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Conserved domains on  [gi|1992515667|ref|NP_001380523|]
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unconventional myosin-VIIb isoform 3 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MyTH4 smart00139
Domain in Myosin and Kinesin Tails; Domain present twice in myosin-VIIa, and also present in 3 ...
 497-644 2.68e-60

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: 202.21  E-value: 2.68e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992515667  497 YSCEPLRQPLLKrvHANVDLWDIACQIFVAILRYMGDYPSRQAWPTLELTDQIFTLALQHPALQDEVYCQILKQLTHNSN 576
Cdd:smart00139   1 YTKDPIKTSLLK--LESDELQKEAVKIFKAILKFMGDIPLPRPDSHLDLVQFILQKGLDHPELRDEIYCQLIKQLTDNPS 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1992515667  577 RHSEERGWQLLWLCTGLFPPSKGLLPHAQKFIDTRR----GKLLAPDCSRRIQKVLRTGPRKQPPHQVEVEA 644
Cdd:smart00139  79 RQSEERGWQLLYLCTSLFPPSERLLPYLLQFLSRRAdpgsEQGLAKYCLYRLERTLKNGARKQPPSRLELEA 150
FERM_C2_MyoVII cd13199
FERM domain C-lobe, repeat 2, of Myosin VII (MyoVII, Myo7); MyoVII, a MyTH-FERM myosin, is an ...
 861-956 2.07e-59

FERM domain C-lobe, repeat 2, 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: 270020  Cd Length: 96  Bit Score: 197.48  E-value: 2.07e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992515667 861 GSAFFEVKQTSEPSYPDVILIAINRHGVLLIHPKTKDLLTTYPFTKISSWSSGSTYFHMALGSLGRGSRLLCETSLGYKM 940
Cdd:cd13199     1 GSAFFEVKQTTDPSLPEILLIAINKNGVSLIDPKTKEILATHPFSKISNWSSGNTYFHMTIGNLVRGSKLLCETSLGYKM 80

                          90
                  ....*....|....*.
gi 1992515667 941 DDLLTSYVQQLLSAMN 956
Cdd:cd13199    81 DDLLTSYISLLLSNMK 96
FERM1_F1_Myosin-VII cd17092
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain 1, F1 sub-domain, found in Myosin-VIIa, ...
 49-147 1.75e-54

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain 1, F1 sub-domain, found in Myosin-VIIa, Myosin-VIIb, and similar proteins; This family includes two nontraditional members of the myosin superfamily, myosin-VIIa and myosin-VIIb. Myosin-VIIa, also termed myosin-7a (Myo7a), has been implicated in the structural organization of hair bundles at the apex of sensory hair cells (SHCs) where it serves mechanotransduction in the process of hearing and balance. Mutations in the MYO7A gene may be associated with Usher Syndrome type 1B (USH1B) and nonsyndromic hearing loss (DFNB2, DFNA11). Myosin-VIIb, also termed myosin-7b (Myo7b), is a high duty ratio motor adapted for generating and maintaining tension. It associates with harmonin and ANKS4B to form a stable ternary complex for anchoring microvilli tip-link cadherins. Like other unconventional myosins, myosin-VII is composed of a conserved motor head, a neck region and a tail region containing two MyTH4 domains, a SH3 domain, and two FERM domains. The FERM domain is made up of three sub-domains, F1, F2, and F3. The family corresponds to the F1 sub-domain of the first FERM domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


:

Pssm-ID: 340612  Cd Length: 99  Bit Score: 184.00  E-value: 1.75e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992515667  49 HIPIQVILATGESLTVPVDSASTSREMCMHIAHKQGLSDHLGFSLQVAVYDKFWSLGSGRDHMMDAIARCEQMAQERGES 128
Cdd:cd17092     1 PIMLPVTFMDGSTKTVEVDSATTARELCRQLAEKLGLKDTFGFSLYIALFDKVSSLGSGTDHVMDAISQCEQYAKEKGAQ 80

                          90
                  ....*....|....*....
gi 1992515667 129 QRQSPWRIYFRKEFFTPWH 147
Cdd:cd17092    81 EREAPWRLYFRKEIFAPWH 99
FERM2_F1_Myosin-VII cd17093
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain 2, F1 sub-domain, found in Myosin-VIIa, ...
 651-748 7.06e-54

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain 2, F1 sub-domain, found in Myosin-VIIa, Myosin-VIIb, and similar proteins; This family includes two nontraditional members of myosin superfamily, myosin-VIIa and myosin-VIIb. Myosin-VIIa, also termed myosin-7a (Myo7a), has been implicated in the structural organization of hair bundles at the apex of sensory hair cells (SHCs) where it serves mechanotransduction in the process of hearing and balance. Mutations in MYO7A gene may be associated with Usher Syndrome type 1B (USH1B) and nonsyndromic hearing loss (DFNB2, DFNA11). Myosin-VIIb, also termed myosin-7b (Myo7b), is a high duty ratio motor adapted for generating and maintaining tension. It associates with harmonin and ANKS4B to form a stable ternary complex for anchoring microvilli tip-link cadherins. Like other unconventional myosins, myosin-VII is composed of a conserved motor head, a neck region and a tail region containing two MyTH4 domains, a SH3 domain, and two FERM domains. The FERM domain is made up of three sub-domains, F1, F2, and F3. The family corresponds to the F1 sub-domain of the second FERM domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


:

Pssm-ID: 340613  Cd Length: 98  Bit Score: 182.05  E-value: 7.06e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992515667 651 RICHKIYFPNDTSEMLEVVANTRVRDVCDSIATRLQLASWEGCSLFIKISDKVISQKEGDFFFDSLREVSDWVKKNKPQK 730
Cdd:cd17093     1 QIFHKVYFPDDTDEAFEVDSSTRARDLCQNIASRLGLKSSEGFSLFVKIADKVISLPEGDFFFDFIRHLTDWIKKARPTK 80

                          90
                  ....*....|....*...
gi 1992515667 731 EGAPVTLPYQVYFMRKLW 748
Cdd:cd17093    81 DGPKPSLTYQVFFMRKLW 98
FERM_C1_MyoVII cd13198
FERM domain C-lobe, repeat 1, of Myosin VII (MyoVII/Myo7); MyoVII, a MyTH-FERM myosin, is an ...
 259-355 4.15e-42

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: 148.90  E-value: 4.15e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992515667 259 LLFSRLFEVITLSGPRLPKTQLILAVNWKGLCFLDQQEKMLLELSFPEVMGLATNREAQ-GGQRLLLSTMH-EEYEFVSP 336
Cdd:cd13198     1 LLFSRFFEATKFSGPSLPKSEVIIAVNWTGIYFVDEQEQVLLELSFPEITGVSSSRGKRdGGQSFTLTTIQgEEFVFQSP 80

