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Conserved domains on  [gi|1034601426|ref|XP_016880626|]
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myosin XVB isoform X21 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Motor_domain super family cl22853
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ...
 1-147 1.21e-79

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.


The actual alignment was detected with superfamily member cd14896:

Pssm-ID: 473979 [Multi-domain]  Cd Length: 644  Bit Score: 277.43  E-value: 1.21e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601426    1 MLGQSQLQLVGSLFQEAEPQSRGGRGRPTLASRFQQALEDLIARLGRSHVYFIQCLTPNPGKLPGLFDVGHVTEQLHQAA 80
Cdd:cd14896    498 MLAQSQLQLVGSLFQEAEPQYGLGQGKPTLASRFQQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAG 577

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034601426   81 ILEAVGTRSANFPVRVPFEAFLASFQALGSEGQEDLSDREKCGAVLSQVLGAESPLYHLGATKVLLQ 147
Cdd:cd14896    578 ILEAIGTRSEGFPVRVPFQAFLARFGALGSERQEALSDRERCGAILSQVLGAESPLYHLGATKVLLK 644
MyTH4 smart00139
Domain in Myosin and Kinesin Tails; Domain present twice in myosin-VIIa, and also present in 3 ...
 1408-1546 4.51e-38

Domain in Myosin and Kinesin Tails; Domain present twice in myosin-VIIa, and also present in 3 other myosins.


:

Pssm-ID: 214535  Cd Length: 152  Bit Score: 140.19  E-value: 4.51e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601426  1408 YTKAPIQESLLSLSDDV-SKLAVASFLALMRFMGDQSKPRGKDEMDLLYELLKLC-QQEKLRDEIYCQVIKQVTGHPRPE 1485
Cdd:smart00139    1 YTKDPIKTSLLKLESDElQKEAVKIFKAILKFMGDIPLPRPDSHLDLVQFILQKGlDHPELRDEIYCQLIKQLTDNPSRQ 80

                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034601426  1486 HCTRGWSFLSLLTGFFPPSTRLMPYLTKFLQ---DSGPSQELARSSQEHLQRTVKYGGrRRMPP 1546
Cdd:smart00139   81 SEERGWQLLYLCTSLFPPSERLLPYLLQFLSrraDPGSEQGLAKYCLYRLERTLKNGA-RKQPP 143
FERM_C_MyoXV cd13201
FERM domain C-lobe of Myosin XV (MyoXV/Myo15); MyoXV, a MyTH-FERM myosin, are actin-based ...
 1754-1855 4.00e-34

FERM domain C-lobe of Myosin XV (MyoXV/Myo15); MyoXV, a MyTH-FERM myosin, are actin-based motor proteins essential for a variety of biological processes in actin cytoskeleton function. Specifically MyoXV functions in the actin organization in hair cells of the organ of Corti. Mutations in Human MyoXVa causes non-syndromic deafness, DFNB3 and the mouse shaker-2 mutation. MyoXV consists of a N-terminal motor/head region, a neck made of 1-3 IQ motifs, and a tail that consists of either a myosin tail homology 4 (MyTH4) domains, followed by an SH3 domain, and a MyTH-FERM domains as in rat Myo15 or two MyTH-FERM domains separated by a SH3 domain as in human Myo15A. The MyTH-FERM domains are thought to mediate dimerization and binding to other proteins or cargo. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


:

Pssm-ID: 270022  Cd Length: 101  Bit Score: 126.95  E-value: 4.00e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601426 1754 GYTVYGVLRVSMQALSGPTLLGLNRQHLILMDPSSQSLYCRIALKSLQRLHLLSPlEEKGPPGLEVNYGSADNPQTIWFE 1833
Cdd:cd13201      1 GSNFFYVQRVSDPRLPGPCLLALNREGLHFLDPKTHETLLRIPLKEVQSTRKLRP-LEDGTPFLDIKYGNLMQQRTIRLE 79

                           90       100
                   ....*....|....*....|..
gi 1034601426 1834 LPQAQELLYTTVFLIDSSASCT 1855
Cdd:cd13201     80 TDQAHEISRLIAQYIEEASENR 101
SH3_MYO15B cd12068
Src Homology 3 domain of Myosin XVb; Myosin XVb, also called KIAA1783, was named based on its ...
 1250-1304 1.36e-30

Src Homology 3 domain of Myosin XVb; Myosin XVb, also called KIAA1783, was named based on its similarity with myosin XVa. It is a transcribed and unprocessed pseudogene whose predicted amino acid sequence contains mutated or deleted amino acid residues that are normally conserved and important for myosin function. The related myosin XVa is important for normal growth of mechanosensory stereocilia of inner ear hair cells. Myosin XVa contains a unique N-terminal extension followed by a motor domain, light chain-binding IQ motifs, and a tail consisting of a pair of MyTH4-FERM tandems separated by a SH3 domain, and a PDZ domain. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies.


:

Pssm-ID: 213001  Cd Length: 55  Bit Score: 115.36  E-value: 1.36e-30
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1034601426 1250 YVIALRSYITDNCSLLSFHRGDLIKLLPVATLEPGWQFGSAGGRSGLFPADIVQP 1304
Cdd:cd12068      1 YVVALRSYITDDKSLLSFHRGDLIKLLPMAGLEPGWQFGSTGGRSGLFPADIVQP 55
MyTH4 pfam00784
MyTH4 domain; Domain in myosin and kinesin tails, present twice in myosin-VIIa, and also ...
 363-465 4.70e-23

MyTH4 domain; Domain in myosin and kinesin tails, present twice in myosin-VIIa, and also present in 3 other myosins.


:

Pssm-ID: 459939  Cd Length: 105  Bit Score: 95.34  E-value: 4.70e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601426  363 YLVRQGQCRPGLRNELFSQLVAQLWQNPDEQQSQRGWALMAVLLSAFPPLPVLQKPLLKFVSDQAP------RGMAALCQ 436
Cdd:pfam00784    3 NILQKGLKRPELRDEIYCQLIKQTTNNPKPESLLRGWQLLALCLGTFPPSKKLLKYLLKFLKRHADdpsrevGKYAQFCL 82

                           90       100
                   ....*....|....*....|....*....
gi 1034601426  437 HKLlgaleQSQLASGAtRAHPPTQLEWLA 465
Cdd:pfam00784   83 KRL-----KRTLKNGG-RKYPPSREEIEA 105
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
 1644-1758 1.81e-18

FERM central domain; This domain is the central structural domain of the FERM domain.


:

Pssm-ID: 459788 [Multi-domain]  Cd Length: 117  Bit Score: 82.70  E-value: 1.81e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601426 1644 ETPLHFDNSTYISTHYSQVLWDYLQGKLPVSakaDAQLARLAALQHL-----SKANRNTPSGQDLLAYVPKQLQRQVNTA 1718
Cdd:pfam00373    1 DLELLLQDEVTRHLLYLQAKDDILEGRLPCS---EEEALLLAALQLQaefgdYQPSSHTSEYLSLESFLPKQLLRKMKSK 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1034601426 1719 SIKNLMGQELRRLEGHSPQEAQISFIEAMSQLPLFGYTVY 1758
Cdd:pfam00373   78 ELEKRVLEAHKNLRGLSAEEAKLKYLQIAQSLPTYGVEFF 117
PH-like super family cl17171
Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like ...
 1152-1246 2.41e-03

Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like and IRS-like PTB domains, the ran-binding domain, the EVH1 domain, a domain in neurobeachin and the third domain of FERM. All of these domains have a PH fold, but lack significant sequence similarity. They are generally involved in targeting to protein to the appropriate cellular location or interacting with a binding partner. This domain family possesses multiple functions including the ability to bind inositol phosphates and to other proteins.


The actual alignment was detected with superfamily member cd13198:

Pssm-ID: 473070  Cd Length: 99  Bit Score: 39.12  E-value: 2.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601426 1152 FSRFF---PVSGES--GSDVqLLAVSHRGLRLLKvtqgpglrpDQLKILCSYSFAEVLGVECR-----GGSTLELS-LKS 1220
Cdd:cd13198      3 FSRFFeatKFSGPSlpKSEV-IIAVNWTGIYFVD---------EQEQVLLELSFPEITGVSSSrgkrdGGQSFTLTtIQG 72

                           90       100
                   ....*....|....*....|....*.
gi 1034601426 1221 EQLVLHTARARAIEALVELFLNELKK 1246
Cdd:cd13198     73 EEFVFQSPNAEDIAELVNYFLEGLRK 98
 
Name Accession Description Interval E-value
MYSc_Myo35 cd14896
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ...
 1-147 1.21e-79

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: 277.43  E-value: 1.21e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601426    1 MLGQSQLQLVGSLFQEAEPQSRGGRGRPTLASRFQQALEDLIARLGRSHVYFIQCLTPNPGKLPGLFDVGHVTEQLHQAA 80
Cdd:cd14896    498 MLAQSQLQLVGSLFQEAEPQYGLGQGKPTLASRFQQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAG 577

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034601426   81 ILEAVGTRSANFPVRVPFEAFLASFQALGSEGQEDLSDREKCGAVLSQVLGAESPLYHLGATKVLLQ 147
Cdd:cd14896    578 ILEAIGTRSEGFPVRVPFQAFLARFGALGSERQEALSDRERCGAILSQVLGAESPLYHLGATKVLLK 644
MyTH4 smart00139
Domain in Myosin and Kinesin Tails; Domain present twice in myosin-VIIa, and also present in 3 ...
 1408-1546 4.51e-38

Domain in Myosin and Kinesin Tails; Domain present twice in myosin-VIIa, and also present in 3 other myosins.


Pssm-ID: 214535  Cd Length: 152  Bit Score: 140.19  E-value: 4.51e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601426  1408 YTKAPIQESLLSLSDDV-SKLAVASFLALMRFMGDQSKPRGKDEMDLLYELLKLC-QQEKLRDEIYCQVIKQVTGHPRPE 1485
Cdd:smart00139    1 YTKDPIKTSLLKLESDElQKEAVKIFKAILKFMGDIPLPRPDSHLDLVQFILQKGlDHPELRDEIYCQLIKQLTDNPSRQ 80

                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034601426  1486 HCTRGWSFLSLLTGFFPPSTRLMPYLTKFLQ---DSGPSQELARSSQEHLQRTVKYGGrRRMPP 1546
Cdd:smart00139   81 SEERGWQLLYLCTSLFPPSERLLPYLLQFLSrraDPGSEQGLAKYCLYRLERTLKNGA-RKQPP 143
MyTH4 pfam00784
MyTH4 domain; Domain in myosin and kinesin tails, present twice in myosin-VIIa, and also ...
 1454-1552 1.60e-34

MyTH4 domain; Domain in myosin and kinesin tails, present twice in myosin-VIIa, and also present in 3 other myosins.


Pssm-ID: 459939  Cd Length: 105  Bit Score: 128.08  E-value: 1.60e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601426 1454 LYELLKLC-QQEKLRDEIYCQVIKQVTGHPRPEHCTRGWSFLSLLTGFFPPSTRLMPYLTKFLQD-----SGPSQELARS 1527
Cdd:pfam00784    1 AQNILQKGlKRPELRDEIYCQLIKQTTNNPKPESLLRGWQLLALCLGTFPPSKKLLKYLLKFLKRhaddpSREVGKYAQF 80

                           90       100
                   ....*....|....*....|....*
gi 1034601426 1528 SQEHLQRTVKYGGRRRMPPPGEMKA 1552
Cdd:pfam00784   81 CLKRLKRTLKNGGRKYPPSREEIEA 105
FERM_C_MyoXV cd13201
FERM domain C-lobe of Myosin XV (MyoXV/Myo15); MyoXV, a MyTH-FERM myosin, are actin-based ...
 1754-1855 4.00e-34

FERM domain C-lobe of Myosin XV (MyoXV/Myo15); MyoXV, a MyTH-FERM myosin, are actin-based motor proteins essential for a variety of biological processes in actin cytoskeleton function. Specifically MyoXV functions in the actin organization in hair cells of the organ of Corti. Mutations in Human MyoXVa causes non-syndromic deafness, DFNB3 and the mouse shaker-2 mutation. MyoXV consists of a N-terminal motor/head region, a neck made of 1-3 IQ motifs, and a tail that consists of either a myosin tail homology 4 (MyTH4) domains, followed by an SH3 domain, and a MyTH-FERM domains as in rat Myo15 or two MyTH-FERM domains separated by a SH3 domain as in human Myo15A. The MyTH-FERM domains are thought to mediate dimerization and binding to other proteins or cargo. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 270022  Cd Length: 101  Bit Score: 126.95  E-value: 4.00e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601426 1754 GYTVYGVLRVSMQALSGPTLLGLNRQHLILMDPSSQSLYCRIALKSLQRLHLLSPlEEKGPPGLEVNYGSADNPQTIWFE 1833
Cdd:cd13201      1 GSNFFYVQRVSDPRLPGPCLLALNREGLHFLDPKTHETLLRIPLKEVQSTRKLRP-LEDGTPFLDIKYGNLMQQRTIRLE 79

                           90       100
                   ....*....|....*....|..
gi 1034601426 1834 LPQAQELLYTTVFLIDSSASCT 1855
Cdd:cd13201     80 TDQAHEISRLIAQYIEEASENR 101
SH3_MYO15B cd12068
Src Homology 3 domain of Myosin XVb; Myosin XVb, also called KIAA1783, was named based on its ...
 1250-1304 1.36e-30

Src Homology 3 domain of Myosin XVb; Myosin XVb, also called KIAA1783, was named based on its similarity with myosin XVa. It is a transcribed and unprocessed pseudogene whose predicted amino acid sequence contains mutated or deleted amino acid residues that are normally conserved and important for myosin function. The related myosin XVa is important for normal growth of mechanosensory stereocilia of inner ear hair cells. Myosin XVa contains a unique N-terminal extension followed by a motor domain, light chain-binding IQ motifs, and a tail consisting of a pair of MyTH4-FERM tandems separated by a SH3 domain, and a PDZ domain. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies.


Pssm-ID: 213001  Cd Length: 55  Bit Score: 115.36  E-value: 1.36e-30
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1034601426 1250 YVIALRSYITDNCSLLSFHRGDLIKLLPVATLEPGWQFGSAGGRSGLFPADIVQP 1304
Cdd:cd12068      1 YVVALRSYITDDKSLLSFHRGDLIKLLPMAGLEPGWQFGSTGGRSGLFPADIVQP 55
MYSc smart00242
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ...
 2-159 1.85e-24

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: 111.10  E-value: 1.85e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601426     2 LGQSQLQLVGSLFQEAEPQSRGGRGRPTLASRFQQALEDLIARLGRSHVYFIQCLTPNPGKLPGLFDVGHVTEQLHQAAI 81
Cdd:smart00242  519 LQSSKNPLIASLFPSGVSNAGSKKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGV 598

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601426    82 LEAVGTRSANFPVRVPFEAFLASFQAL--GSEGQEDLSDREKCGAVLsQVLGAESPLYHLGATKVLLQEQGWQRLEELRD 159
Cdd:smart00242  599 LENIRIRRAGFPYRLPFDEFLQRYRVLlpDTWPPWGGDAKKACEALL-QSLGLDEDEYQLGKTKVFLRPGQLAELEELRE 677
MyTH4 pfam00784
MyTH4 domain; Domain in myosin and kinesin tails, present twice in myosin-VIIa, and also ...
 363-465 4.70e-23

MyTH4 domain; Domain in myosin and kinesin tails, present twice in myosin-VIIa, and also present in 3 other myosins.


