Splicing factor [RNA processing and modification];

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 569408832  23 SDWQELRTEDGLAYYFNRVTQETTWDKPEELMTDEEKQSSKN 64
Cdd:COG5104   15 SEWEELKAPDGRIYYYNKRTGKSSWEKPKELLKGSEEDLDVD 56

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569408832 141 PLILHCLRKRFEAAKIYSAIGTILISINPYTQLDLYTPQMIRKYRNSLeEHREVPPHVFVVADQAYKGLtFESGPNQSIV 220
Cdd:cd00124    1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKG-RSADLPPHVFAVADAAYRAM-LRDGQNQSIL 78

                         90
                 ....*....|
gi 569408832 221 ISGESGAGKS 230
Cdd:cd00124   79 ISGESGAGKT 88

Myosin head (motor domain);

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569408832  129 VADLTLLDEMSVPLILHCLRKRFEAAKIYSAIGTILISINPYTQLDLYTPQMIRKYRNslEEHREVPPHVFVVADQAYKG 208
Cdd:pfam00063   1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRG--KRRGELPPHIFAIADEAYRS 78

                          90       100
                  ....*....|....*....|.
gi 569408832  209 LtFESGPNQSIVISGESGAGK 229
Cdd:pfam00063  79 M-LQDKENQSILISGESGAGK 98

Splicing factor [RNA processing and modification];

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 569408832  23 SDWQELRTEDGLAYYFNRVTQETTWDKPEELMTDEEKQSSKN 64
Cdd:COG5104   15 SEWEELKAPDGRIYYYNKRTGKSSWEKPKELLKGSEEDLDVD 56

Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the N-terminus of many but not all myosins. The function of this domain is unknown.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 569408832   77 WVWVPDETDVYLPARKLDESNGQVVVELESGEERYVNRKDL 117
Cdd:pfam02736   5 LVWVPDPKEGFVKGEIKEEEGDKVTVETEDGKTVTVKKDDV 45

Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.

                           10        20
                   ....*....|....*....|....*...
gi 569408832    25 WQELRTEDGLAYYFNRVTQETTWDKPEE 52
Cdd:smart00456   6 WEERKDPDGRPYYYNHETKETQWEKPRE 33

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569408832 141 PLILHCLRKRFEAAKIYSAIGTILISINPYTQLDLYTPQMIRKYRNSLeEHREVPPHVFVVADQAYKGLtFESGPNQSIV 220
Cdd:cd00124    1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKG-RSADLPPHVFAVADAAYRAM-LRDGQNQSIL 78

                         90
                 ....*....|
gi 569408832 221 ISGESGAGKS 230
Cdd:cd00124   79 ISGESGAGKT 88

Myosin head (motor domain);

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569408832  129 VADLTLLDEMSVPLILHCLRKRFEAAKIYSAIGTILISINPYTQLDLYTPQMIRKYRNslEEHREVPPHVFVVADQAYKG 208
Cdd:pfam00063   1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRG--KRRGELPPHIFAIADEAYRS 78

                          90       100
                  ....*....|....*....|.
gi 569408832  209 LtFESGPNQSIVISGESGAGK 229
Cdd:pfam00063  79 M-LQDKENQSILISGESGAGK 98

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569408832 141 PLILHCLRKRFEAAKIYSAIGTILISINPYTQLDLYTPQMIRKYRNSLEehREVPPHVFVVADQAYKGLTfESGPNQSIV 220
Cdd:cd14872    1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGP--KEMPPHTYNIADDAYRAMI-VDAMNQSIL 77

                         90
                 ....*....|
gi 569408832 221 ISGESGAGKS 230
Cdd:cd14872   78 ISGESGAGKT 87

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569408832 141 PLILHCLRKRFEAAK-IYSAIGTILISINPYTQLDLYTPQMIRKYRNSLEEHREvpPHVFVVADQAYKGLTFESGpNQSI 219
Cdd:cd01380    1 PAVLHNLKVRFCQRNaIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELD--PHIFAIAEEAYRQMARDEK-NQSI 77

                         90
                 ....*....|
gi 569408832 220 VISGESGAGK 229
Cdd:cd01380   78 IVSGESGAGK 87

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569408832 142 LILHCLRKRFEAAKIYSAIGTILISINPYTQL-DLYTPQMIRKYRNSLEEhrEVPPHVFVVADQAYKGLT---FESGPNQ 217
Cdd:cd14890    2 SLLHTLRLRYERDEIYTYVGPILISINPYKSIpDLYSEERMLLYHGTTAG--ELPPHVFAIADHAYTQLIqsgVLDPSNQ 79

                         90
                 ....*....|...
gi 569408832 218 SIVISGESGAGKS 230
Cdd:cd14890   80 SIIISGESGAGKT 92

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569408832 141 PLILHCLRKRFEAAKIYSAIGTILISINPYTQL-DLYTPQMIRKYRNSleEHREVPPHVFVVADQAYKGLTFEsGPNQSI 219
Cdd:cd01384    1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLpHLYDAHMMEQYKGA--PLGELSPHVFAVADAAYRAMINE-GKSQSI 77

