NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1058152126|gb|JAS79711|]
View 

hypothetical protein g.42779, partial [Homalodisca liturata]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
FERM1_F1_Myosin-VII cd17092
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain 1, F1 sub-domain, found in Myosin-VIIa, ...
216-314 2.06e-72

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: 221.74  E-value: 2.06e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1058152126 216 PIMLPITFMDGNTKTLLADSATTARELCNQLSDKIGLKDQFGFSLYIALFDKVSSLGSGGDHVMDAISQCEQYAKEQGAQ 295
Cdd:cd17092     1 PIMLPVTFMDGSTKTVEVDSATTARELCRQLAEKLGLKDTFGFSLYIALFDKVSSLGSGTDHVMDAISQCEQYAKEKGAQ 80
                          90
                  ....*....|....*....
gi 1058152126 296 ERNAPWRLFFRKEIFAPWH 314
Cdd:cd17092    81 EREAPWRLYFRKEIFAPWH 99
MyTH4 smart00139
Domain in Myosin and Kinesin Tails; Domain present twice in myosin-VIIa, and also present in 3 ...
105-212 1.15e-48

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: 162.53  E-value: 1.15e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1058152126  105 RPTSNLEKLHFIIGHGILRAELRDEIYCQICKQLTNNPSKSSHARGWILLSLCVGCFAPSEKFVSYLRAFIREGPP---- 180
Cdd:smart00139  40 RPDSHLDLVQFILQKGLDHPELRDEIYCQLIKQLTDNPSRQSEERGWQLLYLCTSLFPPSERLLPYLLQFLSRRADpgse 119
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1058152126  181 -GYAPYCEDRLKRTFNNGTRNQPPSWLELQATK 212
Cdd:smart00139 120 qGLAKYCLYRLERTLKNGARKQPPSRLELEAIL 152
FERM_B-lobe cd14473
FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C ...
322-407 1.05e-10

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: 58.03  E-value: 1.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1058152126 322 ATNLIYQQVVRGVKFGEYRCDkEEDLAMIAAQQYFIEFATDLNMERLLN--LLPNYIPDYCLTNaeKSIDRWAALIVQAY 399
Cdd:cd14473     1 TRYLLYLQVKRDILEGRLPCS-EETAALLAALALQAEYGDYDPSEHKPKylSLKRFLPKQLLKQ--RKPEEWEKRIVELH 77

                  ....*...
gi 1058152126 400 KKSYYLKE 407
Cdd:cd14473    78 KKLRGLSP 85
 
Name Accession Description Interval E-value
FERM1_F1_Myosin-VII cd17092
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain 1, F1 sub-domain, found in Myosin-VIIa, ...
216-314 2.06e-72

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: 221.74  E-value: 2.06e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1058152126 216 PIMLPITFMDGNTKTLLADSATTARELCNQLSDKIGLKDQFGFSLYIALFDKVSSLGSGGDHVMDAISQCEQYAKEQGAQ 295
Cdd:cd17092     1 PIMLPVTFMDGSTKTVEVDSATTARELCRQLAEKLGLKDTFGFSLYIALFDKVSSLGSGTDHVMDAISQCEQYAKEKGAQ 80
                          90
                  ....*....|....*....
gi 1058152126 296 ERNAPWRLFFRKEIFAPWH 314
Cdd:cd17092    81 EREAPWRLYFRKEIFAPWH 99
MyTH4 smart00139
Domain in Myosin and Kinesin Tails; Domain present twice in myosin-VIIa, and also present in 3 ...
105-212 1.15e-48

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: 162.53  E-value: 1.15e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1058152126  105 RPTSNLEKLHFIIGHGILRAELRDEIYCQICKQLTNNPSKSSHARGWILLSLCVGCFAPSEKFVSYLRAFIREGPP---- 180
Cdd:smart00139  40 RPDSHLDLVQFILQKGLDHPELRDEIYCQLIKQLTDNPSRQSEERGWQLLYLCTSLFPPSERLLPYLLQFLSRRADpgse 119
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1058152126  181 -GYAPYCEDRLKRTFNNGTRNQPPSWLELQATK 212
Cdd:smart00139 120 qGLAKYCLYRLERTLKNGARKQPPSRLELEAIL 152
MyTH4 pfam00784
MyTH4 domain; Domain in myosin and kinesin tails, present twice in myosin-VIIa, and also ...
113-210 3.48e-46