                          90
                  ....*....|....*....
gi 1992515667 337 SSVAIAELVALFLEGLKER 355
Cdd:cd13198    81 NAEDIAELVNYFLEGLRKR 99
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 653-865 6.77e-33

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: 126.26  E-value: 6.77e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992515667  653 CHKIYFPNDTSEMLEVVANTRVRDVCDSIATRLQLASWEGCSLFIKISDKVISqkegdfffdslrevsDWVKKNKPQKEG 732
Cdd:smart00295   1 VLKVYLLDGTTLEFEVDSSTTAEELLETVCRKLGIRESEYFGLQFEDPDEDLR---------------HWLDPAKTLLDQ 65

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992515667  733 APVTLPYQVYFMRKLWLN--ISPGKDVNAdTILHYHQELPKYLRGFHKCSREDAIHLAGLIYKAQFNNDRSQLASVPK-- 808
Cdd:smart00295  66 DVKSEPLTLYFRVKFYPPdpNQLKEDPTR-LNLLYLQVRNDILEGRLPCPEEEALLLAALALQAEFGDYDEELHDLRGel 144

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1992515667  809 ILRELVPENLTRLMSSEEWKKSILLAYDKHKDKTVEEAKVAFLKWICRWPTFGSAFF 865
Cdd:smart00295 145 SLKRFLPKQLLDSRKLKEWRERIVELHKELIGLSPEEAKLKYLELARKLPTYGVELF 201
SH3 super family cl17036
Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction ...
 356-416 1.04e-09

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.


The actual alignment was detected with superfamily member cd11881:

Pssm-ID: 473055  Cd Length: 64  Bit Score: 55.21  E-value: 1.04e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1992515667 356 SIFAMALQD-RKATDDTTLLAFKKGDLLVLTKKQG-LLASENWTLGQNDRTGKTGLVPMACLY 416
Cdd:cd11881     1 SKYVVALQDyPNPSDGSSFLSFAKGDLIILDQDTGeQVMNSGWCNGRNDRTGQRGDFPADCVY 63
 
Name Accession Description Interval E-value
MyTH4 smart00139
Domain in Myosin and Kinesin Tails; Domain present twice in myosin-VIIa, and also present in 3 ...
 497-644 2.68e-60

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: 202.21  E-value: 2.68e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992515667  497 YSCEPLRQPLLKrvHANVDLWDIACQIFVAILRYMGDYPSRQAWPTLELTDQIFTLALQHPALQDEVYCQILKQLTHNSN 576
Cdd:smart00139   1 YTKDPIKTSLLK--LESDELQKEAVKIFKAILKFMGDIPLPRPDSHLDLVQFILQKGLDHPELRDEIYCQLIKQLTDNPS 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1992515667  577 RHSEERGWQLLWLCTGLFPPSKGLLPHAQKFIDTRR----GKLLAPDCSRRIQKVLRTGPRKQPPHQVEVEA 644
Cdd:smart00139  79 RQSEERGWQLLYLCTSLFPPSERLLPYLLQFLSRRAdpgsEQGLAKYCLYRLERTLKNGARKQPPSRLELEA 150
FERM_C2_MyoVII cd13199
FERM domain C-lobe, repeat 2, of Myosin VII (MyoVII, Myo7); MyoVII, a MyTH-FERM myosin, is an ...
 861-956 2.07e-59

FERM domain C-lobe, repeat 2, 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: 270020  Cd Length: 96  Bit Score: 197.48  E-value: 2.07e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992515667 861 GSAFFEVKQTSEPSYPDVILIAINRHGVLLIHPKTKDLLTTYPFTKISSWSSGSTYFHMALGSLGRGSRLLCETSLGYKM 940
Cdd:cd13199     1 GSAFFEVKQTTDPSLPEILLIAINKNGVSLIDPKTKEILATHPFSKISNWSSGNTYFHMTIGNLVRGSKLLCETSLGYKM 80

                          90
                  ....*....|....*.
gi 1992515667 941 DDLLTSYVQQLLSAMN 956
Cdd:cd13199    81 DDLLTSYISLLLSNMK 96
FERM1_F1_Myosin-VII cd17092
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain 1, F1 sub-domain, found in Myosin-VIIa, ...
 49-147 1.75e-54

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain 1, F1 sub-domain, found in Myosin-VIIa, Myosin-VIIb, and similar proteins; This family includes two nontraditional members of the myosin superfamily, myosin-VIIa and myosin-VIIb. Myosin-VIIa, also termed myosin-7a (Myo7a), has been implicated in the structural organization of hair bundles at the apex of sensory hair cells (SHCs) where it serves mechanotransduction in the process of hearing and balance. Mutations in the MYO7A gene may be associated with Usher Syndrome type 1B (USH1B) and nonsyndromic hearing loss (DFNB2, DFNA11). Myosin-VIIb, also termed myosin-7b (Myo7b), is a high duty ratio motor adapted for generating and maintaining tension. It associates with harmonin and ANKS4B to form a stable ternary complex for anchoring microvilli tip-link cadherins. Like other unconventional myosins, myosin-VII is composed of a conserved motor head, a neck region and a tail region containing two MyTH4 domains, a SH3 domain, and two FERM domains. The FERM domain is made up of three sub-domains, F1, F2, and F3. The family corresponds to the F1 sub-domain of the first FERM domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340612  Cd Length: 99  Bit Score: 184.00  E-value: 1.75e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992515667  49 HIPIQVILATGESLTVPVDSASTSREMCMHIAHKQGLSDHLGFSLQVAVYDKFWSLGSGRDHMMDAIARCEQMAQERGES 128
Cdd:cd17092     1 PIMLPVTFMDGSTKTVEVDSATTARELCRQLAEKLGLKDTFGFSLYIALFDKVSSLGSGTDHVMDAISQCEQYAKEKGAQ 80

                          90
                  ....*....|....*....
gi 1992515667 129 QRQSPWRIYFRKEFFTPWH 147
Cdd:cd17092    81 EREAPWRLYFRKEIFAPWH 99
FERM2_F1_Myosin-VII cd17093
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain 2, F1 sub-domain, found in Myosin-VIIa, ...
 651-748 7.06e-54

