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Conserved domains on  [gi|2024511160|ref|XP_040531714|]
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unconventional myosin-Ib isoform X8 [Gallus gallus]

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, ...
33-692 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: 1137.27  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160   33 DSFINNLKKRFDHNEVYTYIGSVVISINPYRPLPIYTPEKVEEYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITG 112
Cdd:cd01378      1 EAINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  113 ESGAGKTEASKFVMSYVAAVCGKG-AEVNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGGVISN 191
Cdd:cd01378     81 ESGAGKTEASKRIMQYIAAVSGGSeSEVERVKDMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEPVGGHITN 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  192 YLLEKSRVVKQPRGERNFHIFYQILSGASEDFLCKLKLERDFSRYNYLGLDSAKVNGVDDAANFRTVRNAMQIVGFMDHE 271
Cdd:cd01378    161 YLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGCFDVDGIDDAADFKEVLNAMKVIGFTEEE 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  272 TQSVFEVVAAVLKLGNIEFKPESRVNgldeSKIKDKNELKEICELTGIDQSVLERAFSFRTVEAKQEK---VSTTLNVAQ 348
Cdd:cd01378    241 QDSIFRILAAILHLGNIQFAEDEEGN----AAISDTSVLDFVAYLLGVDPDQLEKALTHRTIETGGGGrsvYEVPLNVEQ 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  349 AYYARDALAKNLYSRLFSWLVTRINESIKAQTKVRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKEEQ 428
Cdd:cd01378    317 AAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKKKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFIELTLKAEQ 396
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  429 EEYIREGIEWTHIEYFNNAIICDLIENNQTGILAMLDEECLRPGTVTDDTFLEKLNQVCATHQHFESRmskcsrfLNDTT 508
Cdd:cd01378    397 EEYVREGIEWTPIKYFNNKIICDLIEEKPPGIFAILDDACLTAGDATDQTFLQKLNQLFSNHPHFECP-------SGHFE 469
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  509 LPHSCFRIQHYAGKVMYQVEGFVDKNNDLLYRDLSQAMWKASHSLIKALFPEGNPAKiNLKRPPTAGSQFKASVATLMKN 588
Cdd:cd01378    470 LRRGEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEGVDLD-SKKRPPTAGTKFKNSANALVET 548
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  589 LQTKNPNYIRCIKPNDKKAAHIFNDALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKMLCKQTWPHWRGPARAGV 668
Cdd:cd01378    549 LMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYKLLSPKTWPAWDGTWQGGV 628
                          650       660
                   ....*....|....*....|....
gi 2024511160  669 EVLFNELEIPEEEFSFGRSKIFIR 692
Cdd:cd01378    629 ESILKDLNIPPEEYQMGKTKIFIR 652
Myosin_TH1 pfam06017
Unconventional myosin tail, actin- and lipid-binding; Unconventional myosins, ie those that ...
916-1093 5.59e-45

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: 428724  Cd Length: 196  Bit Score: 160.85  E-value: 5.59e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  916 KLEASELFKDKKALYPASVGQPFQGAYLEISKNPKY--KKLKDAV----DEKIIIAEVVNKINRaNGKATSRIFLLTKNN 989
Cdd:pfam06017    1 KDYASDLLKGKKERRRFSLLRRFMGDYLGLENNFSGpgPELRKAVgiggDEKVLFSDRVSKFNR-SSKPSPRILILTDKA 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  990 VLLADQKS------GNIKSEVPLGDVTKVSMSSQNDGFFAVHLKEGSgaasKGDFLFSSDHLIEMATKLYRTTLSQTKQK 1063
Cdd:pfam06017   80 LYLIDPKKfknglqYVLKRRIPLSDITGVSVSPLQDDWVVLHLGSPQ----KGDLLLECDFKTELVTVLSKLYKKKTNKK 155
                          170       180       190
                   ....*....|....*....|....*....|.
gi 2024511160 1064 LNIEISDEFLVQFRQDK-VCVKFIQGSQKNG 1093
Cdd:pfam06017  156 LNVKISDTIEYRKKKGKiRTVKFVKDEPKGK 186
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
753-775 1.12e-03

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


:

Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 37.31  E-value: 1.12e-03
                            10        20
                    ....*....|....*....|...
gi 2024511160   753 KIRSSAVIIQSYIRGWKARKLLR 775
Cdd:smart00015    1 RLTRAAIIIQAAWRGYLARKRYK 23
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
811-833 2.62e-03

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


:

Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 36.15  E-value: 2.62e-03
                            10        20
                    ....*....|....*....|...
gi 2024511160   811 RNKQAIAVIWAYWLGYKVRREYR 833
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, ...
33-692 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: 1137.27  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160   33 DSFINNLKKRFDHNEVYTYIGSVVISINPYRPLPIYTPEKVEEYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITG 112
Cdd:cd01378      1 EAINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  113 ESGAGKTEASKFVMSYVAAVCGKG-AEVNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGGVISN 191
Cdd:cd01378     81 ESGAGKTEASKRIMQYIAAVSGGSeSEVERVKDMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEPVGGHITN 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  192 YLLEKSRVVKQPRGERNFHIFYQILSGASEDFLCKLKLERDFSRYNYLGLDSAKVNGVDDAANFRTVRNAMQIVGFMDHE 271
Cdd:cd01378    161 YLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGCFDVDGIDDAADFKEVLNAMKVIGFTEEE 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  272 TQSVFEVVAAVLKLGNIEFKPESRVNgldeSKIKDKNELKEICELTGIDQSVLERAFSFRTVEAKQEK---VSTTLNVAQ 348
Cdd:cd01378    241 QDSIFRILAAILHLGNIQFAEDEEGN----AAISDTSVLDFVAYLLGVDPDQLEKALTHRTIETGGGGrsvYEVPLNVEQ 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  349 AYYARDALAKNLYSRLFSWLVTRINESIKAQTKVRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKEEQ 428
Cdd:cd01378    317 AAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKKKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFIELTLKAEQ 396
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  429 EEYIREGIEWTHIEYFNNAIICDLIENNQTGILAMLDEECLRPGTVTDDTFLEKLNQVCATHQHFESRmskcsrfLNDTT 508
Cdd:cd01378    397 EEYVREGIEWTPIKYFNNKIICDLIEEKPPGIFAILDDACLTAGDATDQTFLQKLNQLFSNHPHFECP-------SGHFE 469
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  509 LPHSCFRIQHYAGKVMYQVEGFVDKNNDLLYRDLSQAMWKASHSLIKALFPEGNPAKiNLKRPPTAGSQFKASVATLMKN 588
Cdd:cd01378    470 LRRGEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEGVDLD-SKKRPPTAGTKFKNSANALVET 548
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  589 LQTKNPNYIRCIKPNDKKAAHIFNDALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKMLCKQTWPHWRGPARAGV 668
Cdd:cd01378    549 LMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYKLLSPKTWPAWDGTWQGGV 628
                          650       660
                   ....*....|....*....|....
gi 2024511160  669 EVLFNELEIPEEEFSFGRSKIFIR 692
Cdd:cd01378    629 ESILKDLNIPPEEYQMGKTKIFIR 652
MYSc smart00242
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ...
20-705 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: 1030.57  E-value: 0e+00
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160    20 GVGDMVLLEPLNEDSFINNLKKRFDHNEVYTYIGSVVISINPYRPLPIYTPEKVEEYRNRNFYELSPHIFALSDEAYRSL 99
Cdd:smart00242    7 GVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIADNAYRNM 86
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160   100 RDQDKDQCILITGESGAGKTEASKFVMSYVAAVCGKGAEVNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFD 179
Cdd:smart00242   87 LNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNTEVGSVEDQILESNPILEAFGNAKTLRNNNSSRFGKFIEIHFD 166
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160   180 FKGDPLGGVISNYLLEKSRVVKQPRGERNFHIFYQILSGASEDFLCKLKLERDfSRYNYL-GLDSAKVNGVDDAANFRTV 258
Cdd:smart00242  167 AKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSP-EDYRYLnQGGCLTVDGIDDAEEFKET 245
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160   259 RNAMQIVGFMDHETQSVFEVVAAVLKLGNIEFKPESrvNGLDESKIKDKNELKEICELTGIDQSVLERAFSFRTVEAKQE 338
Cdd:smart00242  246 LNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGR--NDNAASTVKDKEELSNAAELLGVDPEELEKALTKRKIKTGGE 323
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160   339 KVSTTLNVAQAYYARDALAKNLYSRLFSWLVTRINESIKAQTKvRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQI 418
Cdd:smart00242  324 VITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDG-STYFIGVLDIYGFEIFEVNSFEQLCINYANEKLQQF 402
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160   419 FIELTLKEEQEEYIREGIEWTHIEYFNNAIICDLIENNQTGILAMLDEECLRPGtVTDDTFLEKLNQVCATHQHFESRMS 498
Cdd:smart00242  403 FNQHVFKLEQEEYEREGIDWTFIDFFDNQDCIDLIEKKPPGILSLLDEECRFPK-GTDQTFLEKLNQHHKKHPHFSKPKK 481
                           490       500       510       520       530       540       550       560
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160   499 KcsrflndttlPHSCFRIQHYAGKVMYQVEGFVDKNNDLLYRDLSQAMWKASHSLIKALFPEGNPAKINLKRPPTAGSQF 578
Cdd:smart00242  482 K----------GRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSGVSNAGSKKRFQTVGSQF 551
                           570       580       590       600       610       620       630       640
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160   579 KASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNDALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKMLCKQTWP 658
Cdd:smart00242  552 KEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRLPFDEFLQRYRVLLPDTWP 631
                           650       660       670       680
                    ....*....|....*....|....*....|....*....|....*..
gi 2024511160   659 HWRGPARAGVEVLFNELEIPEEEFSFGRSKIFIRnPRTLFKLEDLRK 705
Cdd:smart00242  632 PWGGDAKKACEALLQSLGLDEDEYQLGKTKVFLR-PGQLAELEELRE 677
Myosin_head pfam00063
Myosin head (motor domain);
21-692 0e+00

Myosin head (motor domain);


Pssm-ID: 395017  Cd Length: 674  Bit Score: 942.09  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160   21 VGDMVLLEPLNEDSFINNLKKRFDHNEVYTYIGSVVISINPYRPLPIYTPEKVEEYRNRNFYELSPHIFALSDEAYRSLR 100
Cdd:pfam00063    1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  101 DQDKDQCILITGESGAGKTEASKFVMSYVAAVCGKGAEVN--QVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEF 178
Cdd:pfam00063   81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAGNvgRLEEQILQSNPILEAFGNAKTVRNNNSSRFGKYIEIQF 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  179 DFKGDPLGGVISNYLLEKSRVVKQPRGERNFHIFYQILSGASEDFLCKLKLErDFSRYNYL-GLDSAKVNGVDDAANFRT 257
Cdd:pfam00063  161 DAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLT-NPKDYHYLsQSGCYTIDGIDDSEEFKI 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  258 VRNAMQIVGFMDHETQSVFEVVAAVLKLGNIEFKPESRVNGldeSKIKDKNELKEICELTGIDQSVLERAFSFRTVEAKQ 337
Cdd:pfam00063  240 TDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQ---AVPDDTENLQKAASLLGIDSTELEKALCKRRIKTGR 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  338 EKVSTTLNVAQAYYARDALAKNLYSRLFSWLVTRINESIKAQTKVRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQ 417
Cdd:pfam00063  317 ETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTIEKASFIGVLDIYGFEIFEKNSFEQLCINYVNEKLQQ 396
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  418 IFIELTLKEEQEEYIREGIEWTHIEYFNNAIICDLIENNQTGILAMLDEECLRPGtVTDDTFLEKLNQVCATHQHFESrm 497
Cdd:pfam00063  397 FFNHHMFKLEQEEYVREGIEWTFIDFGDNQPCIDLIEKKPLGILSLLDEECLFPK-ATDQTFLDKLYSTFSKHPHFQK-- 473
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  498 skcSRFLNDTtlphsCFRIQHYAGKVMYQVEGFVDKNNDLLYRDLSQAMWKASHSLIKALFPEGNPA------------- 564
Cdd:pfam00063  474 ---PRLQGET-----HFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAesaaanesgkstp 545
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  565 -KINLKRPPTAGSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNDALVCHQIRYLGLLENVRVRRAGYAFRQAYE 643
Cdd:pfam00063  546 kRTKKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQ 625
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*....
gi 2024511160  644 PCLERYKMLCKQTWPHWRGPARAGVEVLFNELEIPEEEFSFGRSKIFIR 692
Cdd:pfam00063  626 EFVQRYRILAPKTWPKWKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
COG5022 COG5022
Myosin heavy chain [General function prediction only];
20-810 0e+00

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 740.35  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160   20 GVGDMVLLEPLNEDSFINNLKKRFDHNEVYTYIGSVVISINPYRPLPIYTPEKVEEYRNRNFYELSPHIFALSDEAYRSL 99
Cdd:COG5022     67 GVDDLTELSYLNEPAVLHNLEKRYNNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNL 146
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  100 RDQDKDQCILITGESGAGKTEASKFVMSYVAAVCG-KGAEVNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEF 178
Cdd:COG5022    147 LSEKENQTIIISGESGAGKTENAKRIMQYLASVTSsSTVEISSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEF 226
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  179 DFKGDPLGGVISNYLLEKSRVVKQPRGERNFHIFYQILSGASEDfLCKLKLERDFSRYNYLGlDSA--KVNGVDDAANFR 256
Cdd:COG5022    227 DENGEICGAKIETYLLEKSRVVHQNKNERNYHIFYQLLAGDPEE-LKKLLLLQNPKDYIYLS-QGGcdKIDGIDDAKEFK 304
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  257 TVRNAMQIVGFMDHETQSVFEVVAAVLKLGNIEFKpESRVnglDESKIKDKNELKEICELTGIDQSVLERAFSFRTVEAK 336
Cdd:COG5022    305 ITLDALKTIGIDEEEQDQIFKILAAILHIGNIEFK-EDRN---GAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTG 380
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  337 QEKVSTTLNVAQAYYARDALAKNLYSRLFSWLVTRINESIKAqTKVRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQ 416
Cdd:COG5022    381 GEWIVVPLNLEQALAIRDSLAKALYSNLFDWIVDRINKSLDH-SAAASNFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQ 459
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  417 QIFIELTLKEEQEEYIREGIEWTHIEYFNNAIICDLIEN-NQTGILAMLDEECLRPgTVTDDTFLEKLNQV--CATHQHF 493
Cdd:COG5022    460 QFFNQHMFKLEQEEYVKEGIEWSFIDYFDNQPCIDLIEKkNPLGILSLLDEECVMP-HATDESFTSKLAQRlnKNSNPKF 538
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  494 ESrmskcSRFLNDTtlphscFRIQHYAGKVMYQVEGFVDKNNDLLYRDLSQAMWKASHSLIKALFPEgnPAKINLK-RPP 572
Cdd:COG5022    539 KK-----SRFRDNK------FVVKHYAGDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDD--EENIESKgRFP 605
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  573 TAGSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNDALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKML 652
Cdd:COG5022    606 TLGSRFKESLNSLMSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRIL 685
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  653 CKQ----TWPHWRGPARAGVEVLFNELEIPEEEFSFGRSKIFIRNPrTLFKLEDLRKQRLEDLATLIEKIYRGWKCRTHF 728
Cdd:COG5022    686 SPSkswtGEYTWKEDTKNAVKSILEELVIDSSKYQIGNTKVFFKAG-VLAALEDMRDAKLDNIATRIQRAIRGRYLRRRY 764
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  729 LLMKKSQIVIAA---------------WFRRY---------AQQKKYQkiRSSAVIIQSYIRGWKARKLLRELKHQKRCN 784
Cdd:COG5022    765 LQALKRIKKIQViqhgfrlrrlvdyelKWRLFiklqpllslLGSRKEY--RSYLACIIKLQKTIKREKKLRETEEVEFSL 842
                          810       820
                   ....*....|....*....|....*.
gi 2024511160  785 EAATIIAAYWHGTQARRELRRLKEEA 810
Cdd:COG5022    843 KAEVLIQKFGRSLKAKKRFSLLKKET 868
PTZ00014 PTZ00014
myosin-A; Provisional
21-745 8.47e-155

myosin-A; Provisional


Pssm-ID: 240229 [Multi-domain]  Cd Length: 821  Bit Score: 481.45  E-value: 8.47e-155
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160   21 VGDMVLLEPLNEDSFINNLKKRFDHNEVYTYIGSVVISINPYRPLPIYTPEKVEEYRN-RNFYELSPHIFALSDEAYRSL 99
Cdd:PTZ00014    98 YGDIGLLPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYRDaKDSDKLPPHVFTTARRALENL 177
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  100 RDQDKDQCILITGESGAGKTEASKFVMSYVAAvcGKGAEVNQ-VKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEF 178
Cdd:PTZ00014   178 HGVKKSQTIIVSGESGAGKTEATKQIMRYFAS--SKSGNMDLkIQNAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQL 255
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  179 DFKGDPLGGVISNYLLEKSRVVKQPRGERNFHIFYQILSGASEDFLCKLKLeRDFSRYNYLGLDSAKVNGVDDAANFRTV 258
Cdd:PTZ00014   256 GEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKL-KSLEEYKYINPKCLDVPGIDDVKDFEEV 334
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  259 RNAMQIVGFMDHETQSVFEVVAAVLKLGNIEFKPESRVNGLDESKIKDKNE--LKEICELTGIDQSVLERAFSFRTVEAK 336
Cdd:PTZ00014   335 MESFDSMGLSESQIEDIFSILSGVLLLGNVEIEGKEEGGLTDAAAISDESLevFNEACELLFLDYESLKKELTVKVTYAG 414
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  337 QEKVSTTLNVAQAYYARDALAKNLYSRLFSWLVTRINESIKAQTKVrKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQ 416
Cdd:PTZ00014   415 NQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGF-KVFIGMLDIFGFEVFKNNSLEQLFINITNEMLQ 493
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  417 QIFIELTLKEEQEEYIREGIEWTHIEYFNNAIICDLIENNQTGILAMLDEECLRPGTvTDDTFLEKLNQVCATHQHFesr 496
Cdd:PTZ00014   494 KNFVDIVFERESKLYKDEGISTEELEYTSNESVIDLLCGKGKSVLSILEDQCLAPGG-TDEKFVSSCNTNLKNNPKY--- 569
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  497 mSKCSRFLNdttlphSCFRIQHYAGKVMYQVEGFVDKNNDLLYRDLSQAMWKASHSLIKALFP-----EGNPAKINLkrp 571
Cdd:PTZ00014   570 -KPAKVDSN------KNFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLFEgveveKGKLAKGQL--- 639
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  572 ptAGSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNDALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKM 651
Cdd:PTZ00014   640 --IGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKY 717
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  652 LCKQTWPHWRGPARAGVEVLFNELEIPEEEFSFGRSKIFIRnPRTLFKLEDLRKQRL---EDLATLIEKIYRGWKCRTHF 728
Cdd:PTZ00014   718 LDLAVSNDSSLDPKEKAEKLLERSGLPKDSYAIGKTMVFLK-KDAAKELTQIQREKLaawEPLVSVLEALILKIKKKRKV 796
                          730
                   ....*....|....*..
gi 2024511160  729 LLMKKSQIVIAAWFRRY 745
Cdd:PTZ00014   797 RKNIKSLVRIQAHLRRH 813
Myosin_TH1 pfam06017
Unconventional myosin tail, actin- and lipid-binding; Unconventional myosins, ie those that ...
916-1093 5.59e-45

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: 428724  Cd Length: 196  Bit Score: 160.85  E-value: 5.59e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  916 KLEASELFKDKKALYPASVGQPFQGAYLEISKNPKY--KKLKDAV----DEKIIIAEVVNKINRaNGKATSRIFLLTKNN 989
Cdd:pfam06017    1 KDYASDLLKGKKERRRFSLLRRFMGDYLGLENNFSGpgPELRKAVgiggDEKVLFSDRVSKFNR-SSKPSPRILILTDKA 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  990 VLLADQKS------GNIKSEVPLGDVTKVSMSSQNDGFFAVHLKEGSgaasKGDFLFSSDHLIEMATKLYRTTLSQTKQK 1063
Cdd:pfam06017   80 LYLIDPKKfknglqYVLKRRIPLSDITGVSVSPLQDDWVVLHLGSPQ----KGDLLLECDFKTELVTVLSKLYKKKTNKK 155
                          170       180       190
                   ....*....|....*....|....*....|.
gi 2024511160 1064 LNIEISDEFLVQFRQDK-VCVKFIQGSQKNG 1093
Cdd:pfam06017  156 LNVKISDTIEYRKKKGKiRTVKFVKDEPKGK 186
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
753-775 1.12e-03

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


Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 37.31  E-value: 1.12e-03
                            10        20
                    ....*....|....*....|...
gi 2024511160   753 KIRSSAVIIQSYIRGWKARKLLR 775
Cdd:smart00015    1 RLTRAAIIIQAAWRGYLARKRYK 23
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
811-833 2.62e-03

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


Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 36.15  E-value: 2.62e-03
                            10        20
                    ....*....|....*....|...
gi 2024511160   811 RNKQAIAVIWAYWLGYKVRREYR 833
Cdd:smart00015    1 RLTRAAIIIQAAWRGYLARKRYK 23
IQ pfam00612
IQ calmodulin-binding motif; Calmodulin-binding motif.
755-775 5.31e-03

IQ calmodulin-binding motif; Calmodulin-binding motif.


Pssm-ID: 425778  Cd Length: 21  Bit Score: 35.37  E-value: 5.31e-03
                           10        20
                   ....*....|....*....|.
gi 2024511160  755 RSSAVIIQSYIRGWKARKLLR 775
Cdd:pfam00612    1 RKAAIKIQAAWRGYLARKRYK 21
 
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, ...
33-692 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: 1137.27  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160   33 DSFINNLKKRFDHNEVYTYIGSVVISINPYRPLPIYTPEKVEEYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITG 112
Cdd:cd01378      1 EAINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  113 ESGAGKTEASKFVMSYVAAVCGKG-AEVNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGGVISN 191
Cdd:cd01378     81 ESGAGKTEASKRIMQYIAAVSGGSeSEVERVKDMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEPVGGHITN 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  192 YLLEKSRVVKQPRGERNFHIFYQILSGASEDFLCKLKLERDFSRYNYLGLDSAKVNGVDDAANFRTVRNAMQIVGFMDHE 271
Cdd:cd01378    161 YLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGCFDVDGIDDAADFKEVLNAMKVIGFTEEE 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  272 TQSVFEVVAAVLKLGNIEFKPESRVNgldeSKIKDKNELKEICELTGIDQSVLERAFSFRTVEAKQEK---VSTTLNVAQ 348
Cdd:cd01378    241 QDSIFRILAAILHLGNIQFAEDEEGN----AAISDTSVLDFVAYLLGVDPDQLEKALTHRTIETGGGGrsvYEVPLNVEQ 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  349 AYYARDALAKNLYSRLFSWLVTRINESIKAQTKVRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKEEQ 428
Cdd:cd01378    317 AAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKKKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFIELTLKAEQ 396
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  429 EEYIREGIEWTHIEYFNNAIICDLIENNQTGILAMLDEECLRPGTVTDDTFLEKLNQVCATHQHFESRmskcsrfLNDTT 508
Cdd:cd01378    397 EEYVREGIEWTPIKYFNNKIICDLIEEKPPGIFAILDDACLTAGDATDQTFLQKLNQLFSNHPHFECP-------SGHFE 469
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  509 LPHSCFRIQHYAGKVMYQVEGFVDKNNDLLYRDLSQAMWKASHSLIKALFPEGNPAKiNLKRPPTAGSQFKASVATLMKN 588
Cdd:cd01378    470 LRRGEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEGVDLD-SKKRPPTAGTKFKNSANALVET 548
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  589 LQTKNPNYIRCIKPNDKKAAHIFNDALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKMLCKQTWPHWRGPARAGV 668
Cdd:cd01378    549 LMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYKLLSPKTWPAWDGTWQGGV 628
                          650       660
                   ....*....|....*....|....
gi 2024511160  669 EVLFNELEIPEEEFSFGRSKIFIR 692
Cdd:cd01378    629 ESILKDLNIPPEEYQMGKTKIFIR 652
MYSc smart00242
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ...
20-705 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: 1030.57  E-value: 0e+00
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160    20 GVGDMVLLEPLNEDSFINNLKKRFDHNEVYTYIGSVVISINPYRPLPIYTPEKVEEYRNRNFYELSPHIFALSDEAYRSL 99
Cdd:smart00242    7 GVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIADNAYRNM 86
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160   100 RDQDKDQCILITGESGAGKTEASKFVMSYVAAVCGKGAEVNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFD 179
Cdd:smart00242   87 LNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNTEVGSVEDQILESNPILEAFGNAKTLRNNNSSRFGKFIEIHFD 166
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160   180 FKGDPLGGVISNYLLEKSRVVKQPRGERNFHIFYQILSGASEDFLCKLKLERDfSRYNYL-GLDSAKVNGVDDAANFRTV 258
Cdd:smart00242  167 AKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSP-EDYRYLnQGGCLTVDGIDDAEEFKET 245
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160   259 RNAMQIVGFMDHETQSVFEVVAAVLKLGNIEFKPESrvNGLDESKIKDKNELKEICELTGIDQSVLERAFSFRTVEAKQE 338
Cdd:smart00242  246 LNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGR--NDNAASTVKDKEELSNAAELLGVDPEELEKALTKRKIKTGGE 323
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160   339 KVSTTLNVAQAYYARDALAKNLYSRLFSWLVTRINESIKAQTKvRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQI 418
Cdd:smart00242  324 VITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDG-STYFIGVLDIYGFEIFEVNSFEQLCINYANEKLQQF 402
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160   419 FIELTLKEEQEEYIREGIEWTHIEYFNNAIICDLIENNQTGILAMLDEECLRPGtVTDDTFLEKLNQVCATHQHFESRMS 498
Cdd:smart00242  403 FNQHVFKLEQEEYEREGIDWTFIDFFDNQDCIDLIEKKPPGILSLLDEECRFPK-GTDQTFLEKLNQHHKKHPHFSKPKK 481
                           490       500       510       520       530       540       550       560
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160   499 KcsrflndttlPHSCFRIQHYAGKVMYQVEGFVDKNNDLLYRDLSQAMWKASHSLIKALFPEGNPAKINLKRPPTAGSQF 578
Cdd:smart00242  482 K----------GRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSGVSNAGSKKRFQTVGSQF 551
                           570       580       590       600       610       620       630       640
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160   579 KASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNDALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKMLCKQTWP 658
Cdd:smart00242  552 KEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRLPFDEFLQRYRVLLPDTWP 631
                           650       660       670       680
                    ....*....|....*....|....*....|....*....|....*..
gi 2024511160   659 HWRGPARAGVEVLFNELEIPEEEFSFGRSKIFIRnPRTLFKLEDLRK 705
Cdd:smart00242  632 PWGGDAKKACEALLQSLGLDEDEYQLGKTKVFLR-PGQLAELEELRE 677
Myosin_head pfam00063
Myosin head (motor domain);
21-692 0e+00

Myosin head (motor domain);


