVKQSENEYMRQFcmfYNYDNSGNIveekrrysiqsALKlfkrrydtKNQMAVSLLRNNLTELEKLQETTFCHFIVCMK 629
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  598 PND-KKAAHIFNEALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKmlCKQTwphwkgPARSGVEVLFNELEIPVE 676
Cdd:cd14938    630 PNEsKRELCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFD--IKNE------DLKEKVEALIKSYQISNY 701
                          730
                   ....*....|.
gi 1057503232  677 EYSFGRSKIFI 687
Cdd:cd14938    702 EWMIGNNMIFL 712
Motor_domain cd01363
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ...
51-178 7.82e-40

Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.


Pssm-ID: 276814 [Multi-domain]  Cd Length: 170  Bit Score: 145.18  E-value: 7.82e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   51 VVISVNPYRSLPIYSPEKVEE-YRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITGESGAGKTEASKLVMSYVAAVC 129
Cdd:cd01363      1 VLVRVNPFKELPIYRDSKIIVfYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1057503232  130 GKGAEVNQ-------------VKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKG 178
Cdd:cd01363     81 FNGINKGEtegwvylteitvtLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEILLDIAG 142
Myosin_TH1 pfam06017
Unconventional myosin tail, actin- and lipid-binding; Unconventional myosins, ie those that ...
912-1089 8.16e-37

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: 461801  Cd Length: 196  Bit Score: 137.34  E-value: 8.16e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  912 KLEASELFKDKKALYPSSVGQPFQGAYLEI--NKNPKYKKLKDAI----EEKIIIAEVVNKINRaNGKSTSRIFLLTNNN 985
Cdd:pfam06017    1 KDYASDLLKGRKERRRFSLLRRFMGDYLGLenNFSGPGPKLRKAVgiggDEKVLFSDRVSKFNR-SSKPSPRILILTDKA 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  986 LLLADQKSGQ------IKSEVPLVDVTKVSMSSQNDGFFAVHLKEGSeaasKGDFLFSSDHLIEMATKLYRTTLSQTKQK 1059
Cdd:pfam06017   80 VYLIDQKKLKnglqyvLKRRIPLSDITGVSVSPLQDDWVVLHLGSPQ----KGDLLLECDFKTELVTHLSKAYKKKTNRK 155
                          170       180       190
                   ....*....|....*....|....*....|.
gi 1057503232 1060 LNIEISDEFLVQFRQDK-VCVKFIQGNQKNG 1089
Cdd:pfam06017  156 LNVKIGDTIEYRKKKGKiRTVKFVKDEPKGK 186
MYSc_Myo33 cd14894
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ...
29-653 3.65e-36

class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276859 [Multi-domain]  Cd Length: 871  Bit Score: 148.35  E-value: 3.65e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   29 ETFINNLKKRFDHSEIYTYIGSVVISV-NPYRSL------PIYSPEKVEEYRNRNFYE--LSPHIFALSDEAY------- 92
Cdd:cd14894      1 EELVDALTSRFDDDRIYTYINHHTMAVmNPYRLLqtarftSIYDEQVVLTYADTANAEtvLAPHPFAIAKQSLvrlffdn 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232   93 -------------RSLrDQDKDQCILITGESGAGKTEASKLVMSYVAAVC------------------------------ 129
Cdd:cd14894     81 ehtmplpstissnRSM-TEGRGQSLFLCGESGSGKTELAKDLLKYLVLVAqpalskgseetckvsgstrqpkiklftsst 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  130 ------------------GKGAEVNQV-------------------------------------------KEQL------ 142
Cdd:cd14894    160 kstiqmrteeartialleAKGVEKYEIvlldlhperwdemtsvsrskrlpqvhvdglffgfyeklehledEEQLrmyfkn 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  143 ----------LQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDP-----LGGVISNYLLEKSRVVKQ------PRG 201
Cdd:cd14894    240 phaakklsivLDSNIVLEAFGHATTSMNLNSSRFGKMTTLQVAFGLHPwefqiCGCHISPFLLEKSRVTSErgresgDQN 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  202 ERNFHVFYQLLSGAS-----EELLNKLKLER-DFSRYNYLSLDSAKVNGV--------DDAANFRTVRNAMQIVGFMDHE 267
Cdd:cd14894    320 ELNFHILYAMVAGVNafpfmRLLAKELHLDGiDCSALTYLGRSDHKLAGFvskedtwkKDVERWQQVIDGLDELNVSPDE 399
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  268 AESVLAVVAAVLKLGNIEFKPESRVNGLDESKIKDKNELKEICELTGIDQ-SVLERAFSFRTV--EAKQEKVSTTLNVAQ 344
Cdd:cd14894    400 QKTIFKVLSAVLWLGNIELDYREVSGKLVMSSTGALNAPQKVVELLELGSvEKLERMLMTKSVslQSTSETFEVTLEKGQ 479
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  345 AYYARDALAKNLYSRLFSWLVNRINESIK----------------AQTKVRKKVMGVLDIYGFEIFEDNSFEQFIINYCN 408
Cdd:cd14894    480 VNHVRDTLARLLYQLAFNYVVFVMNEATKmsalstdgnkhqmdsnASAPEAVSLLKIVDVFGFEDLTHNSLDQLCINYLS 559
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  409 EKLQQifieltlKEEQEEYIREDIEwTHIDYFNNAIICDLIENNTNGILAMLDE-ECLRPGTVTDETFLEKLNQ--VCAT 485
Cdd:cd14894    560 EKLYA-------REEQVIAVAYSSR-PHLTARDSEKDVLFIYEHPLGVFASLEElTILHQSENMNAQQEEKRNKlfVRNI 631
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  486 HQHFESRMSKCSRFLNDTS---------LPhscFRIQHYAGKVLYQVEGFVDKNNDLLYRDLSQAMWKASHALIKSLF-- 554
Cdd:cd14894    632 YDRNSSRLPEPPRVLSNAKrhtpvllnvLP---FVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNSSHFCRMLne 708
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503232  555 -------PEGNPAKINLKRPPTAGS-----QFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNEALVCHQIRYLGLL 622
Cdd:cd14894    709 ssqlgwsPNTNRSMLGSAESRLSGTksfvgQFRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCRSQRLI 788
                          810       820       830
                   ....*....|....*....|....*....|....*
gi 1057503232  623 ENVRVRRAGYAFRQAYE----PCLERYKMLCKQTW 653
Cdd:cd14894    789 RQMEICRNSSSSYSAIDisksTLLTRYGSLLREPY 823
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
749-771 4.59e-03

Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln residues.


Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 35.38  E-value: 4.59e-03
                            10        20
                    ....*....|....*....|...
gi 1057503232   749 QTKSSALVIQSYIRGWKARKILR 771
Cdd:smart00015    1 RLTRAAIIIQAAWRGYLARKRYK 23
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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