                         90
                 ....*....|
gi 569408832 220 VISGESGAGK 229
Cdd:cd01384   78 LVSGESGAGK 87

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569408832 143 ILHCLRKRFEAAKIYSAIGTILISINPYTQLDLYTPQMIRKYRNSLEEhrEVPPHVFVVADQAYKGLTFEsGPNQSIVIS 222
Cdd:cd01377    3 VLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRRE--EMPPHIFAIADNAYRNMLQD-RENQSILIT 79

                 ....*..
gi 569408832 223 GESGAGK 229
Cdd:cd01377   80 GESGAGK 86

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569408832 144 LHCLRKRFEAAKIYSAIGTILISINPYTQL-DLYTPQMIRKYRN-SLEehrEVPPHVFVVADQAYKGLTfESGPNQSIVI 221
Cdd:cd01382    4 LNNIRVRYSKDKIYTYVANILIAVNPYFDIpKLYSSETIKSYQGkSLG---TLPPHVFAIADKAYRDMK-VLKQSQSIIV 79

                 ....*...
gi 569408832 222 SGESGAGK 229
Cdd:cd01382   80 SGESGAGK 87

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569408832 143 ILHCLRKRFEAAKIYSAIGTILISINPYTQLDLYTPQMIRKY----RNSLeehrevPPHVFVVADQAYKGLTfESGPNQS 218
Cdd:cd14883    3 INTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYfgkrMGAL------PPHIFALAEAAYTNMQ-EDGKNQS 75

                         90
                 ....*....|..
gi 569408832 219 IVISGESGAGKS 230
Cdd:cd14883   76 VIISGESGAGKT 87

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569408832 141 PLILHCLRKRFEAAKIYSAIGTILISINPYTQL-DLYTPQMIRKYRNSL------EEHREVPPHVFVVADQAYKGLTFES 213
Cdd:cd14902    1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLpDLYSESQLNAYKASMtstspvSQLSELPPHVFAIGGKAFGGLLKPE 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 569408832 214 GPNQSIVISGESGAGKSlgeiffqTSTTFLFYFY 247
Cdd:cd14902   81 RRNQSILVSGESGSGKT-------ESTKFLMQFL 107

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569408832 141 PLiLHCLRKRFEAAKIYSAIGTILISINPYTQLD-LYTPQMIRKYRNSLEEHREVPPHVFVVADQAY---KGLTFESGPN 216
Cdd:cd14892    2 PL-LDVLRRRYERDAIYTFTADILISINPYKSIPlLYDVPGFDSQRKEEATASSPPPHVFSIAERAYramKGVGKGQGTP 80

                         90
                 ....*....|....
gi 569408832 217 QSIVISGESGAGKS 230
Cdd:cd14892   81 QSIVVSGESGAGKT 94

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569408832 141 PLILHCLRKRFEAAKIYSAIGTILISINPYTQLDLYTPQMIRKYRN-------SLEEHREVPPHVFVVADQAYKGLTFES 213
Cdd:cd14908    1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRQegllrsqGIESPQALGPHVFAIADRSYRQMMSEI 80

                         90
                 ....*....|....*..
gi 569408832 214 GPNQSIVISGESGAGKS 230
Cdd:cd14908   81 RASQSILISGESGAGKT 97

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569408832 142 LILHCLRKRFEAAKIYSAIGTILISINPYTQLDLYTPQMIRKYRnsLEEHREVPPHVFVVADQAYKGLT--FESGP-NQS 218
Cdd:cd14889    2 VLLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYK--CEKKSSLPPHIFAVADRAYQSMLgrLARGPkNQC 79

                         90
                 ....*....|..
gi 569408832 219 IVISGESGAGKS 230
Cdd:cd14889   80 IVISGESGAGKT 91

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569408832 143 ILHCLRKRFEAAKIYSAIGTILISINPYTQLDLYTPQMIRKYRNslEEHREVPPHVFVVADQAYKgLTFESGPNQSIVIS 222
Cdd:cd14896    3 VLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHP--RKALNTTPHIFAIAASAYR-LSQSTGQDQCILLS 79

                 ....*...
gi 569408832 223 GESGAGKS 230
Cdd:cd14896   80 GHSGSGKT 87

myosin-A; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569408832 131 DLTLLDEMSVPLILHCLRKRFEAAKIYSAIGTILISINPYTQLDLYTPQMIRKYRNSlEEHREVPPHVFVVADQAYKGLt 210
Cdd:PTZ00014 100 DIGLLPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYRDA-KDSDKLPPHVFTTARRALENL- 177

                         90       100
                 ....*....|....*....|
gi 569408832 211 FESGPNQSIVISGESGAGKS 230
Cdd:PTZ00014 178 HGVKKSQTIIVSGESGAGKT 197