Pssm-ID: 395017  Cd Length: 674  Bit Score: 942.09  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160   21 VGDMVLLEPLNEDSFINNLKKRFDHNEVYTYIGSVVISINPYRPLPIYTPEKVEEYRNRNFYELSPHIFALSDEAYRSLR 100
Cdd:pfam00063    1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  101 DQDKDQCILITGESGAGKTEASKFVMSYVAAVCGKGAEVN--QVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEF 178
Cdd:pfam00063   81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAGNvgRLEEQILQSNPILEAFGNAKTVRNNNSSRFGKYIEIQF 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  179 DFKGDPLGGVISNYLLEKSRVVKQPRGERNFHIFYQILSGASEDFLCKLKLErDFSRYNYL-GLDSAKVNGVDDAANFRT 257
Cdd:pfam00063  161 DAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLT-NPKDYHYLsQSGCYTIDGIDDSEEFKI 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  258 VRNAMQIVGFMDHETQSVFEVVAAVLKLGNIEFKPESRVNGldeSKIKDKNELKEICELTGIDQSVLERAFSFRTVEAKQ 337
Cdd:pfam00063  240 TDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQ---AVPDDTENLQKAASLLGIDSTELEKALCKRRIKTGR 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  338 EKVSTTLNVAQAYYARDALAKNLYSRLFSWLVTRINESIKAQTKVRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQ 417
Cdd:pfam00063  317 ETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTIEKASFIGVLDIYGFEIFEKNSFEQLCINYVNEKLQQ 396
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  418 IFIELTLKEEQEEYIREGIEWTHIEYFNNAIICDLIENNQTGILAMLDEECLRPGtVTDDTFLEKLNQVCATHQHFESrm 497
Cdd:pfam00063  397 FFNHHMFKLEQEEYVREGIEWTFIDFGDNQPCIDLIEKKPLGILSLLDEECLFPK-ATDQTFLDKLYSTFSKHPHFQK-- 473
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  498 skcSRFLNDTtlphsCFRIQHYAGKVMYQVEGFVDKNNDLLYRDLSQAMWKASHSLIKALFPEGNPA------------- 564
Cdd:pfam00063  474 ---PRLQGET-----HFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAesaaanesgkstp 545
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  565 -KINLKRPPTAGSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNDALVCHQIRYLGLLENVRVRRAGYAFRQAYE 643
Cdd:pfam00063  546 kRTKKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQ 625
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*....
gi 2024511160  644 PCLERYKMLCKQTWPHWRGPARAGVEVLFNELEIPEEEFSFGRSKIFIR 692
Cdd:pfam00063  626 EFVQRYRILAPKTWPKWKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
MYSc cd00124
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ...
33-692 0e+00

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


Pssm-ID: 276950  Cd Length: 633  Bit Score: 784.86  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160   33 DSFINNLKKRFDHNEVYTYIGSVVISINPYRPLPIYTPEKVEEYRNRN-FYELSPHIFALSDEAYRSLRDQDKDQCILIT 111
Cdd:cd00124      1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGrSADLPPHVFAVADAAYRAMLRDGQNQSILIS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  112 GESGAGKTEASKFVMSYVAAVCGKGAEVNQVK-----EQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLG 186
Cdd:cd00124     81 GESGAGKTETTKLVLKYLAALSGSGSSKSSSSassieQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPTGRLVG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  187 GVISNYLLEKSRVVKQPRGERNFHIFYQILSGAS---EDFLCKLKLERDFSRYNYLGL-DSAKVNGVDDAANFRTVRNAM 262
Cdd:cd00124    161 ASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSdgaREELKLELLLSYYYLNDYLNSsGCDRIDGVDDAEEFQELLDAL 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  263 QIVGFMDHETQSVFEVVAAVLKLGNIEFKpESRVNGLDESKIKDKNELKEICELTGIDQSVLERAFSFRTVEAKQEKVST 342
Cdd:cd00124    241 DVLGFSDEEQDSIFRILAAILHLGNIEFE-EDEEDEDSSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGETITK 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  343 TLNVAQAYYARDALAKNLYSRLFSWLVTRINESIKAQTKVRKK-VMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIE 421
Cdd:cd00124    320 PLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAESTsFIGILDIFGFENFEVNSFEQLCINYANEKLQQFFNQ 399
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  422 LTLKEEQEEYIREGIEWTHIEYFNNAIICDLIENNQTGILAMLDEECLRPGTvTDDTFLEKLNQVCATHqhfesrmskcS 501
Cdd:cd00124    400 HVFKLEQEEYEEEGIDWSFIDFPDNQDCLDLIEGKPLGILSLLDEECLFPKG-TDATFLEKLYSAHGSH----------P 468
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  502 RFLNDTTLPHSCFRIQHYAGKVMYQVEGFVDKNNDLLYRDLSQAMwkashslikalfpegnpakinlkrppTAGSQFKAS 581
Cdd:cd00124    469 RFFSKKRKAKLEFGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLL--------------------------RSGSQFRSQ 522
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  582 VATLMKNLQTKNPNYIRCIKPNDKKAAHIFNDALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKMLCKQTWPHWR 661
Cdd:cd00124    523 LDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYRILAPGATEKAS 602
                          650       660       670
                   ....*....|....*....|....*....|.
gi 2024511160  662 GPARAGVEVLFNELEIPEEEFSFGRSKIFIR 692
Cdd:cd00124    603 DSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
COG5022 COG5022
Myosin heavy chain [General function prediction only];
20-810 0e+00

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 740.35  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160   20 GVGDMVLLEPLNEDSFINNLKKRFDHNEVYTYIGSVVISINPYRPLPIYTPEKVEEYRNRNFYELSPHIFALSDEAYRSL 99
Cdd:COG5022     67 GVDDLTELSYLNEPAVLHNLEKRYNNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNL 146
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  100 RDQDKDQCILITGESGAGKTEASKFVMSYVAAVCG-KGAEVNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEF 178
Cdd:COG5022    147 LSEKENQTIIISGESGAGKTENAKRIMQYLASVTSsSTVEISSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEF 226
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  179 DFKGDPLGGVISNYLLEKSRVVKQPRGERNFHIFYQILSGASEDfLCKLKLERDFSRYNYLGlDSA--KVNGVDDAANFR 256
Cdd:COG5022    227 DENGEICGAKIETYLLEKSRVVHQNKNERNYHIFYQLLAGDPEE-LKKLLLLQNPKDYIYLS-QGGcdKIDGIDDAKEFK 304
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  257 TVRNAMQIVGFMDHETQSVFEVVAAVLKLGNIEFKpESRVnglDESKIKDKNELKEICELTGIDQSVLERAFSFRTVEAK 336
Cdd:COG5022    305 ITLDALKTIGIDEEEQDQIFKILAAILHIGNIEFK-EDRN---GAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTG 380
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  337 QEKVSTTLNVAQAYYARDALAKNLYSRLFSWLVTRINESIKAqTKVRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQ 416
Cdd:COG5022    381 GEWIVVPLNLEQALAIRDSLAKALYSNLFDWIVDRINKSLDH-SAAASNFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQ 459
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  417 QIFIELTLKEEQEEYIREGIEWTHIEYFNNAIICDLIEN-NQTGILAMLDEECLRPgTVTDDTFLEKLNQV--CATHQHF 493
Cdd:COG5022    460 QFFNQHMFKLEQEEYVKEGIEWSFIDYFDNQPCIDLIEKkNPLGILSLLDEECVMP-HATDESFTSKLAQRlnKNSNPKF 538
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  494 ESrmskcSRFLNDTtlphscFRIQHYAGKVMYQVEGFVDKNNDLLYRDLSQAMWKASHSLIKALFPEgnPAKINLK-RPP 572
Cdd:COG5022    539 KK-----SRFRDNK------FVVKHYAGDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDD--EENIESKgRFP 605
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  573 TAGSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNDALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKML 652
Cdd:COG5022    606 TLGSRFKESLNSLMSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRIL 685
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  653 CKQ----TWPHWRGPARAGVEVLFNELEIPEEEFSFGRSKIFIRNPrTLFKLEDLRKQRLEDLATLIEKIYRGWKCRTHF 728
Cdd:COG5022    686 SPSkswtGEYTWKEDTKNAVKSILEELVIDSSKYQIGNTKVFFKAG-VLAALEDMRDAKLDNIATRIQRAIRGRYLRRRY 764
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  729 LLMKKSQIVIAA---------------WFRRY---------AQQKKYQkiRSSAVIIQSYIRGWKARKLLRELKHQKRCN 784
Cdd:COG5022    765 LQALKRIKKIQViqhgfrlrrlvdyelKWRLFiklqpllslLGSRKEY--RSYLACIIKLQKTIKREKKLRETEEVEFSL 842
                          810       820
                   ....*....|....*....|....*.
gi 2024511160  785 EAATIIAAYWHGTQARRELRRLKEEA 810
Cdd:COG5022    843 KAEVLIQKFGRSLKAKKRFSLLKKET 868
MYSc_class_II cd01377
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ...
34-692 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: 676.49  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160   34 SFINNLKKRFDHNEVYTYIGSVVISINPYRPLPIYTPEKVEEYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITGE 113
Cdd:cd01377      2 SVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITGE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  114 SGAGKTEASKFVMSYVAAVCG-------KGAEVNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLG 186
Cdd:cd01377     82 SGAGKTENTKKVIQYLASVAAsskkkkeSGKKKGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTGKIAG 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  187 GVISNYLLEKSRVVKQPRGERNFHIFYQILSGASEDFLCKLKLERDFSRYNYLGLDSAKVNGVDDAANFRTVRNAMQIVG 266
Cdd:cd01377    162 ADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYFFLSQGELTIDGVDDAEEFKLTDEAFDILG 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  267 FMDHETQSVFEVVAAVLKLGNIEFKPESRvngLDESKIKDKNELKEICELTGIDQSVLERAFSFRTVEAKQEKVSTTLNV 346
Cdd:cd01377    242 FSEEEKMSIFKIVAAILHLGNIKFKQRRR---EEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKGQNK 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  347 AQAYYARDALAKNLYSRLFSWLVTRINESIKaQTKVRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIF----IEL 422
Cdd:cd01377    319 EQVVFSVGALAKALYERLFLWLVKRINKTLD-TKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFnhhmFVL 397
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  423 tlkeEQEEYIREGIEWTHIEYFNNAIIC-DLIENNQTGILAMLDEECLRPGTvTDDTFLEKLNQVCATHQHFESRMSKCS 501
Cdd:cd01377    398 ----EQEEYKKEGIEWTFIDFGLDLQPTiDLIEKPNMGILSILDEECVFPKA-TDKTFVEKLYSNHLGKSKNFKKPKPKK 472
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  502 rflndttlPHSCFRIQHYAGKVMYQVEGFVDKNNDLLYRDLSQAMWKASHSLIKALFPE-----GNPAKINLKRPP--TA 574
Cdd:cd01377    473 --------SEAHFILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDyeesgGGGGKKKKKGGSfrTV 544
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  575 GSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNDALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKMLCK 654
Cdd:cd01377    545 SQLHKEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAP 624
                          650       660       670
                   ....*....|....*....|....*....|....*...
gi 2024511160  655 QTWPHWRGPARAGVEVLFNELEIPEEEFSFGRSKIFIR 692
Cdd:cd01377    625 NAIPKGFDDGKAACEKILKALQLDPELYRIGNTKVFFK 662
MYSc_Myo5 cd01380
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ...
37-692 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: 673.10  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160   37 NNLKKRF-DHNEVYTYIGSVVISINPYRPLPIYTPEKVEEYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITGESG 115
Cdd:cd01380      5 HNLKVRFcQRNAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVSGESG 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  116 AGKTEASKFVMSYVAAVCGKGAEVNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGGVISNYLLE 195
Cdd:cd01380     85 AGKTVSAKYAMRYFATVGGSSSGETQVEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYRIIGANMRTYLLE 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  196 KSRVVKQPRGERNFHIFYQILSGASEDFLCKLKLErDFSRYNYLGL-DSAKVNGVDDAANFRTVRNAMQIVGFMDHETQS 274
Cdd:cd01380    165 KSRVVFQAEEERNYHIFYQLCAAASLPELKELHLG-SAEDFFYTNQgGSPVIDGVDDAAEFEETRKALTLLGISEEEQME 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  275 VFEVVAAVLKLGNIEFKPESRvnglDESKIKDKNE-LKEICELTGIDQSVLERAFSFRTVEAKQEKVSTTLNVAQAYYAR 353
Cdd:cd01380    244 IFRILAAILHLGNVEIKATRN----DSASISPDDEhLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPLTLQQAIVAR 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  354 DALAKNLYSRLFSWLVTRINESIKAQTKVR-KKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKEEQEEYI 432
Cdd:cd01380    320 DALAKHIYAQLFDWIVDRINKALASPVKEKqHSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHVFKLEQEEYV 399
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  433 REGIEWTHIEYFNNAIICDLIEnNQTGILAMLDEECLRPGTvTDDTFLEKLNQVCATH--QHFESrmskcSRFLNDTtlp 510
Cdd:cd01380    400 KEEIEWSFIDFYDNQPCIDLIE-GKLGILDLLDEECRLPKG-SDENWAQKLYNQHLKKpnKHFKK-----PRFSNTA--- 469
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  511 hscFRIQHYAGKVMYQVEGFVDKNNDLLYRDLSQAMwKASHSlikalfpegnpakinlkRPPTAGSQFKASVATLMKNLQ 590
Cdd:cd01380    470 ---FIVKHFADDVEYQVEGFLEKNRDTVSEEHLNVL-KASKN-----------------RKKTVGSQFRDSLILLMETLN 528
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  591 TKNPNYIRCIKPNDKKAAHIFNDALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKMLCKQTwpHWRG-PARAGVE 669
Cdd:cd01380    529 STTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLPSK--EWLRdDKKKTCE 606
                          650       660
                   ....*....|....*....|....
gi 2024511160  670 VLFNELeIPEEE-FSFGRSKIFIR 692
Cdd:cd01380    607 NILENL-ILDPDkYQFGKTKIFFR 629
MYSc_Myo7 cd01381
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ...
38-692 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 2024511160   38 NLKKRFDHNEVYTYIGSVVISINPYRPLPIYTPEKVEEYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITGESGAG 117
Cdd:cd01381      6 NLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISGESGAG 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  118 KTEASKFVMSYVAAVCGKGAEVNQvkeQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGGVISNYLLEKS 197
Cdd:cd01381     86 KTESTKLILQYLAAISGQHSWIEQ---QILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIEGAKIEQYLLEKS 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  198 RVVKQPRGERNFHIFYQILSGASEDFLCKLKLErDFSRYNYL-GLDSAKVNGVDDAANFRTVRNAMQIVGFMDHETQSVF 276
Cdd:cd01381    163 RIVSQAPDERNYHIFYCMLAGLSAEEKKKLELG-DASDYYYLtQGNCLTCEGRDDAAEFADIRSAMKVLMFTDEEIWDIF 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  277 EVVAAVLKLGNIEFKpESRVNGLDESKIKDKNELKEICELTGIDQSVLERAFSFRTVEAKQEKVSTTLNVAQAYYARDAL 356
Cdd:cd01381    242 KLLAAILHLGNIKFE-ATVVDNLDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSPLSAEQALDVRDAF 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  357 AKNLYSRLFSWLVTRINESI---KAQTKVRKKVmGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKEEQEEYIR 433
Cdd:cd01381    321 VKGIYGRLFIWIVNKINSAIykpRGTDSSRTSI-GVLDIFGFENFEVNSFEQLCINFANENLQQFFVRHIFKLEQEEYDK 399
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  434 EGIEWTHIEYFNNAIICDLIENNQTGILAMLDEECLRP-GtvTDDTFLEKLNQVCATHQHFESRMSKcsrflNDTTlphs 512
Cdd:cd01381    400 EGINWQHIEFVDNQDVLDLIALKPMNIMSLIDEESKFPkG--TDQTMLEKLHSTHGNNKNYLKPKSD-----LNTS---- 468
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  513 cFRIQHYAGKVMYQVEGFVDKNNDLLYRDLSQAMWKASHSLIKALF-PEGNPAKINLKRPPTAGSQFKASVATLMKNLQT 591
Cdd:cd01381    469 -FGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFnEDISMGSETRKKSPTLSSQFRKSLDQLMKTLSA 547
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  592 KNPNYIRCIKPNDKKAAHIFNDALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKMLCKQTWPHWRGPARAGVEVL 671
Cdd:cd01381    548 CQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVLVPGIPPAHKTDCRAATRKI 627
                          650       660
                   ....*....|....*....|.
gi 2024511160  672 FNELEIPEEEFSFGRSKIFIR 692
Cdd:cd01381    628 CCAVLGGDADYQLGKTKIFLK 648
MYSc_Myo11 cd01384
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ...
38-692 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: 637.41  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160   38 NLKKRFDHNEVYTYIGSVVISINPYRPLP-IYTPEKVEEYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITGESGA 116
Cdd:cd01384      6 NLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVSGESGA 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  117 GKTEASKFVMSYVAAVCGKGA-EVNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGGVISNYLLE 195
Cdd:cd01384     86 GKTETTKMLMQYLAYMGGRAVtEGRSVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAGRISGAAIRTYLLE 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  196 KSRVVKQPRGERNFHIFYQILSGASEDFLCKLKLErDFSRYNYLGL-DSAKVNGVDDAANFRTVRNAMQIVGFMDHETQS 274
Cdd:cd01384    166 RSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLK-DPKQFHYLNQsKCFELDGVDDAEEYRATRRAMDVVGISEEEQDA 244
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  275 VFEVVAAVLKLGNIEFKPESRVnglDESKIKD---KNELKEICELTGIDQSVLERAFSFRTVEAKQEKVSTTLNVAQAYY 351
Cdd:cd01384    245 IFRVVAAILHLGNIEFSKGEED---DSSVPKDeksEFHLKAAAELLMCDEKALEDALCKRVIVTPDGIITKPLDPDAATL 321
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  352 ARDALAKNLYSRLFSWLVTRINESIkAQTKVRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKEEQEEY 431
Cdd:cd01384    322 SRDALAKTIYSRLFDWLVDKINRSI-GQDPNSKRLIGVLDIYGFESFKTNSFEQFCINLANEKLQQHFNQHVFKMEQEEY 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  432 IREGIEWTHIEYFNNAIICDLIENNQTGILAMLDEECLRPgTVTDDTFLEKLNQVCATHQHFESrmSKCSRflndttlph 511
Cdd:cd01384    401 TKEEIDWSYIEFVDNQDVLDLIEKKPGGIIALLDEACMFP-RSTHETFAQKLYQTLKDHKRFSK--PKLSR--------- 468
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  512 SCFRIQHYAGKVMYQVEGFVDKNNDLLYRDlSQAMWKAS-HSLIKALFPEGNPAKINLKRPPTA-GSQFKASVATLMKNL 589
Cdd:cd01384    469 TDFTIDHYAGDVTYQTDLFLDKNKDYVVAE-HQALLNASkCPFVAGLFPPLPREGTSSSSKFSSiGSRFKQQLQELMETL 547
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  590 QTKNPNYIRCIKPNDKKAAHIFNDALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKMLCKQTwPHWRGPARAGVE 669
Cdd:cd01384    548 NTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGLLAPEV-LKGSDDEKAACK 626
                          650       660
                   ....*....|....*....|...
gi 2024511160  670 VLFNELEIpeEEFSFGRSKIFIR 692
Cdd:cd01384    627 KILEKAGL--KGYQIGKTKVFLR 647
MYSc_Myo22 cd14883
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ...
38-692 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: 628.97  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160   38 NLKKRFDHNEVYTYIGSVVISINPYRPLPIYTPEKVEEYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITGESGAG 117
Cdd:cd14883      6 NLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGESGAG 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  118 KTEASKFVMSYVAAVCGKGAEVNQvkeQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGGVISNYLLEKS 197
Cdd:cd14883     86 KTETTKLILQYLCAVTNNHSWVEQ---QILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGHIKGAIIQDYLLEQS 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  198 RVVKQPRGERNFHIFYQILSGASED--FLCKLKLeRDFSRYNYLGLD-SAKVNGVDDAANFRTVRNAMQIVGFMDHETQS 274
Cdd:cd14883    163 RITFQAPGERNYHVFYQLLAGAKHSkeLKEKLKL-GEPEDYHYLNQSgCIRIDNINDKKDFDHLRLAMNVLGIPEEMQEG 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  275 VFEVVAAVLKLGNIEFKpesrvnGLDESKI----KDKNELKEICELTGIDQSVLERAFSFRTVEAKQEKVSTTLNVAQAY 350
Cdd:cd14883    242 IFSVLSAILHLGNLTFE------DIDGETGaltvEDKEILKIVAKLLGVDPDKLKKALTIRQINVRGNVTEIPLKVQEAR 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  351 YARDALAKNLYSRLFSWLVTRINESIKAQTKvRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKEEQEE 430
Cdd:cd14883    316 DNRDAMAKALYSRTFAWLVNHINSCTNPGQK-NSRFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHYVFKLEQEE 394
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  431 YIREGIEWTHIEYFNNAIICDLIENNQTGILAMLDEECLRPgTVTDDTFLEKLNQVCATHQHFEsrmsKCSRFLNDTTlp 510
Cdd:cd14883    395 YEKEGINWSHIVFTDNQECLDLIEKPPLGILKLLDEECRFP-KGTDLTYLEKLHAAHEKHPYYE----KPDRRRWKTE-- 467
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  511 hscFRIQHYAGKVMYQVEGFVDKNNDLLYRDLSQAMWKASHSLIKALF-PEGNPAKINL--------------KRPPTAG 575
Cdd:cd14883    468 ---FGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFtYPDLLALTGLsislggdttsrgtsKGKPTVG 544
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  576 SQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNDALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKMLCKQ 655
Cdd:cd14883    545 DTFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCLDPR 624
                          650       660       670
                   ....*....|....*....|....*....|....*..
gi 2024511160  656 TWPHWRGPARAGVEVLFNELEIPEEEFSFGRSKIFIR 692
Cdd:cd14883    625 ARSADHKETCGAVRALMGLGGLPEDEWQVGKTKVFLR 661
MYSc_Myo8 cd01383
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ...
34-692 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: 618.56  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160   34 SFINNLKKRFDHNEVYTYIGSVVISINPYRPLPIYTPEKVEEYRNRNfyELSPHIFALSDEAYRSLRDQDKDQCILITGE 113
Cdd:cd01383      2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYRQKL--LDSPHVYAVADTAYREMMRDEINQSIIISGE 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  114 SGAGKTEASKFVMSYVAAVCGKGaevNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGGVISNYL 193
Cdd:cd01383     80 SGAGKTETAKIAMQYLAALGGGS---SGIENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKICGAKIQTYL 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  194 LEKSRVVKQPRGERNFHIFYQILSGASEDFLCKLKLeRDFSRYNYL-GLDSAKVNGVDDAANFRTVRNAMQIVGFMDHET 272
Cdd:cd01383    157 LEKSRVVQLANGERSYHIFYQLCAGASPALREKLNL-KSASEYKYLnQSNCLTIDGVDDAKKFHELKEALDTVGISKEDQ 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  273 QSVFEVVAAVLKLGNIEFkpeSRVNGLDESKIKDKNELKEICELTGIDQSVLERAFSFRTVEAKQEKVSTTLNVAQAYYA 352
Cdd:cd01383    236 EHIFQMLAAVLWLGNISF---QVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKLTLQQAIDA 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  353 RDALAKNLYSRLFSWLVTRINESIKAQTKVRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKEEQEEYI 432
Cdd:cd01383    313 RDALAKAIYASLFDWLVEQINKSLEVGKRRTGRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLFKLEQEEYE 392
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  433 REGIEWTHIEYFNNAIICDLIENNQTGILAMLDEECLRPGTvTDDTFLEKLNQVCATHQHFESRmskcsrflNDTTlphs 512
Cdd:cd01383    393 LDGIDWTKVDFEDNQECLDLIEKKPLGLISLLDEESNFPKA-TDLTFANKLKQHLKSNSCFKGE--------RGGA---- 459
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  513 cFRIQHYAGKVMYQVEGFVDKNNDLLYRDLSQAMWKASHSLIKAL---FPEGNPAKINLKRPPTAGSQfKASVAT----- 584
Cdd:cd01383    460 -FTIRHYAGEVTYDTSGFLEKNRDLLHSDLIQLLSSCSCQLPQLFaskMLDASRKALPLTKASGSDSQ-KQSVATkfkgq 537
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  585 ---LMKNLQTKNPNYIRCIKPNDKKAAHIFNDALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKMLCKQTWPHWR 661
Cdd:cd01383    538 lfkLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLPEDVSASQ 617
                          650       660       670
                   ....*....|....*....|....*....|...
gi 2024511160  662 GPARAGVEVL--FNeleIPEEEFSFGRSKIFIR 692
Cdd:cd01383    618 DPLSTSVAILqqFN---ILPEMYQVGYTKLFFR 647
MYSc_Myo4 cd14872
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ...
34-654 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: 615.63  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160   34 SFINNLKKRFDHNEVYTYIGSVVISINPYRPLPIYTPEKVEEYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITGE 113
Cdd:cd14872      2 MIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISGE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  114 SGAGKTEASKFVMSYVAAVCGkgaEVNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGGVISNYL 193
Cdd:cd14872     82 SGAGKTEATKQCLSFFAEVAG---STNGVEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRICGASTENYL 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  194 LEKSRVVKQPRGERNFHIFYQILSGASedfLCKLKLERDFSRYNYLGLDSA-KVNGVDDAANFRTVRNAMQIVGFMDHET 272
Cdd:cd14872    159 LEKSRVVYQIKGERNFHIFYQLLASPD---PASRGGWGSSAAYGYLSLSGCiEVEGVDDVADFEEVVLAMEQLGFDDADI 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  273 QSVFEVVAAVLKLGNIEFKPESRVNGLDESKIKDKNELKEICELTGIDQSVLERAFSFRTVEAK-QEKVSTTLNVAQAYY 351
Cdd:cd14872    236 NNVMSLIAAILKLGNIEFASGGGKSLVSGSTVANRDVLKEVATLLGVDAATLEEALTSRLMEIKgCDPTRIPLTPAQATD 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  352 ARDALAKNLYSRLFSWLVTRINESIKAQTKVRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKEEQEEY 431
Cdd:cd14872    316 ACDALAKAAYSRLFDWLVKKINESMRPQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEKLQQHFNQYTFKLEEALY 395
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  432 IREGIEWTHIEYFNNAIICDLIENNQTGILAMLDEECLRPGTvTDDTFLEKLNQVCATHQHFESRMSKCSRFLndttlph 511
Cdd:cd14872    396 QSEGVKFEHIDFIDNQPVLDLIEKKQPGLMLALDDQVKIPKG-SDATFMIAANQTHAAKSTFVYAEVRTSRTE------- 467
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  512 scFRIQHYAGKVMYQVEGFVDKNNDLLYRDLSQAMWKASHSLIKALFPEGNPAKINLKrpPTAGSQFKASVATLMKNLQT 591
Cdd:cd14872    468 --FIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLFPPSEGDQKTSK--VTLGGQFRKQLSALMTALNA 543
                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024511160  592 KNPNYIRCIKPNDKKAAHIFNDALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKMLCK 654
Cdd:cd14872    544 TEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKRYRFLVK 606
MYSc_Myo29 cd14890
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ...
34-692 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: 560.93  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160   34 SFINNLKKRFDHNEVYTYIGSVVISINPYRPLP-IYTPEKVEEYRNRNFYELSPHIFALSDEAYRSLRDQD----KDQCI 108
Cdd:cd14890      2 SLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQSGvldpSNQSI 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  109 LITGESGAGKTEASKFVMSYVAAVCGK----------------GAEVNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGK 172
Cdd:cd14890     82 IISGESGAGKTEATKIIMQYLARITSGfaqgasgegeaaseaiEQTLGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFGK 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  173 YMDIEFDFKGDPLGGVISNYLLEKSRVVKQPRGERNFHIFYQILSGASEDFLCKLKLERDfSRYNYLGLDSAKVNGVDDA 252
Cdd:cd14890    162 FIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTP-VEYFYLRGECSSIPSCDDA 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  253 ANFRTVRNAMQIVGFMDHETQSVFEVVAAVLKLGNIEFKPESRVNGLdeSKIKDKNELKEICELTGIDQSVLERAFSFRT 332
Cdd:cd14890    241 KAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTVL--EDATTLQSLKLAAELLGVNEDALEKALLTRQ 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  333 VEAKQEKVSTTLNVAQAYYARDALAKNLYSRLFSWLVTRINESIkAQTKVRKKVMGVLDIYGFEIFEDNSFEQFIINYCN 412
Cdd:cd14890    319 LFVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTI-SSPDDKWGFIGVLDIYGFEKFEWNTFEQLCINYAN 397
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  413 EKLQQIFIELTLKEEQEEYIREGIEWTHIEYFNNAIICDLIE---NNQTGILAMLDEECLRPGTVTDDTFLEKLnqvcat 489
Cdd:cd14890    398 EKLQRHFNQHMFEVEQVEYSNEGIDWQYITFNDNQACLELIEgkvNGKPGIFITLDDCWRFKGEEANKKFVSQL------ 471
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  490 HQHF--ESRMSKCSR-------FLNDTTLPHSCFRIQHYAGKVMYQVEGFVDKNNDLLYRDLSQAMWKASHSLikalfpe 560
Cdd:cd14890    472 HASFgrKSGSGGTRRgssqhphFVHPKFDADKQFGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSRRSI------- 544
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  561 gnpakinlkRPPTAGSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNDALVCHQIRYLGLLENVRVRRAGYAFRQ 640
Cdd:cd14890    545 ---------REVSVGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGMMEAIQIRQQGFALRE 615
                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2024511160  641 AYEPCLERYKMLCKQtwphwrgpARAG---VEVLFNELEIPEEEFSFGRSKIFIR 692
Cdd:cd14890    616 EHDSFFYDFQVLLPT--------AENIeqlVAVLSKMLGLGKADWQIGSSKIFLK 662
MYSc_Myo15 cd01387
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ...
34-692 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: 557.06  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160   34 SFINNLKKRFDHNEVYTYIGSVVISINPYRPLPIYTPEKVEEYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITGE 113
Cdd:cd01387      2 TVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISGE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  114 SGAGKTEASKFVMSYVAAVCGKGAevNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDfKGDPLGGVISNYL 193
Cdd:cd01387     82 SGSGKTEATKLIMQYLAAVNQRRN--NLVTEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFFE-GGVIVGAITSQYL 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  194 LEKSRVVKQPRGERNFHIFYQILSGASEDFLCKLKLErDFSRYNYLGLD-SAKVNGVDDAANFRTVRNAMQIVGFMDHET 272
Cdd:cd01387    159 LEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQ-EAEKYFYLNQGgNCEIAGKSDADDFRRLLAAMQVLGFSSEEQ 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  273 QSVFEVVAAVLKLGNIEFKPESRVNGLDESKIKDKNELKEICELTGIDQSVLERAFSFRTVEAKQEKVSTTLNVAQAYYA 352
Cdd:cd01387    238 DSIFRILASVLHLGNVYFHKRQLRHGQEGVSVGSDAEIQWVAHLLQISPEGLQKALTFKVTETRRERIFTPLTIDQALDA 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  353 RDALAKNLYSRLFSWLVTRINESIKAQTKvRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKEEQEEYI 432
Cdd:cd01387    318 RDAIAKALYALLFSWLVTRVNAIVYSGTQ-DTLSIAILDIFGFEDLSENSFEQLCINYANENLQYYFNKHVFKLEQEEYI 396
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  433 REGIEWTHIEYFNNAIICDLIENNQTGILAMLDEECLRPgTVTDDTFLEKlnqvCATHQHFESRMSKcsrflndTTLPHS 512
Cdd:cd01387    397 REQIDWTEIAFADNQPVINLISKKPVGILHILDDECNFP-QATDHSFLEK----CHYHHALNELYSK-------PRMPLP 464
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  513 CFRIQHYAGKVMYQVEGFVDKNNDLLYRDLSQAMWKASHSLIKALFPE------------GNPAKINLK-RPPTAGSQFK 579
Cdd:cd01387    465 EFTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSShraqtdkapprlGKGRFVTMKpRTPTVAARFQ 544
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  580 ASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNDALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKMLCKQtwPH 659
Cdd:cd01387    545 DSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYRCLVAL--KL 622
                          650       660       670
                   ....*....|....*....|....*....|....*
gi 2024511160  660 WRG-PARAGVEVLFNELE-IPEEEFSFGRSKIFIR 692
Cdd:cd01387    623 PRPaPGDMCVSLLSRLCTvTPKDMYRLGATKVFLR 657
MYSc_Myo6 cd01382
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ...
34-692 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: 552.24  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160   34 SFINNLKKRFDHNEVYTYIGSVVISINPYRPLP-IYTPEKVEEYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITG 112
Cdd:cd01382      2 TLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVSG 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  113 ESGAGKTEASKFVMSYVAAVCGKGAevNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGGVISNY 192
Cdd:cd01382     82 ESGAGKTESTKYILRYLTESWGSGA--GPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVGGFVSHY 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  193 LLEKSRVVKQPRGERNFHIFYQILSGASEDFlcKLKLERDFSrynylgldsakvngVDDAANFRTVRNAMQIVGFMDHET 272
Cdd:cd01382    160 LLEKSRICVQSKEERNYHIFYRLCAGAPEDL--REKLLKDPL--------------LDDVGDFIRMDKAMKKIGLSDEEK 223
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  273 QSVFEVVAAVLKLGNIEFKpESRVNGLDESKIKDKNE--LKEICELTGIDQSVLERAFSFRTVEAKQEKVSTT-----LN 345
Cdd:cd01382    224 LDIFRVVAAVLHLGNIEFE-ENGSDSGGGCNVKPKSEqsLEYAAELLGLDQDELRVSLTTRVMQTTRGGAKGTvikvpLK 302
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  346 VAQAYYARDALAKNLYSRLFSWLVTRINESIKAQTKVrkKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLK 425
Cdd:cd01382    303 VEEANNARDALAKAIYSKLFDHIVNRINQCIPFETSS--YFIGVLDIAGFEYFEVNSFEQFCINYCNEKLQQFFNERILK 380
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  426 EEQEEYIREGIEWTHIEYFNNAIICDLIENNQTGILAMLDEECLRPgTVTDDTFLEKLNQVCATHQHFES-RMSKCS--R 502
Cdd:cd01382    381 EEQELYEKEGLGVKEVEYVDNQDCIDLIEAKLVGILDLLDEESKLP-KPSDQHFTSAVHQKHKNHFRLSIpRKSKLKihR 459
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  503 FLNDttlpHSCFRIQHYAGKVMYQVEGFVDKNNDLLYRDLSQAMWKASHSLIKALFPEGNPA---------KINLKrppT 573
Cdd:cd01382    460 NLRD----DEGFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFESSTNNnkdskqkagKLSFI---S 532
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  574 AGSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNDALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYkmlc 653
Cdd:cd01382    533 VGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRTSFHDLYNMY---- 608
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|.
gi 2024511160  654 KQTWPH--WRGPARAGVEVLFNELEIPEEEFSFGRSKIFIR 692
Cdd:cd01382    609 KKYLPPklARLDPRLFCKALFKALGLNENDFKFGLTKVFFR 649
MYSc_Myo40 cd14901
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ...
34-691 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: 545.92  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160   34 SFINNLKKRFDHNEVYTYIGSVVISINPYRPLPIYTPEKVEEY------RNRNFYELSPHIFALSDEAYRSL----RDQD 103
Cdd:cd14901      2 SILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMlfasRGQK 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  104 KDQCILITGESGAGKTEASKFVMSYVAAVC------GKGAEVNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIE 177
Cdd:cd14901     82 CDQSILVSGESGAGKTETTKIIMNYLASVSsatthgQNATERENVRDRVLESNPILEAFGNARTNRNNNSSRFGKFIRLG 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  178 FDFKGDPLGGVISNYLLEKSRVVKQPRGERNFHIFYQILSGASEDFLCKLKLErDFSRYNYL----GLDsaKVNGVDDAA 253
Cdd:cd14901    162 FASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLT-HVEEYKYLnssqCYD--RRDGVDDSV 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  254 NFRTVRNAMQIVGFMDHETQSVFEVVAAVLKLGNIEFKPESRVNGldESKIKDKNELKEICELTGIDQSVLERAFSFRTV 333
Cdd:cd14901    239 QYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFVKKDGEGG--TFSMSSLANVRAACDLLGLDMDVLEKTLCTREI 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  334 EAKQEKVSTTLNVAQAYYARDALAKNLYSRLFSWLVTRINESIK-AQTKVRKKVMGVLDIYGFEIFEDNSFEQFIINYCN 412
Cdd:cd14901    317 RAGGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAySESTGASRFIGIVDIFGFEIFATNSLEQLCINFAN 396
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  413 EKLQQIFIELTLKEEQEEYIREGIEWTHIEYFNNAIICDLIENNQTGILAMLDEECLRPGTvTDDTFLEKLNQVCATHQH 492
Cdd:cd14901    397 EKLQQLFGKFVFEMEQDEYVAEAIPWTFVEYPNNDACVAMFEARPTGLFSLLDEQCLLPRG-NDEKLANKYYDLLAKHAS 475
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  493 FESrmSKCSRFLNdttlphsCFRIQHYAGKVMYQVEGFVDKNNDLLYRDLSQAMWKASHSLIkalfpegnpakinlkrPP 572
Cdd:cd14901    476 FSV--SKLQQGKR-------QFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFL----------------SS 530
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  573 TAGSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNDALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKML 652
Cdd:cd14901    531 TVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFPHDAFVHTYSCL 610
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*
gi 2024511160  653 CKQTwPHWRGPARAGVEVLFNELEIPE------EEFSFGRSKIFI 691
Cdd:cd14901    611 APDG-ASDTWKVNELAERLMSQLQHSElniehlPPFQVGKTKVFL 654
MYSc_Myo36 cd14897
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ...
36-692 1.55e-180