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain 2, F1 sub-domain, found in Myosin-VIIa, Myosin-VIIb, and similar proteins; This family includes two nontraditional members of myosin superfamily, myosin-VIIa and myosin-VIIb. Myosin-VIIa, also termed myosin-7a (Myo7a), has been implicated in the structural organization of hair bundles at the apex of sensory hair cells (SHCs) where it serves mechanotransduction in the process of hearing and balance. Mutations in MYO7A gene may be associated with Usher Syndrome type 1B (USH1B) and nonsyndromic hearing loss (DFNB2, DFNA11). Myosin-VIIb, also termed myosin-7b (Myo7b), is a high duty ratio motor adapted for generating and maintaining tension. It associates with harmonin and ANKS4B to form a stable ternary complex for anchoring microvilli tip-link cadherins. Like other unconventional myosins, myosin-VII is composed of a conserved motor head, a neck region and a tail region containing two MyTH4 domains, a SH3 domain, and two FERM domains. The FERM domain is made up of three sub-domains, F1, F2, and F3. The family corresponds to the F1 sub-domain of the second FERM domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340613  Cd Length: 98  Bit Score: 182.05  E-value: 7.06e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992515667 651 RICHKIYFPNDTSEMLEVVANTRVRDVCDSIATRLQLASWEGCSLFIKISDKVISQKEGDFFFDSLREVSDWVKKNKPQK 730
Cdd:cd17093     1 QIFHKVYFPDDTDEAFEVDSSTRARDLCQNIASRLGLKSSEGFSLFVKIADKVISLPEGDFFFDFIRHLTDWIKKARPTK 80

                          90
                  ....*....|....*...
gi 1992515667 731 EGAPVTLPYQVYFMRKLW 748
Cdd:cd17093    81 DGPKPSLTYQVFFMRKLW 98
FERM_C1_MyoVII cd13198
FERM domain C-lobe, repeat 1, of Myosin VII (MyoVII/Myo7); MyoVII, a MyTH-FERM myosin, is an ...
 259-355 4.15e-42

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: 148.90  E-value: 4.15e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992515667 259 LLFSRLFEVITLSGPRLPKTQLILAVNWKGLCFLDQQEKMLLELSFPEVMGLATNREAQ-GGQRLLLSTMH-EEYEFVSP 336
Cdd:cd13198     1 LLFSRFFEATKFSGPSLPKSEVIIAVNWTGIYFVDEQEQVLLELSFPEITGVSSSRGKRdGGQSFTLTTIQgEEFVFQSP 80

                          90
                  ....*....|....*....
gi 1992515667 337 SSVAIAELVALFLEGLKER 355
Cdd:cd13198    81 NAEDIAELVNYFLEGLRKR 99
MyTH4 pfam00784
MyTH4 domain; Domain in myosin and kinesin tails, present twice in myosin-VIIa, and also ...
 546-644 8.07e-40

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: 142.33  E-value: 8.07e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992515667 546 TDQIFTLALQHPALQDEVYCQILKQLTHNSNRHSEERGWQLLWLCTGLFPPSKGLLPHAQKFI------DTRRGKLLAPD 619
Cdd:pfam00784   1 AQNILQKGLKRPELRDEIYCQLIKQTTNNPKPESLLRGWQLLALCLGTFPPSKKLLKYLLKFLkrhaddPSREVGKYAQF 80

                          90       100
                  ....*....|....*....|....*
gi 1992515667 620 CSRRIQKVLRTGPRKQPPHQVEVEA 644
Cdd:pfam00784  81 CLKRLKRTLKNGGRKYPPSREEIEA 105
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 653-865 6.77e-33

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: 126.26  E-value: 6.77e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992515667  653 CHKIYFPNDTSEMLEVVANTRVRDVCDSIATRLQLASWEGCSLFIKISDKVISqkegdfffdslrevsDWVKKNKPQKEG 732
Cdd:smart00295   1 VLKVYLLDGTTLEFEVDSSTTAEELLETVCRKLGIRESEYFGLQFEDPDEDLR---------------HWLDPAKTLLDQ 65

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992515667  733 APVTLPYQVYFMRKLWLN--ISPGKDVNAdTILHYHQELPKYLRGFHKCSREDAIHLAGLIYKAQFNNDRSQLASVPK-- 808
Cdd:smart00295  66 DVKSEPLTLYFRVKFYPPdpNQLKEDPTR-LNLLYLQVRNDILEGRLPCPEEEALLLAALALQAEFGDYDEELHDLRGel 144

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1992515667  809 ILRELVPENLTRLMSSEEWKKSILLAYDKHKDKTVEEAKVAFLKWICRWPTFGSAFF 865
Cdd:smart00295 145 SLKRFLPKQLLDSRKLKEWRERIVELHKELIGLSPEEAKLKYLELARKLPTYGVELF 201
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
 763-865 4.14e-23

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


Pssm-ID: 459788 [Multi-domain]  Cd Length: 117  Bit Score: 95.41  E-value: 4.14e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992515667 763 LHYHQELPKYLRGFHKCSREDAIHLAGLIYKAQFNNDR-SQLASVPKILRELVPENLTRLMSSEEWKKSILLAYDKHKDK 841
Cdd:pfam00373  14 LLYLQAKDDILEGRLPCSEEEALLLAALQLQAEFGDYQpSSHTSEYLSLESFLPKQLLRKMKSKELEKRVLEAHKNLRGL 93

                          90       100
                  ....*....|....*....|....
gi 1992515667 842 TVEEAKVAFLKWICRWPTFGSAFF 865
Cdd:pfam00373  94 SAEEAKLKYLQIAQSLPTYGVEFF 117
FERM_B-lobe cd14473
FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C ...
 763-857 3.75e-17

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: 77.67  E-value: 3.75e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992515667 763 LHYHQELPKYLRGFHKCSREDAIHLAGLIYKAQF-NNDRSQLASVPKILRELVPENLTRLMSSEEWKKSILLAYDKHKDK 841
Cdd:cd14473     4 LLYLQVKRDILEGRLPCSEETAALLAALALQAEYgDYDPSEHKPKYLSLKRFLPKQLLKQRKPEEWEKRIVELHKKLRGL 83

                          90
                  ....*....|....*.
gi 1992515667 842 TVEEAKVAFLKWICRW 857
Cdd:cd14473    84 SPAEAKLKYLKIARKL 99
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 52-172 1.51e-14

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: 73.48  E-value: 1.51e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992515667   52 IQVILATGESLTVPVDSASTSREMCMHIAHKQGLSDHLGFSLQVAVYDKfwslgsgrdhmmdAIARCEQMAQERGESQRQ 131
Cdd:smart00295   2 LKVYLLDGTTLEFEVDSSTTAEELLETVCRKLGIRESEYFGLQFEDPDE-------------DLRHWLDPAKTLLDQDVK 68