Pssm-ID: 459939  Cd Length: 105  Bit Score: 95.34  E-value: 4.70e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601426  363 YLVRQGQCRPGLRNELFSQLVAQLWQNPDEQQSQRGWALMAVLLSAFPPLPVLQKPLLKFVSDQAP------RGMAALCQ 436
Cdd:pfam00784    3 NILQKGLKRPELRDEIYCQLIKQTTNNPKPESLLRGWQLLALCLGTFPPSKKLLKYLLKFLKRHADdpsrevGKYAQFCL 82

                           90       100
                   ....*....|....*....|....*....
gi 1034601426  437 HKLlgaleQSQLASGAtRAHPPTQLEWLA 465
Cdd:pfam00784   83 KRL-----KRTLKNGG-RKYPPSREEIEA 105
MyTH4 smart00139
Domain in Myosin and Kinesin Tails; Domain present twice in myosin-VIIa, and also present in 3 ...
 320-465 1.72e-21

Domain in Myosin and Kinesin Tails; Domain present twice in myosin-VIIa, and also present in 3 other myosins.


Pssm-ID: 214535  Cd Length: 152  Bit Score: 92.81  E-value: 1.72e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601426   320 PLAKPLTQLDGDNPQR-ALDINKVMLRLLGDGSLE-SWQRQIMGAYLVRQGQCRPGLRNELFSQLVAQLWQNPDEQQSQR 397
Cdd:smart00139    5 PIKTSLLKLESDELQKeAVKIFKAILKFMGDIPLPrPDSHLDLVQFILQKGLDHPELRDEIYCQLIKQLTDNPSRQSEER 84

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034601426   398 GWALMAVLLSAFPPLPVLQKPLLKFVSDQAP----RGMAALCQHKLlgaleQSQLASGAtRAHPPTQLEWLA 465
Cdd:smart00139   85 GWQLLYLCTSLFPPSERLLPYLLQFLSRRADpgseQGLAKYCLYRL-----ERTLKNGA-RKQPPSRLELEA 150
COG5022 COG5022
Myosin heavy chain [General function prediction only];
2-203 4.76e-19

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 94.76  E-value: 4.76e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601426    2 LGQSQLQLVGSLF---QEAEPQSRggrgRPTLASRFQQALEDLIARLGRSHVYFIQCLTPNPGKLPGLFDVGHVTEQLHQ 78
Cdd:COG5022    580 LKASTNEFVSTLFddeENIESKGR----FPTLGSRFKESLNSLMSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRC 655

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601426   79 AAILEAVGTRSANFPVRVPFEAFLASFQALGSEGQ------EDLSDREKCGAVLSQvLGAESPLYHLGATKVLLQEQGWQ 152
Cdd:COG5022    656 CGVLETIRISRAGFPSRWTFDEFVQRYRILSPSKSwtgeytWKEDTKNAVKSILEE-LVIDSSKYQIGNTKVFFKAGVLA 734

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1034601426  153 RLEELRDqqrsqalVDLHRSFHtcisrqrvlpRMQARMRGFQARKRYLRRR 203
Cdd:COG5022    735 ALEDMRD-------AKLDNIAT----------RIQRAIRGRYLRRRYLQAL 768
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
 1644-1758 1.81e-18

FERM central domain; This domain is the central structural domain of the FERM domain.


Pssm-ID: 459788 [Multi-domain]  Cd Length: 117  Bit Score: 82.70  E-value: 1.81e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601426 1644 ETPLHFDNSTYISTHYSQVLWDYLQGKLPVSakaDAQLARLAALQHL-----SKANRNTPSGQDLLAYVPKQLQRQVNTA 1718
Cdd:pfam00373    1 DLELLLQDEVTRHLLYLQAKDDILEGRLPCS---EEEALLLAALQLQaefgdYQPSSHTSEYLSLESFLPKQLLRKMKSK 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1034601426 1719 SIKNLMGQELRRLEGHSPQEAQISFIEAMSQLPLFGYTVY 1758
Cdd:pfam00373   78 ELEKRVLEAHKNLRGLSAEEAKLKYLQIAQSLPTYGVEFF 117
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 1562-1758 1.26e-17

Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in myosins, ezrin, radixin, moesin, protein tyrosine phosphatases. Plasma membrane-binding domain. These proteins play structural and regulatory roles in the assembly and stabilization of specialized plasmamembrane domains. Some PDZ domain containing proteins bind one or more of this family. Now includes JAKs.


Pssm-ID: 214604 [Multi-domain]  Cd Length: 201  Bit Score: 83.11  E-value: 1.26e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601426  1562 LLIHLPGGVDYRTNIQTFTVAAEVQEELCRQMGItepQEVQEFALFLIKEKSQLVRPLQPAEYLnsvvVDQDVSLHSRRL 1641
Cdd:smart00295    2 LKVYLLDGTTLEFEVDSSTTAEELLETVCRKLGI---RESEYFGLQFEDPDEDLRHWLDPAKTL----LDQDVKSEPLTL 74

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601426  1642 H------WETPLHF--DNSTYIStHYSQVLWDYLQGKLPVSakaDAQLARLAALQHLSKANRNTPSGQDLL------AYV 1707
Cdd:smart00295   75 YfrvkfyPPDPNQLkeDPTRLNL-LYLQVRNDILEGRLPCP---EEEALLLAALALQAEFGDYDEELHDLRgelslkRFL 150

                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|.
gi 1034601426  1708 PKQLQRQVNTASIKNLMGQELRRLEGHSPQEAQISFIEAMSQLPLFGYTVY 1758
Cdd:smart00295  151 PKQLLDSRKLKEWRERIVELHKELIGLSPEEAKLKYLELARKLPTYGVELF 201
PTZ00014 PTZ00014
myosin-A; Provisional
 1-210 2.01e-15

myosin-A; Provisional


Pssm-ID: 240229 [Multi-domain]  Cd Length: 821  Bit Score: 82.39  E-value: 2.01e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601426    1 MLGQSQLQLVGSLFQEAEPQsRGGRGRPTL-ASRFQQALEDLIARLGRSHVYFIQCLTPNPGKLPGLFDVGHVTEQLHQA 79
Cdd:PTZ00014   611 VVKASPNPLVRDLFEGVEVE-KGKLAKGQLiGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSL 689

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601426   80 AILEAVGTRSANFPVRVPFEAFLASFQALGSEGQED--LSDREKCGAVLSQV-LGAESplYHLGATKVLLQEQGwqrLEE 156
Cdd:PTZ00014   690 SILEALQLRQLGFSYRRTFAEFLSQFKYLDLAVSNDssLDPKEKAEKLLERSgLPKDS--YAIGKTMVFLKKDA---AKE 764

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034601426  157 LRDQQRS-----QALVDLhrsFHTCISRQRVLPRMQARMRGFQARKRYLRRRAALGQLN 210
Cdd:PTZ00014   765 LTQIQREklaawEPLVSV---LEALILKIKKKRKVRKNIKSLVRIQAHLRRHLVIAEIK 820
Myosin_head pfam00063
Myosin head (motor domain);
2-144 1.03e-12

Myosin head (motor domain);


Pssm-ID: 395017 [Multi-domain]  Cd Length: 674  Bit Score: 73.08  E-value: 1.03e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601426    2 LGQSQLQLVGSLFQEAEPQ----------SRGGRGR----PTLASRFQQALEDLIARLGRSHVYFIQCLTPNPGKLPGLF 67
Cdd:pfam00063  514 LKSSSDPLLAELFPDYETAesaaanesgkSTPKRTKkkrfITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVF 593

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034601426   68 DVGHVTEQLHQAAILEAVGTRSANFPVRVPFEAFLASFQALGSEGQ-EDLSDREK-CGAVLSQvLGAESPLYHLGATKV 144
Cdd:pfam00063  594 DNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQEFVQRYRILAPKTWpKWKGDAKKgCEAILQS-LNLDKEEYQFGKTKI 671
FERM_B-lobe cd14473
FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C ...
 1658-1750 2.41e-12

FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C/N, alpha-, and C-lobe/A-lobe, B-lobe, C-lobe/F1, F2, F3). The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases, the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the pleckstrin homology (PH) and phosphotyrosine binding (PTB) domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 271216  Cd Length: 99  Bit Score: 64.58  E-value: 2.41e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601426 1658 HYSQVLWDYLQGKLPVSakaDAQLARLAALQHLSK-----ANRNTPSGQDLLAYVPKQLQRQVNTASIKNLMGQELRRLE 1732
Cdd:cd14473      5 LYLQVKRDILEGRLPCS---EETAALLAALALQAEygdydPSEHKPKYLSLKRFLPKQLLKQRKPEEWEKRIVELHKKLR 81

                           90
                   ....*....|....*...
gi 1034601426 1733 GHSPQEAQISFIEAMSQL 1750
Cdd:cd14473     82 GLSPAEAKLKYLKIARKL 99
SH3_2 pfam07653
Variant SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in ...
 1250-1304 7.29e-10

Variant SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal transduction related to cytoskeletal organization. First described in the Src cytoplasmic tyrosine kinase. The structure is a partly opened beta barrel.


Pssm-ID: 429575 [Multi-domain]  Cd Length: 54  Bit Score: 56.07  E-value: 7.29e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1034601426 1250 YVIALRSYITDNCSLLSFHRGDLIKLLPvaTLEPGWQFGSAGGRSGLFPADIVQP 1304
Cdd:pfam07653    1 YGRVIFDYVGTDKNGLTLKKGDVVKVLG--KDNDGWWEGETGGRVGLVPSTAVEE 53
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
 1247-1303 1.07e-06

Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences containing proline and hydrophobic amino acids. Pro-containing polypeptides may bind to SH3 domains in 2 different binding orientations.


Pssm-ID: 214620 [Multi-domain]  Cd Length: 56  Bit Score: 47.15  E-value: 1.07e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034601426  1247 DSGYVIALRSYITDNCSLLSFHRGDLIKLLpvATLEPGWQFG-SAGGRSGLFPADIVQ 1303
Cdd:smart00326    1 EGPQVRALYDYTAQDPDELSFKKGDIITVL--EKSDDGWWKGrLGRGKEGLFPSNYVE 56
FERM_C1_MyoVII cd13198
FERM domain C-lobe, repeat 1, of Myosin VII (MyoVII/Myo7); MyoVII, a MyTH-FERM myosin, is an ...
 1152-1246 2.41e-03

FERM domain C-lobe, repeat 1, of Myosin VII (MyoVII/Myo7); MyoVII, a MyTH-FERM myosin, is an actin-based motor protein essential for a variety of biological processes in the actin cytoskeleton function. Mutations in MyoVII leads to problems in sensory perception: deafness and blindness in humans (Usher Syndrome), retinal defects and deafness in mice (shaker 1), and aberrant auditory and vestibular function in zebrafish. Myosin VIIAs have plus (barbed) end-directed motor activity on actin filaments and a characteristic actin-activated ATPase activity. MyoVII consists of a conserved spectrin-like, SH3 subdomain N-terminal region, a motor/head region, a neck made of 4-5 IQ motifs, and a tail consisting of a coiled-coil domain, followed by a tandem repeat of myosin tail homology 4 (MyTH4) domains and partial FERM domains that are separated by an SH3 subdomain and are thought to mediate dimerization and binding to other proteins or cargo. Members include: MyoVIIa, MyoVIIb, and MyoVII members that do not have distinct myosin VIIA and myosin VIIB genes. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs) , the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 270019  Cd Length: 99  Bit Score: 39.12  E-value: 2.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601426 1152 FSRFF---PVSGES--GSDVqLLAVSHRGLRLLKvtqgpglrpDQLKILCSYSFAEVLGVECR-----GGSTLELS-LKS 1220
Cdd:cd13198      3 FSRFFeatKFSGPSlpKSEV-IIAVNWTGIYFVD---------EQEQVLLELSFPEITGVSSSrgkrdGGQSFTLTtIQG 72

                           90       100
                   ....*....|....*....|....*.
gi 1034601426 1221 EQLVLHTARARAIEALVELFLNELKK 1246
Cdd:cd13198     73 EEFVFQSPNAEDIAELVNYFLEGLRK 98
 
Name Accession Description Interval E-value
MYSc_Myo35 cd14896
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ...
 1-147 1.21e-79

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: 277.43  E-value: 1.21e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601426    1 MLGQSQLQLVGSLFQEAEPQSRGGRGRPTLASRFQQALEDLIARLGRSHVYFIQCLTPNPGKLPGLFDVGHVTEQLHQAA 80
Cdd:cd14896    498 MLAQSQLQLVGSLFQEAEPQYGLGQGKPTLASRFQQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAG 577

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034601426   81 ILEAVGTRSANFPVRVPFEAFLASFQALGSEGQEDLSDREKCGAVLSQVLGAESPLYHLGATKVLLQ 147
Cdd:cd14896    578 ILEAIGTRSEGFPVRVPFQAFLARFGALGSERQEALSDRERCGAILSQVLGAESPLYHLGATKVLLK 644
MyTH4 smart00139
Domain in Myosin and Kinesin Tails; Domain present twice in myosin-VIIa, and also present in 3 ...
 1408-1546 4.51e-38

Domain in Myosin and Kinesin Tails; Domain present twice in myosin-VIIa, and also present in 3 other myosins.


Pssm-ID: 214535  Cd Length: 152  Bit Score: 140.19  E-value: 4.51e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601426  1408 YTKAPIQESLLSLSDDV-SKLAVASFLALMRFMGDQSKPRGKDEMDLLYELLKLC-QQEKLRDEIYCQVIKQVTGHPRPE 1485
Cdd:smart00139    1 YTKDPIKTSLLKLESDElQKEAVKIFKAILKFMGDIPLPRPDSHLDLVQFILQKGlDHPELRDEIYCQLIKQLTDNPSRQ 80

                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034601426  1486 HCTRGWSFLSLLTGFFPPSTRLMPYLTKFLQ---DSGPSQELARSSQEHLQRTVKYGGrRRMPP 1546
Cdd:smart00139   81 SEERGWQLLYLCTSLFPPSERLLPYLLQFLSrraDPGSEQGLAKYCLYRLERTLKNGA-RKQPP 143
MyTH4 pfam00784
MyTH4 domain; Domain in myosin and kinesin tails, present twice in myosin-VIIa, and also ...
 1454-1552 1.60e-34

MyTH4 domain; Domain in myosin and kinesin tails, present twice in myosin-VIIa, and also present in 3 other myosins.