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: 541.97  E-value: 1.55e-180
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160   36 INNLKKRFDHNEVYTYIGSVVISINPYRPLPIYTPEKVEEYRNRNF-YELSPHIFALSDEAYRSLRDQDKDQCILITGES 114
Cdd:cd14897      4 VQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSVrSQRPPHLFWIADQAYRRLLETGRNQCILVSGES 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  115 GAGKTEASKFVMSYVAAVCGKgaEVNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGGVISNYLL 194
Cdd:cd14897     84 GAGKTESTKYMIKHLMKLSPS--DDSDLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQLLGAKIDDYLL 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  195 EKSRVVKQPRGERNFHIFYQILSGASEDFLCKLKLErDFSRYNYLGLDSAKVNGVDDA-------ANFRTVRNAMQIVGF 267
Cdd:cd14897    162 EKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLE-DPDCHRILRDDNRNRPVFNDSeeleyyrQMFHDLTNIMKLIGF 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  268 MDHETQSVFEVVAAVLKLGNIEFKPESRVNGLdesKIKDKNELKEICELTGIDQSVLERAFSFRTVEAKQEKVSTTLNVA 347
Cdd:cd14897    241 SEEDISVIFTILAAILHLTNIVFIPDEDTDGV---TVADEYPLHAVAKLLGIDEVELTEALISNVNTIRGERIQSWKSLR 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  348 QAYYARDALAKNLYSRLFSWLVTRINESIKAQTKVRKKV----MGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELT 423
Cdd:cd14897    318 QANDSRDALAKDLYSRLFGWIVGQINRNLWPDKDFQIMTrgpsIGILDMSGFENFKINSFDQLCINLSNERLQQYFNDYV 397
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  424 LKEEQEEYIREGIEWTHIEYFNNAIICDLIENNQTGILAMLDEECLRPGTvTDDTFLEKLNQVCATHQHFESRMSKcsrf 503
Cdd:cd14897    398 FPRERSEYEIEGIEWRDIEYHDNDDVLELFFKKPLGILPLLDEESTFPQS-TDSSLVQKLNKYCGESPRYVASPGN---- 472
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  504 lndttlpHSCFRIQHYAGKVMYQVEGFVDKNNDLLYRDLSQAMWKASHSLIKALFPegnpakinlkrpptagSQFKASVA 583
Cdd:cd14897    473 -------RVAFGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLFT----------------SYFKRSLS 529
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  584 TLMKNLQTKNPNYIRCIKPNDKKAAHIFNDALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKMLCKQTWPHWRGP 663
Cdd:cd14897    530 DLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYEDFVKRYKEICDFSNKVRSDD 609
                          650       660
                   ....*....|....*....|....*....
gi 2024511160  664 ARAGVEVLFNELeipEEEFSFGRSKIFIR 692
Cdd:cd14897    610 LGKCQKILKTAG---IKGYQFGKTKVFLK 635
MYSc_Myo9 cd01385
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ...
34-692 1.11e-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: 541.97  E-value: 1.11e-179
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160   34 SFINNLKKRFDHNEVYTYIGSVVISINPYRPLPIYTPEKVEEYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITGE 113
Cdd:cd01385      2 TLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISGE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  114 SGAGKTEASKFVMSYVAAVCGKGAEVNqVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGGVISNYL 193
Cdd:cd01385     82 SGSGKTESTNFLLHHLTALSQKGYGSG-VEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRGAVVEKYL 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  194 LEKSRVVKQPRGERNFHIFYQILSGASEDFLCKLKLERDfSRYNYLG-LDSAKVNGVDDAANFRTVRNAMQIVGFMDHET 272
Cdd:cd01385    161 LEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQP-EDYHYLNqSDCYTLEGEDEKYEFERLKQAMEMVGFLPETQ 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  273 QSVFEVVAAVLKLGNIEFKPEsRVNGLDESKIKDKNELKEICELTGIDQSVLERAFSFRTVEAKQEKVSTTLNVAQAYYA 352
Cdd:cd01385    240 RQIFSVLSAVLHLGNIEYKKK-AYHRDESVTVGNPEVLDIISELLRVKEETLLEALTTKKTVTVGETLILPYKLPEAIAT 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  353 RDALAKNLYSRLFSWLVTRINE---SIKAQTKVRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKEEQE 429
Cdd:cd01385    319 RDAMAKCLYSALFDWIVLRINHallNKKDLEEAKGLSIGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQHIFKLEQE 398
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  430 EYIREGIEWTHIEYFNNAIICDLIENNQTGILAMLDEECLRPGTvTDDTFLEKLNQVCATHQHFESrmskcsrflndTTL 509
Cdd:cd01385    399 EYKKEGISWHNIEYTDNTGCLQLISKKPTGLLCLLDEESNFPGA-TNQTLLAKFKQQHKDNKYYEK-----------PQV 466
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  510 PHSCFRIQHYAGKVMYQVEGFVDKNNDLLYRDLSQAMWKASHSLIKAL-----------------------FPE------ 560
Cdd:cd01385    467 MEPAFIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVRELigidpvavfrwavlrafframaaFREagrrra 546
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  561 ---GNPAKINL-------------KRPPTAGSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNDALVCHQIRYLG 624
Cdd:cd01385    547 qrtAGHSLTLHdrttksllhlhkkKKPPSVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVLRQLRYTG 626
                          650       660       670       680       690       700
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024511160  625 LLENVRVRRAGYAFRQAYEPCLERYKMLCkqtwPHWRGPARAGVEVLFNELEIPEEEFSFGRSKIFIR 692
Cdd:cd01385    627 MLETVRIRRSGYSVRYTFQEFITQFQVLL----PKGLISSKEDIKDFLEKLNLDRDNYQIGKTKVFLK 690
MYSc_Myo42 cd14903
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ...
38-692 1.73e-176

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: 532.43  E-value: 1.73e-176
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160   38 NLKKRFDHNEVYTYIGSVVISINPYRPLP-IYTPEKVEEYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITGESGA 116
Cdd:cd14903      6 NVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVSGESGA 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  117 GKTEASKFVMSYVAAVCGkGAEvNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGGVISNYLLEK 196
Cdd:cd14903     86 GKTETTKILMNHLATIAG-GLN-DSTIKKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKNGTLVGAKCRTYLLEK 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  197 SRVVKQPRGERNFHIFYQILsgASEDFLCKLKLERDfSRYNYLG-LDSAKVNGVDDAANFRTVRNAMQIVGFMDHETQSV 275
Cdd:cd14903    164 TRVISHERPERNYHIFYQLL--ASPDVEERLFLDSA-NECAYTGaNKTIKIEGMSDRKHFARTKEALSLIGVSEEKQEVL 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  276 FEVVAAVLKLGNIEFKPEsrvNGLDESKI--KDKNELKEICELTGIDQSVLERAFSFRTVEAKQEKVSTTLNVAQAYYAR 353
Cdd:cd14903    241 FEVLAGILHLGQLQIQSK---PNDDEKSAiaPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDVYTVPLKKDQAEDCR 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  354 DALAKNLYSRLFSWLVTRINESIKAQTKVRKKVmGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKEEQEEYIR 433
Cdd:cd14903    318 DALAKAIYSNVFDWLVATINASLGNDAKMANHI-GVLDIFGFEHFKHNSFEQFCINYANEKLQQKFTQDVFKTVQIEYEE 396
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  434 EGIEWTHIEYFNNAIICDLIEnNQTGILAMLDEECLRPGTvTDDTFLEKLNQVCATHQHFeSRMSKCSRFLndttlphsc 513
Cdd:cd14903    397 EGIRWAHIDFADNQDVLAVIE-DRLGIISLLNDEVMRPKG-NEESFVSKLSSIHKDEQDV-IEFPRTSRTQ--------- 464
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  514 FRIQHYAGKVMYQVEGFVDKNNDLLYRDLSQAMWKASHSLIKALFPEG----NPAKINLKRP-----------PTAGSQF 578
Cdd:cd14903    465 FTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKEKvespAAASTSLARGarrrrggalttTTVGTQF 544
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  579 KASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNDALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKMLCKQTwP 658
Cdd:cd14903    545 KDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWLFLPEG-R 623
                          650       660       670
                   ....*....|....*....|....*....|....*.
gi 2024511160  659 HWRGPARAGVEVLFN--ELEIPeEEFSFGRSKIFIR 692
Cdd:cd14903    624 NTDVPVAERCEALMKklKLESP-EQYQMGLTRIYFQ 658
MYSc_Myo10 cd14873
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ...
34-692 3.73e-176

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: 531.29  E-value: 3.73e-176
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160   34 SFINNLKKRFDHNEVYTYIGSVVISINPYRPLP-IYTPEKVEEYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITG 112
Cdd:cd14873      2 SIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILISG 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  113 ESGAGKTEASKF------VMSYVAAVCGKGAEVNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLG 186
Cdd:cd14873     82 ESGAGKTESTKLilkflsVISQQSLELSLKEKTSCVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNIQG 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  187 GVISNYLLEKSRVVKQPRGERNFHIFYQILSGASEDFLCKLKLErDFSRYNYL---GLDSAKvnGVDDAANFRTVRNAMQ 263
Cdd:cd14873    162 GRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLS-TPENYHYLnqsGCVEDK--TISDQESFREVITAME 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  264 IVGFMDHETQSVFEVVAAVLKLGNIEFKPESrvngldESKIKDKNELKEICELTGIDQSVLERAFSFRTVEAKQEKVSTT 343
Cdd:cd14873    239 VMQFSKEEVREVSRLLAGILHLGNIEFITAG------GAQVSFKTALGRSAELLGLDPTQLTDALTQRSMFLRGEEILTP 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  344 LNVAQAYYARDALAKNLYSRLFSWLVTRINESIKAQTKVrkKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELT 423
Cdd:cd14873    313 LNVQQAVDSRDSLAMALYARCFEWVIKKINSRIKGKEDF--KSIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKHI 390
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  424 LKEEQEEYIREGIEWTHIEYFNNAIICDLIEnNQTGILAMLDEECLRPgTVTDDTFLEKLNQVCATHQHF-ESRMSKcsr 502
Cdd:cd14873    391 FSLEQLEYSREGLVWEDIDWIDNGECLDLIE-KKLGLLALINEESHFP-QATDSTLLEKLHSQHANNHFYvKPRVAV--- 465
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  503 flndttlphSCFRIQHYAGKVMYQVEGFVDKNNDLLYRDLSQAMWKASHSLIKALFP-------EGNPAKINLKRPPTAG 575
Cdd:cd14873    466 ---------NNFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEhvssrnnQDTLKCGSKHRRPTVS 536
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  576 SQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNDALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKMLCKQ 655
Cdd:cd14873    537 SQFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMRN 616
                          650       660       670
                   ....*....|....*....|....*....|....*..
gi 2024511160  656 TwpHWRGPARAGVEVLFNELEIPEEEFSFGRSKIFIR 692
Cdd:cd14873    617 L--ALPEDVRGKCTSLLQLYDASNSEWQLGKTKVFLR 651
MYSc_Myh10 cd14920
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ...
34-692 1.16e-170

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: 518.03  E-value: 1.16e-170
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160   34 SFINNLKKRFDHNEVYTYIGSVVISINPYRPLPIYTPEKVEEYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITGE 113
Cdd:cd14920      2 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  114 SGAGKTEASKFVMSYVAAVCGK------GAEVNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGG 187
Cdd:cd14920     82 SGAGKTENTKKVIQYLAHVASShkgrkdHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGA 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  188 VISNYLLEKSRVVKQPRGERNFHIFYQILSGASEDFLCKLKLErDFSRYNYLGLDSAKVNGVDDAANFRTVRNAMQIVGF 267
Cdd:cd14920    162 NIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLE-GFNNYRFLSNGYIPIPGQQDKDNFQETMEAMHIMGF 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  268 MDHETQSVFEVVAAVLKLGNIEFKPESRVnglDESKIKDKNELKEICELTGIDQSVLERAFSFRTVEAKQEKVSTTLNVA 347
Cdd:cd14920    241 SHEEILSMLKVVSSVLQFGNISFKKERNT---DQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKE 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  348 QAYYARDALAKNLYSRLFSWLVTRINESIKAQTKVRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKEE 427
Cdd:cd14920    318 QADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILE 397
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  428 QEEYIREGIEWTHIEYFNNAIIC-DLIEN--NQTGILAMLDEECLRPgTVTDDTFLEKLNQVCATHQHFESrmskcSRFL 504
Cdd:cd14920    398 QEEYQREGIEWNFIDFGLDLQPCiDLIERpaNPPGVLALLDEECWFP-KATDKTFVEKLVQEQGSHSKFQK-----PRQL 471
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  505 NDttlpHSCFRIQHYAGKVMYQVEGFVDKNNDLLYRDLSQAMWKASHSLIKALFPE------------------GNPAKI 566
Cdd:cd14920    472 KD----KADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDvdrivgldqvtgmtetafGSAYKT 547
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  567 NLKRPPTAGSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNDALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCL 646
Cdd:cd14920    548 KKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFR 627
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*.
gi 2024511160  647 ERYKMLCKQTWPHWRGPARAGVEVLFNELEIPEEEFSFGRSKIFIR 692
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 ...
33-653 2.57e-169

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: 512.98  E-value: 2.57e-169
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160   33 DSFINNLKKRFDHNEVYTYIGSVVISINPYRPLPIYTPEKVEEYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITG 112
Cdd:cd01379      1 DTIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  113 ESGAGKTEASKFVMSYVAAVcGKGAEVNqVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGGVISNY 192
Cdd:cd01379     81 ESGAGKTESANLLVQQLTVL-GKANNRT-LEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAVTGARISEY 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  193 LLEKSRVVKQPRGERNFHIFYQILSG-ASEDFLCKLKLErDFSRYNYLGLDSAKV-NGVDDAAN---FRTVRNAMQIVGF 267
Cdd:cd01379    159 LLEKSRVVHQAIGERNFHIFYYIYAGlAEDKKLAKYKLP-ENKPPRYLQNDGLTVqDIVNNSGNrekFEEIEQCFKVIGF 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  268 MDHETQSVFEVVAAVLKLGNIEFKP-ESRVNGLDESKIKDKNELKEICELTGIDQSVLERAFSFRTVEAKQEKVSTTLNV 346
Cdd:cd01379    238 TKEEVDSVYSILAAILHIGDIEFTEvESNHQTDKSSRISNPEALNNVAKLLGIEADELQEALTSHSVVTRGETIIRNNTV 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  347 AQAYYARDALAKNLYSRLFSWLVTRINESIKAQTKVRKKVM--GVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTL 424
Cdd:cd01379    318 EEATDARDAMAKALYGRLFSWIVNRINSLLKPDRSASDEPLsiGILDIFGFENFQKNSFEQLCINIANEQIQYYFNQHIF 397
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  425 KEEQEEYIREGIEWTHIEYFNNAIICDLIENNQTGILAMLDEECLRPGTvTDDTFLEKLnqvcatHQHFesrmsKCSRFL 504
Cdd:cd01379    398 AWEQQEYLNEGIDVDLIEYEDNRPLLDMFLQKPMGLLALLDEESRFPKA-TDQTLVEKF------HNNI-----KSKYYW 465
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  505 ndttLPHS---CFRIQHYAGKVMYQVEGFVDKNNDLLYRDLSQAMWKASHSLIKAlfpegnpakinlkrppTAGSQFKAS 581
Cdd:cd01379    466 ----RPKSnalSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVRQ----------------TVATYFRYS 525
                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024511160  582 VATLMKNLQTKNPNYIRCIKPNDKKAAHIFNDALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKMLC 653
Cdd:cd01379    526 LMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRILFADFLKRYYFLA 597
MYSc_Myo31 cd14892
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ...
36-692 5.72e-168

