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Conserved domains on  [gi|158563770|sp|Q3UFK8|]
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RecName: Full=FERM domain-containing protein 8; AltName: Full=iRhom tail-associated protein; Short=iTAP

Protein Classification

FERM_B-lobe and PH-like domain-containing protein( domain architecture ID 10448719)

FERM_B-lobe and PH-like domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
 136-273 1.49e-15

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


:

Pssm-ID: 459788 [Multi-domain]  Cd Length: 117  Bit Score: 72.69  E-value: 1.49e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158563770  136 ELQIHDEEVLRLLYEEAKGNVLTARYPCDLEDCEVLGGLVCRVQLGPYQPGQPAacTLREKLDSFLPAHLCKRGhglfaa 215
Cdd:pfam00373   3 ELLLQDEVTRHLLYLQAKDDILEGRLPCSEEEALLLAALQLQAEFGDYQPSSHT--SEYLSLESFLPKQLLRKM------ 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 158563770  216 frgrgaKTGPGEQGLLNAYRQVKEVTGNNSEREatlgshyraYLLKCHELPFYGCAFF 273
Cdd:pfam00373  75 ------KSKELEKRVLEAHKNLRGLSAEEAKLK---------YLQIAQSLPTYGVEFF 117
 
Name Accession Description Interval E-value
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
 136-273 1.49e-15

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


Pssm-ID: 459788 [Multi-domain]  Cd Length: 117  Bit Score: 72.69  E-value: 1.49e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158563770  136 ELQIHDEEVLRLLYEEAKGNVLTARYPCDLEDCEVLGGLVCRVQLGPYQPGQPAacTLREKLDSFLPAHLCKRGhglfaa 215
Cdd:pfam00373   3 ELLLQDEVTRHLLYLQAKDDILEGRLPCSEEEALLLAALQLQAEFGDYQPSSHT--SEYLSLESFLPKQLLRKM------ 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 158563770  216 frgrgaKTGPGEQGLLNAYRQVKEVTGNNSEREatlgshyraYLLKCHELPFYGCAFF 273
Cdd:pfam00373  75 ------KSKELEKRVLEAHKNLRGLSAEEAKLK---------YLQIAQSLPTYGVEFF 117
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 32-273 2.77e-13

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: 68.48  E-value: 2.77e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158563770    32 VLVYLADDTVVPLAVEnlSSISAHELHRAVREVLQLPDVALeaFALWLVSPLLEVQLKPKHqPYKLGRQWPELLlrftna 111
Cdd:smart00295   2 LKVYLLDGTTLEFEVD--SSTTAEELLETVCRKLGIRESEY--FGLQFEDPDEDLRHWLDP-AKTLLDQDVKSE------ 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158563770   112 sdddvamdEPSLQFRRNvFFPRRRELQIHDEEVLRLLYEEAKGNVLTARYPCDLEDCEVLGGLVCRVQLGPYQPgQPAAC 191
Cdd:smart00295  71 --------PLTLYFRVK-FYPPDPNQLKEDPTRLNLLYLQVRNDILEGRLPCPEEEALLLAALALQAEFGDYDE-ELHDL 140

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158563770   192 TLREKLDSFLPAHLCKRGHGLFAafrgrgaktgpgEQGLLNAYRQVKEVTGNNSEREatlgshyraYLLKCHELPFYGCA 271
Cdd:smart00295 141 RGELSLKRFLPKQLLDSRKLKEW------------RERIVELHKELIGLSPEEAKLK---------YLELARKLPTYGVE 199


                   ..
gi 158563770   272 FF 273
Cdd:smart00295 200 LF 201
FERM_B-lobe cd14473
FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C ...
 147-207 1.20e-05

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: 43.77  E-value: 1.20e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158563770 147 LLYEEAKGNVLTARYPCDLEDCEVLGGLVCRVQLGPYQPGQPAACTLreKLDSFLPAHLCK 207
Cdd:cd14473    4 LLYLQVKRDILEGRLPCSEETAALLAALALQAEYGDYDPSEHKPKYL--SLKRFLPKQLLK 62
 
Name Accession Description Interval E-value
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
 136-273 1.49e-15

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


Pssm-ID: 459788 [Multi-domain]  Cd Length: 117  Bit Score: 72.69  E-value: 1.49e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158563770  136 ELQIHDEEVLRLLYEEAKGNVLTARYPCDLEDCEVLGGLVCRVQLGPYQPGQPAacTLREKLDSFLPAHLCKRGhglfaa 215
Cdd:pfam00373   3 ELLLQDEVTRHLLYLQAKDDILEGRLPCSEEEALLLAALQLQAEFGDYQPSSHT--SEYLSLESFLPKQLLRKM------ 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 158563770  216 frgrgaKTGPGEQGLLNAYRQVKEVTGNNSEREatlgshyraYLLKCHELPFYGCAFF 273
Cdd:pfam00373  75 ------KSKELEKRVLEAHKNLRGLSAEEAKLK---------YLQIAQSLPTYGVEFF 117
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 32-273 2.77e-13

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: 68.48  E-value: 2.77e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158563770    32 VLVYLADDTVVPLAVEnlSSISAHELHRAVREVLQLPDVALeaFALWLVSPLLEVQLKPKHqPYKLGRQWPELLlrftna 111
Cdd:smart00295   2 LKVYLLDGTTLEFEVD--SSTTAEELLETVCRKLGIRESEY--FGLQFEDPDEDLRHWLDP-AKTLLDQDVKSE------ 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158563770   112 sdddvamdEPSLQFRRNvFFPRRRELQIHDEEVLRLLYEEAKGNVLTARYPCDLEDCEVLGGLVCRVQLGPYQPgQPAAC 191
Cdd:smart00295  71 --------PLTLYFRVK-FYPPDPNQLKEDPTRLNLLYLQVRNDILEGRLPCPEEEALLLAALALQAEFGDYDE-ELHDL 140

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158563770   192 TLREKLDSFLPAHLCKRGHGLFAafrgrgaktgpgEQGLLNAYRQVKEVTGNNSEREatlgshyraYLLKCHELPFYGCA 271
Cdd:smart00295 141 RGELSLKRFLPKQLLDSRKLKEW------------RERIVELHKELIGLSPEEAKLK---------YLELARKLPTYGVE 199


                   ..
gi 158563770   272 FF 273
Cdd:smart00295 200 LF 201
FERM_B-lobe cd14473
FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C ...
 147-207 1.20e-05

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: 43.77  E-value: 1.20e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158563770 147 LLYEEAKGNVLTARYPCDLEDCEVLGGLVCRVQLGPYQPGQPAACTLreKLDSFLPAHLCK 207
Cdd:cd14473    4 LLYLQVKRDILEGRLPCSEETAALLAALALQAEYGDYDPSEHKPKYL--SLKRFLPKQLLK 62
 
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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