Pssm-ID: 459939  Cd Length: 105  Bit Score: 128.08  E-value: 1.60e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601426 1454 LYELLKLC-QQEKLRDEIYCQVIKQVTGHPRPEHCTRGWSFLSLLTGFFPPSTRLMPYLTKFLQD-----SGPSQELARS 1527
Cdd:pfam00784    1 AQNILQKGlKRPELRDEIYCQLIKQTTNNPKPESLLRGWQLLALCLGTFPPSKKLLKYLLKFLKRhaddpSREVGKYAQF 80

                           90       100
                   ....*....|....*....|....*
gi 1034601426 1528 SQEHLQRTVKYGGRRRMPPPGEMKA 1552
Cdd:pfam00784   81 CLKRLKRTLKNGGRKYPPSREEIEA 105
FERM_C_MyoXV cd13201
FERM domain C-lobe of Myosin XV (MyoXV/Myo15); MyoXV, a MyTH-FERM myosin, are actin-based ...
 1754-1855 4.00e-34

FERM domain C-lobe of Myosin XV (MyoXV/Myo15); MyoXV, a MyTH-FERM myosin, are actin-based motor proteins essential for a variety of biological processes in actin cytoskeleton function. Specifically MyoXV functions in the actin organization in hair cells of the organ of Corti. Mutations in Human MyoXVa causes non-syndromic deafness, DFNB3 and the mouse shaker-2 mutation. MyoXV consists of a N-terminal motor/head region, a neck made of 1-3 IQ motifs, and a tail that consists of either a myosin tail homology 4 (MyTH4) domains, followed by an SH3 domain, and a MyTH-FERM domains as in rat Myo15 or two MyTH-FERM domains separated by a SH3 domain as in human Myo15A. The MyTH-FERM domains are thought to mediate dimerization and binding to other proteins or cargo. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 270022  Cd Length: 101  Bit Score: 126.95  E-value: 4.00e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601426 1754 GYTVYGVLRVSMQALSGPTLLGLNRQHLILMDPSSQSLYCRIALKSLQRLHLLSPlEEKGPPGLEVNYGSADNPQTIWFE 1833
Cdd:cd13201      1 GSNFFYVQRVSDPRLPGPCLLALNREGLHFLDPKTHETLLRIPLKEVQSTRKLRP-LEDGTPFLDIKYGNLMQQRTIRLE 79

                           90       100
                   ....*....|....*....|..
gi 1034601426 1834 LPQAQELLYTTVFLIDSSASCT 1855
Cdd:cd13201     80 TDQAHEISRLIAQYIEEASENR 101
SH3_MYO15B cd12068
Src Homology 3 domain of Myosin XVb; Myosin XVb, also called KIAA1783, was named based on its ...
 1250-1304 1.36e-30

Src Homology 3 domain of Myosin XVb; Myosin XVb, also called KIAA1783, was named based on its similarity with myosin XVa. It is a transcribed and unprocessed pseudogene whose predicted amino acid sequence contains mutated or deleted amino acid residues that are normally conserved and important for myosin function. The related myosin XVa is important for normal growth of mechanosensory stereocilia of inner ear hair cells. Myosin XVa contains a unique N-terminal extension followed by a motor domain, light chain-binding IQ motifs, and a tail consisting of a pair of MyTH4-FERM tandems separated by a SH3 domain, and a PDZ domain. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies.


Pssm-ID: 213001  Cd Length: 55  Bit Score: 115.36  E-value: 1.36e-30
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1034601426 1250 YVIALRSYITDNCSLLSFHRGDLIKLLPVATLEPGWQFGSAGGRSGLFPADIVQP 1304
Cdd:cd12068      1 YVVALRSYITDDKSLLSFHRGDLIKLLPMAGLEPGWQFGSTGGRSGLFPADIVQP 55
SH3_MYO15 cd11884
Src Homology 3 domain of Myosin XV; This subfamily is composed of proteins with similarity to ...
 1250-1304 4.49e-25

Src Homology 3 domain of Myosin XV; This subfamily is composed of proteins with similarity to Myosin XVa. Myosin XVa is an unconventional myosin that is critical for the normal growth of mechanosensory stereocilia of inner ear hair cells. Mutations in the myosin XVa gene are associated with nonsyndromic hearing loss. Myosin XVa contains a unique N-terminal extension followed by a motor domain, light chain-binding IQ motifs, and a tail consisting of a pair of MyTH4-FERM tandems separated by a SH3 domain, and a PDZ domain. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies.


Pssm-ID: 212817 [Multi-domain]  Cd Length: 56  Bit Score: 99.32  E-value: 4.49e-25
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034601426 1250 YVIALRSYITDNCSLLSFHRGDLIKLLPVAT-LEPGWQFGSAGGRSGLFPADIVQP 1304
Cdd:cd11884      1 YVVAVRAYITRDQTLLSFHKGDVIKLLPKEGpLDPGWLFGTLDGRSGAFPKEYVQP 56
MYSc cd00124
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ...
 31-146 4.98e-25

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


Pssm-ID: 276950 [Multi-domain]  Cd Length: 633  Bit Score: 112.68  E-value: 4.98e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601426   31 ASRFQQALEDLIARLGRSHVYFIQCLTPNPGKLPGLFDVGHVTEQLHQAAILEAVGTRSANFPVRVPFEAFLASFQALGS 110
Cdd:cd00124    516 GSQFRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYRILAP 595

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1034601426  111 EGQEDLSDREKCGAV-LSQVLGAESPLYHLGATKVLL 146
Cdd:cd00124    596 GATEKASDSKKAAVLaLLLLLKLDSSGYQLGKTKVFL 632
MYSc smart00242
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ...
 2-159 1.85e-24

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: 111.10  E-value: 1.85e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601426     2 LGQSQLQLVGSLFQEAEPQSRGGRGRPTLASRFQQALEDLIARLGRSHVYFIQCLTPNPGKLPGLFDVGHVTEQLHQAAI 81
Cdd:smart00242  519 LQSSKNPLIASLFPSGVSNAGSKKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGV 598

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601426    82 LEAVGTRSANFPVRVPFEAFLASFQAL--GSEGQEDLSDREKCGAVLsQVLGAESPLYHLGATKVLLQEQGWQRLEELRD 159
Cdd:smart00242  599 LENIRIRRAGFPYRLPFDEFLQRYRVLlpDTWPPWGGDAKKACEALL-QSLGLDEDEYQLGKTKVFLRPGQLAELEELRE 677
MyTH4 pfam00784
MyTH4 domain; Domain in myosin and kinesin tails, present twice in myosin-VIIa, and also ...
 363-465 4.70e-23

MyTH4 domain; Domain in myosin and kinesin tails, present twice in myosin-VIIa, and also present in 3 other myosins.


Pssm-ID: 459939  Cd Length: 105  Bit Score: 95.34  E-value: 4.70e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601426  363 YLVRQGQCRPGLRNELFSQLVAQLWQNPDEQQSQRGWALMAVLLSAFPPLPVLQKPLLKFVSDQAP------RGMAALCQ 436
Cdd:pfam00784    3 NILQKGLKRPELRDEIYCQLIKQTTNNPKPESLLRGWQLLALCLGTFPPSKKLLKYLLKFLKRHADdpsrevGKYAQFCL 82

                           90       100
                   ....*....|....*....|....*....
gi 1034601426  437 HKLlgaleQSQLASGAtRAHPPTQLEWLA 465
Cdd:pfam00784   83 KRL-----KRTLKNGG-RKYPPSREEIEA 105
MYSc_Myo15 cd01387
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ...
 1-147 2.77e-22

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: 104.06  E-value: 2.77e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601426    1 MLGQSQLQLVGSLFQEAEPQS-----RGGRGR--------PTLASRFQQALEDLIARLGRSHVYFIQCLTPNPGKLPGLF 67
Cdd:cd01387    497 LLVSSRTRVVAHLFSSHRAQTdkappRLGKGRfvtmkprtPTVAARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLF 576

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601426   68 DVGHVTEQLHQAAILEAVGTRSANFPVRVPFEAFLASFQALGSEGQEDLSDREKCGAVLSQVLGAE-SPLYHLGATKVLL 146
Cdd:cd01387    577 DMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYRCLVALKLPRPAPGDMCVSLLSRLCTVTpKDMYRLGATKVFL 656


                   .
gi 1034601426  147 Q 147
Cdd:cd01387    657 R 657
MyTH4 smart00139
Domain in Myosin and Kinesin Tails; Domain present twice in myosin-VIIa, and also present in 3 ...
 320-465 1.72e-21

Domain in Myosin and Kinesin Tails; Domain present twice in myosin-VIIa, and also present in 3 other myosins.


Pssm-ID: 214535  Cd Length: 152  Bit Score: 92.81  E-value: 1.72e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601426   320 PLAKPLTQLDGDNPQR-ALDINKVMLRLLGDGSLE-SWQRQIMGAYLVRQGQCRPGLRNELFSQLVAQLWQNPDEQQSQR 397
Cdd:smart00139    5 PIKTSLLKLESDELQKeAVKIFKAILKFMGDIPLPrPDSHLDLVQFILQKGLDHPELRDEIYCQLIKQLTDNPSRQSEER 84

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034601426   398 GWALMAVLLSAFPPLPVLQKPLLKFVSDQAP----RGMAALCQHKLlgaleQSQLASGAtRAHPPTQLEWLA 465
Cdd:smart00139   85 GWQLLYLCTSLFPPSERLLPYLLQFLSRRADpgseQGLAKYCLYRL-----ERTLKNGA-RKQPPSRLELEA 150
MYSc_Myo10 cd14873
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ...
 1-147 6.26e-20

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: 96.40  E-value: 6.26e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601426    1 MLGQSQLQLVGSLFQEAEPQSRG-------GRGRPTLASRFQQALEDLIARLGRSHVYFIQCLTPNPGKLPGLFDVGHVT 73
Cdd:cd14873    499 LLRESRFDFIYDLFEHVSSRNNQdtlkcgsKHRRPTVSSQFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVL 578

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034601426   74 EQLHQAAILEAVGTRSANFPVRVPFEAFLASFQALGSEGQEDLSDREKCGAVLsQVLGAESPLYHLGATKVLLQ 147
Cdd:cd14873    579 NQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMRNLALPEDVRGKCTSLL-QLYDASNSEWQLGKTKVFLR 651
COG5022 COG5022
Myosin heavy chain [General function prediction only];
2-203 4.76e-19

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 94.76  E-value: 4.76e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601426    2 LGQSQLQLVGSLF---QEAEPQSRggrgRPTLASRFQQALEDLIARLGRSHVYFIQCLTPNPGKLPGLFDVGHVTEQLHQ 78
Cdd:COG5022    580 LKASTNEFVSTLFddeENIESKGR----FPTLGSRFKESLNSLMSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRC 655

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601426   79 AAILEAVGTRSANFPVRVPFEAFLASFQALGSEGQ------EDLSDREKCGAVLSQvLGAESPLYHLGATKVLLQEQGWQ 152
Cdd:COG5022    656 CGVLETIRISRAGFPSRWTFDEFVQRYRILSPSKSwtgeytWKEDTKNAVKSILEE-LVIDSSKYQIGNTKVFFKAGVLA 734

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1034601426  153 RLEELRDqqrsqalVDLHRSFHtcisrqrvlpRMQARMRGFQARKRYLRRR 203
Cdd:COG5022    735 ALEDMRD-------AKLDNIAT----------RIQRAIRGRYLRRRYLQAL 768
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
 1644-1758 1.81e-18

FERM central domain; This domain is the central structural domain of the FERM domain.


Pssm-ID: 459788 [Multi-domain]  Cd Length: 117  Bit Score: 82.70  E-value: 1.81e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601426 1644 ETPLHFDNSTYISTHYSQVLWDYLQGKLPVSakaDAQLARLAALQHL-----SKANRNTPSGQDLLAYVPKQLQRQVNTA 1718
Cdd:pfam00373    1 DLELLLQDEVTRHLLYLQAKDDILEGRLPCS---EEEALLLAALQLQaefgdYQPSSHTSEYLSLESFLPKQLLRKMKSK 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1034601426 1719 SIKNLMGQELRRLEGHSPQEAQISFIEAMSQLPLFGYTVY 1758
Cdd:pfam00373   78 ELEKRVLEAHKNLRGLSAEEAKLKYLQIAQSLPTYGVEFF 117
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 1562-1758 1.26e-17

Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in myosins, ezrin, radixin, moesin, protein tyrosine phosphatases. Plasma membrane-binding domain. These proteins play structural and regulatory roles in the assembly and stabilization of specialized plasmamembrane domains. Some PDZ domain containing proteins bind one or more of this family. Now includes JAKs.


Pssm-ID: 214604 [Multi-domain]  Cd Length: 201  Bit Score: 83.11  E-value: 1.26e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601426  1562 LLIHLPGGVDYRTNIQTFTVAAEVQEELCRQMGItepQEVQEFALFLIKEKSQLVRPLQPAEYLnsvvVDQDVSLHSRRL 1641
Cdd:smart00295    2 LKVYLLDGTTLEFEVDSSTTAEELLETVCRKLGI---RESEYFGLQFEDPDEDLRHWLDPAKTL----LDQDVKSEPLTL 74

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601426  1642 H------WETPLHF--DNSTYIStHYSQVLWDYLQGKLPVSakaDAQLARLAALQHLSKANRNTPSGQDLL------AYV 1707
Cdd:smart00295   75 YfrvkfyPPDPNQLkeDPTRLNL-LYLQVRNDILEGRLPCP---EEEALLLAALALQAEFGDYDEELHDLRgelslkRFL 150

                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|.
gi 1034601426  1708 PKQLQRQVNTASIKNLMGQELRRLEGHSPQEAQISFIEAMSQLPLFGYTVY 1758
Cdd:smart00295  151 PKQLLDSRKLKEWRERIVELHKELIGLSPEEAKLKYLELARKLPTYGVELF 201
MYSc_Myo7 cd01381
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ...
 1-146 2.54e-17

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: 88.08  E-value: 2.54e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601426    1 MLGQSQLQLVGSLFQEAEPQSRGGRGR-PTLASRFQQALEDLIARLGRSHVYFIQCLTPNPGKLPGLFDVGHVTEQLHQA 79
Cdd:cd01381    500 LVQSSKNKFLKQLFNEDISMGSETRKKsPTLSSQFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYS 579

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034601426   80 AILEAVGTRSANFPVRVPFEAFLASFQALGS-----EGQEDLSDREKCGAVlsqVLGAESpLYHLGATKVLL 146
Cdd:cd01381    580 GMMETIRIRKAGYPIRHTFEEFVERYRVLVPgippaHKTDCRAATRKICCA---VLGGDA-DYQLGKTKIFL 647
MYSc_Myo4 cd14872
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ...
 8-145 1.31e-16

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: 85.98  E-value: 1.31e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601426    8 QLVGSLFQEAEPQSRggRGRPTLASRFQQALEDLIARLGRSHVYFIQCLTPNPGKLPGLFDVGHVTEQLHQAAILEAVGT 87
Cdd:cd14872    506 KLIAVLFPPSEGDQK--TSKVTLGGQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKI 583