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: 510.07  E-value: 5.72e-168
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160   36 INNLKKRFDHNEVYTYIGSVVISINPYRPLP-IY-TPEKVEEYRNRNFYELS-PHIFALSDEAYRSLR----DQDKDQCI 108
Cdd:cd14892      4 LDVLRRRYERDAIYTFTADILISINPYKSIPlLYdVPGFDSQRKEEATASSPpPHVFSIAERAYRAMKgvgkGQGTPQSI 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  109 LITGESGAGKTEASKFVMSYVA--------AVCGKGAEV--NQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEF 178
Cdd:cd14892     84 VVSGESGAGKTEASKYIMKYLAtasklakgASTSKGAANahESIEECVLLSNLILEAFGNAKTIRNDNSSRFGKYIQIHY 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  179 DFKGDPLGGVISNYLLEKSRVVKQPRGERNFHIFYQILSGASEDFLCKLKLErDFSRYNYLGLDSA-KVNGVDDAANFRT 257
Cdd:cd14892    164 NSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELT-PAESFLFLNQGNCvEVDGVDDATEFKQ 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  258 VRNAMQIVGFMDHETQSVFEVVAAVLKLGNIEFKPESRVNGLDeSKIKDKNELKEICELTGIDQSVLERAFSFRT-VEAK 336
Cdd:cd14892    243 LRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEENADDEDVF-AQSADGVNVAKAAGLLGVDAAELMFKLVTQTtSTAR 321
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  337 QEKVSTTLNVAQAYYARDALAKNLYSRLFSWLVTRINESIKAQTKV---------RKKVMGVLDIYGFEIFEDNSFEQFI 407
Cdd:cd14892    322 GSVLEIKLTAREAKNALDALCKYLYGELFDWLISRINACHKQQTSGvtggaasptFSPFIGILDIFGFEIMPTNSFEQLC 401
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  408 INYCNEKLQQIFIELTLKEEQEEYIREGIEWTHIEYFNNAIICDLIENNQTGILAMLDEECLRPGTVTDDTFLEKLNQV- 486
Cdd:cd14892    402 INFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQDNQDCLDLIQKKPLGLLPLLEEQMLLKRKTTDKQLLTIYHQTh 481
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  487 CATHQHFESRmskcsRFLNDTtlphscFRIQHYAGKVMYQVEGFVDKNNDLLYRDLsqamwkashslikalfpegnpakI 566
Cdd:cd14892    482 LDKHPHYAKP-----RFECDE------FVLRHYAGDVTYDVHGFLAKNNDNLHDDL-----------------------R 527
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  567 NLKRpptAGSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNDALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCL 646
Cdd:cd14892    528 DLLR---SSSKFRTQLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVRIRREGFPIRRQFEEFY 604
                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2024511160  647 ERYKMLCKQ-----TWPHWRGPARAGVEVL-FNELEIPEEEFSFGRSKIFIR 692
Cdd:cd14892    605 EKFWPLARNkagvaASPDACDATTARKKCEeIVARALERENFQLGRTKVFLR 656
MYSc_Myo27 cd14888
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ...
34-652 6.25e-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: 505.38  E-value: 6.25e-166
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160   34 SFINNLKKRFDHNEVYTYIGSVVISINPYRPLP-IYTPEKVEEYRNRNfYELSPHIFALSDEAYRSLRDQDKDQCILITG 112
Cdd:cd14888      2 SILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFIQPS-ISKSPHVFSTASSAYQGMCNNKKSQTILISG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  113 ESGAGKTEASKFVMSYVAAVcGKGAEVN--QVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDF---------K 181
Cdd:cd14888     81 ESGAGKTESTKYVMKFLACA-GSEDIKKrsLVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFSKlkskrmsgdR 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  182 GDPLGGVISNYLLEKSRVVKQPRGERNFHIFYQILSGASE--------------------DFLCKLKLERDFSRYNYLGL 241
Cdd:cd14888    160 GRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAREakntglsyeendeklakgadAKPISIDMSSFEPHLKFRYL 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  242 DSAKV---NGVDDAANFRTVRNAMQIVGFMDHETQSVFEVVAAVLKLGNIEFK-PESRVNGLDESKIKDKNeLKEICELT 317
Cdd:cd14888    240 TKSSChelPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFEnNEACSEGAVVSASCTDD-LEKVASLL 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  318 GIDQSVLERAFSFRTVEAKQEKVSTTLNVAQAYYARDALAKNLYSRLFSWLVTRINESIKAQTKVRKKVMGVLDIYGFEI 397
Cdd:cd14888    319 GVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGYSKDNSLLFCGVLDIFGFEC 398
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  398 FEDNSFEQFIINYCNEKLQQIFIELTLKEEQEEYIREGIEWTHIEYFNNAIICDLIENNQTGILAMLDEECLRPGTvTDD 477
Cdd:cd14888    399 FQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFPDNQDCVDLLQEKPLGIFCMLDEECFVPGG-KDQ 477
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  478 TFLEKLNQVCATHQHFESRMSKcsrflndttlpHSCFRIQHYAGKVMYQVEGFVDKNNDLLYRDlSQAMWKAS-----HS 552
Cdd:cd14888    478 GLCNKLCQKHKGHKRFDVVKTD-----------PNSFVIVHFAGPVKYCSDGFLEKNKDQLSVD-AQEVIKNSknpfiSN 545
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  553 LIKALFPEGNPAKINLKRPPTAGSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNDALVCHQIRYLGLLENVRVR 632
Cdd:cd14888    546 LFSAYLRRGTDGNTKKKKFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQLKYGGVLQAVQVS 625
                          650       660
                   ....*....|....*....|
gi 2024511160  633 RAGYAFRQAYEPCLERYKML 652
Cdd:cd14888    626 RAGYPVRLSHAEFYNDYRIL 645
MYSc_Myo46 cd14907
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ...
36-692 8.59e-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: 504.95  E-value: 8.59e-166
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160   36 INNLKKRFDHNEVYTYIGSVVISINPYRPLP-IYTPEKVEEYRNR--------NFYELSPHIFALSDEAYRSLRDQDKDQ 106
Cdd:cd14907      4 LINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEQiiqngeyfDIKKEPPHIYAIAALAFKQLFENNKKQ 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  107 CILITGESGAGKTEASKFVMSYVAAVCGK-----------------GAEVNQVKEQLLQSNPVLEAFGNAKTVRNDNSSR 169
Cdd:cd14907     84 AIVISGESGAGKTENAKYAMKFLTQLSQQeqnseevltltssiratSKSTKSIEQKILSCNPILEAFGNAKTVRNDNSSR 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  170 FGKYMDIEFDFK-GDPLGGVISNYLLEKSRVVKQPRGERNFHIFYQILSGASEDFLCKLKLERDFSRYNYLGL---DSAK 245
Cdd:cd14907    164 FGKYVSILVDKKkRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLKNQLSGDRYDYLkksNCYE 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  246 VNGVDDAANFRTVRNAMQIVGFMDHETQSVFEVVAAVLKLGNIEFKpESRVNGLDESKIKDKNELKEICELTGIDQSVLE 325
Cdd:cd14907    244 VDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFD-DSTLDDNSPCCVKNKETLQIIAKLLGIDEEELK 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  326 RAFSFRTVEAKQEKVSTTLNVAQAYYARDALAKNLYSRLFSWLVTRINESI-------KAQTKVRKKVMGVLDIYGFEIF 398
Cdd:cd14907    323 EALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpkdekdQQLFQNKYLSIGLLDIFGFEVF 402
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  399 EDNSFEQFIINYCNEKLQQIFIELTLKEEQEEYIREGIE--WTHIEYFNNAIICDLIENNQTGILAMLDEECLRpGTVTD 476
Cdd:cd14907    403 QNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEdyLNQLSYTDNQDVIDLLDKPPIGIFNLLDDSCKL-ATGTD 481
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  477 DTFLEKLnqvCATHQHFesrmskcSRFLNDTTLPHSCFRIQHYAGKVMYQVEGFVDKNNDLLYRDLSQAMWKASHSLIKA 556
Cdd:cd14907    482 EKLLNKI---KKQHKNN-------SKLIFPNKINKDTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISS 551
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  557 LF--------PEGNPAKINLKRPPTAGSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNDALVCHQIRYLGLLEN 628
Cdd:cd14907    552 IFsgedgsqqQNQSKQKKSQKKDKFLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYLGVLES 631
                          650       660       670       680       690       700
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024511160  629 VRVRRAGYAFRQAYEPCLERYKMLCKQtwphwrgparagveVLfneleipeeefsFGRSKIFIR 692
Cdd:cd14907    632 IRVRKQGYPYRKSYEDFYKQYSLLKKN--------------VL------------FGKTKIFMK 669
MYSc_Myo43 cd14904
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ...
34-652 3.45e-158

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: 484.83  E-value: 3.45e-158
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160   34 SFINNLKKRFDHNEVYTYIGSVVISINPYRPLP-IYTPEKVEEYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITG 112
Cdd:cd14904      2 SILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVSG 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  113 ESGAGKTEASKFVMSYVAAVCG--KGAEVNQVkeqlLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGGVIS 190
Cdd:cd14904     82 ESGAGKTETTKIVMNHLASVAGgrKDKTIAKV----IDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRGKLIGAKCE 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  191 NYLLEKSRVVKQPRGERNFHIFYQILSGASEDFLCKLKLERDFSrYNYLG--LDSAKVNGVDDAANFRTVRNAMQIVGFM 268
Cdd:cd14904    158 TYLLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQ-YQYLGdsLAQMQIPGLDDAKLFASTQKSLSLIGLD 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  269 DHETQSVFEVVAAVLKLGNIEFKpESRVNGldeSKIKDKNELKEICELTGIDQSVLERAFSFRTVEAKQEKVSTTLNVAQ 348
Cdd:cd14904    237 NDAQRTLFKILSGVLHLGEVMFD-KSDENG---SRISNGSQLSQVAKMLGLPTTRIEEALCNRSVVTRNESVTVPLAPVE 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  349 AYYARDALAKNLYSRLFSWLVTRINESIKAQTKVRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKEEQ 428
Cdd:cd14904    313 AEENRDALAKAIYSKLFDWMVVKINAAISTDDDRIKGQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDVFKTVE 392
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  429 EEYIREGIEWTHIEYFNNAIICDLIEnNQTGILAMLDEECLRPgtvtDDTFLEKLNQVCATHQhfESRMSKCSRFlndTT 508
Cdd:cd14904    393 EEYIREGLQWDHIEYQDNQGIVEVID-GKMGIIALMNDHLRQP----RGTEEALVNKIRTNHQ--TKKDNESIDF---PK 462
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  509 LPHSCFRIQHYAGKVMYQVEGFVDKNNDLLYRDLSQAMWKASHSLIKALF--------PEGNPAKINLKRPPTAGSQFKA 580
Cdd:cd14904    463 VKRTQFIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFgsseapseTKEGKSGKGTKAPKSLGSQFKT 542
                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024511160  581 SVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNDALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKML 652
Cdd:cd14904    543 SLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAIM 614
MYSc_Myh2_insects_mollusks cd14911
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ...
34-692 3.74e-157

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: 482.56  E-value: 3.74e-157
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160   34 SFINNLKKRFDHNEVYTYIGSVVISINPYRPLPIYTPEKVEEYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITGE 113
Cdd:cd14911      2 SVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTGE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  114 SGAGKTEASKFV---MSYVAAVCGKGA------------EVNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEF 178
Cdd:cd14911     82 SGAGKTENTKKViqfLAYVAASKPKGSgavphpavnpavLIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  179 DFKGDPLGGVISNYLLEKSRVVKQPRGERNFHIFYQILSGASEDFLCKLKLErDFSRYNYLGLDSAKVNGVDDAANFRTV 258
Cdd:cd14911    162 DASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILD-DVKSYAFLSNGSLPVPGVDDYAEFQAT 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  259 RNAMQIVGFMDHETQSVFEVVAAVLKLGNIEFKPEsRVNglDESKIKDKNELKEICELTGIDQSVLERAFSFRTVEAKQE 338
Cdd:cd14911    241 VKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQE-RNN--DQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRD 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  339 KVSTTLNVAQAYYARDALAKNLYSRLFSWLVTRINESIKAQTKVRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQI 418
Cdd:cd14911    318 FVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQL 397
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  419 FIELTLKEEQEEYIREGIEWTHIEY-FNNAIICDLIEnNQTGILAMLDEECLRPgTVTDDTFLEKLNQVCATHQHFesrM 497
Cdd:cd14911    398 FNHTMFILEQEEYQREGIEWKFIDFgLDLQPTIDLID-KPGGIMALLDEECWFP-KATDKTFVDKLVSAHSMHPKF---M 472
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  498 SKCSRFLNDttlphscFRIQHYAGKVMYQVEGFVDKNNDLLYRDLSQAM-----------WKASHSL---IKALFPEGNP 563
Cdd:cd14911    473 KTDFRGVAD-------FAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLqgsqdpfvvniWKDAEIVgmaQQALTDTQFG 545
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  564 AKINLKRPPTAGSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNDALVCHQIRYLGLLENVRVRRAGYAFRQAYE 643
Cdd:cd14911    546 ARTRKGMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQ 625
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*....
gi 2024511160  644 PCLERYKMLCKQTWPHWRGPARAGVEVLFNELEIPEEEFSFGRSKIFIR 692
Cdd:cd14911    626 EFRQRYELLTPNVIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
MYSc_Myo47 cd14908
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ...
34-692 9.32e-156

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: 479.40  E-value: 9.32e-156
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160   34 SFINNLKKRFDHNEVYTYIGSVVISINPYRPLPIYTPEKVEEYRNRNFY---------ELSPHIFALSDEAYRSL-RDQD 103
Cdd:cd14908      2 AILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRQEGLLrsqgiespqALGPHVFAIADRSYRQMmSEIR 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  104 KDQCILITGESGAGKTEASKFVMSYVAAVCGKGAEVNQ---------VKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYM 174
Cdd:cd14908     82 ASQSILISGESGAGKTESTKIVMLYLTTLGNGEEGAPNegeelgklsIMDRVLQSNPILEAFGNARTLRNDNSSRFGKFI 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  175 DIEFDFKGDPLGGVISNYLLEKSRVVKQPRGERNFHIFYQILSGASEDFLCKLKLERDFSR-------YNYLGL-DSAKV 246
Cdd:cd14908    162 ELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEEEHEKYEFHDGITGglqlpneFHYTGQgGAPDL 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  247 NGVDDAANFRTVRNAMQIVGFMDHETQSVFEVVAAVLKLGNIEFKPESRVNGLDESKIKDKNELKEICELTGIDQSVLER 326
Cdd:cd14908    242 REFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDGAAEIAEEGNEKCLARVAKLLGVDVDKLLR 321
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  327 AFSFRTVEAKQEKVSTTLNVAQAYYARDALAKNLYSRLFSWLVTRINESIKAQT-KVRKKVMGVLDIYGFEIFEDNSFEQ 405
Cdd:cd14908    322 ALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSINWENdKDIRSSVGVLDIFGFECFAHNSFEQ 401
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  406 FIINYCNEKLQQIFIELTLKEEQEEYIREGIEWTHIEYFNNAIICDLIENNQTGILAMLDEECLRPGTVTDDTFLEKLNQ 485
Cdd:cd14908    402 LCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFPDNQDCLDTIQAKKKGILTMLDDECRLGIRGSDANYASRLYE 481
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  486 VCATHQHFEsrMSKCSRFLNDTTL-PHSCFRIQHYAGKVMYQVE-GFVDKNNDLLYRDlsqamwkashslIKALFPEgnp 563
Cdd:cd14908    482 TYLPEKNQT--HSENTRFEATSIQkTKLIFAVRHFAGQVQYTVEtTFCEKNKDEIPLT------------ADSLFES--- 544
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  564 akinlkrpptaGSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNDALVCHQIRYLGLLENVRVRRAGYAFRQAYE 643
Cdd:cd14908    545 -----------GQQFKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRYGGVLEAVRVARSGYPVRLPHK 613
                          650       660       670       680       690       700
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024511160  644 PCLERYKMLC------KQTW-PHWRGPARAGVEVLFNEL-------------EIPEEEFSFGRSKIFIR 692
Cdd:cd14908    614 DFFKRYRMLLplipevVLSWsMERLDPQKLCVKKMCKDLvkgvlspamvsmkNIPEDTMQLGKSKVFMR 682
PTZ00014 PTZ00014
myosin-A; Provisional
21-745 8.47e-155

myosin-A; Provisional


Pssm-ID: 240229 [Multi-domain]  Cd Length: 821  Bit Score: 481.45  E-value: 8.47e-155
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160   21 VGDMVLLEPLNEDSFINNLKKRFDHNEVYTYIGSVVISINPYRPLPIYTPEKVEEYRN-RNFYELSPHIFALSDEAYRSL 99
Cdd:PTZ00014    98 YGDIGLLPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYRDaKDSDKLPPHVFTTARRALENL 177
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  100 RDQDKDQCILITGESGAGKTEASKFVMSYVAAvcGKGAEVNQ-VKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEF 178
Cdd:PTZ00014   178 HGVKKSQTIIVSGESGAGKTEATKQIMRYFAS--SKSGNMDLkIQNAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQL 255
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  179 DFKGDPLGGVISNYLLEKSRVVKQPRGERNFHIFYQILSGASEDFLCKLKLeRDFSRYNYLGLDSAKVNGVDDAANFRTV 258
Cdd:PTZ00014   256 GEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKL-KSLEEYKYINPKCLDVPGIDDVKDFEEV 334
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  259 RNAMQIVGFMDHETQSVFEVVAAVLKLGNIEFKPESRVNGLDESKIKDKNE--LKEICELTGIDQSVLERAFSFRTVEAK 336
Cdd:PTZ00014   335 MESFDSMGLSESQIEDIFSILSGVLLLGNVEIEGKEEGGLTDAAAISDESLevFNEACELLFLDYESLKKELTVKVTYAG 414
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  337 QEKVSTTLNVAQAYYARDALAKNLYSRLFSWLVTRINESIKAQTKVrKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQ 416
Cdd:PTZ00014   415 NQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGF-KVFIGMLDIFGFEVFKNNSLEQLFINITNEMLQ 493
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  417 QIFIELTLKEEQEEYIREGIEWTHIEYFNNAIICDLIENNQTGILAMLDEECLRPGTvTDDTFLEKLNQVCATHQHFesr 496
Cdd:PTZ00014   494 KNFVDIVFERESKLYKDEGISTEELEYTSNESVIDLLCGKGKSVLSILEDQCLAPGG-TDEKFVSSCNTNLKNNPKY--- 569
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  497 mSKCSRFLNdttlphSCFRIQHYAGKVMYQVEGFVDKNNDLLYRDLSQAMWKASHSLIKALFP-----EGNPAKINLkrp 571
Cdd:PTZ00014   570 -KPAKVDSN------KNFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLFEgveveKGKLAKGQL--- 639
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  572 ptAGSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNDALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKM 651
Cdd:PTZ00014   640 --IGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKY 717
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  652 LCKQTWPHWRGPARAGVEVLFNELEIPEEEFSFGRSKIFIRnPRTLFKLEDLRKQRL---EDLATLIEKIYRGWKCRTHF 728
Cdd:PTZ00014   718 LDLAVSNDSSLDPKEKAEKLLERSGLPKDSYAIGKTMVFLK-KDAAKELTQIQREKLaawEPLVSVLEALILKIKKKRKV 796
                          730
                   ....*....|....*..
gi 2024511160  729 LLMKKSQIVIAAWFRRY 745
Cdd:PTZ00014   797 RKNIKSLVRIQAHLRRH 813
MYSc_Myo34 cd14895
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ...
34-692 7.91e-152

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: 469.82  E-value: 7.91e-152
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160   34 SFINNLKKRFDHNEVYTYIGSVVISINPYRPLP-IYtpeKVEEYRNR--NFYELSPHIFALSDEAYRSLR-------DQD 103
Cdd:cd14895      2 AFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIPgLY---DLHKYREEmpGWTALPPHVFSIAEGAYRSLRrrlhepgASK 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  104 KDQCILITGESGAGKTEASKFVMSYVAAVCGKGAEVNQVK-------EQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDI 176
Cdd:cd14895     79 KNQTILVSGESGAGKTETTKFIMNYLAESSKHTTATSSSKrrraisgSELLSANPILESFGNARTLRNDNSSRFGKFVRM 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  177 -----EFDFKGDPLGGVISNYLLEKSRVVKQPRGERNFHIFYQILSGASEDFLCKLKLERDFSR-YNYLGLDSAKV--NG 248
Cdd:cd14895    159 ffeghELDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQLELLSAQeFQYISGGQCYQrnDG 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  249 VDDAANFRTVRNAMQIVGFMDHETQSVFEVVAAVLKLGNIEFKPESRVNGLDE---------------SKIKDKNELKEI 313
Cdd:cd14895    239 VRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEGEEDngaasapcrlasaspSSLTVQQHLDIV 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  314 CELTGIDQSVLERAFSFRTVEAKQEKVSTTLNVAQAYYARDALAKNLYSRLFSWLVTRINESI----------KAQTKVR 383
Cdd:cd14895    319 SKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASpqrqfalnpnKAANKDT 398
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  384 KKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKEEQEEYIREGIEWTHIEYFNNAIICDLIENNQTGILAM 463
Cdd:cd14895    399 TPCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDNSVCLEMLEQRPSGIFSL 478
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  464 LDEECLRPGTvTDDTFLEKLNQVCATHQHFESrmskcSRflndTTLPHSCFRIQHYAGKVMYQVEGFVDKNNDLLYRDLS 543
Cdd:cd14895    479 LDEECVVPKG-SDAGFARKLYQRLQEHSNFSA-----SR----TDQADVAFQIHHYAGAVRYQAEGFCEKNKDQPNAELF 548
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  544 QAMWKASHSLIKAL---FPEGNPAKINLKRPPT-----------AGSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAH 609
Cdd:cd14895    549 SVLGKTSDAHLRELfefFKASESAELSLGQPKLrrrssvlssvgIGSQFKQQLASLLDVVQQTQTHYIRCIKPNDESASD 628
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  610 IFNDALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKML-CKQTWPHWrgPARAGVEVLF-NELEIpeeefsfGRS 687
Cdd:cd14895    629 QFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLvAAKNASDA--TASALIETLKvDHAEL-------GKT 699

                   ....*
gi 2024511160  688 KIFIR 692
Cdd:cd14895    700 RVFLR 704
MYSc_Myo30 cd14891
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ...
26-692 2.37e-151

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: 466.44  E-value: 2.37e-151
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160   26 LLEPLNEDSFINNLKKrfdhnevYTYIGSVVISINPYRPLPiyTPeKVEEYRNRNFYELSPHIFALSDEAYRSLRDQ--- 102
Cdd:cd14891      3 ILHNLEERSKLDNQRP-------YTFMANVLIAVNPLRRLP--EP-DKSDYINTPLDPCPPHPYAIAEMAYQQMCLGsgr 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  103 DKDQCILITGESGAGKTEASKFVMSYV----------------AAVCGKGAEVNQVKEQLLQSNPVLEAFGNAKTVRNDN 166
Cdd:cd14891     73 MQNQSIVISGESGAGKTETSKIILRFLttravggkkasgqdieQSSKKRKLSVTSLDERLMDTNPILESFGNAKTLRNHN 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  167 SSRFGKYMDIEFDFKGDPL-GGVISNYLLEKSRVVKQPRGERNFHIFYQILSGASEDFLCKLKLER--DFSRYNYLGLDS 243
Cdd:cd14891    153 SSRFGKFMKLQFTKDKFKLaGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSpeDFIYLNQSGCVS 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  244 AkvNGVDDAANFRTVRNAMQIVGfMDHETQ-SVFEVVAAVLKLGNIEFKPESRVNGL-DESKIKDKNELKEICELTGIDQ 321
Cdd:cd14891    233 D--DNIDDAANFDNVVSALDTVG-IDEDLQlQIWRILAGLLHLGNIEFDEEDTSEGEaEIASESDKEALATAAELLGVDE 309
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  322 SVLERAFSFRTVEAKQEKVSTTLNVAQAYYARDALAKNLYSRLFSWLVTRINESIKAQTKVRKKVmGVLDIYGFEIFE-D 400
Cdd:cd14891    310 EALEKVITQREIVTRGETFTIKRNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGHDPDPLPYI-GVLDIFGFESFEtK 388
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  401 NSFEQFIINYCNEKLQQIFIELTLKEEQEEYIREGIEWTHIEYFNNAIICDLIENNQTGILAMLDEECLRPGTvTDDTFL 480
Cdd:cd14891    389 NDFEQLLINYANEALQATFNQQVFIAEQELYKSEGIDVGVITWPDNRECLDLIASKPNGILPLLDNEARNPNP-SDAKLN 467
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  481 EKLNQVCATHQHFESRMSKCSRFlndttlphsCFRIQHYAGKVMYQVEGFVDKNNDLLYRDLsqamwkasHSLIKalfpe 560
Cdd:cd14891    468 ETLHKTHKRHPCFPRPHPKDMRE---------MFIVKHYAGTVSYTIGSFIDKNNDIIPEDF--------EDLLA----- 525
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  561 gnpakinlkrpptAGSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNDALVCHQIRYLGLLENVRVRRAGYAFRQ 640
Cdd:cd14891    526 -------------SSAKFSDQMQELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVLKVGLPTRV 592
                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2024511160  641 AYEPCLERYK-MLCKQTWPHWRGPARAGVEVLFNELEIPEEEFSFGRSKIFIR 692
Cdd:cd14891    593 TYAELVDVYKpVLPPSVTRLFAENDRTLTQAILWAFRVPSDAYRLGRTRVFFR 645
MYSc_Myh18 cd14932
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ...
34-692 2.39e-150

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


Pssm-ID: 276895 [Multi-domain]  Cd Length: 676  Bit Score: 464.89  E-value: 2.39e-150
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160   34 SFINNLKKRFDHNEVYTYIGSVVISINPYRPLPIYTPEKVEEYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITGE 113
Cdd:cd14932      2 SVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  114 SGAGKTEASKFVMSYVAAVCG-------KGAEV---NQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGD 183
Cdd:cd14932     82 SGAGKTENTKKVIQYLAYVASsfktkkdQSSIAlshGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  184 PLGGVISNYLLEKSRVVKQPRGERNFHIFYQILSGASEDFLCKLKLErDFSRYNYLGLDSAKVNGVDDAANFRTVRNAMQ 263
Cdd:cd14932    162 IVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLE-DYSKYRFLSNGNVTIPGQQDKELFAETMEAFR 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  264 IVGFMDHETQSVFEVVAAVLKLGNIEFKPESRVnglDESKIKDKNELKEICELTGIDQSVLERAFSFRTVEAKQEKVSTT 343
Cdd:cd14932    241 IMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNS---DQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQKA 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  344 LNVAQAYYARDALAKNLYSRLFSWLVTRINESIKAQTKVRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELT 423
Cdd:cd14932    318 QTQEQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTM 397
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  424 LKEEQEEYIREGIEWTHIEYFNNAIIC-DLIE--NNQTGILAMLDEECLRPgTVTDDTFLEKLNQVCATHQHFEsrmsKC 500
Cdd:cd14932    398 FILEQEEYQREGIEWSFIDFGLDLQPCiELIEkpNGPPGILALLDEECWFP-KATDKSFVEKVVQEQGNNPKFQ----KP 472
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  501 SRFLNDTTlphscFRIQHYAGKVMYQVEGFVDKNNDLLYRDLSQAMWKASHSLIKALFPEGN-----------------P 563
Cdd:cd14932    473 KKLKDDAD-----FCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVDrivgldkvagmgeslhgA 547
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  564 AKINLKRPPTAGSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNDALVCHQIRYLGLLENVRVRRAGYAFRQAYE 643
Cdd:cd14932    548 FKTRKGMFRTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQ 627
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*....
gi 2024511160  644 PCLERYKMLCKQTWPHWRGPARAGVEVLFNELEIPEEEFSFGRSKIFIR 692
Cdd:cd14932    628 EFRQRYEILTPNAIPKGFMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
MYSc_Myh11 cd14921
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ...
34-692 2.19e-149