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1992515667  132 S-PWRIYFRKEFFTPWHDS-REDPVSTELIYRQVLRGVWSGEY 172
Cdd:smart00295  69 SePLTLYFRVKFYPPDPNQlKEDPTRLNLLYLQVRNDILEGRL 111
SH3_MYO7A cd11881
Src Homology 3 domain of Myosin VIIa and similar proteins; Myo7A is an uncoventional myosin ...
 356-416 1.04e-09

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: 55.21  E-value: 1.04e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1992515667 356 SIFAMALQD-RKATDDTTLLAFKKGDLLVLTKKQG-LLASENWTLGQNDRTGKTGLVPMACLY 416
Cdd:cd11881     1 SKYVVALQDyPNPSDGSSFLSFAKGDLIILDQDTGeQVMNSGWCNGRNDRTGQRGDFPADCVY 63
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
 358-411 4.22e-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: 44.84  E-value: 4.22e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1992515667  358 FAMALQDRKATDDTTLlAFKKGDLLVLTKKQgllaSENWTLGQNDRtGKTGLVP 411
Cdd:smart00326   4 QVRALYDYTAQDPDEL-SFKKGDIITVLEKS----DDGWWKGRLGR-GKEGLFP 51
SH3_2 pfam07653
Variant SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in ...
 358-415 4.71e-04

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: 39.12  E-value: 4.71e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1992515667 358 FAMALQDRKATDdTTLLAFKKGDLLVLTKKqgllASENWTLGQndRTGKTGLVPMACL 415
Cdd:pfam07653   1 YGRVIFDYVGTD-KNGLTLKKGDVVKVLGK----DNDGWWEGE--TGGRVGLVPSTAV 51
 
Name Accession Description Interval E-value
MyTH4 smart00139
Domain in Myosin and Kinesin Tails; Domain present twice in myosin-VIIa, and also present in 3 ...
 497-644 2.68e-60

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: 202.21  E-value: 2.68e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992515667  497 YSCEPLRQPLLKrvHANVDLWDIACQIFVAILRYMGDYPSRQAWPTLELTDQIFTLALQHPALQDEVYCQILKQLTHNSN 576
Cdd:smart00139   1 YTKDPIKTSLLK--LESDELQKEAVKIFKAILKFMGDIPLPRPDSHLDLVQFILQKGLDHPELRDEIYCQLIKQLTDNPS 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1992515667  577 RHSEERGWQLLWLCTGLFPPSKGLLPHAQKFIDTRR----GKLLAPDCSRRIQKVLRTGPRKQPPHQVEVEA 644
Cdd:smart00139  79 RQSEERGWQLLYLCTSLFPPSERLLPYLLQFLSRRAdpgsEQGLAKYCLYRLERTLKNGARKQPPSRLELEA 150
FERM_C2_MyoVII cd13199
FERM domain C-lobe, repeat 2, of Myosin VII (MyoVII, Myo7); MyoVII, a MyTH-FERM myosin, is an ...
 861-956 2.07e-59

FERM domain C-lobe, repeat 2, 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: 270020  Cd Length: 96  Bit Score: 197.48  E-value: 2.07e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992515667 861 GSAFFEVKQTSEPSYPDVILIAINRHGVLLIHPKTKDLLTTYPFTKISSWSSGSTYFHMALGSLGRGSRLLCETSLGYKM 940
Cdd:cd13199     1 GSAFFEVKQTTDPSLPEILLIAINKNGVSLIDPKTKEILATHPFSKISNWSSGNTYFHMTIGNLVRGSKLLCETSLGYKM 80

                          90
                  ....*....|....*.
gi 1992515667 941 DDLLTSYVQQLLSAMN 956
Cdd:cd13199    81 DDLLTSYISLLLSNMK 96
FERM1_F1_Myosin-VII cd17092
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain 1, F1 sub-domain, found in Myosin-VIIa, ...
 49-147 1.75e-54

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain 1, F1 sub-domain, found in Myosin-VIIa, Myosin-VIIb, and similar proteins; This family includes two nontraditional members of the myosin superfamily, myosin-VIIa and myosin-VIIb. Myosin-VIIa, also termed myosin-7a (Myo7a), has been implicated in the structural organization of hair bundles at the apex of sensory hair cells (SHCs) where it serves mechanotransduction in the process of hearing and balance. Mutations in the MYO7A gene may be associated with Usher Syndrome type 1B (USH1B) and nonsyndromic hearing loss (DFNB2, DFNA11). Myosin-VIIb, also termed myosin-7b (Myo7b), is a high duty ratio motor adapted for generating and maintaining tension. It associates with harmonin and ANKS4B to form a stable ternary complex for anchoring microvilli tip-link cadherins. Like other unconventional myosins, myosin-VII is composed of a conserved motor head, a neck region and a tail region containing two MyTH4 domains, a SH3 domain, and two FERM domains. The FERM domain is made up of three sub-domains, F1, F2, and F3. The family corresponds to the F1 sub-domain of the first FERM domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340612  Cd Length: 99  Bit Score: 184.00  E-value: 1.75e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992515667  49 HIPIQVILATGESLTVPVDSASTSREMCMHIAHKQGLSDHLGFSLQVAVYDKFWSLGSGRDHMMDAIARCEQMAQERGES 128
Cdd:cd17092     1 PIMLPVTFMDGSTKTVEVDSATTARELCRQLAEKLGLKDTFGFSLYIALFDKVSSLGSGTDHVMDAISQCEQYAKEKGAQ 80

                          90
                  ....*....|....*....
gi 1992515667 129 QRQSPWRIYFRKEFFTPWH 147
Cdd:cd17092    81 EREAPWRLYFRKEIFAPWH 99
FERM2_F1_Myosin-VII cd17093
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain 2, F1 sub-domain, found in Myosin-VIIa, ...
 651-748 7.06e-54

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain 2, F1 sub-domain, found in Myosin-VIIa, Myosin-VIIb, and similar proteins; This family includes two nontraditional members of myosin superfamily, myosin-VIIa and myosin-VIIb. Myosin-VIIa, also termed myosin-7a (Myo7a), has been implicated in the structural organization of hair bundles at the apex of sensory hair cells (SHCs) where it serves mechanotransduction in the process of hearing and balance. Mutations in MYO7A gene may be associated with Usher Syndrome type 1B (USH1B) and nonsyndromic hearing loss (DFNB2, DFNA11). Myosin-VIIb, also termed myosin-7b (Myo7b), is a high duty ratio motor adapted for generating and maintaining tension. It associates with harmonin and ANKS4B to form a stable ternary complex for anchoring microvilli tip-link cadherins. Like other unconventional myosins, myosin-VII is composed of a conserved motor head, a neck region and a tail region containing two MyTH4 domains, a SH3 domain, and two FERM domains. The FERM domain is made up of three sub-domains, F1, F2, and F3. The family corresponds to the F1 sub-domain of the second FERM domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340613  Cd Length: 98  Bit Score: 182.05  E-value: 7.06e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992515667 651 RICHKIYFPNDTSEMLEVVANTRVRDVCDSIATRLQLASWEGCSLFIKISDKVISQKEGDFFFDSLREVSDWVKKNKPQK 730
Cdd:cd17093     1 QIFHKVYFPDDTDEAFEVDSSTRARDLCQNIASRLGLKSSEGFSLFVKIADKVISLPEGDFFFDFIRHLTDWIKKARPTK 80

                          90
                  ....*....|....*...
gi 1992515667 731 EGAPVTLPYQVYFMRKLW 748
Cdd:cd17093    81 DGPKPSLTYQVFFMRKLW 98
FERM_C1_MyoVII cd13198
FERM domain C-lobe, repeat 1, of Myosin VII (MyoVII/Myo7); MyoVII, a MyTH-FERM myosin, is an ...
 259-355 4.15e-42

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: 148.90  E-value: 4.15e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992515667 259 LLFSRLFEVITLSGPRLPKTQLILAVNWKGLCFLDQQEKMLLELSFPEVMGLATNREAQ-GGQRLLLSTMH-EEYEFVSP 336
Cdd:cd13198     1 LLFSRFFEATKFSGPSLPKSEVIIAVNWTGIYFVDEQEQVLLELSFPEITGVSSSRGKRdGGQSFTLTTIQgEEFVFQSP 80

                          90
                  ....*....|....*....
gi 1992515667 337 SSVAIAELVALFLEGLKER 355
Cdd:cd13198    81 NAEDIAELVNYFLEGLRKR 99
MyTH4 pfam00784
MyTH4 domain; Domain in myosin and kinesin tails, present twice in myosin-VIIa, and also ...
 546-644 8.07e-40

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: 142.33  E-value: 8.07e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992515667 546 TDQIFTLALQHPALQDEVYCQILKQLTHNSNRHSEERGWQLLWLCTGLFPPSKGLLPHAQKFI------DTRRGKLLAPD 619
Cdd:pfam00784   1 AQNILQKGLKRPELRDEIYCQLIKQTTNNPKPESLLRGWQLLALCLGTFPPSKKLLKYLLKFLkrhaddPSREVGKYAQF 80

                          90       100
                  ....*....|....*....|....*
gi 1992515667 620 CSRRIQKVLRTGPRKQPPHQVEVEA 644
Cdd:pfam00784  81 CLKRLKRTLKNGGRKYPPSREEIEA 105
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 653-865 6.77e-33

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: 126.26  E-value: 6.77e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992515667  653 CHKIYFPNDTSEMLEVVANTRVRDVCDSIATRLQLASWEGCSLFIKISDKVISqkegdfffdslrevsDWVKKNKPQKEG 732
Cdd:smart00295   1 VLKVYLLDGTTLEFEVDSSTTAEELLETVCRKLGIRESEYFGLQFEDPDEDLR---------------HWLDPAKTLLDQ 65

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992515667  733 APVTLPYQVYFMRKLWLN--ISPGKDVNAdTILHYHQELPKYLRGFHKCSREDAIHLAGLIYKAQFNNDRSQLASVPK-- 808
Cdd:smart00295  66 DVKSEPLTLYFRVKFYPPdpNQLKEDPTR-LNLLYLQVRNDILEGRLPCPEEEALLLAALALQAEFGDYDEELHDLRGel 144

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1992515667  809 ILRELVPENLTRLMSSEEWKKSILLAYDKHKDKTVEEAKVAFLKWICRWPTFGSAFF 865
Cdd:smart00295 145 SLKRFLPKQLLDSRKLKEWRERIVELHKELIGLSPEEAKLKYLELARKLPTYGVELF 201
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
 763-865 4.14e-23

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


Pssm-ID: 459788 [Multi-domain]  Cd Length: 117  Bit Score: 95.41  E-value: 4.14e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992515667 763 LHYHQELPKYLRGFHKCSREDAIHLAGLIYKAQFNNDR-SQLASVPKILRELVPENLTRLMSSEEWKKSILLAYDKHKDK 841
Cdd:pfam00373  14 LLYLQAKDDILEGRLPCSEEEALLLAALQLQAEFGDYQpSSHTSEYLSLESFLPKQLLRKMKSKELEKRVLEAHKNLRGL 93

                          90       100
                  ....*....|....*....|....
gi 1992515667 842 TVEEAKVAFLKWICRWPTFGSAFF 865
Cdd:pfam00373  94 SAEEAKLKYLQIAQSLPTYGVEFF 117
FERM_B-lobe cd14473
FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C ...
 763-857 3.75e-17

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: 77.67  E-value: 3.75e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992515667 763 LHYHQELPKYLRGFHKCSREDAIHLAGLIYKAQF-NNDRSQLASVPKILRELVPENLTRLMSSEEWKKSILLAYDKHKDK 841
Cdd:cd14473     4 LLYLQVKRDILEGRLPCSEETAALLAALALQAEYgDYDPSEHKPKYLSLKRFLPKQLLKQRKPEEWEKRIVELHKKLRGL 83

                          90
                  ....*....|....*.
gi 1992515667 842 TVEEAKVAFLKWICRW 857
Cdd:cd14473    84 SPAEAKLKYLKIARKL 99
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 52-172 1.51e-14

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: 73.48  E-value: 1.51e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992515667   52 IQVILATGESLTVPVDSASTSREMCMHIAHKQGLSDHLGFSLQVAVYDKfwslgsgrdhmmdAIARCEQMAQERGESQRQ 131
Cdd:smart00295   2 LKVYLLDGTTLEFEVDSSTTAEELLETVCRKLGIRESEYFGLQFEDPDE-------------DLRHWLDPAKTLLDQDVK 68

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1992515667  132 S-PWRIYFRKEFFTPWHDS-REDPVSTELIYRQVLRGVWSGEY 172
Cdd:smart00295  69 SePLTLYFRVKFYPPDPNQlKEDPTRLNLLYLQVRNDILEGRL 111
FERM_C-lobe cd00836
FERM domain C-lobe; The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N ...
 861-952 7.77e-14