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601426   88 RSANFPVRVPFEAFLASFQALGSEGQEDLS--DREKCGAVLSQVLGAESPLYhLGATKVL 145
Cdd:cd14872    584 RKTGYPFRYSHERFLKRYRFLVKTIAKRVGpdDRQRCDLLLKSLKQDFSKVQ-VGKTRVL 642
MYSc_Myo22 cd14883
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ...
 1-146 9.02e-16

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: 83.14  E-value: 9.02e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601426    1 MLGQSQLQLVGSLF---QEAEP------------QSRGGRGRPTLASRFQQALEDLIARLGRSHVYFIQCLTPNPGKLPG 65
Cdd:cd14883    499 LMSRSKNKFVKELFtypDLLALtglsislggdttSRGTSKGKPTVGDTFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPN 578

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601426   66 LFDVGHVTEQLHQAAILEAVGTRSANFPVRVPFEAFLASFQALgSEGQEDLSDREKCGAV--LSQVLGAESPLYHLGATK 143
Cdd:cd14883    579 VFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCL-DPRARSADHKETCGAVraLMGLGGLPEDEWQVGKTK 657


                   ...
gi 1034601426  144 VLL 146
Cdd:cd14883    658 VFL 660
MYSc_Myo11 cd01384
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ...
 1-146 1.40e-15

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: 82.34  E-value: 1.40e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601426    1 MLGQSQLQLVGSLFqeaEPQSRGGRGRPT----LASRFQQALEDLIARLGRSHVYFIQCLTPNPGKLPGLFDVGHVTEQL 76
Cdd:cd01384    502 LLNASKCPFVAGLF---PPLPREGTSSSSkfssIGSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQL 578

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601426   77 HQAAILEAVGTRSANFPVRVPFEAFLASFQALGSEGQEDLSDREKCGAVLSQVLGAESplYHLGATKVLL 146
Cdd:cd01384    579 RCGGVLEAVRISCAGYPTRKPFEEFLDRFGLLAPEVLKGSDDEKAACKKILEKAGLKG--YQIGKTKVFL 646
PTZ00014 PTZ00014
myosin-A; Provisional
 1-210 2.01e-15

myosin-A; Provisional


Pssm-ID: 240229 [Multi-domain]  Cd Length: 821  Bit Score: 82.39  E-value: 2.01e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601426    1 MLGQSQLQLVGSLFQEAEPQsRGGRGRPTL-ASRFQQALEDLIARLGRSHVYFIQCLTPNPGKLPGLFDVGHVTEQLHQA 79
Cdd:PTZ00014   611 VVKASPNPLVRDLFEGVEVE-KGKLAKGQLiGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSL 689

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601426   80 AILEAVGTRSANFPVRVPFEAFLASFQALGSEGQED--LSDREKCGAVLSQV-LGAESplYHLGATKVLLQEQGwqrLEE 156
Cdd:PTZ00014   690 SILEALQLRQLGFSYRRTFAEFLSQFKYLDLAVSNDssLDPKEKAEKLLERSgLPKDS--YAIGKTMVFLKKDA---AKE 764

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034601426  157 LRDQQRS-----QALVDLhrsFHTCISRQRVLPRMQARMRGFQARKRYLRRRAALGQLN 210
Cdd:PTZ00014   765 LTQIQREklaawEPLVSV---LEALILKIKKKRKVRKNIKSLVRIQAHLRRHLVIAEIK 820
MYSc_Myo29 cd14890
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ...
 29-147 3.34e-14

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: 77.89  E-value: 3.34e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601426   29 TLASRFQQALEDLIARLGRSHVYFIQCLTPNPGKLPGLFDVGHVTEQLHQAAILEAVGTRSANFPVRVPFEAFLASFQAL 108
Cdd:cd14890    548 SVGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGMMEAIQIRQQGFALREEHDSFFYDFQVL 627

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1034601426  109 gsegQEDLSDREKCGAVLSQVLGAESPLYHLGATKVLLQ 147
Cdd:cd14890    628 ----LPTAENIEQLVAVLSKMLGLGKADWQIGSSKIFLK 662
MYSc_Myo16 cd14878
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ...
 29-147 4.77e-14

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: 77.55  E-value: 4.77e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601426   29 TLASRFQQALEDLIARLGRSHVYFIQCLTPNPGKLPGLFDVGHVTEQLHQAAILEAVGTRSANFPVRVPFEAFLASFQAL 108
Cdd:cd14878    538 TIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPL 617

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1034601426  109 GSE---GQEDLSDREKCGAVLSQvlgAESPLYHLGATKVLLQ 147
Cdd:cd14878    618 ADTllgEKKKQSAEERCRLVLQQ---CKLQGWQMGVRKVFLK 656
MYSc_Myo42 cd14903
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ...
 15-147 6.09e-14

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: 77.12  E-value: 6.09e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601426   15 QEAEPQSRGGRGRP----TLASRFQQALEDLIARLGRSHVYFIQCLTPNPGKLPGLFDVGHVTEQLHQAAILEAVGTRSA 90
Cdd:cd14903    521 TSLARGARRRRGGAltttTVGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRA 600

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034601426   91 NFPVRVPFEAFLASFQALGSEG-QEDLSDREKCGAVLSQvLGAESPL-YHLGATKVLLQ 147
Cdd:cd14903    601 AYPNRLLHEEFLDKFWLFLPEGrNTDVPVAERCEALMKK-LKLESPEqYQMGLTRIYFQ 658
MYSc_Myo40 cd14901
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ...
 29-146 6.17e-14

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: 77.14  E-value: 6.17e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601426   29 TLASRFQQALEDLIARLGRSHVYFIQCLTPNPGKLPGLFDVGHVTEQLHQAAILEAVGTRSANFPVRVPFEAFLASFQAL 108
Cdd:cd14901    531 TVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFPHDAFVHTYSCL 610

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1034601426  109 GSEGQED------LSDREKCGAVLSQVLGAESPLYHLGATKVLL 146
Cdd:cd14901    611 APDGASDtwkvneLAERLMSQLQHSELNIEHLPPFQVGKTKVFL 654
Myosin_head pfam00063
Myosin head (motor domain);
2-144 1.03e-12

Myosin head (motor domain);


Pssm-ID: 395017 [Multi-domain]  Cd Length: 674  Bit Score: 73.08  E-value: 1.03e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601426    2 LGQSQLQLVGSLFQEAEPQ----------SRGGRGR----PTLASRFQQALEDLIARLGRSHVYFIQCLTPNPGKLPGLF 67
Cdd:pfam00063  514 LKSSSDPLLAELFPDYETAesaaanesgkSTPKRTKkkrfITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVF 593

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034601426   68 DVGHVTEQLHQAAILEAVGTRSANFPVRVPFEAFLASFQALGSEGQ-EDLSDREK-CGAVLSQvLGAESPLYHLGATKV 144
Cdd:pfam00063  594 DNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQEFVQRYRILAPKTWpKWKGDAKKgCEAILQS-LNLDKEEYQFGKTKI 671
FERM_B-lobe cd14473
FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C ...
 1658-1750 2.41e-12

FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C/N, alpha-, and C-lobe/A-lobe, B-lobe, C-lobe/F1, F2, F3). The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases, the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the pleckstrin homology (PH) and phosphotyrosine binding (PTB) domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 271216  Cd Length: 99  Bit Score: 64.58  E-value: 2.41e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601426 1658 HYSQVLWDYLQGKLPVSakaDAQLARLAALQHLSK-----ANRNTPSGQDLLAYVPKQLQRQVNTASIKNLMGQELRRLE 1732
Cdd:cd14473      5 LYLQVKRDILEGRLPCS---EETAALLAALALQAEygdydPSEHKPKYLSLKRFLPKQLLKQRKPEEWEKRIVELHKKLR 81

                           90
                   ....*....|....*...
gi 1034601426 1733 GHSPQEAQISFIEAMSQL 1750
Cdd:cd14473     82 GLSPAEAKLKYLKIARKL 99
MYSc_Myo31 cd14892
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ...
 31-146 3.34e-12

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: 71.71  E-value: 3.34e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601426   31 ASRFQQALEDLIARLGRSHVYFIQCLTPNPGKLPGLFDVGHVTEQLHQAAILEAVGTRSANFPVRVPFEAFLASFQAL-- 108
Cdd:cd14892    533 SSKFRTQLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVRIRREGFPIRRQFEEFYEKFWPLar 612

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1034601426  109 ---GSEGQEDLSD----REKCGAVLSQVLGAEspLYHLGATKVLL 146
Cdd:cd14892    613 nkaGVAASPDACDattaRKKCEEIVARALERE--NFQLGRTKVFL 655
MYSc_Myo14 cd14876
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ...
 9-146 3.85e-12

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: 71.56  E-value: 3.85e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601426    9 LVGSLFqEAEPQSRGGRGRPTL-ASRFQQALEDLIARLGRSHVYFIQCLTPNPGKLPGLFDVGHVTEQLHQAAILEAVGT 87
Cdd:cd14876    510 VVKALF-EGVVVEKGKIAKGSLiGSQFLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQL 588

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034601426   88 RSANFPVRVPFEAFLASFQ--ALGSEGQEDLSDREKCGAVLSQVlGAESPLYHLGATKVLL 146
Cdd:cd14876    589 RQLGYSYRRPFEEFLYQFKflDLGIANDKSLDPKVAALKLLESS-GLSEDEYAIGKTMVFL 648
MYSc_Myo36 cd14897
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ...
 30-147 4.07e-12

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: 71.26  E-value: 4.07e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601426   30 LASRFQQALEDLIARLGRSHVYFIQCLTPNPGKLPGLFDVGHVTEQLHQAAILEAVGTRSANFPVRVPFEAFLASFQALG 109
Cdd:cd14897    520 FTSYFKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYEDFVKRYKEIC 599

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1034601426  110 SEGQEDLSDRE-KCGAVLsQVLGAESplYHLGATKVLLQ 147
Cdd:cd14897    600 DFSNKVRSDDLgKCQKIL-KTAGIKG--YQFGKTKVFLK 635
MYSc_Myo8 cd01383
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ...
 19-146 4.19e-12

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: 71.19  E-value: 4.19e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601426   19 PQSRGGRGRPTLASRFQQALEDLIARLGRSHVYFIQCLTPNPGKLPGLFDVGHVTEQLHQAAILEAVGTRSANFPVRVPF 98
Cdd:cd01383    519 KASGSDSQKQSVATKFKGQLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTH 598

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1034601426   99 EAFLASFQAL----GSEGQEDLSDrekCGAVLSQvLGAESPLYHLGATKVLL 146
Cdd:cd01383    599 QEFARRYGFLlpedVSASQDPLST---SVAILQQ-FNILPEMYQVGYTKLFF 646
MYSc_Myo43 cd14904
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ...
 5-142 9.77e-12

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: 69.97  E-value: 9.77e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601426    5 SQLQLVGSLFQEAE--------PQSRGGRGRPTLASRFQQALEDLIARLGRSHVYFIQCLTPNPGKLPGLFDVGHVTEQL 76
Cdd:cd14904    503 SSLDLLTELFGSSEapsetkegKSGKGTKAPKSLGSQFKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQL 582

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034601426   77 HQAAILEAVGTRSANFPVRVPFEAFLASFQALGSEGQEDLSDREKCGAVLSQVlGAESPL-YHLGAT 142
Cdd:cd14904    583 RSAGVIEAIRITRSGYPSRLTPKELATRYAIMFPPSMHSKDVRRTCSVFMTAI-GRKSPLeYQIGKS 648
SH3_MYO15A cd12067
Src Homology 3 domain of Myosin XVa; Myosin XVa is an unconventional myosin that is critical ...
 1250-1304 1.14e-11

Src Homology 3 domain of Myosin XVa; Myosin XVa is an unconventional myosin that is critical for the normal growth of mechanosensory stereocilia of inner ear hair cells. Mutations in the myosin XVa gene are associated with nonsyndromic hearing loss. Myosin XVa contains a unique N-terminal extension followed by a motor domain, light chain-binding IQ motifs, and a tail consisting of a pair of MyTH4-FERM tandems separated by a SH3 domain, and a PDZ domain. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies.


Pssm-ID: 213000  Cd Length: 80  Bit Score: 62.13  E-value: 1.14e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601426 1250 YVIALRSYITDNCSLLSFHRGDLIKLLP-----------------VATLEP--------GWQFGSAGGRSGLFPADIVQP 1304
Cdd:cd12067      1 YVVAVRNYLPEDPALLSFHKGDIIHLQPlegpkvgqyygcvvrkkVMYLEElkrgtpdfGWKFGAIHGRSGVFPAELVQP 80
MYSc_Myo9 cd01385
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ...
 28-146 5.38e-11

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: 67.79  E-value: 5.38e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601426   28 PTLASRFQQALEDLIARLGRSHVYFIQCLTPNPGKLPGLFDVGHVTEQLHQAAILEAVGTRSANFPVRVPFEAFLASFQA 107
Cdd:cd01385    574 PSVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVLRQLRYTGMLETVRIRRSGYSVRYTFQEFITQFQV 653

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1034601426  108 LGSEGQedLSDREKCGAVLSQV-LGAESplYHLGATKVLL 146
Cdd:cd01385    654 LLPKGL--ISSKEDIKDFLEKLnLDRDN--YQIGKTKVFL 689
MYSc_Myo27 cd14888
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ...
 25-117 1.34e-10

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: 66.25  E-value: 1.34e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601426   25 RGRPTLASRFQQALEDLIARLGRSHVYFIQCLTPNPGKLPGLFDVGHVTEQLHQAAILEAVGTRSANFPVRVPFEAFLAS 104
Cdd:cd14888    562 KKFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQLKYGGVLQAVQVSRAGYPVRLSHAEFYND 641

                           90
                   ....*....|....
gi 1034601426  105 FQALGS-EGQEDLS 117
Cdd:cd14888    642 YRILLNgEGKKQLS 655
MYSc_Myo41 cd14902
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ...
 19-108 2.10e-10

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: 65.68  E-value: 2.10e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601426   19 PQSRGGRGR------PTLASRFQQALEDLIARLGRSHVYFIQCLTPNPGKLPGLFDVGHVTEQLHQAAILEAVGTRSANF 92
Cdd:cd14902    544 DNGAAGRRRysmlraPSVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLEAVRIARHGY 623

                           90
                   ....*....|....*.
gi 1034601426   93 PVRVPFEAFLASFQAL 108
Cdd:cd14902    624 SVRLAHASFIELFSGF 639
SH3_2 pfam07653
Variant SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in ...
 1250-1304 7.29e-10

Variant SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal transduction related to cytoskeletal organization. First described in the Src cytoplasmic tyrosine kinase. The structure is a partly opened beta barrel.