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: 462.56  E-value: 2.19e-149
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160   34 SFINNLKKRFDHNEVYTYIGSVVISINPYRPLPIYTPEKVEEYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITGE 113
Cdd:cd14921      2 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  114 SGAGKTEASKFVMSYVAAVCG--KGAE----VNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGG 187
Cdd:cd14921     82 SGAGKTENTKKVIQYLAVVASshKGKKdtsiTGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGA 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  188 VISNYLLEKSRVVKQPRGERNFHIFYQILSGASEDFLCKLKLErDFSRYNYLGLDSAKVNGVDDAANFRTVRNAMQIVGF 267
Cdd:cd14921    162 NIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLE-GFNNYTFLSNGFVPIPAAQDDEMFQETLEAMSIMGF 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  268 MDHETQSVFEVVAAVLKLGNIEFKPESRVnglDESKIKDKNELKEICELTGIDQSVLERAFSFRTVEAKQEKVSTTLNVA 347
Cdd:cd14921    241 SEEEQLSILKVVSSVLQLGNIVFKKERNT---DQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKE 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  348 QAYYARDALAKNLYSRLFSWLVTRINESIKAQTKVRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKEE 427
Cdd:cd14921    318 QADFAIEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILE 397
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  428 QEEYIREGIEWTHIEYFNNAIIC-DLIE--NNQTGILAMLDEECLRPgTVTDDTFLEKLNQVCATHQHFESrmskcSRFL 504
Cdd:cd14921    398 QEEYQREGIEWNFIDFGLDLQPCiELIErpNNPPGVLALLDEECWFP-KATDKSFVEKLCTEQGNHPKFQK-----PKQL 471
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  505 NDTTLphscFRIQHYAGKVMYQVEGFVDKNNDLLYRDLSQAMWKASHSLIKALF--------------------PEGNPA 564
Cdd:cd14921    472 KDKTE----FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWkdvdrivgldqmakmtesslPSASKT 547
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  565 KINLKRppTAGSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNDALVCHQIRYLGLLENVRVRRAGYAFRQAYEP 644
Cdd:cd14921    548 KKGMFR--TVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQE 625
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*...
gi 2024511160  645 CLERYKMLCKQTWPHWRGPARAGVEVLFNELEIPEEEFSFGRSKIFIR 692
Cdd:cd14921    626 FRQRYEILAANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
MYSc_Myh3 cd14913
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ...
38-692 1.00e-147

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: 457.98  E-value: 1.00e-147
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160   38 NLKKRFDHNEVYTYIGSVVISINPYRPLPIYTPEKVEEYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITGESGAG 117
Cdd:cd14913      6 NLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESGAG 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  118 KTEASKFVMSYVAAVCGKGAEVNQ--------VKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGGVI 189
Cdd:cd14913     86 KTVNTKRVIQYFATIAATGDLAKKkdskmkgtLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLASADI 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  190 SNYLLEKSRVVKQPRGERNFHIFYQILSGASEDFLCKLKLERDFSRYNYLGLDSAKVNGVDDAANFRTVRNAMQIVGFMD 269
Cdd:cd14913    166 ETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPYDYPFISQGEILVASIDDAEELLATDSAIDILGFTP 245
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  270 HETQSVFEVVAAVLKLGNIEFKPESRvnglDESKIKDKNELKE-ICELTGIDQSVLERAFSFRTVEAKQEKVSTTLNVAQ 348
Cdd:cd14913    246 EEKSGLYKLTGAVMHYGNMKFKQKQR----EEQAEPDGTEVADkTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTVDQ 321
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  349 AYYARDALAKNLYSRLFSWLVTRINESIkaQTKV-RKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKEE 427
Cdd:cd14913    322 VHHAVNALSKSVYEKLFLWMVTRINQQL--DTKLpRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVLE 399
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  428 QEEYIREGIEWTHIEYFNNAIIC-DLIEnNQTGILAMLDEECLRPgTVTDDTFLEKLnqvcathqhFESRMSKCSRFLND 506
Cdd:cd14913    400 QEEYKKEGIEWTFIDFGMDLAACiELIE-KPMGIFSILEEECMFP-KATDTSFKNKL---------YDQHLGKSNNFQKP 468
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  507 TTL---PHSCFRIQHYAGKVMYQVEGFVDKNNDLLYRDLSQAMWKASHSLIKALFP--EGNPAKINLKRPP--------T 573
Cdd:cd14913    469 KVVkgrAEAHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYAtfATADADSGKKKVAkkkgssfqT 548
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  574 AGSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNDALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKMLC 653
Cdd:cd14913    549 VSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLN 628
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|
gi 2024511160  654 KQTWPHWRG-PARAGVEVLFNELEIPEEEFSFGRSKIFIR 692
Cdd:cd14913    629 ASAIPEGQFiDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
MYSc_Myo28 cd14889
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ...
35-658 2.40e-147

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: 456.68  E-value: 2.40e-147
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160   35 FINNLKKRFDHNEVYTYIGSVVISINPYRPLPIYTPEKVEEYRNRNFYELSPHIFALSDEAYRSLRDQ----DKDQCILI 110
Cdd:cd14889      3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLGRlargPKNQCIVI 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  111 TGESGAGKTEASKFVMSYVAAVCgKGAevNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFdFKGDPLGGVIS 190
Cdd:cd14889     83 SGESGAGKTESTKLLLRQIMELC-RGN--SQLEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRF-RNGHVKGAKIN 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  191 NYLLEKSRVVKQPRGERNFHIFYQILSGAS-EDFLCKLKLERDFSRYNYLGLDSAkvngvDDAANFRT----VRNAMQIV 265
Cdd:cd14889    159 EYLLEKSRVVHQDGGEENFHIFYYMFAGISaEDRENYGLLDPGKYRYLNNGAGCK-----REVQYWKKkydeVCNAMDMV 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  266 GFMDHETQSVFEVVAAVLKLGNIEFKPESrvNGLDESKIKDKNELKEICELTGIDQSVLERAFSFRTVEAKQEKVSTTLN 345
Cdd:cd14889    234 GFTEQEEVDMFTILAGILSLGNITFEMDD--DEALKVENDSNGWLKAAAGQFGVSEEDLLKTLTCTVTFTRGEQIQRHHT 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  346 VAQAYYARDALAKNLYSRLFSWLVTRINESI--KAQTKVRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELT 423
Cdd:cd14889    312 KQQAEDARDSIAKVAYGRVFGWIVSKINQLLapKDDSSVELREIGILDIFGFENFAVNRFEQACINLANEQLQYFFNHHI 391
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  424 LKEEQEEYIREGIEWTHIEYFNNAIICDLIENNQTGILAMLDEECLRPgTVTDDTFLEKLNQVCATHQHFESRMSKCSRf 503
Cdd:cd14889    392 FLMEQKEYKKEGIDWKEITYKDNKPILDLFLNKPIGILSLLDEQSHFP-QATDESFVDKLNIHFKGNSYYGKSRSKSPK- 469
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  504 lndttlphscFRIQHYAGKVMYQVEGFVDKNNDLLYRDLSQAMWKASHSLIKALF----------------PEGNPAKIN 567
Cdd:cd14889    470 ----------FTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFtatrsrtgtlmpraklPQAGSDNFN 539
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  568 LKRPPTAGSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNDALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLE 647
Cdd:cd14889    540 STRKQSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFSWRPSFAEFAE 619
                          650
                   ....*....|..
gi 2024511160  648 RYK-MLCKQTWP 658
Cdd:cd14889    620 RYKiLLCEPALP 631
MYSc_Myo39 cd14900
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ...
33-659 3.77e-147

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: 454.76  E-value: 3.77e-147
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160   33 DSFINNLKKRFDHNEVYTYIGSVVISINPYRPLP-IYTPEKVEEY-----------RNRNFYELSPHIFALSDEAYRSLR 100
Cdd:cd14900      1 TTILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssstRNKGSDPMPPHIYQVAGEAYKAMM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  101 D----QDKDQCILITGESGAGKTEASKFVMSYVAAV--------CGKGAEVNQVKEQLLQSNPVLEAFGNAKTVRNDNSS 168
Cdd:cd14900     81 LglngVMSDQSILVSGESGSGKTESTKFLMEYLAQAgdnnlaasVSMGKSTSGIAAKVLQTNILLESFGNARTLRNDNSS 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  169 RFGKYMDIEFDFKGDPLGGVISNYLLEKSRVVKQPRGERNFHIFYQILSGASEDflcklKLERDfsrynylgldsakvng 248
Cdd:cd14900    161 RFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASEA-----ARKRD---------------- 219
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  249 vddaaNFRTVRNAMQIVGFMDHETQSVFEVVAAVLKLGNIEFK--PESRVNGLDESKIKDKNE--LKEICELTGIDQSVL 324
Cdd:cd14900    220 -----MYRRVMDAMDIIGFTPHERAGIFDLLAALLHIGNLTFEhdENSDRLGQLKSDLAPSSIwsRDAAATLLSVDATKL 294
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  325 ERAFSFRTVEAKQEKVSTTLNVAQAYYARDALAKNLYSRLFSWLVTRINESIK----AQTKVRKKVMGVLDIYGFEIFED 400
Cdd:cd14900    295 EKALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLKmddsSKSHGGLHFIGILDIFGFEVFPK 374
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  401 NSFEQFIINYCNEKLQQIFIELTLKEEQEEYIREGIEWTHIEYFNNAIICDLIENNQTGILAMLDEECLRPGTvTDDTFL 480
Cdd:cd14900    375 NSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFCDNQDCVNLISQRPTGILSLIDEECVMPKG-SDTTLA 453
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  481 EKLNQVCATHQHFESRMSKCSRFLndttlphscFRIQHYAGKVMYQVEGFVDKNNDLLYRDlsqamwkashslIKALFpe 560
Cdd:cd14900    454 SKLYRACGSHPRFSASRIQRARGL---------FTIVHYAGHVEYSTDGFLEKNKDVLHQE------------AVDLF-- 510
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  561 gnpakinlkrppTAGSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNDALVCHQIRYLGLLENVRVRRAGYAFRQ 640
Cdd:cd14900    511 ------------VYGLQFKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVMEAVRVARAGFPIRL 578
                          650
                   ....*....|....*....
gi 2024511160  641 AYEPCLERYKMLCKQTWPH 659
Cdd:cd14900    579 LHDEFVARYFSLARAKNRL 597
MYSc_Myo35 cd14896
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ...
34-692 2.16e-146

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: 453.47  E-value: 2.16e-146
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160   34 SFINNLKKRFDHNEVYTYIGSVVISINPYRPLPIYTPEKVEEYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITGE 113
Cdd:cd14896      2 SVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSGH 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  114 SGAGKTEASKFVMSYVAAVCGKGAEVN--QVKEQLlqsnPVLEAFGNAKTVRNDNSSRFGKYMDIEFDfKGDPLGGVISN 191
Cdd:cd14896     82 SGSGKTEAAKKIVQFLSSLYQDQTEDRlrQPEDVL----PILESFGHAKTILNANASRFGQVLRLHLQ-HGVIVGASVSH 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  192 YLLEKSRVVKQPRGERNFHIFYQILSGASEDFLCKLKLERDFSrYNYLGLDSA-KVNGVDDAANFRTVRNAMQIVGFMDH 270
Cdd:cd14896    157 YLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQGPET-YYYLNQGGAcRLQGKEDAQDFEGLLKALQGLGLCAE 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  271 ETQSVFEVVAAVLKLGNIEFKPESRvNGLDESKIKDKNELKEICELTGIDQSVLERAFSFRTVEAKQEKVSTTLNVAQAY 350
Cdd:cd14896    236 ELTAIWAVLAAILQLGNICFSSSER-ESQEVAAVSSWAEIHTAARLLQVPPERLEGAVTHRVTETPYGRVSRPLPVEGAI 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  351 YARDALAKNLYSRLFSWLVTRINESIKAQTKVRK-KVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKEEQE 429
Cdd:cd14896    315 DARDALAKTLYSRLFTWLLKRINAWLAPPGEAESdATIGVVDAYGFEALRVNGLEQLCINLASERLQLFSSQTLLAQEEE 394
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  430 EYIREGIEWTHIEYFNNAIICDLIENNQTGILAMLDEECLRPgTVTDDTFLEKlnqvCATHQHFESRMSKcsrflndTTL 509
Cdd:cd14896    395 ECQRELLPWVPIPQPPRESCLDLLVDQPHSLLSILDDQTWLS-QATDHTFLQK----CHYHHGDHPSYAK-------PQL 462
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  510 PHSCFRIQHYAGKVMYQVEGFVDKNNDLLYRDLSQAMWKASHSLIKALFPEGNPAKINLKRPPTAGSQFKASVATLMKNL 589
Cdd:cd14896    463 PLPVFTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQEAEPQYGLGQGKPTLASRFQQSLGDLTARL 542
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  590 QTKNPNYIRCIKPNDKKAAHIFNDALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKMLCKQTWPHWRGPARAGVe 669
Cdd:cd14896    543 GRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGALGSERQEALSDRERCGA- 621
                          650       660
                   ....*....|....*....|...
gi 2024511160  670 VLFNELEIPEEEFSFGRSKIFIR 692
Cdd:cd14896    622 ILSQVLGAESPLYHLGATKVLLK 644
MYSc_Myh9 cd14919
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ...
34-692 4.24e-145

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: 451.08  E-value: 4.24e-145
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160   34 SFINNLKKRFDHNEVYTYIGSVVISINPYRPLPIYTPEKVEEYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITGE 113
Cdd:cd14919      2 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  114 SGAGKTEASKFVMSYVAAVCGK---GAEVNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGGVIS 190
Cdd:cd14919     82 SGAGKTENTKKVIQYLAHVASShksKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIE 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  191 NYLLEKSRVVKQPRGERNFHIFYQILSGASEDFLCKLKLErDFSRYNYLGLDSAKVNGVDDAANFRTVRNAMQIVGFMDH 270
Cdd:cd14919    162 TYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLE-PYNKYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGIPEE 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  271 ETQSVFEVVAAVLKLGNIEFKPESRVnglDESKIKDKNELKEICELTGIDQSVLERAFSFRTVEAKQEKVSTTLNVAQAY 350
Cdd:cd14919    241 EQMGLLRVISGVLQLGNIVFKKERNT---DQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQAD 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  351 YARDALAKNLYSRLFSWLVTRINESIKAQTKVRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKEEQEE 430
Cdd:cd14919    318 FAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEE 397
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  431 YIREGIEWTHIEYFNNAIIC-DLIEN--NQTGILAMLDEECLRPgTVTDDTFLEKLNQVCATHQHFESrmskcSRFLNDT 507
Cdd:cd14919    398 YQREGIEWNFIDFGLDLQPCiDLIEKpaGPPGILALLDEECWFP-KATDKSFVEKVVQEQGTHPKFQK-----PKQLKDK 471
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  508 tlphSCFRIQHYAGKVMYQVEGFVDKNNDLLYRDLSQAMWKASHSLIKALFPEGN----------------PAKINLKRP 571
Cdd:cd14919    472 ----ADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDriigldqvagmsetalPGAFKTRKG 547
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  572 --PTAGSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNDALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERY 649
Cdd:cd14919    548 mfRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRY 627
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|...
gi 2024511160  650 KMLCKQTWPHWRGPARAGVEVLFNELEIPEEEFSFGRSKIFIR 692
Cdd:cd14919    628 EILTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
MYSc_Myh15_mammals cd14929
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ...
34-692 1.24e-144

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: 449.43  E-value: 1.24e-144
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160   34 SFINNLKKRFDHNEVYTYIGSVVISINPYRPLPIYTPEKVEEYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITGE 113
Cdd:cd14929      2 SVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTGE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  114 SGAGKTEASKFVMSY---VAAVCGKGAEVNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGGVIS 190
Cdd:cd14929     82 SGAGKTVNTKHIIQYfatIAAMIESKKKLGALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSADID 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  191 NYLLEKSRVVKQPRGERNFHIFYQILSGASE--DFLCklkLERDFSRYNYLGLDSAKVNGVDDAANFRTVRNAMQIVGFM 268
Cdd:cd14929    162 IYLLEKSRVIFQQPGERNYHIFYQILSGKKElrDLLL---VSANPSDFHFCSCGAVAVESLDDAEELLATEQAMDILGFL 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  269 DHETQSVFEVVAAVLKLGNIEFKPESRVNGL--DESKIKDKNELkeiceLTGIDQSVLERAFSFRTVEAKQEKVSTTLNV 346
Cdd:cd14929    239 PDEKYGCYKLTGAIMHFGNMKFKQKPREEQLeaDGTENADKAAF-----LMGINSSELVKGLIHPRIKVGNEYVTRSQNI 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  347 AQAYYARDALAKNLYSRLFSWLVTRINESIKAQTKvRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKE 426
Cdd:cd14929    314 EQVTYAVGALSKSIYERMFKWLVARINRVLDAKLS-RQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMFVL 392
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  427 EQEEYIREGIEWTHIEYFNNAIIC-DLIEnNQTGILAMLDEECLRPgTVTDDTFLEKLnqvcathqhFESRMSKCSRFLN 505
Cdd:cd14929    393 EQEEYRKEGIDWVSIDFGLDLQACiDLIE-KPMGIFSILEEECMFP-KATDLTFKTKL---------FDNHFGKSVHFQK 461
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  506 DTTLPHSC---FRIQHYAGKVMYQVEGFVDKNNDLLYRDLSQAMWKASHSLIKALFPE---GNPAKINLKRPPTAGSQF- 578
Cdd:cd14929    462 PKPDKKKFeahFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENyisTDSAIQFGEKKRKKGASFq 541
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  579 ------KASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNDALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKML 652
Cdd:cd14929    542 tvaslhKENLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCIL 621
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|.
gi 2024511160  653 CKQTWPHWR-GPARAGVEVLFNELEIPEEEFSFGRSKIFIR 692
Cdd:cd14929    622 NPRTFPKSKfVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
MYSc_Myo41 cd14902
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ...
39-658 1.48e-142

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: 445.88  E-value: 1.48e-142
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160   39 LKKRFDHNEVYTYIGSVVISINPYRPLP-IYTPEKVEEYR--------NRNFYELSPHIFALSDEAYRSLRDQDK-DQCI 108
Cdd:cd14902      7 LSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLKPERrNQSI 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  109 LITGESGAGKTEASKFVMSYVAAV-----CGKGAEVNQVK--EQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFK 181
Cdd:cd14902     87 LVSGESGSGKTESTKFLMQFLTSVgrdqsSTEQEGSDAVEigKRILQTNPILESFGNAQTIRNDNSSRFGKFIKIQFGAN 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  182 GDPLGGVISNYLLEKSRVVKQPRGERNFHIFYQILSGASEDFLCKLKLER--DFSRYNYLGLDSAKVNGV--DDAANFRT 257
Cdd:cd14902    167 NEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKggKYELLNSYGPSFARKRAVadKYAQLYVE 246
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  258 VRNAMQIVGFMDHETQSVFEVVAAVLKLGNIEFKPESrvNGLDESKIKDKNE--LKEICELTGIDQSVLERAFSFRTVEA 335
Cdd:cd14902    247 TVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAEN--GQEDATAVTAASRfhLAKCAELMGVDVDKLETLLSSREIKA 324
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  336 KQEKVSTTLNVAQAYYARDALAKNLYSRLFSWLVTRINESIKA--------QTKVRKKVMGVLDIYGFEIFEDNSFEQFI 407
Cdd:cd14902    325 GVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINYfdsavsisDEDEELATIGILDIFGFESLNRNGFEQLC 404
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  408 INYCNEKLQQIFIELTLKEEQEEYIREGIEWTHIEYFNNAIICDLIENNQTGILAMLDEECLRPgtvtddtflEKLNQVC 487
Cdd:cd14902    405 INYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYPSNAACLALFDDKSNGLFSLLDQECLMP---------KGSNQAL 475
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  488 ATHqhfesrmskcsrfLNDTTLPHSCFRIQHYAGKVMYQVEGFVDKNNDLLYRDLSQAMWKASHSLIKALFPEGN---PA 564
Cdd:cd14902    476 STK-------------FYRYHGGLGQFVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVVVAIGADENrdsPG 542
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  565 KINLK---------RPPTAGSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNDALVCHQIRYLGLLENVRVRRAG 635
Cdd:cd14902    543 ADNGAagrrrysmlRAPSVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLEAVRIARHG 622
                          650       660
                   ....*....|....*....|....
gi 2024511160  636 YAFRQAYEPCLERYK-MLCKQTWP 658
Cdd:cd14902    623 YSVRLAHASFIELFSgFKCFLSTR 646
MYSc_Myo14 cd14876
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ...
39-692 2.58e-142

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: 442.89  E-value: 2.58e-142
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160   39 LKKRFDHNEVYTYIGSVVISINPYRPLPIYTPEKVEEYRN-RNFYELSPHIFALSDEAYRSLRDQDKDQCILITGESGAG 117
Cdd:cd14876      7 LKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDaPDLTKLPPHVFYTARRALENLHGVNKSQTIIVSGESGAG 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  118 KTEASKFVMSYVAAVcGKGAEVNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGGVISNYLLEKS 197
Cdd:cd14876     87 KTEATKQIMRYFASA-KSGNMDLRIQTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVASEGGIRYGSVVAFLLEKS 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  198 RVVKQPRGERNFHIFYQILSGASEDFLCKLKLeRDFSRYNYLGLDSAKVNGVDDAANFRTVRNAMQIVGFMDHETQSVFE 277
Cdd:cd14876    166 RIVTQDDNERSYHIFYQLLKGADSEMKSKYHL-LGLKEYKFLNPKCLDVPGIDDVADFEEVLESLKSMGLTEEQIDTVFS 244
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  278 VVAAVLKLGNIEFKPESRvNGLDES-KI--KDKNELKEICELTGIDQSVLERAFSFRTVEAKQEKVSTTLNVAQAYYARD 354
Cdd:cd14876    245 IVSGVLLLGNVKITGKTE-QGVDDAaAIsnESLEVFKEACSLLFLDPEALKRELTVKVTKAGGQEIEGRWTKDDAEMLKL 323
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  355 ALAKNLYSRLFSWLVTRINESIKAQTKVrKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKEEQEEYIRE 434
Cdd:cd14876    324 SLAKAMYDKLFLWIIRNLNSTIEPPGGF-KNFMGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFIDIVFERESKLYKDE 402
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  435 GIEWTHIEYFNNAIICDLIENNQTGILAMLDEECLRPGTvTDDTFLEKLNQVCATHQHFESrmSKCSRFLNdttlphscF 514
Cdd:cd14876    403 GIPTAELEYTSNAEVIDVLCGKGKSVLSILEDQCLAPGG-SDEKFVSACVSKLKSNGKFKP--AKVDSNIN--------F 471
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  515 RIQHYAGKVMYQVEGFVDKNNDLLYRDLSQAMWKASHSLIKALFP-----EGNPAKINLkrpptAGSQFKASVATLMKNL 589
Cdd:cd14876    472 IVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEgvvveKGKIAKGSL-----IGSQFLKQLESLMGLI 546
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  590 QTKNPNYIRCIKPNDKKAAHIFNDALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKMLCKQTWPHWRGPARAGVE 669
Cdd:cd14876    547 NSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEFLYQFKFLDLGIANDKSLDPKVAAL 626
                          650       660
                   ....*....|....*....|...
gi 2024511160  670 VLFNELEIPEEEFSFGRSKIFIR 692
Cdd:cd14876    627 KLLESSGLSEDEYAIGKTMVFLK 649
MYSc_Myh7 cd14917
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ...
38-692 5.49e-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: 443.00  E-value: 5.49e-142
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160   38 NLKKRFDHNEVYTYIGSVVISINPYRPLPIYTPEKVEEYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITGESGAG 117
Cdd:cd14917      6 NLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGESGAG 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  118 KTEASKFVMSYVAAVCGKGAEVNQ--------VKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGGVI 189
Cdd:cd14917     86 KTVNTKRVIQYFAVIAAIGDRSKKdqtpgkgtLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASADI 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  190 SNYLLEKSRVVKQPRGERNFHIFYQILSGASEDFLCKLKLERDFSRYNYLGLDSAKVNGVDDAANFRTVRNAMQIVGFMD 269
Cdd:cd14917    166 ETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNAFDVLGFTS 245
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  270 HETQSVFEVVAAVLKLGNIEFKPESRVnglDESKIKDKNELKEICELTGIDQSVLERAFSFRTVEAKQEKVSTTLNVAQA 349
Cdd:cd14917    246 EEKNSMYKLTGAIMHFGNMKFKQKQRE---EQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQQV 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  350 YYARDALAKNLYSRLFSWLVTRINESIKAQtKVRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKEEQE 429
Cdd:cd14917    323 IYATGALAKAVYEKMFNWMVTRINATLETK-QPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQE 401
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  430 EYIREGIEWTHIEYFNNAIIC-DLIEnNQTGILAMLDEECLRPgTVTDDTFLEKLnqvcathqhFESRMSKCSRFLNDTT 508
Cdd:cd14917    402 EYKKEGIEWTFIDFGMDLQACiDLIE-KPMGIMSILEEECMFP-KATDMTFKAKL---------FDNHLGKSNNFQKPRN 470
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  509 L---PHSCFRIQHYAGKVMYQVEGFVDKNNDLLYRDLSQAMWKASHSLIKALFPE--GNPAKINL-KRPPTAGSQFKASV 582
Cdd:cd14917    471 IkgkPEAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFANyaGADAPIEKgKGKAKKGSSFQTVS 550
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  583 A-------TLMKNLQTKNPNYIRCIKPNDKKAAHIFNDALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKMLCKQ 655
Cdd:cd14917    551 AlhrenlnKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPA 630
                          650       660       670
                   ....*....|....*....|....*....|....*...
gi 2024511160  656 TWPHWRG-PARAGVEVLFNELEIPEEEFSFGRSKIFIR 692
Cdd:cd14917    631 AIPEGQFiDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
MYSc_Myh7b cd14927
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ...
34-692 7.11e-142

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: 442.86  E-value: 7.11e-142
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160   34 SFINNLKKRFDHNEVYTYIGSVVISINPYRPLPIYTPEKVEEYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITGE 113
Cdd:cd14927      2 SVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITGE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  114 SGAGKTEASKFVMSYVAAVCGKGAEVNQ------------VKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFK 181
Cdd:cd14927     82 SGAGKTVNTKRVIQYFAIVAALGDGPGKkaqflatktggtLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPT 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  182 GDPLGGVISNYLLEKSRVVKQPRGERNFHIFYQILSGASEDFLCKLKLERDFSRYNYLGLDSAKVNGVDDAANFRTVRNA 261
Cdd:cd14927    162 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLVSMNPYDYHFCSQGVTTVDNMDDGEELMATDHA 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  262 MQIVGFMDHETQSVFEVVAAVLKLGNIEFKPESRvnglDESKIKDKNE-LKEICELTGIDQSVLERAFSFRTVEAKQEKV 340
Cdd:cd14927    242 MDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQR----EEQAEADGTEsADKAAYLMGVSSADLLKGLLHPRVKVGNEYV 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  341 STTLNVAQAYYARDALAKNLYSRLFSWLVTRINESIKAQTKvRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFI 420
Cdd:cd14927    318 TKGQSVEQVVYAVGALAKATYDRMFKWLVSRINQTLDTKLP-RQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFN 396
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  421 ELTLKEEQEEYIREGIEWTHIEYFNNAIIC-DLIEnNQTGILAMLDEECLRPgTVTDDTFLEKL--NQVCATHQHFESRM 497
Cdd:cd14927    397 HHMFILEQEEYKREGIEWVFIDFGLDLQACiDLIE-KPLGILSILEEECMFP-KASDASFKAKLydNHLGKSPNFQKPRP 474
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  498 SKCSRFlndttlpHSCFRIQHYAGKVMYQVEGFVDKNNDLLYRDLSQAMWKASHSLIKALF-------PEGNP-AKINLK 569
Cdd:cd14927    475 DKKRKY-------EAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYenyvgsdSTEDPkSGVKEK 547
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  570 RPPTAGSQ-----FKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNDALVCHQIRYLGLLENVRVRRAGYAFRQAYEP 644
Cdd:cd14927    548 RKKAASFQtvsqlHKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYAD 627
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*....
gi 2024511160  645 CLERYKMLCKQTWPHWR-GPARAGVEVLFNELEIPEEEFSFGRSKIFIR 692
Cdd:cd14927    628 FKQRYRILNPSAIPDDKfVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
MYSc_Myh14_mammals cd14930
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ...
34-692 1.83e-141