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: 154.27  E-value: 3.48e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1058152126 113 LHFIIGHGILRAELRDEIYCQICKQLTNNPSKSSHARGWILLSLCVGCFAPSEKFVSYLRAFIREGPP-------GYAPY 185
Cdd:pfam00784   1 AQNILQKGLKRPELRDEIYCQLIKQTTNNPKPESLLRGWQLLALCLGTFPPSKKLLKYLLKFLKRHADdpsrevgKYAQF 80
                          90       100
                  ....*....|....*....|....*
gi 1058152126 186 CEDRLKRTFNNGTRNQPPSWLELQA 210
Cdd:pfam00784  81 CLKRLKRTLKNGGRKYPPSREEIEA 105
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
218-401 7.75e-30

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: 114.31  E-value: 7.75e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1058152126  218 MLPITFMDGNTKTLLADSATTARELCNQLSDKIGLKDQFGFSLYIALFDKVsslgsggdhvmdaISQCEQYAKEQGAQER 297
Cdd:smart00295   1 VLKVYLLDGTTLEFEVDSSTTAEELLETVCRKLGIRESEYFGLQFEDPDED-------------LRHWLDPAKTLLDQDV 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1058152126  298 N-APWRLFFRKEIFAPWH-DPTEDQVATNLIYQQVVRGVKFGEYRCDKEEdLAMIAAQQYFIEF---ATDLNMERLLNLL 372
Cdd:smart00295  68 KsEPLTLYFRVKFYPPDPnQLKEDPTRLNLLYLQVRNDILEGRLPCPEEE-ALLLAALALQAEFgdyDEELHDLRGELSL 146
                          170       180
                   ....*....|....*....|....*....
gi 1058152126  373 PNYIPDYclTNAEKSIDRWAALIVQAYKK 401
Cdd:smart00295 147 KRFLPKQ--LLDSRKLKEWRERIVELHKE 173
FERM_B-lobe cd14473
FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C ...
322-407 1.05e-10

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: 58.03  E-value: 1.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1058152126 322 ATNLIYQQVVRGVKFGEYRCDkEEDLAMIAAQQYFIEFATDLNMERLLN--LLPNYIPDYCLTNaeKSIDRWAALIVQAY 399
Cdd:cd14473     1 TRYLLYLQVKRDILEGRLPCS-EETAALLAALALQAEYGDYDPSEHKPKylSLKRFLPKQLLKQ--RKPEEWEKRIVELH 77

                  ....*...
gi 1058152126 400 KKSYYLKE 407
Cdd:cd14473    78 KKLRGLSP 85
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
318-401 3.04e-03

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


Pssm-ID: 459788 [Multi-domain]  Cd Length: 117  Bit Score: 37.25  E-value: 3.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1058152126 318 EDQVATNLIYQQVVRGVKFGEYRCDkEEDLAMIAAQQYFIEF------ATDLNMERLLNLLPNYipdycLTNAEKSiDRW 391
Cdd:pfam00373   7 QDEVTRHLLYLQAKDDILEGRLPCS-EEEALLLAALQLQAEFgdyqpsSHTSEYLSLESFLPKQ-----LLRKMKS-KEL 79
                          90
                  ....*....|
gi 1058152126 392 AALIVQAYKK 401
Cdd:pfam00373  80 EKRVLEAHKN 89
 
Name Accession Description Interval E-value
FERM1_F1_Myosin-VII cd17092
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain 1, F1 sub-domain, found in Myosin-VIIa, ...
216-314 2.06e-72

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: 221.74  E-value: 2.06e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1058152126 216 PIMLPITFMDGNTKTLLADSATTARELCNQLSDKIGLKDQFGFSLYIALFDKVSSLGSGGDHVMDAISQCEQYAKEQGAQ 295
Cdd:cd17092     1 PIMLPVTFMDGSTKTVEVDSATTARELCRQLAEKLGLKDTFGFSLYIALFDKVSSLGSGTDHVMDAISQCEQYAKEKGAQ 80
                          90
                  ....*....|....*....
gi 1058152126 296 ERNAPWRLFFRKEIFAPWH 314
Cdd:cd17092    81 EREAPWRLYFRKEIFAPWH 99
MyTH4 smart00139
Domain in Myosin and Kinesin Tails; Domain present twice in myosin-VIIa, and also present in 3 ...
105-212 1.15e-48