FERM domain C-lobe; 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: 275389  Cd Length: 93  Bit Score: 67.79  E-value: 7.77e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992515667 861 GSAFFEVKQTSEPsyPDVILIAINRHGVLLIHPKTKDLLTTYPFTKISSWS-SGSTYFHMALGSLGRGSRLLCETS--LG 937
Cdd:cd00836     1 GVEFFPVKDKSKK--GSPIILGVNPEGISVYDELTGQPLVLFPWPNIKKISfSGAKKFTIVVADEDKQSKLLFQTPsrQA 78

                          90
                  ....*....|....*
gi 1992515667 938 YKMDDLLTSYVQQLL 952
Cdd:cd00836    79 KEIWKLIVGYHRFLL 93
FERM_F0_F1 cd01765
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0 sub-domain and F1 sub-domain, found ...
 652-746 2.42e-11

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0 sub-domain and F1 sub-domain, found in FERM (Four.1/Ezrin/Radixin/Moesin) family proteins; FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain is present at the N-terminus of a large and diverse group of proteins that mediate linkage of the cytoskeleton to the plasma membrane. FERM-containing proteins are ubiquitous components of the cytocortex and are involved in cell transport, cell structure and signaling functions. The FERM domain is made up of three sub-domains, F1, F2, and F3. The family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N), which is structurally similar to ubiquitin.


Pssm-ID: 340464  Cd Length: 80  Bit Score: 60.29  E-value: 2.42e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992515667 652 ICHKIYFPNDTSEMLEVVANTRVRDVCDSIATRLQLASWEGCSLFIKISDKVisqkegDFFFDSLREVSDWVKKnkpqke 731
Cdd:cd01765     1 ISCRVRLLDGTELTLEVSKKATGQELFDKVCEKLNLLEKDYFGLFYEDNDGQ------KHWLDLDKKISKQLKR------ 68

                          90
                  ....*....|....*
gi 1992515667 732 gapvTLPYQVYFMRK 746
Cdd:cd01765    69 ----SGPYQFYFRVK 79
FERM_C_MyoXV cd13201
FERM domain C-lobe of Myosin XV (MyoXV/Myo15); MyoXV, a MyTH-FERM myosin, are actin-based ...
 861-924 5.14e-10

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: 57.23  E-value: 5.14e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992515667 861 GSAFFEVKQTSEPSYPDVILIAINRHGVLLIHPKTKDLLTTYPFT------KISSWSSGSTYFHMALGSL 924
Cdd:cd13201     1 GSNFFYVQRVSDPRLPGPCLLALNREGLHFLDPKTHETLLRIPLKevqstrKLRPLEDGTPFLDIKYGNL 70
FERM_F0_F1 cd01765
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0 sub-domain and F1 sub-domain, found ...
 50-142 8.61e-10

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0 sub-domain and F1 sub-domain, found in FERM (Four.1/Ezrin/Radixin/Moesin) family proteins; FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain is present at the N-terminus of a large and diverse group of proteins that mediate linkage of the cytoskeleton to the plasma membrane. FERM-containing proteins are ubiquitous components of the cytocortex and are involved in cell transport, cell structure and signaling functions. The FERM domain is made up of three sub-domains, F1, F2, and F3. The family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N), which is structurally similar to ubiquitin.


Pssm-ID: 340464  Cd Length: 80  Bit Score: 56.06  E-value: 8.61e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992515667  50 IPIQVILATGESLTVPVDSASTSREMCMHIAHKQGLSDHLGFSLQ-VAVYDKFWSLGSgRDHMMDAIarceqmaqerges 128
Cdd:cd01765     1 ISCRVRLLDGTELTLEVSKKATGQELFDKVCEKLNLLEKDYFGLFyEDNDGQKHWLDL-DKKISKQL------------- 66

                          90
                  ....*....|....
gi 1992515667 129 QRQSPWRIYFRKEF 142
Cdd:cd01765    67 KRSGPYQFYFRVKF 80
SH3_MYO7A cd11881
Src Homology 3 domain of Myosin VIIa and similar proteins; Myo7A is an uncoventional myosin ...
 356-416 1.04e-09

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: 55.21  E-value: 1.04e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1992515667 356 SIFAMALQD-RKATDDTTLLAFKKGDLLVLTKKQG-LLASENWTLGQNDRTGKTGLVPMACLY 416
Cdd:cd11881     1 SKYVVALQDyPNPSDGSSFLSFAKGDLIILDQDTGeQVMNSGWCNGRNDRTGQRGDFPADCVY 63
FERM_C2_myosin_like cd13204
FERM domain C-lobe, repeat 2, of Myosin-like proteins; These myosin-like proteins are ...
 861-947 1.48e-08

FERM domain C-lobe, repeat 2, of Myosin-like proteins; These myosin-like proteins are unidentified though they are sequence similar to myosin 1/myo1, myosin 7/myoVII, and myosin 10/myoX. These myosin-like proteins contain an N-terminal motor/head region and a C-terminal tail consisting of two myosin tail homology 4 (MyTH4) and twos FERM domains. In myoX the FERM domain forms a supramodule with its MyTH4 domain which binds to the negatively charged E-hook region in the tails of alpha- and beta-tubulin forming a proposed motorized link between actin filaments and microtubules and a similar thing might happen in these myosins. 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 second FERM_N repeat is present in this hierarchy. 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: 270025  Cd Length: 93  Bit Score: 52.82  E-value: 1.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992515667 861 GSAFFEVKQTSEPSYPDVILIAINRHGVLLIHPKTKDLLTTYPFTKISSWSSGSTYFHMALGSLGRGSRLLCETSLGYKM 940
Cdd:cd13204     1 GSTVFDVTQSYTSNLPKTLWLAIDQSGVHLLERRTKEPLCSYDYSSIVSYSPSLNSLMIVTGSLTKGSKFIFNTNQAFQI 80


                  ....*..
gi 1992515667 941 DDLLTSY 947
Cdd:cd13204    81 ANLIRDY 87
FERM2_F1_Myosin-VII cd17093
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain 2, F1 sub-domain, found in Myosin-VIIa, ...
 50-115 8.27e-07