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


Pssm-ID: 276893 [Multi-domain]  Cd Length: 670  Bit Score: 441.46  E-value: 1.83e-141
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160   34 SFINNLKKRFDHNEVYTYIGSVVISINPYRPLPIYTPEKVEEYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITGE 113
Cdd:cd14930      2 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  114 SGAGKTEASKFVMSYVAAVCG--KGAE----VNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGG 187
Cdd:cd14930     82 SGAGKTENTKKVIQYLAHVASspKGRKepgvPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVGA 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  188 VISNYLLEKSRVVKQPRGERNFHIFYQILSGASEDFLCKLKLErDFSRYNYLGLDSAKVNGvDDAANFRTVRNAMQIVGF 267
Cdd:cd14930    162 NIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLE-PCSHYRFLTNGPSSSPG-QERELFQETLESLRVLGF 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  268 MDHETQSVFEVVAAVLKLGNIEFKPESRVnglDESKIKDKNELKEICELTGIDQSVLERAFSFRTVEAKQEKVSTTLNVA 347
Cdd:cd14930    240 SHEEITSMLRMVSAVLQFGNIVLKRERNT---DQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKE 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  348 QAYYARDALAKNLYSRLFSWLVTRINESIKAQTKVRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKEE 427
Cdd:cd14930    317 QADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLE 396
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  428 QEEYIREGIEWTHIEYFNNAIIC-DLIEN--NQTGILAMLDEECLRPgTVTDDTFLEKLNQVCATHQHFESrmskcSRFL 504
Cdd:cd14930    397 QEEYQREGIPWTFLDFGLDLQPCiDLIERpaNPPGLLALLDEECWFP-KATDKSFVEKVAQEQGGHPKFQR-----PRHL 470
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  505 NDttlpHSCFRIQHYAGKVMYQVEGFVDKNNDLLYRDLSQAMWKASHSLIKALF-------------------PEGNPAK 565
Cdd:cd14930    471 RD----QADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWkdvegivgleqvsslgdgpPGGRPRR 546
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  566 INLKrppTAGSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNDALVCHQIRYLGLLENVRVRRAGYAFRQAYEPC 645
Cdd:cd14930    547 GMFR---TVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEF 623
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*..
gi 2024511160  646 LERYKMLCKQTWPHWRGPARAGVEVLFNELEIPEEEFSFGRSKIFIR 692
Cdd:cd14930    624 RQRYEILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
MYSc_Myh19 cd15896
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ...
34-692 2.97e-140

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: 438.35  E-value: 2.97e-140
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160   34 SFINNLKKRFDHNEVYTYIGSVVISINPYRPLPIYTPEKVEEYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITGE 113
Cdd:cd15896      2 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  114 SGAGKTEASKFVMSYVAAVCGK----------GAEVNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGD 183
Cdd:cd15896     82 SGAGKTENTKKVIQYLAHVASShktkkdqnslALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  184 PLGGVISNYLLEKSRVVKQPRGERNFHIFYQILSGASEDFLCKLKLErDFSRYNYLGLDSAKVNGVDDAANFRTVRNAMQ 263
Cdd:cd15896    162 IVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLE-NYNNYRFLSNGNVTIPGQQDKDLFTETMEAFR 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  264 IVGFMDHETQSVFEVVAAVLKLGNIEFKPESRVnglDESKIKDKNELKEICELTGIDQSVLERAFSFRTVEAKQEKVSTT 343
Cdd:cd15896    241 IMGIPEDEQIGMLKVVASVLQLGNMSFKKERHT---DQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQKA 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  344 LNVAQAYYARDALAKNLYSRLFSWLVTRINESIKAQTKVRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELT 423
Cdd:cd15896    318 QTQEQAEFAVEALAKATYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTM 397
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  424 LKEEQEEYIREGIEWTHIEYFNNAIIC-DLIENNQT--GILAMLDEECLRPgTVTDDTFLEKLNQVCATHQHFESrmskc 500
Cdd:cd15896    398 FILEQEEYQREGIEWSFIDFGLDLQPCiDLIEKPASppGILALLDEECWFP-KATDKSFVEKVLQEQGTHPKFFK----- 471
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  501 SRFLNDttlpHSCFRIQHYAGKVMYQVEGFVDKNNDLLYRDLSQAMWKASHSLIKALFPEGN--------------PAKI 566
Cdd:cd15896    472 PKKLKD----EADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVDrivgldkvsgmsemPGAF 547
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  567 NLKRP--PTAGSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNDALVCHQIRYLGLLENVRVRRAGYAFRQAYEP 644
Cdd:cd15896    548 KTRKGmfRTVGQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQE 627
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*...
gi 2024511160  645 CLERYKMLCKQTWPHWRGPARAGVEVLFNELEIPEEEFSFGRSKIFIR 692
Cdd:cd15896    628 FRQRYEILTPNAIPKGFMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
MYSc_Myh1_insects_crustaceans cd14909
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ...
34-692 7.23e-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: 7.23e-140
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160   34 SFINNLKKRFDHNEVYTYIGSVVISINPYRPLPIYTPEKVEEYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITGE 113
Cdd:cd14909      2 SVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITGE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  114 SGAGKTEASKFVMSYVAAVCG------KGAEVNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGG 187
Cdd:cd14909     82 SGAGKTENTKKVIAYFATVGAskktdeAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLAGA 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  188 VISNYLLEKSRVVKQPRGERNFHIFYQILSGASEDFLCKLKLERDFSRYNYLGLDSAKVNGVDDAANFRTVRNAMQIVGF 267
Cdd:cd14909    162 DIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLSDNIYDYYIVSQGKVTVPNVDDGEEFSLTDQAFDILGF 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  268 MDHETQSVFEVVAAVLKLGNIEFKPESRvnglDESKIKDKNELKE-ICELTGIDQSVLERAFSFRTVEAKQEKVSTTLNV 346
Cdd:cd14909    242 TKQEKEDVYRITAAVMHMGGMKFKQRGR----EEQAEQDGEEEGGrVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNV 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  347 AQAYYARDALAKNLYSRLFSWLVTRINESIKAQTKvRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKE 426
Cdd:cd14909    318 QQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQK-RQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVL 396
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  427 EQEEYIREGIEWTHIEYFNNAIIC-DLIEnNQTGILAMLDEECLRPgTVTDDTFLEKLNqvcATHqhfesrMSKCSRFLN 505
Cdd:cd14909    397 EQEEYKREGIDWAFIDFGMDLLACiDLIE-KPMGILSILEEESMFP-KATDQTFSEKLT---NTH------LGKSAPFQK 465
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  506 DTTLPHSC----FRIQHYAGKVMYQVEGFVDKNNDLLYRDLSQAMWKASHSLIKALFPE-----GNPAKINLKRP----- 571
Cdd:cd14909    466 PKPPKPGQqaahFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADhagqsGGGEQAKGGRGkkggg 545
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  572 -PTAGSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNDALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYK 650
Cdd:cd14909    546 fATVSSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYK 625
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|..
gi 2024511160  651 MLCKQTWPHWRGPARAGvEVLFNELEIPEEEFSFGRSKIFIR 692
Cdd:cd14909    626 ILNPAGIQGEEDPKKAA-EIILESIALDPDQYRLGHTKVFFR 666
MYSc_Myh16 cd14934
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ...
34-692 1.86e-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: 436.00  E-value: 1.86e-139
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160   34 SFINNLKKRFDHNEVYTYIGSVVISINPYRPLPIYTPEKVEEYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITGE 113
Cdd:cd14934      2 SVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITGE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  114 SGAGKTEASKFVMSYVAAVCGKGAEV----NQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGGVI 189
Cdd:cd14934     82 SGAGKTENTKKVIQYFANIGGTGKQSsdgkGSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKLAGADI 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  190 SNYLLEKSRVVKQPRGERNFHIFYQILSGASEDFLCKLKLERDFSRYNYLGLDSAKVNGVDDAANFRTVRNAMQIVGFMD 269
Cdd:cd14934    162 ESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLLVPNPKEYHWVSQGVTVVDNMDDGEELQITDVAFDVLGFSA 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  270 HETQSVFEVVAAVLKLGNIEF--KPESRVNGLDESKIKDKnelkeICELTGIDQSVLERAFSFRTVEAKQEKVSTTLNVA 347
Cdd:cd14934    242 EEKIGVYKLTGGIMHFGNMKFkqKPREEQAEVDTTEVADK-----VAHLMGLNSGELQKGITRPRVKVGNEFVQKGQNME 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  348 QAYYARDALAKNLYSRLFSWLVTRINESIKAQTKvRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKEE 427
Cdd:cd14934    317 QCNNSIGALGKAVYDKMFKWLVVRINKTLDTKMQ-RQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFVLE 395
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  428 QEEYIREGIEWTHIEYFNNAIIC-DLIEnNQTGILAMLDEECLRPgTVTDDTFLEKLnqvcathqhFESRMSKCSRFLND 506
Cdd:cd14934    396 QEEYKREGIEWVFIDFGLDLQACiDLLE-KPMGIFSILEEQCVFP-KATDATFKAAL---------YDNHLGKSSNFLKP 464
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  507 T----TLPHSCFRIQHYAGKVMYQVEGFVDKNNDLLyRDLSQAMWKASHSLIKALFPEGNPAKINLKRPP------TAGS 576
Cdd:cd14934    465 KggkgKGPEAHFELVHYAGTVGYNITGWLEKNKDPL-NETVVGLFQKSSLGLLALLFKEEEAPAGSKKQKrgssfmTVSN 543
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  577 QFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNDALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKMLCKQT 656
Cdd:cd14934    544 FYREQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLNPNV 623
                          650       660       670
                   ....*....|....*....|....*....|....*.
gi 2024511160  657 WPHWRGPARAGVEVLFNELEIPEEEFSFGRSKIFIR 692
Cdd:cd14934    624 IPQGFVDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
MYSc_Myo45 cd14906
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ...
34-654 8.84e-138

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: 433.25  E-value: 8.84e-138
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160   34 SFINNLKKRFDHNEVYTYIGSVVISINPYRPLP-IYTPEKVEEYRNRNFY-ELSPHIFALSDEAYRSLRDQDKDQCILIT 111
Cdd:cd14906      2 IILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQNkSPIPHIYAVALRAYQSMVSEKKNQSIIIS 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  112 GESGAGKTEASKFVMSYVAAVCGKGAEV--------NQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEF---DF 180
Cdd:cd14906     82 GESGSGKTEASKTILQYLINTSSSNQQQnnnnnnnnNSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFrssDG 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  181 KGDplGGVISNYLLEKSRVVKQP-RGERNFHIFYQILSGASEDFLCKLKLERDFSRYNYL---------------GLDSA 244
Cdd:cd14906    162 KID--GASIETYLLEKSRISHRPdNINLSYHIFYYLVYGASKDERSKWGLNNDPSKYRYLdarddvissfksqssNKNSN 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  245 KVNGVDDAANFRTVRNAMQIVGFMDHETQSVFEVVAAVLKLGNIEFKPESRVNGLDESKIKDKNELKEICELTGIDQSVL 324
Cdd:cd14906    240 HNNKTESIESFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSDFSKYAYQKDKVTASLESVSKLLGYIESVF 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  325 ERAFSFRTVEA--KQEKVSTTLNVAQAYYARDALAKNLYSRLFSWLVTRINESIKAQT----------KVRKKVMGVLDI 392
Cdd:cd14906    320 KQALLNRNLKAggRGSVYCRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRKFNQNTqsndlaggsnKKNNLFIGVLDI 399
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  393 YGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKEEQEEYIREGIEWTHIEYFNNAIICDLIENNQTGILAMLDEECLRPG 472
Cdd:cd14906    400 FGFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNFIDNKECIELIEKKSDGILSLLDDECIMPK 479
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  473 TvTDDTFLEKLN-QVCATHQHFESrmskcsrflndtTLPHSCFRIQHYAGKVMYQVEGFVDKNNDLLYRDLSQAMWKASH 551
Cdd:cd14906    480 G-SEQSLLEKYNkQYHNTNQYYQR------------TLAKGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSN 546
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  552 SLIKALFPEGNPAKINLKRPPTAG----SQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNDALVCHQIRYLGLLE 627
Cdd:cd14906    547 FLKKSLFQQQITSTTNTTKKQTQSntvsGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLSQLRNVGVLN 626
                          650       660
                   ....*....|....*....|....*..
gi 2024511160  628 NVRVRRAGYAFRQAYEPCLERYKMLCK 654
Cdd:cd14906    627 TIKVRKMGYSYRRDFNQFFSRYKCIVD 653
MYSc_Myo19 cd14880
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ...
39-691 3.98e-134

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: 421.57  E-value: 3.98e-134
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160   39 LKKRFDHNEVYTYIGSVVISINPYRPLP-IYTPEKVEEYRNR-NFYELSPHIFALSDEAYRSLRDQDK--DQCILITGES 114
Cdd:cd14880      7 LQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAApQPQKLKPHIFTVGEQTYRNVKSLIEpvNQSIVVSGES 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  115 GAGKTEASKFVMSYVAAV------CGKGAEVNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGGV 188
Cdd:cd14880     87 GAGKTWTSRCLMKFYAVVaasptsWESHKIAERIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQLNRAQQMTGAA 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  189 ISNYLLEKSRVVKQPRGERNFHIFYQILSGASEDFLCKLKLERdfsRYNYLGLDSAKVNGVDDAanFRTVRNAMQIVGfM 268
Cdd:cd14880    167 VQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPE---GAAFSWLPNPERNLEEDC--FEVTREAMLHLG-I 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  269 DHETQS-VFEVVAAVLKLGNIEFkpesrVNGLDESKI-----KDKNELKEICELTGIDQSVLERAFSFRTVEA-KQEKV- 340
Cdd:cd14880    241 DTPTQNnIFKVLAGLLHLGNIQF-----ADSEDEAQPcqpmdDTKESVRTSALLLKLPEDHLLETLQIRTIRAgKQQQVf 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  341 STTLNVAQAYYARDALAKNLYSRLFSWLVTRINESIKAQTKVRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFI 420
Cdd:cd14880    316 KKPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSICADTDSWTTFIGLLDVYGFESFPENSLEQLCINYANEKLQQHFV 395
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  421 ELTLKEEQEEYIREGIEWTHIEYFNNAIICDLIENNQTGILAMLDEEClrpgtvtddtfleKLNQVCATHQ---HFESRM 497
Cdd:cd14880    396 AHYLRAQQEEYAVEGLEWSFINYQDNQTCLDLIEGSPISICSLINEEC-------------RLNRPSSAAQlqtRIESAL 462
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  498 SKCSRFLNDTTLPHSCFRIQHYAGKVMYQVEGFVDKNNDLLYRDLSQAMWKASHSLIKALFP--EGNPAKINLK---RPP 572
Cdd:cd14880    463 AGNPCLGHNKLSREPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPanPEEKTQEEPSgqsRAP 542
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  573 --TAGSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNDALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYK 650
Cdd:cd14880    543 vlTVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQNFVERYK 622
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|.
gi 2024511160  651 MLCKqtwphwRGPARAGVEVLFNELEIPEEEFSFGRSKIFI 691
Cdd:cd14880    623 LLRR------LRPHTSSGPHSPYPAKGLSEPVHCGRTKVFM 657
MYSc_Myh6 cd14916
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ...
38-692 4.69e-133

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: 419.46  E-value: 4.69e-133
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160   38 NLKKRFDHNEVYTYIGSVVISINPYRPLPIYTPEKVEEYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITGESGAG 117
Cdd:cd14916      6 NLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGESGAG 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  118 KTEASKFVMSYVAAVCGKG---------AEVNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGGV 188
Cdd:cd14916     86 KTVNTKRVIQYFASIAAIGdrskkenpnANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASAD 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  189 ISNYLLEKSRVVKQPRGERNFHIFYQILSGASEDFLCKLKLERDFSRYNYLGLDSAKVNGVDDAANFRTVRNAMQIVGFM 268
Cdd:cd14916    166 IETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELLATDSAFDVLGFT 245
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  269 DHETQSVFEVVAAVLKLGNIEFKPESRVNGLDESKIKDKNelkEICELTGIDQSVLERAFSFRTVEAKQEKVSTTLNVAQ 348
Cdd:cd14916    246 AEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDAD---KSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSVQQ 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  349 AYYARDALAKNLYSRLFSWLVTRINESIKAQtKVRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKEEQ 428
Cdd:cd14916    323 VYYSIGALAKSVYEKMFNWMVTRINATLETK-QPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQ 401
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  429 EEYIREGIEWTHIEYFNNAIIC-DLIEnNQTGILAMLDEECLRPgTVTDDTFLEKLnqvcathqhFESRMSKCSRF---L 504
Cdd:cd14916    402 EEYKKEGIEWEFIDFGMDLQACiDLIE-KPMGIMSILEEECMFP-KASDMTFKAKL---------YDNHLGKSNNFqkpR 470
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  505 NDTTLPHSCFRIQHYAGKVMYQVEGFVDKNNDLLYRDLSQAMWKASHSLIKALFP-----------EGNPAKINLKRPPT 573
Cdd:cd14916    471 NVKGKQEAHFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFStyasadtgdsgKGKGGKKKGSSFQT 550
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  574 AGSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNDALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKMLC 653
Cdd:cd14916    551 VSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILN 630
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|
gi 2024511160  654 KQTWPHWRG-PARAGVEVLFNELEIPEEEFSFGRSKIFIR 692
Cdd:cd14916    631 PAAIPEGQFiDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
MYSc_Myh8 cd14918
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ...
38-692 5.91e-130

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: 411.05  E-value: 5.91e-130
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160   38 NLKKRFDHNEVYTYIGSVVISINPYRPLPIYTPEKVEEYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITGESGAG 117
Cdd:cd14918      6 NLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESGAG 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  118 KTEASKFVMSYVA--AVCGK------GAEVNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGGVI 189
Cdd:cd14918     86 KTVNTKRVIQYFAtiAVTGEkkkeesGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLASADI 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  190 SNYLLEKSRVVKQPRGERNFHIFYQILSGASEDFLCKLKLERDFSRYNYLGLDSAKVNGVDDAANFRTVRNAMQIVGFMD 269
Cdd:cd14918    166 ETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAIDILGFTP 245
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  270 HETQSVFEVVAAVLKLGNIEFKPESRvnglDESKIKDKNELKE-ICELTGIDQSVLERAFSFRTVEAKQEKVSTTLNVAQ 348
Cdd:cd14918    246 EEKVSIYKLTGAVMHYGNMKFKQKQR----EEQAEPDGTEVADkAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVQQ 321
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  349 AYYARDALAKNLYSRLFSWLVTRINESIKAQtKVRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKEEQ 428
Cdd:cd14918    322 VYNAVGALAKAVYEKMFLWMVTRINQQLDTK-QPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQ 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  429 EEYIREGIEWTHIEYFNNAIICDLIENNQTGILAMLDEECLRPgTVTDDTFLEKLnqvcathqhFESRMSKCSRFLNDTT 508
Cdd:cd14918    401 EEYKKEGIEWTFIDFGMDLAACIELIEKPLGIFSILEEECMFP-KATDTSFKNKL---------YDQHLGKSANFQKPKV 470
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  509 L---PHSCFRIQHYAGKVMYQVEGFVDKNNDLLYRDLSQAMWKASHSLIKALFP------EGNPAKINLKRP----PTAG 575
Cdd:cd14918    471 VkgkAEAHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFStyasaeADSGAKKGAKKKgssfQTVS 550
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  576 SQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNDALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKMLCKQ 655
Cdd:cd14918    551 ALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNAS 630
                          650       660       670
                   ....*....|....*....|....*....|....*...
gi 2024511160  656 TWPHWRG-PARAGVEVLFNELEIPEEEFSFGRSKIFIR 692
Cdd:cd14918    631 AIPEGQFiDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
MYSc_Myh4 cd14915
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ...
38-692 9.66e-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: 405.27  E-value: 9.66e-128
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160   38 NLKKRFDHNEVYTYIGSVVISINPYRPLPIYTPEKVEEYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITGESGAG 117
Cdd:cd14915      6 NLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESGAG 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  118 KTEASKFVMSYVAAVCGKGAEVNQ----------VKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGG 187
Cdd:cd14915     86 KTVNTKRVIQYFATIAVTGEKKKEeaasgkmqgtLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASA 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  188 VISNYLLEKSRVVKQPRGERNFHIFYQILSGASEDFLCKLKLERDFSRYNYLGLDSAKVNGVDDAANFRTVRNAMQIVGF 267
Cdd:cd14915    166 DIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITTNPYDFAFVSQGEITVPSIDDQEELMATDSAVDILGF 245
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  268 MDHETQSVFEVVAAVLKLGNIEFKPESRvnglDESKIKDKNELKE-ICELTGIDQSVLERAFSFRTVEAKQEKVSTTLNV 346
Cdd:cd14915    246 SADEKVAIYKLTGAVMHYGNMKFKQKQR----EEQAEPDGTEVADkAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQTV 321
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  347 AQAYYARDALAKNLYSRLFSWLVTRINESIKAQtKVRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKE 426
Cdd:cd14915    322 QQVYNSVGALAKAIYEKMFLWMVTRINQQLDTK-QPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  427 EQEEYIREGIEWTHIEYFNNAIICDLIENNQTGILAMLDEECLRPgTVTDDTFLEKLnqvcathqhFESRMSKCSRFLND 506
Cdd:cd14915    401 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFP-KATDTSFKNKL---------YEQHLGKSNNFQKP 470
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  507 TTL---PHSCFRIQHYAGKVMYQVEGFVDKNNDLLYRDLSQAMWKASHSLIKALF-------PEGNPAKINLKRP----P 572
Cdd:cd14915    471 KPAkgkAEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFsggqtaeAEGGGGKKGGKKKgssfQ 550
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  573 TAGSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNDALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKML 652
Cdd:cd14915    551 TVSALFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVL 630
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|.
gi 2024511160  653 CKQTWPHWRG-PARAGVEVLFNELEIPEEEFSFGRSKIFIR 692
Cdd:cd14915    631 NASAIPEGQFiDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
MYSc_Myh13 cd14923
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ...
38-692 9.97e-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: 405.22  E-value: 9.97e-128
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160   38 NLKKRFDHNEVYTYIGSVVISINPYRPLPIYTPEKVEEYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITGESGAG 117
Cdd:cd14923      6 NLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGESGAG 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  118 KTEASKFVMSYVA--AVCGKGAEVNQ-------VKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGGV 188
Cdd:cd14923     86 KTVNTKRVIQYFAtiAVTGDKKKEQQpgkmqgtLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASAD 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  189 ISNYLLEKSRVVKQPRGERNFHIFYQILSGASEDFLCKLKLERDFSRYNYLGLDSAKVNGVDDAANFRTVRNAMQIVGFM 268
Cdd:cd14923    166 IETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLISTNPFDFPFVSQGEVTVASIDDSEELLATDNAIDILGFS 245
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  269 DHETQSVFEVVAAVLKLGNIEFKPESRvnglDESKIKDKNELKEIC-ELTGIDQSVLERAFSFRTVEAKQEKVSTTLNVA 347
Cdd:cd14923    246 SEEKVGIYKLTGAVMHYGNMKFKQKQR----EEQAEPDGTEVADKAgYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQNVQ 321
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  348 QAYYARDALAKNLYSRLFSWLVTRINESIKAQtKVRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKEE 427
Cdd:cd14923    322 QVTNSVGALAKAVYEKMFLWMVTRINQQLDTK-QPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLE 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  428 QEEYIREGIEWTHIEYFNNAIICDLIENNQTGILAMLDEECLRPgTVTDDTFLEKLnqvcathqhFESRMSKCSRFLNDT 507
Cdd:cd14923    401 QEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFP-KATDTSFKNKL---------YDQHLGKSNNFQKPK 470
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  508 TL---PHSCFRIQHYAGKVMYQVEGFVDKNNDLLYRDLSQAMWKASHSLIKALFP--------EGNPAKINLKRP----P 572
Cdd:cd14923    471 PAkgkAEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSnyagaeagDSGGSKKGGKKKgssfQ 550
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  573 TAGSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNDALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKML 652
Cdd:cd14923    551 TVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRIL 630
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|.
gi 2024511160  653 CKQTWPHWRG-PARAGVEVLFNELEIPEEEFSFGRSKIFIR 692
Cdd:cd14923    631 NASAIPEGQFiDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
MYSc_Myh2_mammals cd14912
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ...
38-692 2.85e-127