Pssm-ID: 429575 [Multi-domain]  Cd Length: 54  Bit Score: 56.07  E-value: 7.29e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1034601426 1250 YVIALRSYITDNCSLLSFHRGDLIKLLPvaTLEPGWQFGSAGGRSGLFPADIVQP 1304
Cdd:pfam07653    1 YGRVIFDYVGTDKNGLTLKKGDVVKVLG--KDNDGWWEGETGGRVGLVPSTAVEE 53
MYSc_Myo24A cd14937
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ...
 1-147 1.12e-09

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: 63.50  E-value: 1.12e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601426    1 MLGQSQLQLVGSLFQEAEPQSRGGRgRPTLASRFQQALEDLIARLGRSHVYFIQCLTPNPGKLPGLFDVGHVTEQLHQAA 80
Cdd:cd14937    493 LLKVSNNKLVRSLYEDVEVSESLGR-KNLITFKYLKNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLS 571

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034601426   81 ILEAVGTrSANFPVRVPFEAFLASFQALGSEGQED--LSDREKCGAVLSQVLgaESPLYHLGATKVLLQ 147
Cdd:cd14937    572 IIETLNI-SFFFQYKYTFDVFLSYFEYLDYSTSKDssLTDKEKVSMILQNTV--DPDLYKVGKTMVFLK 637
MYSc_Myo46 cd14907
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ...
 4-101 3.91e-09

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: 61.59  E-value: 3.91e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601426    4 QSQLQLVGSLFQEAEPQSRGGRGRPT--------LASRFQQALEDLIARLGRSHVYFIQCLTPNPGKLPGLFDVGHVTEQ 75
Cdd:cd14907    543 NSKNRIISSIFSGEDGSQQQNQSKQKksqkkdkfLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQ 622

                           90       100
                   ....*....|....*....|....*.
gi 1034601426   76 LHQAAILEAVGTRSANFPVRVPFEAF 101
Cdd:cd14907    623 IRYLGVLESIRVRKQGYPYRKSYEDF 648
MYSc_Myo19 cd14880
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ...
 1-146 5.27e-09

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: 61.02  E-value: 5.27e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601426    1 MLGQSQLQLVGSLF----QEAEPQSRGGRGRP---TLASRFQQALEDLIARLGRSHVYFIQCLTPNPGKLPGLFDVGHVT 73
Cdd:cd14880    510 LLQQSQDPLLQKLFpanpEEKTQEEPSGQSRApvlTVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVL 589

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034601426   74 EQLHQAAILEAVGTRSANFPVRVPFEAFLASFQALgsegqEDLSDREKCGAVLSQVLGAESPLYHLGATKVLL 146
Cdd:cd14880    590 SQLEACGLVETIHISAAGFPIRVSHQNFVERYKLL-----RRLRPHTSSGPHSPYPAKGLSEPVHCGRTKVFM 657
MYSc_Myo25 cd14886
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ...
 30-147 1.67e-08

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: 59.51  E-value: 1.67e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601426   30 LASRFQQALEDLIARLGRSHVYFIQCLTPNPGKLPGLFDVGHVTEQLHQAAILEAVGTRSANFPVRVPFEAF------LA 103
Cdd:cd14886    530 LGSTFQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFfhrnkiLI 609

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1034601426  104 SFQALGSEGQEDLsdREKCGAVLsQVLGAESPLYHLGATKVLLQ 147
Cdd:cd14886    610 SHNSSSQNAGEDL--VEAVKSIL-ENLGIPCSDYRIGKTKVFLR 650
MYSc_Myh2_mammals cd14912
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ...
 4-147 2.06e-08

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: 59.36  E-value: 2.06e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601426    4 QSQLQLVGSLF---QEAEPQSRGGRGRP----------TLASRFQQALEDLIARLGRSHVYFIQCLTPNPGKLPGLFDVG 70
Cdd:cd14912    515 KSAMKTLAYLFsgaQTAEGASAGGGAKKggkkkgssfqTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHE 594

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601426   71 HVTEQLHQAAILEAVGTRSANFPVRVPFEAFLASFQALGS----EGQedLSDREKCGAVLSQVLGAESPLYHLGATKVLL 146
Cdd:cd14912    595 LVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNAsaipEGQ--FIDSKKASEKLLASIDIDHTQYKFGHTKVFF 672


                   .
gi 1034601426  147 Q 147
Cdd:cd14912    673 K 673
MYSc_Myo13 cd14875
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ...
 25-147 2.44e-08

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: 59.05  E-value: 2.44e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601426   25 RGRPTLASRFQQALEDLIARLGRSHVYFIQCLTPNPGKLPGLFDVGHVTEQLHQAAILEAVGTRSANFPVRVPFEAFLAS 104
Cdd:cd14875    535 RRKQTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRRPIEQFCRY 614

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1034601426  105 FQALGSEGQEDLSDREK----CGAVLS---QVLGAESPLYHLGATKVLLQ 147
Cdd:cd14875    615 FYLIMPRSTASLFKQEKyseaAKDFLAyyqRLYGWAKPNYAVGKTKVFLR 664
MYSc_Myh1_mammals cd14910
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ...
 4-147 2.87e-08

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: 58.97  E-value: 2.87e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601426    4 QSQLQLVGSLFQ---EAEPQSRGGR--GRP------TLASRFQQALEDLIARLGRSHVYFIQCLTPNPGKLPGLFDVGHV 72
Cdd:cd14910    515 KSSMKTLALLFSgaaAAEAEEGGGKkgGKKkgssfqTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELV 594

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034601426   73 TEQLHQAAILEAVGTRSANFPVRVPFEAFLASFQALGS----EGQedLSDREKCGAVLSQVLGAESPLYHLGATKVLLQ 147
Cdd:cd14910    595 LHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNAsaipEGQ--FIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
MYSc_Myh15_mammals cd14929
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ...
 11-147 6.25e-08

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: 57.68  E-value: 6.25e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601426   11 GSLFQEAEPQSRGGRGRPTLASRFQQALEDLIARLGRSHVYFIQCLTPNPGKLPGLFDVGHVTEQLHQAAILEAVGTRSA 90
Cdd:cd14929    524 DSAIQFGEKKRKKGASFQTVASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICRE 603

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601426   91 NFPVRVPFEAFLASFQALGSE---GQEDLSDREKCGAVLSqVLGAESPLYHLGATKVLLQ 147
Cdd:cd14929    604 GFPNRLLYADFKQRYCILNPRtfpKSKFVSSRKAAEELLG-SLEIDHTQYRFGITKVFFK 662
MYSc_Myo28 cd14889
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ...
 23-147 8.81e-08

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: 57.22  E-value: 8.81e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601426   23 GGRGRP-TLASRFQQALEDLIARLGRSHVYFIQCLTPNPGKLPGLFDVGHVTEQLHQAAILEAVGTRSANFPVRVPFEAF 101
Cdd:cd14889    538 FNSTRKqSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFSWRPSFAEF 617

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1034601426  102 LASFQALGSEgqEDLS-DREKCGAVL--SQVLGaesplYHLGATKVLLQ 147
Cdd:cd14889    618 AERYKILLCE--PALPgTKQSCLRILkaTKLVG-----WKCGKTRLFFK 659
SH3 cd00174
Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction ...
 1250-1299 1.03e-07

Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction domains that bind proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. Thus, they are referred to as proline-recognition domains (PRDs). SH3 domains are less selective and show more diverse specificity compared to other PRDs. They have been shown to bind peptide sequences that lack the PxxP motif; examples include the PxxDY motif of Eps8 and the RKxxYxxY sequence in SKAP55. SH3 domain containing proteins play versatile and diverse roles in the cell, including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies, among others. Many members of this superfamily are adaptor proteins that associate with a number of protein partners, facilitating complex formation and signal transduction.


Pssm-ID: 212690 [Multi-domain]  Cd Length: 51  Bit Score: 50.15  E-value: 1.03e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1034601426 1250 YVIALRSYITDNCSLLSFHRGDLIKLLpvATLEPGWQFG-SAGGRSGLFPA 1299
Cdd:cd00174      1 YARALYDYEAQDDDELSFKKGDIITVL--EKDDDGWWEGeLNGGREGLFPA 49
MYSc_Myh6 cd14916
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ...
 4-147 1.81e-07

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: 56.22  E-value: 1.81e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601426    4 QSQLQLVGSLFQEAEPQSRG----GRGRPTLASRFQ-------QALEDLIARLGRSHVYFIQCLTPNPGKLPGLFDVGHV 72
Cdd:cd14916    514 KSSLKLMATLFSTYASADTGdsgkGKGGKKKGSSFQtvsalhrENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLV 593

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034601426   73 TEQLHQAAILEAVGTRSANFPVRVPFEAFLASFQALG----SEGQedLSDREKCGAVLSQVLGAESPLYHLGATKVLLQ 147
Cdd:cd14916    594 MHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNpaaiPEGQ--FIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
MYSc_Myh10 cd14920
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ...
 1-147 2.34e-07

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: 55.79  E-value: 2.34e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601426    1 MLGQSQLQLVGSLFQEAEPQSRGGRGRpTLASRFQQALEDLIARLGRSHVYFIQCLTPNPGKLPGLFDVGHVTEQLHQAA 80
Cdd:cd14920    527 IVGLDQVTGMTETAFGSAYKTKKGMFR-TVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNG 605

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034601426   81 ILEAVGTRSANFPVRVPFEAFLASFQALGSEG-QEDLSDREKCGAVLSQVLGAESPLYHLGATKVLLQ 147
Cdd:cd14920    606 VLEGIRICRQGFPNRIVFQEFRQRYEILTPNAiPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
MYSc_Myo26 cd14887
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ...
 27-144 3.36e-07

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: 55.42  E-value: 3.36e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601426   27 RPTLASRFQQALEDLIARLGRSHVYFIQCLTPNPGKLPGLFDVGHVTEQLHQAAILEAVGTRSANFPVRVPFEAFLASFQ 106
Cdd:cd14887    605 RSTLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVELWRRYE 684

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1034601426  107 A-LGSEGQEDLSDREKCGAVLsQVLGAESPLYHLGATKV 144
Cdd:cd14887    685 TkLPMALREALTPKMFCKIVL-MFLEINSNSYTFGKTKI 722
MYSc_Myo39 cd14900
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ...
 33-110 4.44e-07

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: 54.93  E-value: 4.44e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034601426   33 RFQQALEDLIARLGRSHVYFIQCLTPNPGKLPGLFDVGHVTEQLHQAAILEAVGTRSANFPVRVPFEAFLASFQALGS 110
Cdd:cd14900    515 QFKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVMEAVRVARAGFPIRLLHDEFVARYFSLAR 592
MYSc_Myo34 cd14895
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ...
 30-147 5.54e-07

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: 54.57  E-value: 5.54e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601426   30 LASRFQQALEDLIARLGRSHVYFIQCLTPNPGKLPGLFDVGHVTEQLHQAAILEAVGTRSANFPVRVPFEAFLASFQAL- 108
Cdd:cd14895    593 IGSQFKQQLASLLDVVQQTQTHYIRCIKPNDESASDQFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLv 672

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1034601426  109 GSEGQEDLSDREKCGAVlsQVLGAEsplyhLGATKVLLQ 147
Cdd:cd14895    673 AAKNASDATASALIETL--KVDHAE-----LGKTRVFLR 704
MYSc_Myo20 cd14881
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ...
 34-135 9.25e-07

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: 53.96  E-value: 9.25e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601426   34 FQQALEDLIARLGRSHVYFIQCLTPNPGKLPGLFDVGHVTEQLHQAAILEAVGTRSANFPVRVPFEAFLASFQAL---GS 110
Cdd:cd14881    510 FHTRLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAGGYPHRMRFKAFNARYRLLapfRL 589

                           90       100
                   ....*....|....*....|....*
gi 1034601426  111 EGQEDLSdREKCGAVLSQVLGAESP 135
Cdd:cd14881    590 LRRVEEK-ALEDCALILQFLEAQPP 613
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
 1247-1303 1.07e-06

Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences containing proline and hydrophobic amino acids. Pro-containing polypeptides may bind to SH3 domains in 2 different binding orientations.


Pssm-ID: 214620 [Multi-domain]  Cd Length: 56  Bit Score: 47.15  E-value: 1.07e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034601426  1247 DSGYVIALRSYITDNCSLLSFHRGDLIKLLpvATLEPGWQFG-SAGGRSGLFPADIVQ 1303
Cdd:smart00326    1 EGPQVRALYDYTAQDPDELSFKKGDIITVL--EKSDDGWWKGrLGRGKEGLFPSNYVE 56
MYSc_Myh7b cd14927
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ...
 4-147 1.14e-06

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: 53.80  E-value: 1.14e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601426    4 QSQLQLVGSLFQE------AEPQSRGGRGRPTLASRFQ-------QALEDLIARLGRSHVYFIQCLTPNPGKLPGLFDVG 70
Cdd:cd14927    518 KSQNKLLATLYENyvgsdsTEDPKSGVKEKRKKAASFQtvsqlhkENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPF 597

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034601426   71 HVTEQLHQAAILEAVGTRSANFPVRVPFEAFLASFQALGSEGQEDLS--DREKCGAVLSQVLGAESPLYHLGATKVLLQ 147
Cdd:cd14927    598 LVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYRILNPSAIPDDKfvDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
MYSc_Myo47 cd14908
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ...
 31-115 1.69e-06

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: 52.99  E-value: 1.69e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601426   31 ASRFQQALEDLIARLGRSHVYFIQCLTPNPGKLPGLFDVGHVTEQLHQAAILEAVGTRSANFPVRVPFEAFLASFQALGS 110
Cdd:cd14908    545 GQQFKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRYGGVLEAVRVARSGYPVRLPHKDFFKRYRMLLP 624


                   ....*
gi 1034601426  111 EGQED 115
Cdd:cd14908    625 LIPEV 629
MYSc_Myo38 cd14899
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ...
 29-129 4.13e-06

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: 52.02  E-value: 4.13e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601426   29 TLASRFQQALEDLIARLGRSHVYFIQCLTPNPGKLPGLFDVGHVTEQLHQAAILEAVGTRSANFPVRVPFEAFLASFQ-- 106
Cdd:cd14899    608 SVGTQFKIQLNELLSTVRATTPRYVRCIKPNDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRYRrv 687

                           90       100
                   ....*....|....*....|....*
gi 1034601426  107 --ALGSEGQEDLSDREKCGAVLSQV 129
Cdd:cd14899    688 llSLYKWGDNDFERQMRCGVSLGKT 712
SH3_9 pfam14604
Variant SH3 domain;
1253-1303 4.45e-06

Variant SH3 domain;


Pssm-ID: 434066 [Multi-domain]  Cd Length: 49  Bit Score: 45.30  E-value: 4.45e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1034601426 1253 ALRSYITDNCSLLSFHRGDLIKLLPVAtlEPGWQFGSAGGRSGLFPADIVQ 1303
Cdd:pfam14604    1 ALYPYEPKDDDELSLQRGDVITVIEES--EDGWWEGINTGRTGLVPANYVE 49
SH3_Intersectin_5 cd11840
Fifth Src homology 3 domain (or SH3E) of Intersectin; Intersectins (ITSNs) are adaptor ...
 1251-1304 7.65e-06