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: 162.53  E-value: 1.15e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1058152126  105 RPTSNLEKLHFIIGHGILRAELRDEIYCQICKQLTNNPSKSSHARGWILLSLCVGCFAPSEKFVSYLRAFIREGPP---- 180
Cdd:smart00139  40 RPDSHLDLVQFILQKGLDHPELRDEIYCQLIKQLTDNPSRQSEERGWQLLYLCTSLFPPSERLLPYLLQFLSRRADpgse 119
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1058152126  181 -GYAPYCEDRLKRTFNNGTRNQPPSWLELQATK 212
Cdd:smart00139 120 qGLAKYCLYRLERTLKNGARKQPPSRLELEAIL 152
MyTH4 pfam00784
MyTH4 domain; Domain in myosin and kinesin tails, present twice in myosin-VIIa, and also ...
113-210 3.48e-46

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: 154.27  E-value: 3.48e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1058152126 113 LHFIIGHGILRAELRDEIYCQICKQLTNNPSKSSHARGWILLSLCVGCFAPSEKFVSYLRAFIREGPP-------GYAPY 185
Cdd:pfam00784   1 AQNILQKGLKRPELRDEIYCQLIKQTTNNPKPESLLRGWQLLALCLGTFPPSKKLLKYLLKFLKRHADdpsrevgKYAQF 80
                          90       100
                  ....*....|....*....|....*
gi 1058152126 186 CEDRLKRTFNNGTRNQPPSWLELQA 210
Cdd:pfam00784  81 CLKRLKRTLKNGGRKYPPSREEIEA 105
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
218-401 7.75e-30

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: 114.31  E-value: 7.75e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1058152126  218 MLPITFMDGNTKTLLADSATTARELCNQLSDKIGLKDQFGFSLYIALFDKVsslgsggdhvmdaISQCEQYAKEQGAQER 297
Cdd:smart00295   1 VLKVYLLDGTTLEFEVDSSTTAEELLETVCRKLGIRESEYFGLQFEDPDED-------------LRHWLDPAKTLLDQDV 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1058152126  298 N-APWRLFFRKEIFAPWH-DPTEDQVATNLIYQQVVRGVKFGEYRCDKEEdLAMIAAQQYFIEF---ATDLNMERLLNLL 372
Cdd:smart00295  68 KsEPLTLYFRVKFYPPDPnQLKEDPTRLNLLYLQVRNDILEGRLPCPEEE-ALLLAALALQAEFgdyDEELHDLRGELSL 146
                          170       180
                   ....*....|....*....|....*....
gi 1058152126  373 PNYIPDYclTNAEKSIDRWAALIVQAYKK 401
Cdd:smart00295 147 KRFLPKQ--LLDSRKLKEWRERIVELHKE 173
FERM_F1_DdMyo7_like cd17208
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in Dictyostelium ...
215-310 6.27e-15

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in Dictyostelium discoideum Myosin-VIIa (DdMyo7) and similar proteins; DdMyo7, also termed Myosin-I heavy chain, or class VII unconventional myosin, or M7, plays a role in adhesion in Dictyostelium where it is a component of a complex of proteins that serve to link membrane receptors to the underlying actin cytoskeleton. It interacts with talinA, an actin-binding protein with a known role in cell-substrate adhesion. DdMyo7 is required for phagocytosis. It is also essential for the extension of filopodia, plasma membrane protrusions filled with parallel bundles of F-actin. Members in this family contain a myosin motor domain, two MyTH4 domains, two FERM (Band 4.1, ezrin, radixin, moesin) domains, and two Pleckstrin homology (PH) domains. Some family members contain an extra SH3 domain. Each FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340728  Cd Length: 98  Bit Score: 69.97  E-value: 6.27e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1058152126 215 KPIMLPITFMDGNTKTLLADSATTARELCNQLSDKIGLK-DQFGFSLYIALFDKVSSLGSgGDHVMDAISQCEQYAKEQG 293
Cdd:cd17208     2 RPIVARFYFLDGQFKALEFDSAATAAEVLEQLKQKIGLRsTADGFALYEVFGGIERAILP-EEKVADVLSKWEKLQRTMA 80
                          90
                  ....*....|....*..
gi 1058152126 294 AQERNAPWRLFFRKEIF 310
Cdd:cd17208    81 SCAAQQAVKFVFKKRLF 97
FERM2_F1_Myosin-VII cd17093
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain 2, F1 sub-domain, found in Myosin-VIIa, ...
216-309 7.30e-12

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: 61.49  E-value: 7.30e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1058152126 216 PIMLPITFMDGNTKTLLADSATTARELCNQLSDKIGLKDQFGFSLYIALFDKVSSLGSgGDHVMDAISQCEQY-AKEQGA 294
Cdd:cd17093     1 QIFHKVYFPDDTDEAFEVDSSTRARDLCQNIASRLGLKSSEGFSLFVKIADKVISLPE-GDFFFDFIRHLTDWiKKARPT 79
                          90
                  ....*....|....*...
gi 1058152126 295 QERNAP---WRLFFRKEI 309
Cdd:cd17093    80 KDGPKPsltYQVFFMRKL 97
FERM_B-lobe cd14473
FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C ...
322-407 1.05e-10