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain 2, F1 sub-domain, found in Myosin-VIIa, Myosin-VIIb, and similar proteins; This family includes two nontraditional members of myosin superfamily, myosin-VIIa and myosin-VIIb. Myosin-VIIa, also termed myosin-7a (Myo7a), has been implicated in the structural organization of hair bundles at the apex of sensory hair cells (SHCs) where it serves mechanotransduction in the process of hearing and balance. Mutations in MYO7A gene may be associated with Usher Syndrome type 1B (USH1B) and nonsyndromic hearing loss (DFNB2, DFNA11). Myosin-VIIb, also termed myosin-7b (Myo7b), is a high duty ratio motor adapted for generating and maintaining tension. It associates with harmonin and ANKS4B to form a stable ternary complex for anchoring microvilli tip-link cadherins. Like other unconventional myosins, myosin-VII is composed of a conserved motor head, a neck region and a tail region containing two MyTH4 domains, a SH3 domain, and two FERM domains. The FERM domain is made up of three sub-domains, F1, F2, and F3. The family corresponds to the F1 sub-domain of the second FERM domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340613  Cd Length: 98  Bit Score: 48.00  E-value: 8.27e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1992515667  50 IPIQVILATGESLTVPVDSASTSREMCMHIAHKQGLSDHLGFSLQVAVYDKFWSLGSGrDHMMDAI 115
Cdd:cd17093     2 IFHKVYFPDDTDEAFEVDSSTRARDLCQNIASRLGLKSSEGFSLFVKIADKVISLPEG-DFFFDFI 66
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
 358-411 4.22e-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: 44.84  E-value: 4.22e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1992515667  358 FAMALQDRKATDDTTLlAFKKGDLLVLTKKQgllaSENWTLGQNDRtGKTGLVP 411
Cdd:smart00326   4 QVRALYDYTAQDPDEL-SFKKGDIITVLEKS----DDGWWKGRLGR-GKEGLFP 51
SH3 cd00174
Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction ...
 358-414 1.35e-05

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: 43.22  E-value: 1.35e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1992515667 358 FAMALQDRKATDDTtLLAFKKGDLLVLTKKQgllaSENWTLGQNDRtGKTGLVPMAC 414
Cdd:cd00174     1 YARALYDYEAQDDD-ELSFKKGDIITVLEKD----DDGWWEGELNG-GREGLFPANY 51
SH3_MYO15 cd11884
Src Homology 3 domain of Myosin XV; This subfamily is composed of proteins with similarity to ...
 358-411 2.33e-05

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: 42.70  E-value: 2.33e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1992515667 358 FAMALQDRkATDDTTLLAFKKGDLLVLTKKQGLLaSENWTLGQNDrtGKTGLVP 411
Cdd:cd11884     1 YVVAVRAY-ITRDQTLLSFHKGDVIKLLPKEGPL-DPGWLFGTLD--GRSGAFP 50
FERM_C1_myosin_like cd13203
FERM domain C-lobe, repeat 1, of Myosin-like proteins; These myosin-like proteins are ...
 861-909 4.51e-05

FERM domain C-lobe, repeat 1, of Myosin-like proteins; These myosin-like proteins are unidentified though they are sequence similar to myosin 1/myo1, myosin 7/myoVII, and myosin 10/myoX. These myosin-like proteins contain an N-terminal motor/head region and a C-terminal tail consisting of two myosin tail homology 4 (MyTH4) and twos FERM domains. In myoX the FERM domain forms a supramodule with its MyTH4 domain which binds to the negatively charged E-hook region in the tails of alpha- and beta-tubulin forming a proposed motorized link between actin filaments and microtubules and a similar thing might happen in these myosins. 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 first FERM_N repeat is present in this hierarchy. 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: 270024  Cd Length: 97  Bit Score: 43.18  E-value: 4.51e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1992515667 861 GSAFFEVKQTSEPSYPDVILIAINRHGVLLIHPKTKDLLTTYPFTKISS 909
Cdd:cd13203     1 GTTLFDVTYKGYWSYPNNLILGVHCDGFKFVNPDTKEILAEYRYSDLES 49
FERM1_F1_Myosin-VII cd17092
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain 1, F1 sub-domain, found in Myosin-VIIa, ...
 656-746 1.22e-04

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain 1, F1 sub-domain, found in Myosin-VIIa, Myosin-VIIb, and similar proteins; This family includes two nontraditional members of the myosin superfamily, myosin-VIIa and myosin-VIIb. Myosin-VIIa, also termed myosin-7a (Myo7a), has been implicated in the structural organization of hair bundles at the apex of sensory hair cells (SHCs) where it serves mechanotransduction in the process of hearing and balance. Mutations in the MYO7A gene may be associated with Usher Syndrome type 1B (USH1B) and nonsyndromic hearing loss (DFNB2, DFNA11). Myosin-VIIb, also termed myosin-7b (Myo7b), is a high duty ratio motor adapted for generating and maintaining tension. It associates with harmonin and ANKS4B to form a stable ternary complex for anchoring microvilli tip-link cadherins. Like other unconventional myosins, myosin-VII is composed of a conserved motor head, a neck region and a tail region containing two MyTH4 domains, a SH3 domain, and two FERM domains. The FERM domain is made up of three sub-domains, F1, F2, and F3. The family corresponds to the F1 sub-domain of the first FERM domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340612  Cd Length: 99  Bit Score: 41.86  E-value: 1.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992515667 656 IYFPNDTSEMLEVVANTRVRDVCDSIATRLQLASWEGCSLFIKISDKVISQKEG-DFFFDSLREVSDWVK-KNKPQKEga 733
Cdd:cd17092     6 VTFMDGSTKTVEVDSATTARELCRQLAEKLGLKDTFGFSLYIALFDKVSSLGSGtDHVMDAISQCEQYAKeKGAQERE-- 83

                          90
                  ....*....|...
gi 1992515667 734 pvtLPYQVYFmRK 746
Cdd:cd17092    84 ---APWRLYF-RK 92
FERM_C_Talin cd10569
FERM domain C-lobe/F3 of Talin; Talin (also called filopodin) plays an important role in ...
 861-952 3.39e-04