Fifth Src homology 3 domain (or SH3E) of Intersectin; Intersectins (ITSNs) are adaptor proteins that function in exo- and endocytosis, actin cytoskeletal reorganization, and signal transduction. They are essential for initiating clathrin-coated pit formation. They bind to many proteins through their multidomain structure and facilitate the assembly of multimeric complexes. Vertebrates contain two ITSN proteins, ITSN1 and ITSN2, which exist in alternatively spliced short and long isoforms. The short isoforms contain two Eps15 homology domains (EH1 and EH2), a coiled-coil region and five SH3 domains (SH3A-E), while the long isoforms, in addition, contain RhoGEF (also called Dbl-homologous or DH), Pleckstrin homology (PH) and C2 domains. ITSN1 and ITSN2 are both widely expressed, with variations depending on tissue type and stage of development. The fifth SH3 domain (or SH3E) of ITSN1 has been shown to bind many protein partners including SGIP1, Sos1, dynamin1/2, CIN85, c-Cbl, SHIP2, N-WASP, and synaptojanin-1, among others. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212774 [Multi-domain]  Cd Length: 53  Bit Score: 44.71  E-value: 7.65e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1034601426 1251 VIALRSYITDNCSLLSFHRGDLIKLLpvATLEPGWQFGSAGGRSGLFPADIVQP 1304
Cdd:cd11840      2 VIALFPYTAQNEDELSFQKGDIINVL--SKDDPDWWRGELNGQTGLFPSNYVEP 53
MYSc_Myo37 cd14898
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ...
 27-121 8.69e-06

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: 50.67  E-value: 8.69e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601426   27 RPTLASRFQQALEDLIARLGRSHVYFIQCLTPNPGKLPGLFDVGHVTEQLHQAAILEAVGTRSANFPVRVPFEAFLASFQ 106
Cdd:cd14898    477 KEDLVKYFKDSMNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYR 556

                           90
                   ....*....|....*
gi 1034601426  107 ALGSEGqEDLSDREK 121
Cdd:cd14898    557 ILGITL-FEVVDYRK 570
SH3_GRAP_C cd11951
C-terminal Src homology 3 domain of GRB2-related adaptor protein; GRAP is a GRB-2 like adaptor ...
 1250-1304 1.35e-05

C-terminal Src homology 3 domain of GRB2-related adaptor protein; GRAP is a GRB-2 like adaptor protein that is highly expressed in lymphoid tissues. It acts as a negative regulator of T cell receptor (TCR)-induced lymphocyte proliferation by downregulating the signaling to the Ras/ERK pathway. It has been identified as a regulator of TGFbeta signaling in diabetic kidney tubules and may have a role in the pathogenesis of the disease. GRAP contains an N-terminal SH3 domain, a central SH2 domain, and a C-terminal SH3 domain. The C-terminal SH3 domains (SH3c) of the related proteins, GRB2 and GRAP2, have been shown to bind to classical PxxP motif ligands, as well as to non-classical motifs. GRB2 SH3c binds Gab2 (Grb2-associated binder 2) through epitopes containing RxxK motifs, while the SH3c of GRAP2 binds to the phosphatase-like protein HD-PTP via a RxxxxK motif. SH3 domains are protein interaction domains that typically bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212884  Cd Length: 53  Bit Score: 44.02  E-value: 1.35e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1034601426 1250 YVIALRSYITDNCSLLSFHRGDLIKLLPVAtlEPGWQFGSAGGRSGLFPADIVQP 1304
Cdd:cd11951      1 FVQAQYDFSAEDPSQLSFRRGDIIEVLDCP--DPNWWRGRISGRVGFFPRNYVHP 53
MYSc_Myh11 cd14921
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ...
 29-147 1.80e-05

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: 49.63  E-value: 1.80e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601426   29 TLASRFQQALEDLIARLGRSHVYFIQCLTPNPGKLPGLFDVGHVTEQLHQAAILEAVGTRSANFPVRVPFEAFLASFQAL 108
Cdd:cd14921    554 TVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 633

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1034601426  109 GSEG-QEDLSDREKCGAVLSQVLGAESPLYHLGATKVLLQ 147
Cdd:cd14921    634 AANAiPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
SH3_Shank cd11832
Src homology 3 domain of SH3 and multiple ankyrin repeat domains (Shank) proteins; Shank ...
 1250-1300 4.89e-05

Src homology 3 domain of SH3 and multiple ankyrin repeat domains (Shank) proteins; Shank proteins carry scaffolding functions through multiple sites of protein-protein interaction in its domain architecture, including ankyrin (ANK) repeats, a long proline rich region, as well as SH3, PDZ, and SAM domains. They bind a variety of membrane and cytosolic proteins, and exist in alternatively spliced isoforms. They are highly enriched in postsynaptic density (PSD) where they interact with the cytoskeleton and with postsynaptic membrane receptors including NMDA and glutamate receptors. They are crucial in the construction and organization of the PSD and dendritic spines of excitatory synapses. There are three members of this family (Shank1, Shank2, Shank3) which show distinct and cell-type specific patterns of expression. Shank1 is brain-specific; Shank2 is found in neurons, glia, endocrine cells, liver, and kidney; Shank3 is widely expressed. The SH3 domain of Shank binds GRIP, a scaffold protein that binds AMPA receptors and Eph receptors/ligands. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212766  Cd Length: 50  Bit Score: 42.42  E-value: 4.89e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1034601426 1250 YVIALRSYITDNCSLLSFHRGDLIKLLPVAtlEPGWQFGSAGGRSGLFPAD 1300
Cdd:cd11832      1 YFIAVKSYSPQEEGEISLHKGDRVKVLSIG--EGGFWEGSVRGRTGWFPSD 49
SH3_SH3RF_1 cd11786
First Src Homology 3 domain of SH3 domain containing ring finger proteins; This model ...
 1253-1303 1.15e-04

First Src Homology 3 domain of SH3 domain containing ring finger proteins; This model represents the first SH3 domain of SH3RF1 (or POSH), SH3RF2 (or POSHER), SH3RF3 (POSH2), and similar domains. Members of this family are scaffold proteins that function as E3 ubiquitin-protein ligases. They all contain an N-terminal RING finger domain and multiple SH3 domains; SH3RF1 and SH3RF3 have four SH3 domains while SH3RF2 has three. SH3RF1 plays a role in calcium homeostasis through the control of the ubiquitin domain protein Herp. It may also have a role in regulating death receptor mediated and JNK mediated apoptosis. SH3RF3 interacts with p21-activated kinase 2 (PAK2) and GTP-loaded Rac1. It may play a role in regulating JNK mediated apoptosis in certain conditions. SH3RF2 acts as an anti-apoptotic regulator of the JNK pathway by binding to and promoting the degradation of SH3RF1. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212720 [Multi-domain]  Cd Length: 53  Bit Score: 41.58  E-value: 1.15e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1034601426 1253 ALRSYITDNCSLLSFHRGDLIKLLpvATLEPGWQFGSAGGRSGLFPADIVQ 1303
Cdd:cd11786      4 ALYNYEGKEPGDLSFKKGDIILLR--KRIDENWYHGECNGKQGFFPASYVQ 52
SH3_Intersectin_1 cd11836
First Src homology 3 domain (or SH3A) of Intersectin; Intersectins (ITSNs) are adaptor ...
 1253-1303 1.80e-04

First Src homology 3 domain (or SH3A) of Intersectin; Intersectins (ITSNs) are adaptor proteins that function in exo- and endocytosis, actin cytoskeletal reorganization, and signal transduction. They are essential for initiating clathrin-coated pit formation. They bind to many proteins through their multidomain structure and facilitate the assembly of multimeric complexes. Vertebrates contain two ITSN proteins, ITSN1 and ITSN2, which exist in alternatively spliced short and long isoforms. The short isoforms contain two Eps15 homology domains (EH1 and EH2), a coiled-coil region and five SH3 domains (SH3A-E), while the long isoforms, in addition, contain RhoGEF (also called Dbl-homologous or DH), Pleckstrin homology (PH) and C2 domains. ITSN1 and ITSN2 are both widely expressed, with variations depending on tissue type and stage of development. The first SH3 domain (or SH3A) of ITSN1 has been shown to bind many proteins including Sos1, dynamin1/2, CIN85, c-Cbl, PI3K-C2, SHIP2, N-WASP, and CdGAP, among others. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212770 [Multi-domain]  Cd Length: 55  Bit Score: 40.80  E-value: 1.80e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1034601426 1253 ALRSYITDNCSLLSFHRGDLIKLLPVATLEPGWQFGSAGGRSGLFPADIVQ 1303
Cdd:cd11836      4 ALYAFEARNPDEISFQPGDIIQVDESQVAEPGWLAGELKGKTGWFPANYVE 54
SH3_CD2AP_3 cd12056
Third Src Homology 3 domain (SH3C) of CD2-associated protein; CD2AP, also called CMS (Cas ...
 1250-1302 2.44e-04

Third Src Homology 3 domain (SH3C) of CD2-associated protein; CD2AP, also called CMS (Cas ligand with Multiple SH3 domains) or METS1 (Mesenchyme-to-Epithelium Transition protein with SH3 domains), is a cytosolic adaptor protein that plays a role in regulating the cytoskeleton. It is critical in cell-to-cell union necessary for kidney function. It also stabilizes the contact between a T cell and antigen-presenting cells. It is primarily expressed in podocytes at the cytoplasmic face of the slit diaphragm and serves as a linker anchoring podocin and nephrin to the actin cytoskeleton. CD2AP contains three SH3 domains, a proline-rich region, and a C-terminal coiled-coil domain. All of these domains enable CD2AP to bind various protein partners and assemble complexes that have been implicated in many different functions. This alignment model represents the third SH3 domain (SH3C) of CD2AP. SH3C has been shown to bind ubiquitin. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212989 [Multi-domain]  Cd Length: 57  Bit Score: 40.58  E-value: 2.44e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1034601426 1250 YVIALRSYITDNCSLLSFHRGDLIKLLPVATLEPGWQFGSAGGRSGLFPADIV 1302
Cdd:cd12056      3 YCKALFHYEGTNEDELDFKEGEIILIISKDTGEPGWWKGELNGKEGVFPDNFV 55
SH3_GRB2_like_C cd11805
C-terminal Src homology 3 domain of Growth factor receptor-bound protein 2 (GRB2) and related ...
 1265-1304 4.02e-04

C-terminal Src homology 3 domain of Growth factor receptor-bound protein 2 (GRB2) and related proteins; This family includes the adaptor protein GRB2 and related proteins including Drosophila melanogaster Downstream of receptor kinase (DRK), Caenorhabditis elegans Sex muscle abnormal protein 5 (Sem-5), GRB2-related adaptor protein (GRAP), GRAP2, and similar proteins. Family members contain an N-terminal SH3 domain, a central SH2 domain, and a C-terminal SH3 domain. GRB2/Sem-5/DRK is a critical signaling molecule that regulates the Ras pathway by linking tyrosine kinases to the Ras guanine nucleotide releasing protein Sos (son of sevenless), which converts Ras to the active GTP-bound state. GRAP2 plays an important role in T cell receptor (TCR) signaling by promoting the formation of the SLP-76:LAT complex, which couples the TCR to the Ras pathway. GRAP acts as a negative regulator of T cell receptor (TCR)-induced lymphocyte proliferation by downregulating the signaling to the Ras/ERK pathway. The C-terminal SH3 domains (SH3c) of GRB2 and GRAP2 have been shown to bind to classical PxxP motif ligands, as well as to non-classical motifs. GRB2 SH3c binds Gab2 (Grb2-associated binder 2) through epitopes containing RxxK motifs, while the SH3c of GRAP2 binds to the phosphatase-like protein HD-PTP via a RxxxxK motif. SH3 domains are protein interaction domains that typically bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212739 [Multi-domain]  Cd Length: 53  Bit Score: 39.92  E-value: 4.02e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1034601426 1265 LSFHRGDLIKLLPVATlePGWQFGSAGGRSGLFPADIVQP 1304
Cdd:cd11805     16 LEFRRGDIITVLDSSD--PDWWKGELRGRVGIFPANYVQP 53
SH3_CD2AP-like_3 cd11875
Third Src Homology 3 domain (SH3C) of CD2-associated protein and similar proteins; This ...
 1250-1304 4.21e-04

Third Src Homology 3 domain (SH3C) of CD2-associated protein and similar proteins; This subfamily is composed of the third SH3 domain (SH3C) of CD2AP, CIN85 (Cbl-interacting protein of 85 kDa), and similar domains. CD2AP and CIN85 are adaptor proteins that bind to protein partners and assemble complexes that have been implicated in T cell activation, kidney function, and apoptosis of neuronal cells. They also associate with endocytic proteins, actin cytoskeleton components, and other adaptor proteins involved in receptor tyrosine kinase (RTK) signaling. CD2AP and the main isoform of CIN85 contain three SH3 domains, a proline-rich region, and a C-terminal coiled-coil domain. All of these domains enable CD2AP and CIN85 to bind various protein partners and assemble complexes that have been implicated in many different functions. SH3C of both proteins have been shown to bind to ubiquitin. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212808 [Multi-domain]  Cd Length: 55  Bit Score: 40.03  E-value: 4.21e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1034601426 1250 YVIALRSYITDNCSLLSFHRGDLIKLLPVATLEPGWQFGSAGGRSGLFPADIVQP 1304
Cdd:cd11875      1 KARVLFDYEAENEDELTLREGDIVTILSKDCEDKGWWKGELNGKRGVFPDNFVEP 55
SH3_FCHSD1_2 cd11895
Second Src Homology 3 domain of FCH and double SH3 domains protein 1; FCHSD1 has a domain ...
 1253-1303 5.95e-04

Second Src Homology 3 domain of FCH and double SH3 domains protein 1; FCHSD1 has a domain structure consisting of an N-terminal F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs), two SH3, and C-terminal proline-rich domains. It has only been characterized in silico and its function is unknown. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212828  Cd Length: 58  Bit Score: 39.56  E-value: 5.95e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1034601426 1253 ALRSYITDNCSLLSFHRGDLIKLLPVAT--LEPGWQFGSAGGRSGLFPADIVQ 1303
Cdd:cd11895      4 ALYSYTGQSPEELSFPEGALIRLLPRAQdgVDDGFWRGEFGGRVGVFPSLLVE 56
SH3_Intersectin2_5 cd11996
Fifth Src homology 3 domain (or SH3E) of Intersectin-2; Intersectin-2 (ITSN2) is an adaptor ...
 1249-1303 6.28e-04

Fifth Src homology 3 domain (or SH3E) of Intersectin-2; Intersectin-2 (ITSN2) is an adaptor protein that functions in exo- and endocytosis, actin cytoskeletal reorganization, and signal transduction. It plays a role in clathrin-coated pit (CCP) formation. It binds to many proteins through its multidomain structure and facilitate the assembly of multimeric complexes. ITSN2 also functions as a specific GEF for Cdc42 activation in epithelial morphogenesis, and is required in mitotic spindle orientation. It exists in alternatively spliced short and long isoforms. The short isoform contains two Eps15 homology domains (EH1 and EH2), a coiled-coil region and five SH3 domains (SH3A-E), while the long isoform, in addition, contains RhoGEF (also called Dbl-homologous or DH), Pleckstrin homology (PH) and C2 domains. The fifth SH3 domain (or SH3E) of ITSN2 is expected to bind protein partners, similar to ITSN1 which has been shown to bind many protein partners including SGIP1, Sos1, dynamin1/2, CIN85, c-Cbl, SHIP2, N-WASP, and synaptojanin-1, among others. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212929 [Multi-domain]  Cd Length: 54  Bit Score: 39.58  E-value: 6.28e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1034601426 1249 GYVIALRSYITDNCSLLSFHRGDLIKLLPVAtlEPGWQFGSAGGRSGLFPADIVQ 1303
Cdd:cd11996      1 CQVIAMYDYTANNEDELSFSKGQLINVLNKD--DPDWWQGEINGVTGLFPSNYVK 53
SH3_Ysc84p_like cd11842
Src homology 3 domain of Ysc84p and similar fungal proteins; This family is composed of the ...
 1250-1303 7.44e-04

Src homology 3 domain of Ysc84p and similar fungal proteins; This family is composed of the Saccharomyces cerevisiae proteins, Ysc84p (also called LAS17-binding protein 4, Lsb4p) and Lsb3p, and similar fungal proteins. They contain an N-terminal SYLF domain (also called DUF500) and a C-terminal SH3 domain. Ysc84p localizes to actin patches and plays an important in actin polymerization during endocytosis. The N-terminal domain of both Ysc84p and Lsb3p can bind and bundle actin filaments. A study of the yeast SH3 domain interactome predicts that the SH3 domains of Lsb3p and Lsb4p may function as molecular hubs for the assembly of endocytic complexes. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212776 [Multi-domain]  Cd Length: 55  Bit Score: 39.33  E-value: 7.44e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1034601426 1250 YVIALRSYITDNCSLLSFHRGDLIKLLPVATLEPGWQFGSAGGRSGLFPADIVQ 1303
Cdd:cd11842      1 KAVALYDFAGEQPGDLAFQKGDIITILKKSDSQNDWWTGRIGGREGIFPANYVE 54
SH3_Shank3 cd11984
Src homology 3 domain of SH3 and multiple ankyrin repeat domains protein 3; Shank3, also ...
 1252-1302 8.19e-04

Src homology 3 domain of SH3 and multiple ankyrin repeat domains protein 3; Shank3, also called ProSAP2 (Proline-rich synapse-associated protein 2), is widely expressed. It plays a role in the formation of dendritic spines and synapses. Haploinsufficiency of the Shank3 gene causes the 22q13 deletion/Phelan-McDermid syndrome, and variants of Shank3 have been implicated in autism spectrum disorder, schizophrenia, and intellectual disability. Shank proteins carry scaffolding functions through multiple sites of protein-protein interaction in its domain architecture, including ankyrin (ANK) repeats, a long proline rich region, as well as SH3, PDZ, and SAM domains. The SH3 domain of Shank binds GRIP, a scaffold protein that binds AMPA receptors and Eph receptors/ligands. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212917  Cd Length: 52  Bit Score: 39.16  E-value: 8.19e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1034601426 1252 IALRSYITDNCSLLSFHRGDLIKLLPVAtlEPGWQFGSAGGRSGLFPADIV 1302
Cdd:cd11984      4 IAVKAYSPQGEGEIQLNRGERVKVLSIG--EGGFWEGTVKGRTGWFPADCV 52
SH3_GRAF-like cd11882
Src Homology 3 domain of GTPase Regulator Associated with Focal adhesion kinase and similar ...
 1251-1304 8.34e-04

Src Homology 3 domain of GTPase Regulator Associated with Focal adhesion kinase and similar proteins; This subfamily is composed of Rho GTPase activating proteins (GAPs) with similarity to GRAF. Members contain an N-terminal BAR domain, followed by a Pleckstrin homology (PH) domain, a Rho GAP domain, and a C-terminal SH3 domain. Although vertebrates harbor four Rho GAPs in the GRAF subfamily including GRAF, GRAF2, GRAF3, and Oligophrenin-1 (OPHN1), only three are included in this model. OPHN1 contains the BAR, PH and GAP domains, but not the C-terminal SH3 domain. GRAF and GRAF2 show GAP activity towards RhoA and Cdc42. GRAF influences Rho-mediated cytoskeletal rearrangements and binds focal adhesion kinase. GRAF2 regulates caspase-activated p21-activated protein kinase-2. The SH3 domain of GRAF and GRAF2 binds PKNbeta, a target of the small GTPase Rho. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies.


Pssm-ID: 212815 [Multi-domain]  Cd Length: 54  Bit Score: 39.20  E-value: 8.34e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1034601426 1251 VIALRSYITDNCSLLSFHRGDLIKLLpVATLEPGWQFGSAGGRSGLFPADIVQP 1304
Cdd:cd11882      2 ARALYACKAEDESELSFEPGQIITNV-QPSDEPGWLEGTLNGRTGLIPENYVEF 54
SH3_Intersectin_3 cd11838
Third Src homology 3 domain (or SH3C) of Intersectin; Intersectins (ITSNs) are adaptor ...
 1250-1304 1.05e-03

Third Src homology 3 domain (or SH3C) of Intersectin; Intersectins (ITSNs) are adaptor proteins that function in exo- and endocytosis, actin cytoskeletal reorganization, and signal transduction. They are essential for initiating clathrin-coated pit formation. They bind to many proteins through their multidomain structure and facilitate the assembly of multimeric complexes. Vertebrates contain two ITSN proteins, ITSN1 and ITSN2, which exist in alternatively spliced short and long isoforms. The short isoforms contain two Eps15 homology domains (EH1 and EH2), a coiled-coil region and five SH3 domains (SH3A-E), while the long isoforms, in addition, contain RhoGEF (also called Dbl-homologous or DH), Pleckstrin homology (PH) and C2 domains. ITSN1 and ITSN2 are both widely expressed, with variations depending on tissue type and stage of development. The third SH3 domain (or SH3C) of ITSN1 has been shown to bind many proteins including dynamin1/2, CIN85, c-Cbl, SHIP2, Reps1, synaptojanin-1, and WNK, among others. The SH3C of ITSN2 has been shown to bind the K15 protein of Kaposi's sarcoma-associated herpesvirus. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212772 [Multi-domain]  Cd Length: 52  Bit Score: 38.55  E-value: 1.05e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1034601426 1250 YVIALRSYITDNCSLLSFHRGDLIKllpVATLEPGWQFGSAGGRSGLFPADIVQP 1304
Cdd:cd11838      1 EYIALYPYESNEPGDLTFNAGDVIL---VTKKDGEWWTGTIGDRTGIFPSNYVRP 52
SH3_MYO7A cd11881
Src Homology 3 domain of Myosin VIIa and similar proteins; Myo7A is an uncoventional myosin ...
 1248-1302 1.07e-03

Src Homology 3 domain of Myosin VIIa and similar proteins; Myo7A is an uncoventional myosin that is involved in organelle transport. It is required for sensory function in both Drosophila and mammals. Mutations in the Myo7A gene cause both syndromic deaf-blindness [Usher syndrome I (USH1)] and nonsyndromic (DFNB2 and DFNA11) deafness in humans. It contains an N-terminal motor domain, light chain-binding IQ motifs, a coiled-coil region for heavy chain dimerization, and a tail consisting of a pair of MyTH4-FERM tandems separated by a SH3 domain. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies.


Pssm-ID: 212814  Cd Length: 64  Bit Score: 39.03  E-value: 1.07e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034601426 1248 SGYVIALRSYI--TDNCSLLSFHRGDLIKL---LPVATLEPGWQFG--SAGGRSGLFPADIV 1302
Cdd:cd11881      1 SKYVVALQDYPnpSDGSSFLSFAKGDLIILdqdTGEQVMNSGWCNGrnDRTGQRGDFPADCV 62
SH3_Irsp53_BAIAP2L cd11779
Src Homology 3 domain of Insulin Receptor tyrosine kinase Substrate p53, Brain-specific ...
 1251-1304 1.16e-03

Src Homology 3 domain of Insulin Receptor tyrosine kinase Substrate p53, Brain-specific Angiogenesis Inhibitor 1-Associated Protein 2 (BAIAP2)-Like proteins, and similar proteins; Proteins in this family include IRSp53, BAIAP2L1, BAIAP2L2, and similar proteins. They all contain an Inverse-Bin/Amphiphysin/Rvs (I-BAR) or IMD domain in addition to the SH3 domain. IRSp53, also known as BAIAP2, is a scaffolding protein that takes part in many signaling pathways including Cdc42-induced filopodia formation, Rac-mediated lamellipodia extension, and spine morphogenesis. IRSp53 exists as multiple splicing variants that differ mainly at the C-termini. BAIAP2L1, also called IRTKS (Insulin Receptor Tyrosine Kinase Substrate), serves as a substrate for the insulin receptor and binds the small GTPase Rac. It plays a role in regulating the actin cytoskeleton and colocalizes with F-actin, cortactin, VASP, and vinculin. IRSp53 and IRTKS also mediate the recruitment of effector proteins Tir and EspFu, which regulate host cell actin reorganization, to bacterial attachment sites. BAIAP2L2 co-localizes with clathrin plaques but its function has not been determined. The SH3 domains of IRSp53 and IRTKS have been shown to bind the proline-rich C-terminus of EspFu. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212713 [Multi-domain]  Cd Length: 57  Bit Score: 38.84  E-value: 1.16e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034601426 1251 VIALRSYITDNCSLLSFHRGDLIKLLpVATLEPGWQFGS--AGGRSGLFPADIVQP 1304
Cdd:cd11779      3 VKALYPHAAGGETQLSFEEGDVITLL-GPEPRDGWHYGEneRSGRRGWFPIAYTEP 57
SH3_p67phox_C cd12046
C-terminal (or second) Src Homology 3 domain of the p67phox subunit of NADPH oxidase; p67phox, ...
 1250-1304 1.18e-03

C-terminal (or second) Src Homology 3 domain of the p67phox subunit of NADPH oxidase; p67phox, also called Neutrophil cytosol factor 2 (NCF-2), is a cytosolic subunit of the phagocytic NADPH oxidase complex (also called Nox2 or gp91phox) which plays a crucial role in the cellular response to bacterial infection. NADPH oxidase catalyzes the transfer of electrons from NADPH to oxygen during phagocytosis forming superoxide and reactive oxygen species. p67phox plays a regulatory role and contains N-terminal TPR, first SH3 (or N-terminal or central SH3), PB1, and C-terminal SH3 domains. It binds, via its C-terminal SH3 domain, to a proline-rich region of p47phox and upon activation, this complex assembles with flavocytochrome b558, the Nox2-p22phox heterodimer. Concurrently, RacGTP translocates to the membrane and interacts with the TPR domain of p67phox, which leads to the activation of NADPH oxidase. The PB1 domain of p67phox binds to its partner PB1 domain in p40phox, and this facilitates the assembly of p47phox-p67phox at the membrane. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212979 [Multi-domain]  Cd Length: 53  Bit Score: 38.63  E-value: 1.18e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1034601426 1250 YVIALRSYITDNCSLLSFHRGDLIKLLpvATLEPGWQFGSAGGRSGLFPADIVQP 1304
Cdd:cd12046      1 QVVALFSYEASQPEDLEFQKGDVILVL--SKVNEDWLEGQCKGKIGIFPSAFVED 53
SH3_Abi cd11826
Src homology 3 domain of Abl Interactor proteins; Abl interactor (Abi) proteins are adaptor ...
 1250-1303 1.28e-03

Src homology 3 domain of Abl Interactor proteins; Abl interactor (Abi) proteins are adaptor proteins serving as binding partners and substrates of Abl tyrosine kinases. They are involved in regulating actin cytoskeletal reorganization and play important roles in membrane-ruffling, endocytosis, cell motility, and cell migration. They localize to sites of actin polymerization in epithelial adherens junction and immune synapses, as well as to the leading edge of lamellipodia. Vertebrates contain two Abi proteins, Abi1 and Abi2. Abi1 displays a wide expression pattern while Abi2 is highly expressed in the eye and brain. Abi proteins contain a homeobox homology domain, a proline-rich region, and a SH3 domain. The SH3 domain of Abi binds to a PxxP motif in Abl. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212760 [Multi-domain]  Cd Length: 52  Bit Score: 38.46  E-value: 1.28e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1034601426 1250 YVIALRSYITDNCSLLSFHRGDLIKLLpvATLEPGWQFGSAGGRSGLFPADIVQ 1303
Cdd:cd11826      1 KVVALYDYTADKDDELSFQEGDIIYVT--KKNDDGWYEGVLNGVTGLFPGNYVE 52
FERM_C1_MyoVII cd13198
FERM domain C-lobe, repeat 1, of Myosin VII (MyoVII/Myo7); MyoVII, a MyTH-FERM myosin, is an ...
 1152-1246 2.41e-03

FERM domain C-lobe, repeat 1, of Myosin VII (MyoVII/Myo7); MyoVII, a MyTH-FERM myosin, is an actin-based motor protein essential for a variety of biological processes in the actin cytoskeleton function. Mutations in MyoVII leads to problems in sensory perception: deafness and blindness in humans (Usher Syndrome), retinal defects and deafness in mice (shaker 1), and aberrant auditory and vestibular function in zebrafish. Myosin VIIAs have plus (barbed) end-directed motor activity on actin filaments and a characteristic actin-activated ATPase activity. MyoVII consists of a conserved spectrin-like, SH3 subdomain N-terminal region, a motor/head region, a neck made of 4-5 IQ motifs, and a tail consisting of a coiled-coil domain, followed by a tandem repeat of myosin tail homology 4 (MyTH4) domains and partial FERM domains that are separated by an SH3 subdomain and are thought to mediate dimerization and binding to other proteins or cargo. Members include: MyoVIIa, MyoVIIb, and MyoVII members that do not have distinct myosin VIIA and myosin VIIB genes. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs) , the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 270019  Cd Length: 99  Bit Score: 39.12  E-value: 2.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601426 1152 FSRFF---PVSGES--GSDVqLLAVSHRGLRLLKvtqgpglrpDQLKILCSYSFAEVLGVECR-----GGSTLELS-LKS 1220
Cdd:cd13198      3 FSRFFeatKFSGPSlpKSEV-IIAVNWTGIYFVD---------EQEQVLLELSFPEITGVSSSrgkrdGGQSFTLTtIQG 72

                           90       100
                   ....*....|....*....|....*.
gi 1034601426 1221 EQLVLHTARARAIEALVELFLNELKK 1246
Cdd:cd13198     73 EEFVFQSPNAEDIAELVNYFLEGLRK 98
SH3_AHI-1 cd11812
Src Homology 3 domain of Abelson helper integration site-1 (AHI-1); AHI-1, also called ...
 1251-1302 2.63e-03