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: 58.03  E-value: 1.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1058152126 322 ATNLIYQQVVRGVKFGEYRCDkEEDLAMIAAQQYFIEFATDLNMERLLN--LLPNYIPDYCLTNaeKSIDRWAALIVQAY 399
Cdd:cd14473     1 TRYLLYLQVKRDILEGRLPCS-EETAALLAALALQAEYGDYDPSEHKPKylSLKRFLPKQLLKQ--RKPEEWEKRIVELH 77

                  ....*...
gi 1058152126 400 KKSYYLKE 407
Cdd:cd14473    78 KKLRGLSP 85
FERM_F1_Myo10_like cd17110
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in unconventional ...
215-310 1.58e-10

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in unconventional myosin-X and similar proteins; Myosin-X, also termed myosin-10 (Myo10), is an untraditional member of myosin superfamily. It is an actin-based motor protein that plays a critical role in diverse cellular motile events, such as filopodia formation/extension, phagocytosis, cell migration, and mitotic spindle maintenance, as well as a number of disease states including cancer metastasis and pathogen infection. Myosin-X functions as an important regulator of cytoskeleton that modulates cell motilities in many different cellular contexts. It regulates neuronal radial migration through interacting with N-cadherin. Like other unconventional myosins, Myosin-X is composed of a conserved motor head, a neck region and a variable tail. The neck region consists of three IQ motifs (light chain-binding sites), and a predicted stalk of coiled coil. The tail contains three PEST regions, three PH domains, a MyTH4 domain, and a FERM domain. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N). Amoebozoan Dictyostelium discoideum myosin VII (DdMyo7) and uncharacterized pleckstrin homology domain-containing family H member 3 (PLEKHH3) are also included in this family. Like metazoan Myo10, DdMyo7 is essential for the extension of filopodia, plasma membrane protrusions filled with parallel bundles of F-actin.


Pssm-ID: 340630  Cd Length: 97  Bit Score: 57.39  E-value: 1.58e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1058152126 215 KPIMLPITFMDGNTKTLLADSATTARELCNQLSDKIGLKD-QFGFSLYiALFDKVSSLGSGGDHVMDAISQCEQYAKEqG 293
Cdd:cd17110     2 QELTVTVTCQGGRTCKVAIDSWTTCGEVSKDLARRLGLERsRNGFALF-ETSGDIERALEAKTRVVDVLSKWEKLAAT-G 79
                          90
                  ....*....|....*..
gi 1058152126 294 AQERNAPWRLFFRKEIF 310
Cdd:cd17110    80 SSPGDDGWKLLFKLYLF 96
FERM_F0_F1 cd01765
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0 sub-domain and F1 sub-domain, found ...
217-307 2.56e-07

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: 47.97  E-value: 2.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1058152126 217 IMLPITFMDGNTKTLLADSATTARELCNQLSDKIGLKDQFGFSLYIALFDKVS-SLGSgGDHVMDAISqceqyakeqgaq 295
Cdd:cd01765     1 ISCRVRLLDGTELTLEVSKKATGQELFDKVCEKLNLLEKDYFGLFYEDNDGQKhWLDL-DKKISKQLK------------ 67
                          90
                  ....*....|..
gi 1058152126 296 eRNAPWRLFFRK 307
Cdd:cd01765    68 -RSGPYQFYFRV 78
FERM_F1_PLEKHH2 cd17179
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in pleckstrin ...
216-310 1.50e-05

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in pleckstrin homology domain-containing family H member 2 (PLEKHH2); PLEKHH2 is a novel podocyte protein downregulated in human focal segmental glomerulosclerosis. It is highly enriched in renal glomerular podocytes, and acts as a novel, important component of the podocyte foot processes. PLEKHH2 contains a putative alpha-helical coiled-coil segment within the N-terminal half, and two Pleckstrin homology (PH) domains, a MyTH4 domain, and a FERM (Band 4.1, ezrin, radixin, moesin) domain within the C-terminal half. The FERM domain is made up of three sub-domains, F1, F2, and F3. The family corresponds to F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N). PLEKHH2 is involved in matrix adhesion and actin dynamics. It directly interacts through its FERM domain with the focal adhesion protein Hic-5 and actin.