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: 404.11  E-value: 2.85e-127
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160   38 NLKKRFDHNEVYTYIGSVVISINPYRPLPIYTPEKVEEYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITGESGAG 117
Cdd:cd14912      6 NLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESGAG 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  118 KTEASKFVMSYVAAVCGKGAEVNQ----------VKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGG 187
Cdd:cd14912     86 KTVNTKRVIQYFATIAVTGEKKKEeitsgkmqgtLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLASA 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  188 VISNYLLEKSRVVKQPRGERNFHIFYQILSGASEDFLCKLKLERDFSRYNYLGLDSAKVNGVDDAANFRTVRNAMQIVGF 267
Cdd:cd14912    166 DIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSAIDILGF 245
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  268 MDHETQSVFEVVAAVLKLGNIEFKPESRvnglDESKIKDKNELKE-ICELTGIDQSVLERAFSFRTVEAKQEKVSTTLNV 346
Cdd:cd14912    246 TNEEKVSIYKLTGAVMHYGNLKFKQKQR----EEQAEPDGTEVADkAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTV 321
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  347 AQAYYARDALAKNLYSRLFSWLVTRINESIKAQtKVRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKE 426
Cdd:cd14912    322 EQVTNAVGALAKAVYEKMFLWMVARINQQLDTK-QPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  427 EQEEYIREGIEWTHIEYFNNAIICDLIENNQTGILAMLDEECLRPgTVTDDTFLEKLnqvcathqhFESRMSKCSRFLND 506
Cdd:cd14912    401 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFP-KATDTSFKNKL---------YEQHLGKSANFQKP 470
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  507 TTL---PHSCFRIQHYAGKVMYQVEGFVDKNNDLLYRDLSQAMWKASHSLIKALFP---------EGNPAKINLKRP--- 571
Cdd:cd14912    471 KVVkgkAEAHFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSgaqtaegasAGGGAKKGGKKKgss 550
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  572 -PTAGSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNDALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYK 650
Cdd:cd14912    551 fQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYK 630
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|...
gi 2024511160  651 MLCKQTWPHWRG-PARAGVEVLFNELEIPEEEFSFGRSKIFIR 692
Cdd:cd14912    631 VLNASAIPEGQFiDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
MYSc_Myh1_mammals cd14910
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ...
38-692 3.28e-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: 404.11  E-value: 3.28e-127
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160   38 NLKKRFDHNEVYTYIGSVVISINPYRPLPIYTPEKVEEYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITGESGAG 117
Cdd:cd14910      6 NLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESGAG 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  118 KTEASKFVMSYVA--AVCG--KGAEVNQ------VKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGG 187
Cdd:cd14910     86 KTVNTKRVIQYFAtiAVTGekKKEEATSgkmqgtLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLASA 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  188 VISNYLLEKSRVVKQPRGERNFHIFYQILSGASEDFLCKLKLERDFSRYNYLGLDSAKVNGVDDAANFRTVRNAMQIVGF 267
Cdd:cd14910    166 DIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAIEILGF 245
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  268 MDHETQSVFEVVAAVLKLGNIEFKPESRvnglDESKIKDKNELKE-ICELTGIDQSVLERAFSFRTVEAKQEKVSTTLNV 346
Cdd:cd14910    246 TSDERVSIYKLTGAVMHYGNMKFKQKQR----EEQAEPDGTEVADkAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQTV 321
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  347 AQAYYARDALAKNLYSRLFSWLVTRINESIKAQtKVRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKE 426
Cdd:cd14910    322 QQVYNAVGALAKAVYDKMFLWMVTRINQQLDTK-QPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  427 EQEEYIREGIEWTHIEYFNNAIICDLIENNQTGILAMLDEECLRPgTVTDDTFLEKLnqvcathqhFESRMSKCSRFLND 506
Cdd:cd14910    401 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFP-KATDTSFKNKL---------YEQHLGKSNNFQKP 470
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  507 TTLP---HSCFRIQHYAGKVMYQVEGFVDKNNDLLYRDLSQAMWKASHSLIKALFPEGNPAKINLKRPPTAGSQ------ 577
Cdd:cd14910    471 KPAKgkvEAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGAAAAEAEEGGGKKGGKKkgssfq 550
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  578 -----FKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNDALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKML 652
Cdd:cd14910    551 tvsalFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVL 630
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|.
gi 2024511160  653 CKQTWPHWRG-PARAGVEVLFNELEIPEEEFSFGRSKIFIR 692
Cdd:cd14910    631 NASAIPEGQFiDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
MYSc_Myo25 cd14886
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ...
36-692 4.41e-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: 397.72  E-value: 4.41e-125
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160   36 INNLKKRFDHNEVYTYIGSVVISINPYRPLP-IYTPEKVEEYR----NRNF-YELSPHIFALSDEAYRSLRDQDKDQCIL 109
Cdd:cd14886      4 IDILRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRqadtSRGFpSDLPPHSYAVAQSALNGLISDGISQSCI 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  110 ITGESGAGKTEASKFVMSYVAAvcGKGAEVNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGGVI 189
Cdd:cd14886     84 VSGESGAGKTETAKQLMNFFAY--GHSTSSTDVQSLILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGPDGGLKGGKI 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  190 SNYLLEKSRVVKQPRGERNFHIFYQILSGASEDFLCKLKLeRDFSRYNYL-GLDSAKVNGVDDAANFRTVRNAMQIVgFM 268
Cdd:cd14886    162 TSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGF-KSLESYNFLnASKCYDAPGIDDQKEFAPVRSQLEKL-FS 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  269 DHETQSVFEVVAAVLKLGNIEFKPESRVNGLDESKIKDKNELKEICELTGIDQSVLERAFSFRTVEAKQEKVSTTLNVAQ 348
Cdd:cd14886    240 KNEIDSFYKCISGILLAGNIEFSEEGDMGVINAAKISNDEDFGKMCELLGIESSKAAQAIITKVVVINNETIISPVTQAQ 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  349 AYYARDALAKNLYSRLFSWLVTRINESIKAQTkVRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKEEQ 428
Cdd:cd14886    320 AEVNIRAVAKDLYGALFELCVDTLNEIIQFDA-DARPWIGILDIYGFEFFERNTYEQLLINYANERLQQYFINQVFKSEI 398
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  429 EEYIREGIEWTHIEYFNNAIICDLIENNQTGILAMLDEECL-RPGTVtddtflEKLNQVCATHQHFESRMSKCSRFLNdt 507
Cdd:cd14886    399 QEYEIEGIDHSMITFTDNSNVLAVFDKPNLSIFSFLEEQCLiQTGSS------EKFTSSCKSKIKNNSFIPGKGSQCN-- 470
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  508 tlphscFRIQHYAGKVMYQVEGFVDKNNDLLYRDLSQAMWKASHSLIKALFpEGNPAKINLKRPPTAGSQFKASVATLMK 587
Cdd:cd14886    471 ------FTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNKAF-SDIPNEDGNMKGKFLGSTFQLSIDQLMK 543
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  588 NLQTKNPNYIRCIKPNDKKAAHIFNDALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKMLCKQTWPHWRGPA--R 665
Cdd:cd14886    544 TLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFFHRNKILISHNSSSQNAGEdlV 623
                          650       660
                   ....*....|....*....|....*..
gi 2024511160  666 AGVEVLFNELEIPEEEFSFGRSKIFIR 692
Cdd:cd14886    624 EAVKSILENLGIPCSDYRIGKTKVFLR 650
MYSc_Myo38 cd14899
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ...
34-668 3.72e-120

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: 386.76  E-value: 3.72e-120
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160   34 SFINNLKKRFDHNEVYTYIGSVVISINPYRPLP-IYTPEKVEEY---RNRNFYE-------LSPHIFALSDEAYRSLRDQ 102
Cdd:cd14899      2 SILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYaydHNSQFGDrvtstdpREPHLFAVARAAYIDIVQN 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  103 DKDQCILITGESGAGKTEASKFVMSYVAAVCGKGAEVNQ---------------VKEQLLQSNPVLEAFGNAKTVRNDNS 167
Cdd:cd14899     82 GRSQSILISGESGAGKTEATKIIMTYFAVHCGTGNNNLTnsesisppaspsrttIEEQVLQSNPILEAFGNARTVRNDNS 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  168 SRFGKYMDIEF-DFKGDPLGGVISNYLLEKSRVVKQPRGERNFHIFYQILSGaseDFLCKLKLER----------DFSRY 236
Cdd:cd14899    162 SRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSA---DNNCVSKEQKqvlalsggpqSFRLL 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  237 NYlGLDSAKVNGVDDAANFRTVRNAMQIVGFMDHETQSVFEVVAAVLKLGNIEFK--PESRVNGL--DESKIKDK----- 307
Cdd:cd14899    239 NQ-SLCSKRRDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEqiPHKGDDTVfaDEARVMSSttgaf 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  308 NELKEICELTGIDQSVLERAFSFRTVEAKQEKVSTTLNVAQAYYARDALAKNLYSRLFSWLVTRINESIKAQTKV----- 382
Cdd:cd14899    318 DHFTKAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLQRQASApwgad 397
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  383 ---------RKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKEEQEEYIREGIEWTHIEYFNNAIICDLI 453
Cdd:cd14899    398 esdvddeedATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFPNNRACLELF 477
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  454 ENNQTGILAMLDEECLRPGTvTDDTFLEKLN---QVCATHQHFESrmskcSRFLNDTTLphscFRIQHYAGKVMYQVEGF 530
Cdd:cd14899    478 EHRPIGIFSLTDQECVFPQG-TDRALVAKYYlefEKKNSHPHFRS-----APLIQRTTQ----FVVAHYAGCVTYTIDGF 547
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  531 VDKNNDLLYRDLSQAMWKASHSLIKALFPEGNPAKINLKRPP------------------TAGSQFKASVATLMKNLQTK 592
Cdd:cd14899    548 LAKNKDSFCESAAQLLAGSSNPLIQALAAGSNDEDANGDSELdgfggrtrrraksaiaavSVGTQFKIQLNELLSTVRAT 627
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  593 NPNYIRCIKPNDKKAAHIFNDALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKM----LCKQTWPHWRGPARAGV 668
Cdd:cd14899    628 TPRYVRCIKPNDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRYRRvllsLYKWGDNDFERQMRCGV 707
MYSc_Myo17 cd14879
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ...
30-710 2.58e-117

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: 376.89  E-value: 2.58e-117
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160   30 LNEDSFINNLKKRFDHNEVYTYIGS-VVISINPYRPLPIYTPEKVEEYRNRNFYELS-------PHIFALSDEAYRSLRD 101
Cdd:cd14879      1 PSDDAITSHLASRFRSDLPYTRLGSsALVAVNPYKYLSSNSDASLGEYGSEYYDTTSgskeplpPHAYDLAARAYLRMRR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  102 QDKDQCILITGESGAGKTEASKFVMSYV---AAVCGKGAevnQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEF 178
Cdd:cd14879     81 RSEDQAVVFLGETGSGKSESRRLLLRQLlrlSSHSKKGT---KLSSQISAAEFVLDSFGNAKTLTNPNASRFGRYTELQF 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  179 DFKGDPLGGVISNYLLEKSRVVKQPRGERNFHIFYQILSGASEDflcklklERDfsrynYLGLD---------------- 242
Cdd:cd14879    158 NERGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPE-------ERQ-----HLGLDdpsdyallasygchpl 225
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  243 SAKVnGVDDAANFRTVRNAMQIVGFMDHETQSVFEVVAAVLKLGNIEFKpESRVNGLDESKIKDKNELKEICELTGIDQS 322
Cdd:cd14879    226 PLGP-GSDDAEGFQELKTALKTLGFKRKHVAQICQLLAAILHLGNLEFT-YDHEGGEESAVVKNTDVLDIVAAFLGVSPE 303
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  323 VLERAFSFRTVEAKQEKVSTTLNVAQAYYARDALAKNLYSRLFSWLVTRINESIKAQTKVRKKVMGVLDIYGFEIF---E 399
Cdd:cd14879    304 DLETSLTYKTKLVRKELCTVFLDPEGAAAQRDELARTLYSLLFAWVVETINQKLCAPEDDFATFISLLDFPGFQNRsstG 383
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  400 DNSFEQFIINYCNEKLQQIFIELTLKEEQEEYIREGIEWTHIEYFNNAIICDLIENNQTGILAMLDEECLRPGTVTDDTF 479
Cdd:cd14879    384 GNSLDQFCVNFANERLHNYVLRSFFERKAEELEAEGVSVPATSYFDNSDCVRLLRGKPGGLLGILDDQTRRMPKKTDEQM 463
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  480 LEKLNQVCATHQHFESRMSKCSRflNDttlpHSCFRIQHYAGKVMYQVEGFVDKNNDLLyrdlsqamwkashslikalfp 559
Cdd:cd14879    464 LEALRKRFGNHSSFIAVGNFATR--SG----SASFTVNHYAGEVTYSVEGFLERNGDVL--------------------- 516
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  560 egNPAKINLKRPPTagsQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNDALVCHQIRYLGLLENVRVRRAGYAFR 639
Cdd:cd14879    517 --SPDFVNLLRGAT---QLNAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQIRSLGLPELAARLRVEYVVS 591
                          650       660       670       680       690       700       710
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024511160  640 QAYEPCLERYKMlckqtWPHWRGPARAGVEVLFNeLEIPEEEFSFGRSKIFirnprtlfkLEDLRKQRLED 710
Cdd:cd14879    592 LEHAEFCERYKS-----TLRGSAAERIRQCARAN-GWWEGRDYVLGNTKVF---------LSYAAWRMLED 647
MYSc_Myo13 cd14875
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ...
39-692 5.11e-116

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: 373.76  E-value: 5.11e-116
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160   39 LKKRFDH-NEVYTYIGSVVISINPYRPLPIYTPEKVEEYRNR-NFYELSPHIFALSDEAYRSLRDQDKD-QCILITGESG 115
Cdd:cd14875      7 IKERFEKlHQQYSLMGEMVLSVNPFRLMPFNSEEERKKYLALpDPRLLPPHIWQVAHKAFNAIFVQGLGnQSVVISGESG 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  116 AGKTEASKFVMSYVAAV-CGKGAEVNQ------VKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFD-FKGDPLGG 187
Cdd:cd14875     87 SGKTENAKMLIAYLGQLsYMHSSNTSQrsiadkIDENLKWSNPVMESFGNARTVRNDNSSRFGKYIKLYFDpTSGVMVGG 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  188 VISNYLLEKSRVVKQPRGERNFHIFYQILSGASED---FLCKLKLERDFSRYNylGLDSAKVNGVD-----DAANFRTVR 259
Cdd:cd14875    167 QTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEekkELGGLKTAQDYKCLN--GGNTFVRRGVDgktldDAHEFQNVR 244
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  260 NAMQIVGFMDHETQSVFEVVAAVLKLGNIEFKPESRvnglDESKIKDKNELKEICELTGIDQSVLERAFsfrTVEAKQEK 339
Cdd:cd14875    245 HALSMIGVELETQNSIFRVLASILHLMEVEFESDQN----DKAQIADETPFLTACRLLQLDPAKLRECF---LVKSKTSL 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  340 VSTTLNVAQAYYARDALAKNLYSRLFSWLVTRINESIKAQTKV-RKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQI 418
Cdd:cd14875    318 VTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNASITPQGDCsGCKYIGLLDIFGFENFTRNSFEQLCINYANESLQNH 397
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  419 FIELTLKEEQEEYIREGIEWTHIEYFNNAIICDLIENNQTGILAMLDEEC-LRPGTVtdDTFleklnqvcaTHQHFESRM 497
Cdd:cd14875    398 YNKYTFINDEEECRREGIQIPKIEFPDNSECVNMFDQKRTGIFSMLDEECnFKGGTT--ERF---------TTNLWDQWA 466
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  498 SKCSRFLN-DTTLPHScFRIQHYAGKVMYQVEGFVDKNNDLLYRDLSQAMWKASHSLIKALFPEGnpaKINLKRPPTAGS 576
Cdd:cd14875    467 NKSPYFVLpKSTIPNQ-FGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTLLSTE---KGLARRKQTVAI 542
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  577 QFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNDALVCHQIRYLGLLENVRVRRAGYAFRQAYEP-CLERYKMLCKQ 655
Cdd:cd14875    543 RFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRRPIEQfCRYFYLIMPRS 622
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|..
gi 2024511160  656 TWPHWR-----GPARAGVEVLFNELEIPEEEFSFGRSKIFIR 692
Cdd:cd14875    623 TASLFKqekysEAAKDFLAYYQRLYGWAKPNYAVGKTKVFLR 664
MYSc_Myo16 cd14878
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ...
34-652 7.14e-107

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: 349.11  E-value: 7.14e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160   34 SFINNLKKRFDHNEVYTYIGSVVISINPYRPLPIYTPEKVEEYRN---RNFYELSPHIFALSDEAYRSLRDQDKDQCILI 110
Cdd:cd14878      2 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYLSssgQLCSSLPPHLFSCAERAFHQLFQERRPQCFIL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  111 TGESGAGKTEASKFVMSYVAavCGKGAEVNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEF-DFKGDPLGGVI 189
Cdd:cd14878     82 SGERGSGKTEASKQIMKHLT--CRASSSRTTFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFcERKKHLTGARI 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  190 SNYLLEKSRVVKQPRGERNFHIFYQILSGASEDFLCKLKLeRDFSRYNYLGL----DSAKVNGVDDAANFRTVRNAMQIV 265
Cdd:cd14878    160 YTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHL-NNLCAHRYLNQtmreDVSTAERSLNREKLAVLKQALNVV 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  266 GFMDHETQSVFEVVAAVLKLGNIEFkpeSRVNGLDESKIKDKNELKEICELTGIDQSVLERAFSFRTVEAKQEKVSTTLN 345
Cdd:cd14878    239 GFSSLEVENLFVILSAILHLGDIRF---TALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHT 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  346 VAQAYYARDALAKNLYSRLFSWLVTRINESIKAQ---TKVRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIEL 422
Cdd:cd14878    316 IQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLQSQdeqKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEV 395
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  423 TLKEEQEEYIREGIEW-THIEYFNNAIICDLIENNQTGILAMLDEEC--LRPGTVTDDTFLEKLNQVCATHQHFESrmsk 499
Cdd:cd14878    396 LFLQEQTECVQEGVTMeTAYSPGNQTGVLDFFFQKPSGFLSLLDEESqmIWSVEPNLPKKLQSLLESSNTNAVYSP---- 471
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  500 cSRFLNDTTLPH---SCFRIQHYAGKVMYQVEGFVDKNNDLLYRDLSQAMWKASHSLIKALFPegnpakinlKRPPTAGS 576
Cdd:cd14878    472 -MKDGNGNVALKdqgTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQ---------SKLVTIAS 541
                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024511160  577 QFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNDALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKML 652
Cdd:cd14878    542 QLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPL 617
MYSc_Myo26 cd14887
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ...
36-692 2.54e-99

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: 330.84  E-value: 2.54e-99
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160   36 INNLKKRF--------DHNEVYTYIGSVVISINPYRPLPIYTPEKVEEYRNRNFYELSPHIFALSDEAYRSLRDQDKDQC 107
Cdd:cd14887      4 LENLYQRYnkayinkeNRNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRRSQS 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  108 ILITGESGAGKTEASKFVMSYVAAVCG--KGAEVNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPL 185
Cdd:cd14887     84 ILISGESGAGKTETSKHVLTYLAAVSDrrHGADSQGLEARLLQSGPVLEAFGNAHTVLNANSSRFGKMLLLHFTGRGKLT 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  186 GGVISNYLLEKSRVVKQPRGERNFHIFYQILSGAsedflcklKLERDFsrynylglDSAKVNGVDDAANFRTVRNAMQIV 265
Cdd:cd14887    164 RASVATYLLANERVVRIPSDEFSFHIFYALCNAA--------VAAATQ--------KSSAGEGDPESTDLRRITAAMKTV 227
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  266 GFMDHETQSVFEVVAAVLKLGNIEF-----KPESRVNGLDESKI------KDKNELKEI-CELTGIDQS--------VLE 325
Cdd:cd14887    228 GIGGGEQADIFKLLAAILHLGNVEFttdqePETSKKRKLTSVSVgceetaADRSHSSEVkCLSSGLKVTeasrkhlkTVA 307
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  326 RAFSFRTVEAKQEKVSTTL------------NVAQAYYARDALAKNLYSRLFSWLVTRINESIK-----------AQTKV 382
Cdd:cd14887    308 RLLGLPPGVEGEEMLRLALvsrsvretrsffDLDGAAAARDAACKNLYSRAFDAVVARINAGLQrsakpsesdsdEDTPS 387
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  383 RKKV--MGVLDIYGFEIFED---NSFEQFIINYCNEKLQQIFIELTLKEEQEEYIREGIEWTHIEY---FNNAIICDLIE 454
Cdd:cd14887    388 TTGTqtIGILDLFGFEDLRNhskNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGVFQNQDCSafpFSFPLASTLTS 467
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  455 NNQT-----------------------GILAMLDEECL-----RPGTVTDDTFLEKLNQVCATHQHFESRMSKCSRflnd 506
Cdd:cd14887    468 SPSStspfsptpsfrsssafatspslpSSLSSLSSSLSssppvWEGRDNSDLFYEKLNKNIINSAKYKNITPALSR---- 543
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  507 ttlPHSCFRIQHYAGKVMYQVEGFVDKNNDLLYRDLSQAMWKASHSLIKALFPEGNPAKINLKRPPTAGSQFKASVATLM 586
Cdd:cd14887    544 ---ENLEFTVSHFACDVTYDARDFCRANREATSDELERLFLACSTYTRLVGSKKNSGVRAISSRRSTLSAQFASQLQQVL 620
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  587 KNLQTKNPNYIRCIKPNDKKAAHIFNDALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKMLCKQTWPHWRGPARA 666
Cdd:cd14887    621 KALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVELWRRYETKLPMALREALTPKMF 700
                          730       740
                   ....*....|....*....|....*.
gi 2024511160  667 GVEVLFnELEIPEEEFSFGRSKIFIR 692
Cdd:cd14887    701 CKIVLM-FLEINSNSYTFGKTKIFFR 725
MYSc_Myo24A cd14937
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ...
36-642 3.19e-98

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: 325.05  E-value: 3.19e-98
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160   36 INNLKKRFDHNEVYTYIGSVVISINPYRPLPIytpeKVEEYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITGESG 115
Cdd:cd14937      4 LNMLALRYKKNYIYTIAEPMLISINPYQVIDV----DINEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISGESG 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  116 AGKTEASKFVMS-YVAAVcgkgAEVNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGGVISNYLL 194
Cdd:cd14937     80 SGKTEASKLVIKyYLSGV----KEDNEISNTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIVSSSIEIFLL 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  195 EKSRVVKQPRGERNFHIFYQILSGASEDFLCKLKLeRDFSRYNYLGLDSAKVNGVDDAANFRTVRNAMQIVGFMDHEtQS 274
Cdd:cd14937    156 ENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKI-RSENEYKYIVNKNVVIPEIDDAKDFGNLMISFDKMNMHDMK-DD 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  275 VFEVVAAVLKLGNIEFKPESRVNGLDESKIKDKN--ELKEICELTGIDQSVLERAFSFRTVEAKQEKVSTTLNVAQAYYA 352
Cdd:cd14937    234 LFLTLSGLLLLGNVEYQEIEKGGKTNCSELDKNNleLVNEISNLLGINYENLKDCLVFTEKTIANQKIEIPLSVEESVSI 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  353 RDALAKNLYSRLFSWLVTRINESIKaQTKVRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKEEQEEYI 432
Cdd:cd14937    314 CKSISKDLYNKIFSYITKRINNFLN-NNKELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIHSIYLYIVYEKETELYK 392
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  433 REGIEWTHIEYFNNAIICDLIENNqTGILAMLDEECLRPGTvTDDTFLEKLNQVCATHQHFesrmSKCSRFLNDTtlphs 512
Cdd:cd14937    393 AEDILIESVKYTTNESIIDLLRGK-TSIISILEDSCLGPVK-NDESIVSVYTNKFSKHEKY----ASTKKDINKN----- 461
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  513 cFRIQHYAGKVMYQVEGFVDKNNDLLYRDLSQAMWKASHSLIKALFPEGNPAKiNLKRPPTAGSQFKASVATLMKNLQTK 592
Cdd:cd14937    462 -FVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDVEVSE-SLGRKNLITFKYLKNLNNIISYLKST 539
                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|
gi 2024511160  593 NPNYIRCIKPNDKKAAHIFNDALVCHQIRYLGLLENVRVRragYAFRQAY 642
Cdd:cd14937    540 NIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNIS---FFFQYKY 586
MYSc_Myo37 cd14898
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ...
33-652 1.77e-93

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: 310.29  E-value: 1.77e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160   33 DSFINNLKKRFDHNEVYTYIGSVVISINPYRPlpIYTPEKVEEYRnRNFYELSPHIFALSDEAYRSLRDQDkDQCILITG 112
Cdd:cd14898      1 NATLEILEKRYASGKIYTKSGLVFLALNPYET--IYGAGAMKAYL-KNYSHVEPHVYDVAEASVQDLLVHG-NQTIVISG 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  113 ESGAGKTEASKFVMSYVAAvcgKGAEVNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDfkGDPLGGVISNY 192
Cdd:cd14898     77 ESGSGKTENAKLVIKYLVE---RTASTTSIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKFD--GKITGAKFETY 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  193 LLEKSRVVKQPRGERNFHIFYQILsgASEDFlcklKLERDFSRYNYLGLDsaKVNGVDDAANFRTVRNAMQIVGFMDheT 272
Cdd:cd14898    152 LLEKSRVTHHEKGERNFHIFYQFC--ASKRL----NIKNDFIDTSSTAGN--KESIVQLSEKYKMTCSAMKSLGIAN--F 221
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  273 QSVFEVVAAVLKLGNIEFKPESRVngldesKIKDKNELKEICELTGIDQSVLERAFSFRTVEAKQEKVSTTLNVAQAYYA 352
Cdd:cd14898    222 KSIEDCLLGILYLGSIQFVNDGIL------KLQRNESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIEVFNTLKQARTI 295
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  353 RDALAKNLYSRLFSWLVTRINESIKAQTKvrkKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKEEQEEYI 432
Cdd:cd14898    296 RNSMARLLYSNVFNYITASINNCLEGSGE---RSISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMFRAKQGMYK 372
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  433 REGIEWTHIEYFNNAIICDLIEnNQTGILAMLDEECLRP-GTVtddtfleklnqvcathqhfESRMSKCSRFLND--TTL 509
Cdd:cd14898    373 EEGIEWPDVEFFDNNQCIRDFE-KPCGLMDLISEESFNAwGNV-------------------KNLLVKIKKYLNGfiNTK 432
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  510 PHSCFRIQHYAGKVMYQVEGFVDKNND----LLYRDLSQAMWKASHSLIKalfpegnpakinlkrpptagsQFKASVATL 585
Cdd:cd14898    433 ARDKIKVSHYAGDVEYDLRDFLDKNREkgqlLIFKNLLINDEGSKEDLVK---------------------YFKDSMNKL 491
                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024511160  586 MKNLQTKNPNYIRCIKPNDKKAAHIFNDALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKML 652
Cdd:cd14898    492 LNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRIL 558
MYSc_Myo20 cd14881
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ...
33-653 2.73e-91

