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Conserved domains on  [gi|269849595|sp|Q9BZ68|]
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PUTATIVE PSEUDOGENE: RecName: Full=Putative FERM domain-containing protein FRMD8P1; AltName: Full=FERM domain-containing 8 pseudogene 1

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.
 136-272 3.43e-14

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


:

Pssm-ID: 459788 [Multi-domain]  Cd Length: 117  Bit Score: 68.45  E-value: 3.43e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269849595  136 ELQIPDEEVLRLLYEEAKGNVLAARYLCDVEDCEALGALVCRVQLVTYQPdwPAACDLREKLDSFLPAHLCKRgqglfaa 215
Cdd:pfam00373   3 ELLLQDEVTRHLLYLQAKDDILEGRLPCSEEEALLLAALQLQAEFGDYQP--SSHTSEYLSLESFLPKQLLRK------- 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 269849595  216 lrgRGARAgpGEQSLLNAYRKVQEVSSDggcEAalgthYRAYLLKCHKLPFYGCAFF 272
Cdd:pfam00373  74 ---MKSKE--LEKRVLEAHKNLRGLSAE---EA-----KLKYLQIAQSLPTYGVEFF 117
 
Name Accession Description Interval E-value
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
 136-272 3.43e-14

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


Pssm-ID: 459788 [Multi-domain]  Cd Length: 117  Bit Score: 68.45  E-value: 3.43e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269849595  136 ELQIPDEEVLRLLYEEAKGNVLAARYLCDVEDCEALGALVCRVQLVTYQPdwPAACDLREKLDSFLPAHLCKRgqglfaa 215
Cdd:pfam00373   3 ELLLQDEVTRHLLYLQAKDDILEGRLPCSEEEALLLAALQLQAEFGDYQP--SSHTSEYLSLESFLPKQLLRK------- 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 269849595  216 lrgRGARAgpGEQSLLNAYRKVQEVSSDggcEAalgthYRAYLLKCHKLPFYGCAFF 272
Cdd:pfam00373  74 ---MKSKE--LEKRVLEAHKNLRGLSAE---EA-----KLKYLQIAQSLPTYGVEFF 117
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 32-272 1.46e-08

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: 54.22  E-value: 1.46e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269849595    32 VLVYLADDTVVPLAVEnlPSLRAHELHCAVREVLKLPDIALdvFALWLVSPLLEVQLKPKNqPYKLGRQWPELllrftsa 111
Cdd:smart00295   2 LKVYLLDGTTLEFEVD--SSTTAEELLETVCRKLGIRESEY--FGLQFEDPDEDLRHWLDP-AKTLLDQDVKS------- 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269849595   112 pdddvamdEPF-LQFRRNvFFPKGRELQIPDEEVLRLLYEEAKGNVLAARYLCDVEDCEALGALVCRVQLVTYQPDwPAA 190
Cdd:smart00295  70 --------EPLtLYFRVK-FYPPDPNQLKEDPTRLNLLYLQVRNDILEGRLPCPEEEALLLAALALQAEFGDYDEE-LHD 139

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269849595   191 CDLREKLDSFLPAHLCKRGQGLFAalrgrgaragpgEQSLLNAYRKVQEVSSDggcEAALgthyrAYLLKCHKLPFYGCA 270
Cdd:smart00295 140 LRGELSLKRFLPKQLLDSRKLKEW------------RERIVELHKELIGLSPE---EAKL-----KYLELARKLPTYGVE 199


                   ..
gi 269849595   271 FF 272
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 4.84e-03

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: 36.07  E-value: 4.84e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 269849595 147 LLYEEAKGNVLAARYLCDVEDCEALGALVCRVQLVTYQPDwpAACDLREKLDSFLPAHLCK 207
Cdd:cd14473    4 LLYLQVKRDILEGRLPCSEETAALLAALALQAEYGDYDPS--EHKPKYLSLKRFLPKQLLK 62
 
Name Accession Description Interval E-value
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
 136-272 3.43e-14

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


Pssm-ID: 459788 [Multi-domain]  Cd Length: 117  Bit Score: 68.45  E-value: 3.43e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269849595  136 ELQIPDEEVLRLLYEEAKGNVLAARYLCDVEDCEALGALVCRVQLVTYQPdwPAACDLREKLDSFLPAHLCKRgqglfaa 215
Cdd:pfam00373   3 ELLLQDEVTRHLLYLQAKDDILEGRLPCSEEEALLLAALQLQAEFGDYQP--SSHTSEYLSLESFLPKQLLRK------- 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 269849595  216 lrgRGARAgpGEQSLLNAYRKVQEVSSDggcEAalgthYRAYLLKCHKLPFYGCAFF 272
Cdd:pfam00373  74 ---MKSKE--LEKRVLEAHKNLRGLSAE---EA-----KLKYLQIAQSLPTYGVEFF 117
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 32-272 1.46e-08

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: 54.22  E-value: 1.46e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269849595    32 VLVYLADDTVVPLAVEnlPSLRAHELHCAVREVLKLPDIALdvFALWLVSPLLEVQLKPKNqPYKLGRQWPELllrftsa 111
Cdd:smart00295   2 LKVYLLDGTTLEFEVD--SSTTAEELLETVCRKLGIRESEY--FGLQFEDPDEDLRHWLDP-AKTLLDQDVKS------- 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269849595   112 pdddvamdEPF-LQFRRNvFFPKGRELQIPDEEVLRLLYEEAKGNVLAARYLCDVEDCEALGALVCRVQLVTYQPDwPAA 190
Cdd:smart00295  70 --------EPLtLYFRVK-FYPPDPNQLKEDPTRLNLLYLQVRNDILEGRLPCPEEEALLLAALALQAEFGDYDEE-LHD 139

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269849595   191 CDLREKLDSFLPAHLCKRGQGLFAalrgrgaragpgEQSLLNAYRKVQEVSSDggcEAALgthyrAYLLKCHKLPFYGCA 270
Cdd:smart00295 140 LRGELSLKRFLPKQLLDSRKLKEW------------RERIVELHKELIGLSPE---EAKL-----KYLELARKLPTYGVE 199


                   ..
gi 269849595   271 FF 272
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 4.84e-03

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: 36.07  E-value: 4.84e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 269849595 147 LLYEEAKGNVLAARYLCDVEDCEALGALVCRVQLVTYQPDwpAACDLREKLDSFLPAHLCK 207
Cdd:cd14473    4 LLYLQVKRDILEGRLPCSEETAALLAALALQAEYGDYDPS--EHKPKYLSLKRFLPKQLLK 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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