Src Homology 3 domain of Abelson helper integration site-1 (AHI-1); AHI-1, also called Jouberin, is expressed in high levels in the brain, gonad tissues, and skeletal muscle. It is an adaptor protein that interacts with the small GTPase Rab8a and regulates it distribution and function, affecting cilium formation and vesicle transport. Mutations in the AHI-1 gene can cause Joubert syndrome, a disorder characterized by brainstem malformations, cerebellar aplasia/hypoplasia, and retinal dystrophy. AHI-1 variation is also associated with susceptibility to schizophrenia and type 2 diabetes mellitus progression. AHI-1 contains WD40 and SH3 domains. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212746 [Multi-domain]  Cd Length: 52  Bit Score: 37.49  E-value: 2.63e-03
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gi 1034601426 1251 VIALRSYITDNCSLLSFHRGDLIKLLpvATLEPGWQFGS-AGGRSGLFPADIV 1302
Cdd:cd11812      2 VVALYDYTANRSDELTIHRGDIIRVL--YKDNDNWWFGSlVNGQQGYFPANYV 52
SH3_D21-like cd12142
Src Homology 3 domain of SH3 domain-containing protein 21 (SH3D21) and similar proteins; ...
 1257-1304 3.20e-03

Src Homology 3 domain of SH3 domain-containing protein 21 (SH3D21) and similar proteins; N-terminal SH3 domain of the uncharacterized protein SH3 domain-containing protein 21, and similar uncharacterized domains, it belongs to the CD2AP-like_3 subfamily of proteins. The CD2AP-like_3 subfamily is composed of the third SH3 domain (SH3C) of CD2AP, CIN85 (Cbl-interacting protein of 85 kDa), and similar domains. CD2AP and CIN85 are adaptor proteins that bind to protein partners and assemble complexes that have been implicated in T cell activation, kidney function, and apoptosis of neuronal cells. They also associate with endocytic proteins, actin cytoskeleton components, and other adaptor proteins involved in receptor tyrosine kinase (RTK) signaling. CD2AP and the main isoform of CIN85 contain three SH3 domains, a proline-rich region, and a C-terminal coiled-coil domain. All of these domains enable CD2AP and CIN85 to bind various protein partners and assemble complexes that have been implicated in many different functions. SH3C of both proteins have been shown to bind to ubiquitin. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 213018 [Multi-domain]  Cd Length: 55  Bit Score: 37.44  E-value: 3.20e-03
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gi 1034601426 1257 YITDNCSLLSFHRGDLIKLLPVATLEPGWQFGSAGGRSGLFPADIVQP 1304
Cdd:cd12142      8 YNPVAPDELALKKGDVIEVISKETEDEGWWEGELNGRRGFFPDNFVMP 55
SH3_BAIAP2L2 cd11914
Src Homology 3 domain of Brain-specific Angiogenesis Inhibitor 1-Associated Protein 2-Like 2; ...
 1261-1304 3.58e-03

Src Homology 3 domain of Brain-specific Angiogenesis Inhibitor 1-Associated Protein 2-Like 2; BAIAP2L2 co-localizes with clathrin plaques but its function has not been determined. It contains an N-terminal IMD or Inverse-Bin/Amphiphysin/Rvs (I-BAR) domain, an SH3 domain, and a WASP homology 2 (WH2) actin-binding motif at the C-terminus. The related proteins, BAIAP2L1 and IRSp53, function as regulators of membrane dynamics and the actin cytoskeleton. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212847 [Multi-domain]  Cd Length: 59  Bit Score: 37.49  E-value: 3.58e-03
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gi 1034601426 1261 NCSLLSFHRGDLIKLLpVATLEPGWQFGSAGG--RSGLFPADIVQP 1304
Cdd:cd11914     14 NPTLLRFNRGDIITVL-VPEARNGWLYGKLEGssRQGWFPEAYVKA 58
SH3_MyoIe_If_like cd11827
Src homology 3 domain of Myosins Ie, If, and similar proteins; Myosins Ie (MyoIe) and If ...
 1253-1303 3.87e-03

Src homology 3 domain of Myosins Ie, If, and similar proteins; Myosins Ie (MyoIe) and If (MyoIf) are nonmuscle, unconventional, long tailed, class I myosins containing an N-terminal motor domain and a myosin tail with TH1, TH2, and SH3 domains. MyoIe interacts with the endocytic proteins, dynamin and synaptojanin-1, through its SH3 domain; it may play a role in clathrin-dependent endocytosis. In the kidney, MyoIe is critical for podocyte function and normal glomerular filtration. Mutations in MyoIe is associated with focal segmental glomerulosclerosis, a disease characterized by massive proteinuria and progression to end-stage kidney disease. MyoIf is predominantly expressed in the immune system; it plays a role in immune cell motility and innate immunity. Mutations in MyoIf may be associated with the loss of hearing. The MyoIf gene has also been found to be fused to the MLL (Mixed lineage leukemia) gene in infant acute myeloid leukemias (AML). SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212761 [Multi-domain]  Cd Length: 53  Bit Score: 37.01  E-value: 3.87e-03
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gi 1034601426 1253 ALRSYITDNCSLLSFHRGDLIKLLpvatLE--PGWQFGSAGGRSGLFPADIVQ 1303
Cdd:cd11827      4 ALYAYDAQDTDELSFNEGDIIEIL----KEdpSGWWTGRLRGKEGLFPGNYVE 52
SH3_GRB2_C cd11949
C-terminal Src homology 3 domain of Growth factor receptor-bound protein 2; GRB2 is a critical ...
 1265-1304 5.40e-03

C-terminal Src homology 3 domain of Growth factor receptor-bound protein 2; GRB2 is a critical signaling molecule that regulates the Ras pathway by linking tyrosine kinases to the Ras guanine nucleotide releasing protein Sos (son of sevenless), which converts Ras to the active GTP-bound state. It is ubiquitously expressed in all tissues throughout development and is important in cell cycle progression, motility, morphogenesis, and angiogenesis. In lymphocytes, GRB2 is associated with antigen receptor signaling components. GRB2 contains an N-terminal SH3 domain, a central SH2 domain, and a C-terminal SH3 domain. The C-terminal SH3 domain of GRB2 binds to Gab2 (Grb2-associated binder 2) through epitopes containing RxxK motifs, as well as to the proline-rich C-terminus of FGRF2. SH3 domains are protein interaction domains that typically bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212882 [Multi-domain]  Cd Length: 53  Bit Score: 36.74  E-value: 5.40e-03
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gi 1034601426 1265 LSFHRGDLIKLlpVATLEPGWQFGSAGGRSGLFPADIVQP 1304
Cdd:cd11949     16 LGFRRGDFIEV--MDNSDPNWWKGACHGQTGMFPRNYVTP 53
SH3_Nostrin cd11823
Src homology 3 domain of Nitric Oxide Synthase TRaffic INducer; Nostrin is expressed in ...
 1253-1303 5.58e-03

Src homology 3 domain of Nitric Oxide Synthase TRaffic INducer; Nostrin is expressed in endothelial and epithelial cells and is involved in the regulation, trafficking and targeting of endothelial NOS (eNOS). It facilitates the endocytosis of eNOS by coordinating the functions of dynamin and the Wiskott-Aldrich syndrome protein (WASP). Increased expression of Nostrin may be correlated to preeclampsia. Nostrin contains an N-terminal F-BAR domain and a C-terminal SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212757 [Multi-domain]  Cd Length: 53  Bit Score: 36.55  E-value: 5.58e-03
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                   ....*....|....*....|....*....|....*....|....*....|.
gi 1034601426 1253 ALRSYITDNCSLLSFHRGDLIKLLpvATLEPGWQFGSAGGRSGLFPADIVQ 1303
Cdd:cd11823      4 ALYSYTANREDELSLQPGDIIEVH--EKQDDGWWLGELNGKKGIFPATYVE 52
SH3_ARHGEF9_like cd11828
Src homology 3 domain of ARHGEF9-like Rho guanine nucleotide exchange factors; Members of this ...
 1250-1303 7.59e-03

Src homology 3 domain of ARHGEF9-like Rho guanine nucleotide exchange factors; Members of this family contain a SH3 domain followed by RhoGEF (also called Dbl-homologous or DH) and Pleckstrin Homology (PH) domains. They include the Rho guanine nucleotide exchange factors ARHGEF9, ASEF (also called ARHGEF4), ASEF2, and similar proteins. GEFs activate small GTPases by exchanging bound GDP for free GTP. ARHGEF9 specifically activates Cdc42, while both ASEF and ASEF2 can activate Rac1 and Cdc42. ARHGEF9 is highly expressed in the brain and it interacts with gephyrin, a postsynaptic protein associated with GABA and glycine receptors. ASEF plays a role in angiogenesis and cell migration. ASEF2 is important in cell migration and adhesion dynamics. ASEF exists in an autoinhibited form and is activated upon binding of the tumor suppressor APC (adenomatous polyposis coli), leading to the activation of Rac1 or Cdc42. In its autoinhibited form, the SH3 domain of ASEF forms an extensive interface with the DH and PH domains, blocking the Rac binding site. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212762 [Multi-domain]  Cd Length: 53  Bit Score: 36.21  E-value: 7.59e-03
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gi 1034601426 1250 YVIALRSYITDNCSLLSFHRGDLIKLLPVAtlEPGWQFGSAGGRSGLFPADIVQ 1303
Cdd:cd11828      1 LAEALWDHVTMDPEELGFKAGDVIEVLDMS--DKDWWWGSIRDEEGWFPASFVR 52
SH3_Intersectin2_1 cd11988
First Src homology 3 domain (or SH3A) of Intersectin-2; Intersectin-2 (ITSN2) is an adaptor ...
 1253-1303 7.94e-03

First Src homology 3 domain (or SH3A) of Intersectin-2; Intersectin-2 (ITSN2) is an adaptor protein that functions in exo- and endocytosis, actin cytoskeletal reorganization, and signal transduction. It plays a role in clathrin-coated pit (CCP) formation. It binds to many proteins through its multidomain structure and facilitate the assembly of multimeric complexes. ITSN2 also functions as a specific GEF for Cdc42 activation in epithelial morphogenesis, and is required in mitotic spindle orientation. It exists in alternatively spliced short and long isoforms. The short isoform contains two Eps15 homology domains (EH1 and EH2), a coiled-coil region and five SH3 domains (SH3A-E), while the long isoform, in addition, contains RhoGEF (also called Dbl-homologous or DH), Pleckstrin homology (PH) and C2 domains. The first SH3 domain (or SH3A) of ITSN2 is expected to bind many protein partners, similar to ITSN1 which has been shown to bind Sos1, dynamin1/2, CIN85, c-Cbl, PI3K-C2, SHIP2, N-WASP, and CdGAP, among others. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212921 [Multi-domain]  Cd Length: 57  Bit Score: 36.39  E-value: 7.94e-03
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gi 1034601426 1253 ALRSYITDNCSLLSFHRGDLIKLLPVATLEPGWQFGSAGGRSGLFPADIVQ 1303
Cdd:cd11988      6 ALYPFEARNHDEMSFNAGDIIQVDEKTVGEPGWLYGSFQGNFGWFPCNYVE 56
SH3_GRAP2_C cd11950
C-terminal Src homology 3 domain of GRB2-related adaptor protein 2; GRAP2 is also called GADS ...
 1265-1304 8.33e-03

C-terminal Src homology 3 domain of GRB2-related adaptor protein 2; GRAP2 is also called GADS (GRB2-related adapter downstream of Shc), GrpL, GRB2L, Mona, or GRID (Grb2-related protein with insert domain). It is expressed specifically in the hematopoietic system. It plays an important role in T cell receptor (TCR) signaling by promoting the formation of the SLP-76:LAT complex, which couples the TCR to the Ras pathway. It also has roles in antigen-receptor and tyrosine kinase mediated signaling. GRAP2 is unique from other GRB2-like adaptor proteins in that it can be regulated by caspase cleavage. It contains an N-terminal SH3 domain, a central SH2 domain, and a C-terminal SH3 domain. The C-terminal SH3 domain of GRAP2 binds to different motifs found in substrate peptides including the typical PxxP motif in hematopoietic progenitor kinase 1 (HPK1), the RxxK motif in SLP-76 and HPK1, and the RxxxxK motif in phosphatase-like protein HD-PTP. SH3 domains are protein interaction domains that typically bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212883 [Multi-domain]  Cd Length: 53  Bit Score: 36.34  E-value: 8.33e-03
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gi 1034601426 1265 LSFHRGDLIKLLPVAtlEPGWQFGSAGGRSGLFPADIVQP 1304
Cdd:cd11950     16 LGFNSGDVIEVLDSS--NPSWWKGRLHGKLGLFPANYVAP 53
SH3_Intersectin1_5 cd11995
Fifth Src homology 3 domain (or SH3E) of Intersectin-1; Intersectin-1 (ITSN1) is an adaptor ...
 1251-1303 8.54e-03

Fifth Src homology 3 domain (or SH3E) of Intersectin-1; Intersectin-1 (ITSN1) is an adaptor protein that functions in exo- and endocytosis, actin cytoskeletal reorganization, and signal transduction. It plays a role in clathrin-coated pit (CCP) formation. It binds to many proteins through its multidomain structure and facilitate the assembly of multimeric complexes. ITSN1 localizes in membranous organelles, CCPs, the Golgi complex, and may be involved in the cell membrane trafficking system. It exists in alternatively spliced short and long isoforms. The short isoform contains two Eps15 homology domains (EH1 and EH2), a coiled-coil region and five SH3 domains (SH3A-E), while the long isoform, in addition, contains RhoGEF (also called Dbl-homologous or DH), Pleckstrin homology (PH) and C2 domains. The fifth SH3 domain (or SH3E) of ITSN1 has been shown to bind many protein partners including SGIP1, Sos1, dynamin1/2, CIN85, c-Cbl, SHIP2, N-WASP, and synaptojanin-1, among others. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212928 [Multi-domain]  Cd Length: 54  Bit Score: 36.09  E-value: 8.54e-03
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gi 1034601426 1251 VIALRSYITDNCSLLSFHRGDLIKLLpvATLEPGWQFGSAGGRSGLFPADIVQ 1303
Cdd:cd11995      3 VIGMYDYTAQNDDELAFSKGQIINVL--NKEDPDWWKGELNGQVGLFPSNYVK 53
SH3_Endophilin_A cd11803
Src homology 3 domain of Endophilin-A; Endophilins play roles in synaptic vesicle formation, ...
 1265-1303 9.88e-03

Src homology 3 domain of Endophilin-A; Endophilins play roles in synaptic vesicle formation, virus budding, mitochondrial morphology maintenance, receptor-mediated endocytosis inhibition, and endosomal sorting. They are classified into two types, A and B. Vertebrates contain three endophilin-A isoforms (A1, A2, and A3). Endophilin-A proteins are enriched in the brain and play multiple roles in receptor-mediated endocytosis. They tubulate membranes and regulate calcium influx into neurons to trigger the activation of the endocytic machinery. They are also involved in the sorting of plasma membrane proteins, actin filament assembly, and the uncoating of clathrin-coated vesicles for fusion with endosomes. Endophilins contain an N-terminal N-BAR domain (BAR domain with an additional N-terminal amphipathic helix), followed by a variable region containing proline clusters, and a C-terminal SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212737 [Multi-domain]  Cd Length: 55  Bit Score: 36.08  E-value: 9.88e-03
                           10        20        30
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gi 1034601426 1265 LSFHRGDLIKLlpVATLEPGWQFGSAGGRSGLFPADIVQ 1303
Cdd:cd11803     17 LGFKEGDIITL--TNQIDENWYEGMVNGQSGFFPVNYVE 53
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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