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: 306.27  E-value: 2.73e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160   33 DSFINNLKKRFDHNEVYTYIGSVVISINPYR----PLPIYTPEKVEeyrnrnfyeLSPHIFALSDEAYRSLRDQDKDQCI 108
Cdd:cd14881      1 DAVMKCLQARFYAKEFFTNVGPILLSVNPYRdvgnPLTLTSTRSSP---------LAPQLLKVVQEAVRQQSETGYPQAI 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  109 LITGESGAGKTEASKFVMSYVAAVCGKGAEVNQVKeQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDfKGDPLGGV 188
Cdd:cd14881     72 ILSGTSGSGKTYASMLLLRQLFDVAGGGPETDAFK-HLAAAFTVLRSLGSAKTATNSESSRIGHFIEVQVT-DGALYRTK 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  189 ISNYLLEKSRVVKQPRGERNFHIFYQILSGASEDFLCKLKLErDFSRYN--YLGLDSAKVNGVDDAANFRTVRNAMQIVG 266
Cdd:cd14881    150 IHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLD-GYSPANlrYLSHGDTRQNEAEDAARFQAWKACLGILG 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  267 --FMDhetqsVFEVVAAVLKLGNIEFkpeSRVNGLDESkIKDKNELKEICELTGIDQSVLERAFSFRTVEAKQEKVSTTL 344
Cdd:cd14881    229 ipFLD-----VVRVLAAVLLLGNVQF---IDGGGLEVD-VKGETELKSVAALLGVSGAALFRGLTTRTHNARGQLVKSVC 299
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  345 NVAQAYYARDALAKNLYSRLFSWLVTRINeSIK-----AQTKVRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIF 419
Cdd:cd14881    300 DANMSNMTRDALAKALYCRTVATIVRRAN-SLKrlgstLGTHATDGFIGILDMFGFEDPKPSQLEHLCINLCAETMQHFY 378
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  420 IELTLKEEQEEYIREGIEW-THIEYFNNAIICDLIENNQTGILAMLDEECLRPGTVtdDTFLEKLNqvcATHQH----FE 494
Cdd:cd14881    379 NTHIFKSSIESCRDEGIQCeVEVDYVDNVPCIDLISSLRTGLLSMLDVECSPRGTA--ESYVAKIK---VQHRQnprlFE 453
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  495 SRMSKCSRFLndttlphscfrIQHYAGKVMYQVEGFVDKNNDLLYRDLSQAMWKASHSLIKAlfpegnpakinlkrppTA 574
Cdd:cd14881    454 AKPQDDRMFG-----------IRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYKQNCNFGFA----------------TH 506
                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024511160  575 GSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNDALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKMLC 653
Cdd:cd14881    507 TQDFHTRLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAGGYPHRMRFKAFNARYRLLA 585
MYSc_Myo44 cd14905
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ...
33-652 8.93e-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: 295.08  E-value: 8.93e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160   33 DSFINNLKKRFDHNEVYTYIGSVVISINPYRPLP-IYTPEKVEEYRNRNfyELSPHIFALSDEAYRSLRDQDKDQCILIT 111
Cdd:cd14905      1 DTLINIIQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNYNQRR--GLPPHLFALAAKAISDMQDFRRDQLIFIG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  112 GESGAGKTEASKFVMSYVAAVcgKGAEVNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGGVISN 191
Cdd:cd14905     79 GESGSGKSENTKIIIQYLLTT--DLSRSKYLRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQGAKLYS 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  192 YLLEKSRVVKQPRGERNFHIFYQILSGASEDFLCKLKLErDFSRYNYLGL-DSAKVNGVDDAANFRTVRNAMQIVGFMDH 270
Cdd:cd14905    157 YFLDENRVTYQNKGERNFHIFYQFLKGITDEEKAAYQLG-DINSYHYLNQgGSISVESIDDNRVFDRLKMSFVFFDFPSE 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  271 ETQSVFEVVAAVLKLGNIEFKPEsrvNGldESKIKDKNELKEICELTGIDQSVLERAFSfrtveakqekVSTTLNVAQAY 350
Cdd:cd14905    236 KIDLIFKTLSFIIILGNVTFFQK---NG--KTEVKDRTLIESLSHNITFDSTKLENILI----------SDRSMPVNEAV 300
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  351 YARDALAKNLYSRLFSWLVTRINESIKAQTkvRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKEEQEE 430
Cdd:cd14905    301 ENRDSLARSLYSALFHWIIDFLNSKLKPTQ--YSHTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVLKQEQRE 378
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  431 YIREGIEW-THIEYFNNAIICDLIENnqtgILAMLDEECLRPGTvTDDTFLEKLNQVCATHQHFESRMSKcsrflndttl 509
Cdd:cd14905    379 YQTERIPWmTPISFKDNEESVEMMEK----IINLLDQESKNINS-SDQIFLEKLQNFLSRHHLFGKKPNK---------- 443
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  510 phscFRIQHYAGKVMYQVEGFVDKNND-LLYR---------------------------------DLSQAMWKASHSLIK 555
Cdd:cd14905    444 ----FGIEHYFGQFYYDVRGFIIKNRDeILQRtnvlhknsitkylfsrdgvfninatvaelnqmfDAKNTAKKSPLSIVK 519
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  556 ALFPEGNPAKINLKRPP-----------------TAGSQFKASVATlmkNLQTKNPN----YIRCIKPNDKKAAHIFNDA 614
Cdd:cd14905    520 VLLSCGSNNPNNVNNPNnnsgggggggnsgggsgSGGSTYTTYSST---NKAINNSNcdfhFIRCIKPNSKKTHLTFDVK 596
                          650       660       670
                   ....*....|....*....|....*....|....*...
gi 2024511160  615 LVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKML 652
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 ...
34-650 1.67e-79

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


Pssm-ID: 276850 [Multi-domain]  Cd Length: 685  Bit Score: 274.86  E-value: 1.67e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160   34 SFINNLKKRFDHNEVYTYIGSVVISINPYRPLP-IYTPEKVEEY----RNRNFYE---LSPHIFALSDEAYRSLRDQDKD 105
Cdd:cd14884      2 NVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYlhkkSNSAASAapfPKAHIYDIANMAYKNMRGKLKR 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  106 QCILITGESGAGKTEASKFVMSYVAAVCGKgAEVNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFD------ 179
Cdd:cd14884     82 QTIVVSGHSGSGKTENCKFLFKYFHYIQTD-SQMTERIDKLIYINNILESMSNATTIKNNNSSRCGRINLLIFEeventq 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  180 ---FKGDPLGGVISNYLLEKSRVVKQPRGERNFHIFYQILSGASEDFLCKLKLERDFSRYNYL----------------- 239
Cdd:cd14884    161 knmFNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGLSDEDLARRNLVRNCGVYGLLnpdeshqkrsvkgtlrl 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  240 ---GLDSAKVNGVDDAANFRTVRNAMQIVGFMDHETQSVFEVVAAVLKLGNiefkpesrvngldeskikdkNELKEICEL 316
Cdd:cd14884    241 gsdSLDPSEEEKAKDEKNFVALLHGLHYIKYDERQINEFFDIIAGILHLGN--------------------RAYKAAAEC 300
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  317 TGIDQSVLERAFSFRTVEAKQEKVSTTLNVAQAYYARDALAKNLYSRLFSWLVTRIN----------ESIKAQT-KVRKK 385
Cdd:cd14884    301 LQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINrnvlkckekdESDNEDIySINEA 380
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  386 VMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKEEQEEYIREGIEWTHIE---YFNNAIICDLIENNQTGILA 462
Cdd:cd14884    381 IISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDVapsYSDTLIFIAKIFRRLDDITK 460
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  463 MLDEECLRpgtvTDDTFLEKLNQVCATHQHFESRMS-KCSRFLNDTT-----LPHSCFRIQHYAGKVMYQVEGFVDKNND 536
Cdd:cd14884    461 LKNQGQKK----TDDHFFRYLLNNERQQQLEGKVSYgFVLNHDADGTakkqnIKKNIFFIRHYAGLVTYRINNWIDKNSD 536
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  537 LLYRDLSQAMWKASHSLIKALFPEGNPAKINlkrppTAGSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNDALV 616
Cdd:cd14884    537 KIETSIETLISCSSNRFLREANNGGNKGNFL-----SVSKKYIKELDNLFTQLQSTDMYYIRCFLPNAKMLPNTFKRLLV 611
                          650       660       670
                   ....*....|....*....|....*....|....
gi 2024511160  617 CHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYK 650
Cdd:cd14884    612 YRQLKQCGSNEMIKILNRGLSHKIPKKETAAALK 645
MYSc_Myo32 cd14893
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ...
39-691 4.93e-78

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: 272.23  E-value: 4.93e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160   39 LKKRFDHNEVYTYIGSVVISINPYRPLPIYTPEKVEEYRNRN----FYELS------PHIFALSDEAYRSLRDQDKDQCI 108
Cdd:cd14893      7 LRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSReqtpLYEKDtvndapPHVFALAQNALRCMQDAGEDQAV 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  109 LITGESGAGKTEASKFVMSYVAAVcGKGAE-----------VNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIE 177
Cdd:cd14893     87 ILLGGMGAGKSEAAKLIVQYLCEI-GDETEprpdsegasgvLHPIGQQILHAFTILEAFGNAATRQNRNSSRFAKMISVE 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  178 FDFKGDPLGGVISNYLLEKSRVVKQPRGERNFHIFYQILSGASEDFLCKLKLERDFSRYNYLGLDSAK---VNGVDDAAN 254
Cdd:cd14893    166 FSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQHDPTLRDSLEMNKCVNEFVMLKQADplaTNFALDARD 245
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  255 FRTVRNAMQIVGFMDHETQSVFEVVAAVLKLGNIEFKPE----SRVNGLDESKI--------KDKNELKEICELTGIDQS 322
Cdd:cd14893    246 YRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFVPDpeggKSVGGANSTTVsdaqscalKDPAQILLAAKLLEVEPV 325
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  323 VLERAFSFRTVEAKQ--EKVST--TLNVAQAYYARDALAKNLYSRLFSWLVTRINESI--------KAQTKVRKKVMGVL 390
Cdd:cd14893    326 VLDNYFRTRQFFSKDgnKTVSSlkVVTVHQARKARDTFVRSLYESLFNFLVETLNGILggifdryeKSNIVINSQGVHVL 405
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  391 DIYGFEIFED--NSFEQFIINYCNEKLQQIFIELTL---------KEEQEE---YIREGIEWTHIEyfNNAIicDLIENN 456
Cdd:cd14893    406 DMVGFENLTPsqNSFDQLCFNYWSEKVHHFYVQNTLainfsfledESQQVEnrlTVNSNVDITSEQ--EKCL--QLFEDK 481
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  457 QTGILAMLDEEClRPGTVTDDTFLEKLNQVCATHQHFeSRMSKCSRFLNDTTLPHS----CFRIQHYAGKVMYQVEGFVD 532
Cdd:cd14893    482 PFGIFDLLTENC-KVRLPNDEDFVNKLFSGNEAVGGL-SRPNMGADTTNEYLAPSKdwrlLFIVQHHCGKVTYNGKGLSS 559
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  533 KNNDLLYRDLSQAMWKASHSLIKALFP---EGNPAKINLKRPPTAGSQFKASVATLMKNLQTKN---------------- 593
Cdd:cd14893    560 KNMLSISSTCAAIMQSSKNAVLHAVGAaqmAAASSEKAAKQTEERGSTSSKFRKSASSARESKNitdsaatdvynqadal 639
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  594 --------PNYIRCIKPNDKKAAHIFNDALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKMLCKQtwphwrgpaR 665
Cdd:cd14893    640 lhalnhtgKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRYKNVCGH---------R 710
                          730       740       750
                   ....*....|....*....|....*....|
gi 2024511160  666 AGVEVLFNELE----IPEEEFSFGRSKIFI 691
Cdd:cd14893    711 GTLESLLRSLSaigvLEEEKFVVGKTKVYL 740
MYSc_Myo18 cd01386
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ...
34-692 3.10e-75

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: 263.02  E-value: 3.10e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160   34 SFINNLKKRFDHNEVYTYIGSVVISINPYRPLPIYTPEKVEEYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITGE 113
Cdd:cd01386      2 SVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLGR 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  114 SGAGKTEASKFVMSYVAAVcgKGAEVNQVKEQLLQS-NPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGGVISNY 192
Cdd:cd01386     82 SGSGKTTNCRHILEYLVTA--AGSVGGVLSVEKLNAaLTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQLASASIQTL 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  193 LLEKSRVVKQPRGERNFHIFYQILSGASEDFLCKLKLERDFSRYNYLGLDSAKVNGV-DDAANFRTVRNAMQIVGFMDHE 271
Cdd:cd01386    160 LLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLAESNSFGIVPLQKPEDKqKAAAAFSKLQAAMKTLGISEEE 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  272 TQSVFEVVAAVLKLGNIEFKPESRVNgldESKIKDKNELKEICELTGIDQSVLERA--------------FSFRTVEAKQ 337
Cdd:cd01386    240 QRAIWSILAAIYHLGAAGATKAASAG---RKQFARPEWAQRAAYLLGCTLEELSSAifkhhlsggpqqstTSSGQESPAR 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  338 EKVSTTLNVAQAyyARDALAKNLYSRLFSWLVTRINESIKAQTKVRKKVMgVLDIYGFeifeDN----------SFEQFI 407
Cdd:cd01386    317 SSSGGPKLTGVE--ALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSSIT-IVDTPGF----QNpahsgsqrgaTFEDLC 389
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  408 INYCNEKLQQIFIELTLKEEQEEYIREGIEWTHIE-YFNNAIICDLIENNQT--------------GILAMLDEECLRPG 472
Cdd:cd01386    390 HNYAQERLQLLFHERTFVAPLERYKQENVEVDFDLpELSPGALVALIDQAPQqalvrsdlrdedrrGLLWLLDEEALYPG 469
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  473 TvTDDTFLEKLnqvCAthQHFESRMSKCSRFLNDTTLPHScFRIQHYAGK--VMYQVEGFVDK-NNDLLYRDLSQAMwka 549
Cdd:cd01386    470 S-SDDTFLERL---FS--HYGDKEGGKGHSLLRRSEGPLQ-FVLGHLLGTnpVEYDVSGWLKAaKENPSAQNATQLL--- 539
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  550 SHSLIKALFPEgnpakinlKRPPTAgsQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAH------------IFNDALVC 617
Cdd:cd01386    540 QESQKETAAVK--------RKSPCL--QIKFQVDALIDTLRRTGLHFVHCLLPQHNAGKDerstsspaagdeLLDVPLLR 609
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  618 HQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKMLCKQ-----TWPHWRGPARAGVEVLFNELEIPEEEFSFGRSKIFIR 692
Cdd:cd01386    610 SQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPltkklGLNSEVADERKAVEELLEELDLEKSSYRIGLSQVFFR 689
MYSc_Myo12 cd14874
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ...
38-652 1.49e-72

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: 254.03  E-value: 1.49e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160   38 NLKKRFDHNEVYTYIGSVVISINPYRPLPIYTPEKVEEYrnrnfyelspHIFALSDEAYRSL-RDQDKDQCILITGESGA 116
Cdd:cd14874      6 NLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIkSMSSNAESIVFGGESGS 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  117 GKTEASKFVMSYVAAvcGKGAEVNQVKEQLLQSnpVLEAFGNAKTVRNDNSSRFGKYMDIEFdfKGDPLGGVISNYL--L 194
Cdd:cd14874     76 GKSYNAFQVFKYLTS--QPKSKVTTKHSSAIES--VFKSFGCAKTLKNDEATRFGCSIDLLY--KRNVLTGLNLKYTvpL 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  195 EKSRVVKQPRGERNFHIFYQILSGASEDFLCKLKLeRDFSRYNYLGLDSAKVNGVDDAANFRTVRNAMQIVGFMDHETQS 274
Cdd:cd14874    150 EVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGI-KGLQKFFYINQGNSTENIQSDVNHFKHLEDALHVLGFSDDHCIS 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  275 VFEVVAAVLKLGNIEFKPESRVNG-LDESKIKDKNELKEICELTGIDQSVLERAFSFRTveakqeKVSTTLNVAQAYYAR 353
Cdd:cd14874    229 IYKIISTILHIGNIYFRTKRNPNVeQDVVEIGNMSEVKWVAFLLEVDFDQLVNFLLPKS------EDGTTIDLNAALDNR 302
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  354 DALAKNLYSRLFSWLVTRIneSIKAQTKVRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKEEQEEYIR 433
Cdd:cd14874    303 DSFAMLIYEELFKWVLNRI--GLHLKCPLHTGVISILDHYGFEKYNNNGVEEFLINSVNERIENLFVKHSFHDQLVDYAK 380
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  434 EGIEwthIEY-----FNNAIICDLIENNQTGILAMLDEECLRPgTVTDDTFLEKLNQvcathQHFESrmskcSRFLNDTT 508
Cdd:cd14874    381 DGIS---VDYkvpnsIENGKTVELLFKKPYGLLPLLTDECKFP-KGSHESYLEHCNL-----NHTDR-----SSYGKARN 446
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  509 LPHSCFRIQHYAGKVMYQVEGFVDKNNDLLYRDLSQAMWKASHSLIKALFPE--GNPAKINLkrppTAGSQFKASVATLM 586
Cdd:cd14874    447 KERLEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFESysSNTSDMIV----SQAQFILRGAQEIA 522
                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024511160  587 KNLQTKNPNYIRCIKPNDKKAAHIFNDALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKML 652
Cdd:cd14874    523 DKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYRCL 588
MYSc_Myo21 cd14882
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ...
33-652 4.32e-65

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


Pssm-ID: 276848  Cd Length: 642  Bit Score: 232.71  E-value: 4.32e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160   33 DSFINNLKKRFDHNEVYTYIGSVVISINPYRPLPIYTPEKVEEYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITG 112
Cdd:cd14882      1 ENILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  113 ESGAGKTEASKFVMSYVAaVCGKGaeVNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGGVISNY 192
Cdd:cd14882     81 ESYSGKTTNARLLIKHLC-YLGDG--NRGATGRVESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMSGAIFWMY 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  193 LLEKSRVVKQPRGERNFHIFYQILSG-ASEDFLCKLKLERDfSRYNYLGLD------SAKVNGVDDAANFRTVRNAMQIV 265
Cdd:cd14882    158 QLEKLRVSTTDGNQSNFHIFYYFYDFiEAQNRLKEYNLKAG-RNYRYLRIPpevppsKLKYRRDDPEGNVERYKEFEEIL 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  266 GFMDHE---TQSVFEVVAAVLKLGNIEFkpesrVNGLDESKIKDKNELKEICELTGIDQSVLERAFSFRTVEAKQEKVST 342
Cdd:cd14882    237 KDLDFNeeqLETVRKVLAAILNLGEIRF-----RQNGGYAELENTEIASRVAELLRLDEKKFMWALTNYCLIKGGSAERR 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  343 TLNVAQAYYARDALAKNLYSRLFSWLVTRINESIKAQTKV--RKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFI 420
Cdd:cd14882    312 KHTTEEARDARDVLASTLYSRLVDWIINRINMKMSFPRAVfgDKYSISIHDMFGFECFHRNRLEQLMVNTLNEQMQYHYN 391
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  421 ELTLKEEQEEYIREGIEWTHIEYFNNAIICDLIENNQTGILAMLDEEclrpgtvtddtfleklNQVCATHQH-FESRMSK 499
Cdd:cd14882    392 QRIFISEMLEMEEEDIPTINLRFYDNKTAVDQLMTKPDGLFYIIDDA----------------SRSCQDQNYiMDRIKEK 455
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  500 CSRFLNdttlPHSC--FRIQHYAGKVMYQVEGFVDKNNDLLYRDLSQAMWKASHSLIKALFPEGNPAKINlkrppTAGSQ 577
Cdd:cd14882    456 HSQFVK----KHSAheFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTNSQVRNMR-----TLAAT 526
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  578 FKASVATLMKNLqTKNPN-----YIRCIKPNDKKAAHIFNDALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKML 652
Cdd:cd14882    527 FRATSLELLKML-SIGANsggthFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRIPFQEFLRRYQFL 605
Myosin_TH1 pfam06017
Unconventional myosin tail, actin- and lipid-binding; Unconventional myosins, ie those that ...
916-1093 5.59e-45

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: 428724  Cd Length: 196  Bit Score: 160.85  E-value: 5.59e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  916 KLEASELFKDKKALYPASVGQPFQGAYLEISKNPKY--KKLKDAV----DEKIIIAEVVNKINRaNGKATSRIFLLTKNN 989
Cdd:pfam06017    1 KDYASDLLKGKKERRRFSLLRRFMGDYLGLENNFSGpgPELRKAVgiggDEKVLFSDRVSKFNR-SSKPSPRILILTDKA 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  990 VLLADQKS------GNIKSEVPLGDVTKVSMSSQNDGFFAVHLKEGSgaasKGDFLFSSDHLIEMATKLYRTTLSQTKQK 1063
Cdd:pfam06017   80 LYLIDPKKfknglqYVLKRRIPLSDITGVSVSPLQDDWVVLHLGSPQ----KGDLLLECDFKTELVTVLSKLYKKKTNKK 155
                          170       180       190
                   ....*....|....*....|....*....|.
gi 2024511160 1064 LNIEISDEFLVQFRQDK-VCVKFIQGSQKNG 1093
Cdd:pfam06017  156 LNVKISDTIEYRKKKGKiRTVKFVKDEPKGK 186
MYSc_Myo24B cd14938
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ...
34-691 6.17e-45

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: 174.25  E-value: 6.17e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160   34 SFINNLKKRFDHNEVYTYIGSVVISINPYRPLPIYTPEKVEEYR-NRNFYELSPHIFALSDEAYRSLRDQDKDQCILITG 112
Cdd:cd14938      2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKcIDCIEDLSLNEYHVVHNALKNLNELKRNQSIIISG 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  113 ESGAGKTEASKFVMSYVA-AVCGKGAEVNQVKEQ--------------------LLQSNPVLEAFGNAKTVRNDNSSRFG 171
Cdd:cd14938     82 ESGSGKSEIAKNIINFIAyQVKGSRRLPTNLNDQeednihneentdyqfnmsemLKHVNVVMEAFGNAKTVKNNNSSRFS 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  172 KYMDIEFDfKGDPLGGVISNYLLEKSRVVKQPRGERNFHIFYQILSGASEDFLcKLKLERDFSRYNYLGLDSAKVNGVDD 251
Cdd:cd14938    162 KFCTIHIE-NEEIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFK-KMYFLKNIENYSMLNNEKGFEKFSDY 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  252 AANFRTVRNAMQIVGFMDHETQSVFEVVAAVLKLGNIE----FKPESRVNGLDESKIKDKNELK----EICELTGIDQSV 323
Cdd:cd14938    240 SGKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNTEivkaFRKKSLLMGKNQCGQNINYETIlselENSEDIGLDENV 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  324 LERAFSFRTVEAKQE---KVSTT------------LNVAQAYYARDALAKNLYSRLFSWLVTRINESIKAQTK--VRKKV 386
Cdd:cd14938    320 KNLLLACKLLSFDIEtfvKYFTTnyifndsilikvHNETKIQKKLENFIKTCYEELFNWIIYKINEKCTQLQNinINTNY 399
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  387 MGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKEEQEEYIREGIEWTH-IEYFNNAIICDLIENNQTGILAMLD 465
Cdd:cd14938    400 INVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYnSENIDNEPLYNLLVGPTEGSLFSLL 479
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  466 EEcLRPGTVTDDTFLeklnqvcatHQHFESRMSKCSRFL--NDTTLPHSCFRIQHYAGKVMYQVEGFVDKNNDLLYRDLS 543
Cdd:cd14938    480 EN-VSTKTIFDKSNL---------HSSIIRKFSRNSKYIkkDDITGNKKTFVITHSCGDIIYNAENFVEKNIDILTNRFI 549
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  544 QAMWKASHSLIKAL---FPEGNPAKI-----------NLK--------RPPTAGSQFKASVATLMKNLQTKNPNYIRCIK 601
Cdd:cd14938    550 DMVKQSENEYMRQFcmfYNYDNSGNIveekrrysiqsALKlfkrrydtKNQMAVSLLRNNLTELEKLQETTFCHFIVCMK 629
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  602 PND-KKAAHIFNDALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKmlCKQTwphwrgPARAGVEVLFNELEIPEE 680
Cdd:cd14938    630 PNEsKRELCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFD--IKNE------DLKEKVEALIKSYQISNY 701
                          730
                   ....*....|.
gi 2024511160  681 EFSFGRSKIFI 691
Cdd:cd14938    702 EWMIGNNMIFL 712
Motor_domain cd01363
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ...
55-182 3.18e-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: 146.34  E-value: 3.18e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160   55 VVISINPYRPLPIYTPEKVEE-YRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITGESGAGKTEASKFVMSYVAAVC 133
Cdd:cd01363      1 VLVRVNPFKELPIYRDSKIIVfYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024511160  134 GKGAEVNQ-------------VKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKG 182
Cdd:cd01363     81 FNGINKGEtegwvylteitvtLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEILLDIAG 142
MYSc_Myo33 cd14894
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ...
33-657 2.82e-38

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: 154.90  E-value: 2.82e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160   33 DSFINNLKKRFDHNEVYTYIGSVVISI-NPYRPL------PIYTPEKVEEYRNRNFYE--LSPHIFALSDEAY------- 96
Cdd:cd14894      1 EELVDALTSRFDDDRIYTYINHHTMAVmNPYRLLqtarftSIYDEQVVLTYADTANAEtvLAPHPFAIAKQSLvrlffdn 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160   97 -------------RSLrDQDKDQCILITGESGAGKTEASKFVMSYVAAVC------------------------------ 133
Cdd:cd14894     81 ehtmplpstissnRSM-TEGRGQSLFLCGESGSGKTELAKDLLKYLVLVAqpalskgseetckvsgstrqpkiklftsst 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  134 ------------------GKGAEVNQV-------------------------------------------KEQL------ 146
Cdd:cd14894    160 kstiqmrteeartialleAKGVEKYEIvlldlhperwdemtsvsrskrlpqvhvdglffgfyeklehledEEQLrmyfkn 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  147 ----------LQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDP-----LGGVISNYLLEKSRVVKQ------PRG 205
Cdd:cd14894    240 phaakklsivLDSNIVLEAFGHATTSMNLNSSRFGKMTTLQVAFGLHPwefqiCGCHISPFLLEKSRVTSErgresgDQN 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  206 ERNFHIFYQILSGASEDFLCKLKLER------DFSRYNYLGLDSAKVNGV--------DDAANFRTVRNAMQIVGFMDHE 271
Cdd:cd14894    320 ELNFHILYAMVAGVNAFPFMRLLAKElhldgiDCSALTYLGRSDHKLAGFvskedtwkKDVERWQQVIDGLDELNVSPDE 399
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  272 TQSVFEVVAAVLKLGNIEFKPESRVNGLDESKIKDKNELKEICELTGIDQ-SVLERAFSFRTV--EAKQEKVSTTLNVAQ 348
Cdd:cd14894    400 QKTIFKVLSAVLWLGNIELDYREVSGKLVMSSTGALNAPQKVVELLELGSvEKLERMLMTKSVslQSTSETFEVTLEKGQ 479
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  349 AYYARDALAKNLYSRLFSWLVTRINESIK----------------AQTKVRKKVMGVLDIYGFEIFEDNSFEQFIINYCN 412
Cdd:cd14894    480 VNHVRDTLARLLYQLAFNYVVFVMNEATKmsalstdgnkhqmdsnASAPEAVSLLKIVDVFGFEDLTHNSLDQLCINYLS 559
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  413 EKLQQifieltlKEEQEEYIREGIEwTHIEYFNNAIICDLIENNQTGILAMLDE-ECLRPGTVTDDTFLEKLNQ--VCAT 489
Cdd:cd14894    560 EKLYA-------REEQVIAVAYSSR-PHLTARDSEKDVLFIYEHPLGVFASLEElTILHQSENMNAQQEEKRNKlfVRNI 631
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  490 HQHFESRMSKCSRFLND---------TTLPhscFRIQHYAGKVMYQVEGFVDKNNDLLYRDLSQAMWKASHSLIKALF-- 558
Cdd:cd14894    632 YDRNSSRLPEPPRVLSNakrhtpvllNVLP---FVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNSSHFCRMLne 708
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511160  559 -------PEGNPAKINLKRPPTAGS-----QFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNDALVCHQIRYLGLL 626
Cdd:cd14894    709 ssqlgwsPNTNRSMLGSAESRLSGTksfvgQFRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCRSQRLI 788
                          810       820       830
                   ....*....|....*....|....*....|....*
gi 2024511160  627 ENVRVRRAGYAFRQAYE----PCLERYKMLCKQTW 657
Cdd:cd14894    789 RQMEICRNSSSSYSAIDisksTLLTRYGSLLREPY 823
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
753-775 1.12e-03

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


Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 37.31  E-value: 1.12e-03
                            10        20
                    ....*....|....*....|...
gi 2024511160   753 KIRSSAVIIQSYIRGWKARKLLR 775
Cdd:smart00015    1 RLTRAAIIIQAAWRGYLARKRYK 23
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
811-833 2.62e-03

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


Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 36.15  E-value: 2.62e-03
                            10        20
                    ....*....|....*....|...
gi 2024511160   811 RNKQAIAVIWAYWLGYKVRREYR 833
Cdd:smart00015    1 RLTRAAIIIQAAWRGYLARKRYK 23
IQ pfam00612
IQ calmodulin-binding motif; Calmodulin-binding motif.
755-775 5.31e-03

IQ calmodulin-binding motif; Calmodulin-binding motif.


Pssm-ID: 425778  Cd Length: 21  Bit Score: 35.37  E-value: 5.31e-03
                           10        20
                   ....*....|....*....|.
gi 2024511160  755 RSSAVIIQSYIRGWKARKLLR 775
Cdd:pfam00612    1 RKAAIKIQAAWRGYLARKRYK 21
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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