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569408832 147 LRKRFEAAKIYSAIGTILISINPYTQLDLYTPQMIRKYRNSLEEhrEVPPHVFVVADQAYKGLTfESGPNQSIVISGESG 226
Cdd:cd01387    7 LKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALG--ELPPHLFAIANLAFAKML-DAKQNQCVVISGESG 83

                 ....
gi 569408832 227 AGKS 230
Cdd:cd01387   84 SGKT 87

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569408832 141 PLILHCLRKRFEAAKIYSAIGTILISINPYTQLDLYTPQMIRKYRNSlEEHREVPPHVFVVADQAYKGLtFESGPNQSIV 220
Cdd:cd14876    1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDA-PDLTKLPPHVFYTARRALENL-HGVNKSQTII 78

                         90
                 ....*....|
gi 569408832 221 ISGESGAGKS 230
Cdd:cd14876   79 VSGESGAGKT 88

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569408832 143 ILHCLRKRFEAAKIYSAIGTILISINPYTQLDLYTPQMIRKYRNslEEHREVPPHVFVVADQAYKGLtFESGPNQSIVIS 222
Cdd:cd14909    3 VLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRG--KRRNEVPPHIFAISDGAYVDM-LTNHVNQSMLIT 79

                 ....*...
gi 569408832 223 GESGAGKS 230
Cdd:cd14909   80 GESGAGKT 87

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569408832 141 PLILHCLRKRFEAAKIYSAIGTILISINPYTQLDLYTPQMIRKYRNslEEHREVPPHVFVVADQAYKGLTFESgPNQSIV 220
Cdd:cd14917    1 PAVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRG--KKRSEAPPHIFSISDNAYQYMLTDR-ENQSIL 77

                         90
                 ....*....|.
gi 569408832 221 ISGESGAGKSL 231
Cdd:cd14917   78 ITGESGAGKTV 88

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569408832 143 ILHCLRKRFEAAKIYSAIGTILISINPYTQLDLYTPQMIRKYRNslEEHREVPPHVFVVADQAYKGLtFESGPNQSIVIS 222
Cdd:cd14930    3 VLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRG--KKRHEVPPHVYAVTEGAYRSM-LQDREDQSILCT 79

                 ....*...
gi 569408832 223 GESGAGKS 230
Cdd:cd14930   80 GESGAGKT 87

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569408832 143 ILHCLRKRFEAAKI-YSAIGTILISINPYTQLDLYTPQMIRKYRnSLEEHREVPPHVFVVADQAYKGLTFESGPNQSIVI 221
Cdd:cd14875    3 LLHCIKERFEKLHQqYSLMGEMVLSVNPFRLMPFNSEEERKKYL-ALPDPRLLPPHIWQVAHKAFNAIFVQGLGNQSVVI 81

                 ....*....
gi 569408832 222 SGESGAGKS 230
Cdd:cd14875   82 SGESGSGKT 90

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569408832 143 ILHCLRKRFEAAKIYSAIGTILISINPYTQLDLYTPQMIRKYRNslEEHREVPPHVFVVADQAYKGLtFESGPNQSIVIS 222
Cdd:cd14927    3 VLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKG--KRRSEAPPHIYAIADNAYNDM-LRNRENQSMLIT 79

                 ....*....
gi 569408832 223 GESGAGKSL 231
Cdd:cd14927   80 GESGAGKTV 88

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569408832 143 ILHCLRKRFEAAKIYSAIGTILISINPYTQL-DLYTPQMIRKYRNSLEEhREVPPHVFVVADQAYKGLTFESGP-NQSIV 220
Cdd:cd14880    3 VLRCLQARYTADTFYTNAGCTLVALNPFKPVpQLYSPELMREYHAAPQP-QKLKPHIFTVGEQTYRNVKSLIEPvNQSIV 81

                         90
                 ....*....|
gi 569408832 221 ISGESGAGKS 230
Cdd:cd14880   82 VSGESGAGKT 91

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569408832 142 LILHCLRKRFEAAKIYSAIGTILISINPYTQL-DLYTPQMIRKYRN---SLEEHREVPPHVFVVADQAYKGLTfESGPNQ 217
Cdd:cd14886    2 VVIDILRDRFAKDKIYTYAGKLLVALNPFKQIrNLYGTEVIGRYRQadtSRGFPSDLPPHSYAVAQSALNGLI-SDGISQ 80

                         90
                 ....*....|...
gi 569408832 218 SIVISGESGAGKS 230
Cdd:cd14886   81 SCIVSGESGAGKT 93

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569408832 143 ILHCLRKRFEAAKIYSAIGTILISINPYTQLDLYTPQMIRKYRNslEEHREVPPHVFVVADQAYKGLtFESGPNQSIVIS 222
Cdd:cd14921    3 VLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKG--KKRHEMPPHIYAIADTAYRSM-LQDREDQSILCT 79

                 ....*...
gi 569408832 223 GESGAGKS 230
Cdd:cd14921   80 GESGAGKT 87