FERM domain C-lobe/F3 of Talin; Talin (also called filopodin) plays an important role in initiating actin filament growth in motile cell protrusions. It is responsible for linking the cytoplasmic domains of integrins to the actin-based cytoskeleton, and is involved in vinculin, integrin and actin interactions. At the leading edge of motile cells, talin colocalises with the hyaluronan receptor layilin in transient adhesions, some of which become more stable focal adhesions (FA). During this maturation process, layilin is replaced with integrins, where localized production of PI(4,5)P(2) by type 1 phosphatidyl inositol phosphate kinase type 1gamma (PIPK1gamma) is thought to play a role in FA assembly. Talins are composed of a N-terminal region FERM domain which us made up of 3 subdomains (N, alpha-, and C-lobe; or- A-lobe, B-lobe, and C-lobe; or F1, F2, and F3) connected by short linkers, a talin rod which binds vinculin, and a conserved C-terminal region with actin- and integrin-binding sites. There are 2 additional actin-binding domains, one in the talin rod and the other in the FERM domain. Both the F2 and F3 FERM subdomains contribute to F-actin binding. Subdomain F3 of the FERM domain contains overlapping binding sites for integrin cytoplasmic domains and for the type 1 gamma isoform of PIP-kinase (phosphatidylinositol 4-phosphate 5-kinase). The FERM domain has a cloverleaf tripart structure . 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: 269973  Cd Length: 92  Bit Score: 40.40  E-value: 3.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992515667 861 GSAFFEVKQTSEPSYPDVI-LIAINRHGVLLIHPKTKDLLTTYPFTKISSWSSGSTYFHMALGSLgRGSRLLCETSLGYK 939
Cdd:cd10569     1 GVTFFLVKEKMKGKNKLVPrLLGITKESVLRLDEETKEVLKVWPLTTIKRWAASPKSFTLDFGDY-SENYYSVQTTEGEQ 79

                          90
                  ....*....|...
gi 1992515667 940 MDDLLTSYVQQLL 952
Cdd:cd10569    80 ISQLISGYIDIIL 92
SH3_2 pfam07653
Variant SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in ...
 358-415 4.71e-04

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: 39.12  E-value: 4.71e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1992515667 358 FAMALQDRKATDdTTLLAFKKGDLLVLTKKqgllASENWTLGQndRTGKTGLVPMACL 415
Cdd:pfam07653   1 YGRVIFDYVGTD-KNGLTLKKGDVVKVLGK----DNDGWWEGE--TGGRVGLVPSTAV 51
SH3_Irsp53_BAIAP2L cd11779
Src Homology 3 domain of Insulin Receptor tyrosine kinase Substrate p53, Brain-specific ...
 367-419 8.92e-04

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: 38.46  E-value: 8.92e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1992515667 367 ATDDTTLLAFKKGDLLvltkkqGLLASEN---WTLGQNDRTGKTGLVPMAclYTIP 419
Cdd:cd11779    10 AAGGETQLSFEEGDVI------TLLGPEPrdgWHYGENERSGRRGWFPIA--YTEP 57
SH3_1 pfam00018
SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal ...
 361-411 1.03e-03

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: 394975 [Multi-domain]  Cd Length: 47  Bit Score: 37.95  E-value: 1.03e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1992515667 361 ALQDRKATDDTTLlAFKKGDLLVLTKKQGllasENWTLGQNDrTGKTGLVP 411
Cdd:pfam00018   2 ALYDYTAQEPDEL-SFKKGDIIIVLEKSE----DGWWKGRNK-GGKEGLIP 46
SH3_Irsp53 cd11915
Src Homology 3 domain of Insulin Receptor tyrosine kinase Substrate p53; IRSp53 is also known ...
 355-417 1.08e-03

Src Homology 3 domain of Insulin Receptor tyrosine kinase Substrate p53; IRSp53 is also known as BAIAP2 (Brain-specific Angiogenesis Inhibitor 1-Associated Protein 2). It 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. One variant (T-form) is expressed exclusively in human breast cancer cells. The gene encoding IRSp53 is a putative susceptibility gene for Gilles de la Tourette syndrome. IRSp53 can also mediate the recruitment of effector proteins Tir and EspFu, which regulate host cell actin reorganization, to bacterial attachment sites. It contains an N-terminal IMD, a CRIB (Cdc42 and Rac interactive binding motif), an SH3 domain, and a WASP homology 2 (WH2) actin-binding motif at the C-terminus. The SH3 domain of IRSp53 has 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: 212848  Cd Length: 59  Bit Score: 38.07  E-value: 1.08e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1992515667 355 RSIFAMAlqdrkATDDTTLLAFKKGDLLVLTKKQgllASENWTLGQNDRTGKTGLVPMAclYT 417
Cdd:cd11915     4 QAIFSHA-----AGDNSTLLSFKEGDYITLLVPE---ARDGWHYGECEKTKMRGWFPFS--YT 56
SH3_MYO15B cd12068
Src Homology 3 domain of Myosin XVb; Myosin XVb, also called KIAA1783, was named based on its ...
 368-411 2.63e-03

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: 36.78  E-value: 2.63e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1992515667 368 TDDTTLLAFKKGDLLVLTKKQGLLASenWTLGQNDrtGKTGLVP 411
Cdd:cd12068    10 TDDKSLLSFHRGDLIKLLPMAGLEPG--WQFGSTG--GRSGLFP 49
SH3_9 pfam14604
Variant SH3 domain;
361-416 5.63e-03

Variant SH3 domain;


Pssm-ID: 434066 [Multi-domain]  Cd Length: 49  Bit Score: 35.67  E-value: 5.63e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1992515667 361 ALQDRKATDDTtLLAFKKGDLLVLTKKqgllASENWTLGQNdrTGKTGLVPMACLY 416
Cdd:pfam14604   1 ALYPYEPKDDD-ELSLQRGDVITVIEE----SEDGWWEGIN--TGRTGLVPANYVE 49
SH3_Nbp2-like cd11865
Src Homology 3 domain of Saccharomyces cerevisiae Nap1-binding protein 2 and similar fungal ...
 359-411 9.90e-03

Src Homology 3 domain of Saccharomyces cerevisiae Nap1-binding protein 2 and similar fungal proteins; This subfamily includes Saccharomyces cerevisiae Nbp2 (Nucleosome assembly protein 1 (Nap1)-binding protein 2), Schizosaccharomyces pombe Skb5, and similar proteins. Nbp2 interacts with Nap1, which is essential for maintaining proper nucleosome structures in transcription and replication. It is also the binding partner of the yeast type II protein phosphatase Ptc1p and serves as a scaffolding protein that brings seven kinases in close contact to Ptc1p. Nbp2 plays a role many cell processes including organelle inheritance, mating hormone response, cell wall stress, mitotic cell growth at elevated temperatures, and high osmolarity. Skb5 interacts with the p21-activated kinase (PAK) homolog Shk1, which is critical for fission yeast cell viability. Skb5 activates Shk1 and plays a role in regulating cell morphology and growth under hypertonic conditions. Nbp2 and Skb5 contain an 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: 212799  Cd Length: 55  Bit Score: 35.18  E-value: 9.90e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1992515667 359 AMALQDRKATDDTTLlAFKKGDLLVLTKKQGllasENWTLGQNDRTGKTGLVP 411
Cdd:cd11865     2 AVALYDFEPEHDNEL-GFAEGQILFILYKHG----QGWLIAEDESGGKTGLVP 49
 
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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