Pssm-ID: 340699  Cd Length: 103  Bit Score: 43.42  E-value: 1.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1058152126 216 PIMLPITFMDGNTKTLLADSATTARELCNQLSDKIGLKD--QFGFSLYIalfDKVSslGSGGDHVM-------DAISQCE 286
Cdd:cd17179     1 PFSIPVHFMNGTYQVVGFDASTTVEEFLNTLNQDTGMRKpgQSGFALFT---DDPS--GKDLEHCLqgnikicDIISKWE 75
                          90       100
                  ....*....|....*....|....*.
gi 1058152126 287 QYAKEQ--GAQERNAPWRLFFRKEIF 310
Cdd:cd17179    76 QASKEQhpGKCEGTRTVRLTYKNRLY 101
FERM_F1_PLEKHH1 cd17178
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in pleckstrin ...
216-310 2.93e-04

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in pleckstrin homology domain-containing family H member 1 (PLEKHH1); PLEKHH1 is a homolog of Caenorhabditis elegans MAX-1 that has been implicated in motor neuron axon guidance. PLEKHH1 is critical in vascular patterning in vertebrate species through acting upstream of the ephrin pathway. PLEKHH1 contains a putative alpha-helical coiled-coil segment within the N-terminal half, and two Pleckstrin homology (PH) domains, a MyTH4 domain, and a FERM (Band 4.1, ezrin, radixin, moesin) domain within the C-terminal half. The FERM domain is made up of three sub-domains, F1, F2, and F3. The family corresponds to F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340698  Cd Length: 106  Bit Score: 39.95  E-value: 2.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1058152126 216 PIMLPITFMDGNTKTLLADSATTARELCNQLSDKIGLK--DQFGFSLYIalfDKVSSLG-----SGGDHVMDAISQCEQY 288
Cdd:cd17178     1 PFSIPVHFMNGTYQVVGFDGSTTVDEFLQTLNQETGMRkpSHSGFALFT---DDPSGKDlehclQGSVKICDVISKWEQA 77
                          90       100
                  ....*....|....*....|....
gi 1058152126 289 AKE--QGAQERNAPWRLFFRKEIF 310
Cdd:cd17178    78 LKElhPGKYEGTRTVRLTYKSRLY 101
FERM_F1_Max1_like cd17094
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in Caenorhabditis ...
216-306 3.08e-04

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in Caenorhabditis elegans max-1 and its homologs PLEKHH1 and PLEKHH2; Caenorhabditis elegans max-1 is expressed and functions in motor neurons. MAX-1 protein plays a possible role in netrin-induced axon repulsion by modulating the UNC-5 receptor signaling pathway. PLEKHH1 is critically required in vascular patterning in vertebrate species through acting upstream of the ephrin pathway. PLEKHH2 is highly enriched in renal glomerular podocytes, and acts as a novel, important component of the podocyte foot processes. It is involved in matrix adhesion and actin dynamics. Members in this family all contain two Pleckstrin homology (PH) domains, a MyTH4 domain, and a FERM (Band 4.1, ezrin, radixin, moesin) domain within the C-terminal half. The FERM domain is made up of three sub-domains, F1, F2, and F3. The family corresponds to F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340614  Cd Length: 102  Bit Score: 39.92  E-value: 3.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1058152126 216 PIMLPITFMDGNTKTLLADSATTARELCNQLSDKIGLKD--QFGFSLYI--ALFDKVSSLGSGGDHVMDAISQCEQYAKE 291
Cdd:cd17094     1 PISIPVHLPNGTYQVVGFDGSTTVEEFLQTLNLELGIRPpsQSGFALFSddPIGKDIEHCLQPSVKICDVISKWERASRE 80
                          90
                  ....*....|....*..
gi 1058152126 292 --QGAQERNAPWRLFFR 306
Cdd:cd17094    81 ahSGKVDSSRVIRLTYK 97
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
318-401 3.04e-03

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


Pssm-ID: 459788 [Multi-domain]  Cd Length: 117  Bit Score: 37.25  E-value: 3.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1058152126 318 EDQVATNLIYQQVVRGVKFGEYRCDkEEDLAMIAAQQYFIEF------ATDLNMERLLNLLPNYipdycLTNAEKSiDRW 391
Cdd:pfam00373   7 QDEVTRHLLYLQAKDDILEGRLPCS-EEEALLLAALQLQAEFgdyqpsSHTSEYLSLESFLPKQ-----LLRKMKS-KEL 79
                          90
                  ....*....|
gi 1058152126 392 AALIVQAYKK 401
Cdd:pfam00373  80 EKRVLEAHKN 89
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH