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Conserved domains on  [gi|808356672|ref|NP_001293864|]
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FERM domain-containing protein [Caenorhabditis elegans]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PH-like super family cl17171
Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like ...
52-197 6.62e-47

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


The actual alignment was detected with superfamily member cd13191:

Pssm-ID: 473070  Cd Length: 113  Bit Score: 162.13  E-value: 6.62e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356672  52 GYRMYEALNENNDKCILSIGYKGIYIYRrsrHQNLITPYLAYPWRVIDNLYYRDKKFSIEIREPKKNESsenvsddvili 131
Cdd:cd13191    1 GVHYYEVKDKNGIPWWLGVSYKGIGQYD---LQDKVKPRKFFQWKQLENLYFRDRKFSIEVRDPRRNSH----------- 66
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 808356672 132 ndrqlseafshpttqvscgRRRSNNQQPRVLLFPFTCQTPLVCRTVWMSAIAQHRFFLERKELKKK 197
Cdd:cd13191   67 -------------------RSRRTFQSSSVSVHVWYGQTPALCKTIWSMAIAQHQFYLDRKQSKKK 113
CUPID super family cl13287
Cytohesin Ubiquitin Protein Inducing Domain; C1ORF106 also known as INAVA (Innate Immune ...
248-403 8.67e-21

Cytohesin Ubiquitin Protein Inducing Domain; C1ORF106 also known as INAVA (Innate Immune Activator), is identified as a risk factor for the chronic inflammatory bowel diseases (IBD). Mice lacking the protein show defects in intestinal barrier integrity at steady state and greater susceptibility to mucosal infection. INAVA carries CUPID (Cytohesin Ubiquitin Protein Inducing Domain). Three other human proteins contain CUPID: FRMD4A, FRMD4B, and CCDC120- proteins implicated in neurite outgrowth, and in human cancer, Alzheimer's, celiac, and heart disease. All appear to bind the ARF-GEF (guanine nucleotide-exchange factors) cytohesin family members, such as proteins (ARF 1-4), which regulate cell membrane and F-actin dynamics. INAVA-CUPID binds cytohesin 2 (also known as ARNO), targets the molecule to lateral membranes of epithelial monolayers, and enables ARNO to affect F-actin assembly that underlies cell-cell junctions and barrier function. In the case of inflammatory signalling, ARNO can coordinate CUPID function by binding and inhibiting CUPID activity of acting as an enhancer of TRAF6 dependent polyubiquitination. In other words, ARNO acts as a negative-regulator of inflammatory responses. In summary, INAVA-CUPID exhibits dual functions, coordinated directly by ARNO, that bridge epithelial barrier function with extracellular signals and inflammation.


The actual alignment was detected with superfamily member pfam11819:

Pssm-ID: 463360  Cd Length: 136  Bit Score: 88.91  E-value: 8.67e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356672  248 KIGDGSTSSLPMSSakpmstqtsePQLPDVPEPNESlhnktidefqkdqEKCDRLKARKAELEMRLRQKMQELKDVCVEE 327
Cdd:pfam11819   5 EIISSSSGSLLSSG----------SDSSTSSEKQKK-------------EKTAALKKKQQALQERLELKLEELKKLCLRE 61
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 808356672  328 GDITGEMPVEINdvVLPGDDFPRLKRRVGTAYSIPDELIKADKAD-KMSQLETDVELHRRIVAAASRLATDKNTNKS 403
Cdd:pfam11819  62 AELTGKLPKEYP--LEPGEKPPQVRRRVGTAFKLDEQHVLQYAEDpELESLEREFALQQQIVEAARRLALEPNLSKT 136
FERM_M super family cl47539
FERM central domain; This domain is the central structural domain of the FERM domain.
6-56 1.50e-07

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


The actual alignment was detected with superfamily member pfam00373:

Pssm-ID: 459788 [Multi-domain]  Cd Length: 117  Bit Score: 50.35  E-value: 1.50e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 808356672    6 PPYILLKTDQSEVERRVFEKFRYYRRLPVGTGMISFIKLAEKSESYGYRMY 56
Cdd:pfam00373  67 PKQLLRKMKSKELEKRVLEAHKNLRGLSAEEAKLKYLQIAQSLPTYGVEFF 117
 
Name Accession Description Interval E-value
FERM_C_FRMD4A_FRMD4B cd13191
FERM domain C-lobe of FERM domain-containing protein 4A and 4B (FRMD4A and 4B); FRMD4A is part ...
52-197 6.62e-47

FERM domain C-lobe of FERM domain-containing protein 4A and 4B (FRMD4A and 4B); FRMD4A is part of the Par-3/FRMD4A/cytohesin-1 complex that activates Arf6, a central player in actin cytoskeleton dynamics and membrane trafficking, during junctional remodeling and epithelial polarization. The Par-3/Par-6/aPKC/Cdc42 complex regulates the conversion of primordial adherens junctions (AJs) into belt-like AJs and the formation of linear actin cables. When primordial AJs are formed, Par-3 recruits scaffolding protein FRMD4A which connects Par-3 and the Arf6 guanine-nucleotide exchange factor (GEF), cytohesin-1. FRMD4B (also called GRP1-binding protein, GRSP1) is a novel member of GRP1 signaling complexes that are recruited to plasma membrane ruffles in response to insulin receptor signaling. The GRSP1/FRMD4B protein contains a FERM protein domain as well as two coiled coil domains and may function as a scaffolding protein. GRP1 and GRSP1 interact through the coiled coil domains in the two proteins. 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: 270012  Cd Length: 113  Bit Score: 162.13  E-value: 6.62e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356672  52 GYRMYEALNENNDKCILSIGYKGIYIYRrsrHQNLITPYLAYPWRVIDNLYYRDKKFSIEIREPKKNESsenvsddvili 131
Cdd:cd13191    1 GVHYYEVKDKNGIPWWLGVSYKGIGQYD---LQDKVKPRKFFQWKQLENLYFRDRKFSIEVRDPRRNSH----------- 66
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 808356672 132 ndrqlseafshpttqvscgRRRSNNQQPRVLLFPFTCQTPLVCRTVWMSAIAQHRFFLERKELKKK 197
Cdd:cd13191   67 -------------------RSRRTFQSSSVSVHVWYGQTPALCKTIWSMAIAQHQFYLDRKQSKKK 113
CUPID pfam11819
Cytohesin Ubiquitin Protein Inducing Domain; C1ORF106 also known as INAVA (Innate Immune ...
248-403 8.67e-21

Cytohesin Ubiquitin Protein Inducing Domain; C1ORF106 also known as INAVA (Innate Immune Activator), is identified as a risk factor for the chronic inflammatory bowel diseases (IBD). Mice lacking the protein show defects in intestinal barrier integrity at steady state and greater susceptibility to mucosal infection. INAVA carries CUPID (Cytohesin Ubiquitin Protein Inducing Domain). Three other human proteins contain CUPID: FRMD4A, FRMD4B, and CCDC120- proteins implicated in neurite outgrowth, and in human cancer, Alzheimer's, celiac, and heart disease. All appear to bind the ARF-GEF (guanine nucleotide-exchange factors) cytohesin family members, such as proteins (ARF 1-4), which regulate cell membrane and F-actin dynamics. INAVA-CUPID binds cytohesin 2 (also known as ARNO), targets the molecule to lateral membranes of epithelial monolayers, and enables ARNO to affect F-actin assembly that underlies cell-cell junctions and barrier function. In the case of inflammatory signalling, ARNO can coordinate CUPID function by binding and inhibiting CUPID activity of acting as an enhancer of TRAF6 dependent polyubiquitination. In other words, ARNO acts as a negative-regulator of inflammatory responses. In summary, INAVA-CUPID exhibits dual functions, coordinated directly by ARNO, that bridge epithelial barrier function with extracellular signals and inflammation.


Pssm-ID: 463360  Cd Length: 136  Bit Score: 88.91  E-value: 8.67e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356672  248 KIGDGSTSSLPMSSakpmstqtsePQLPDVPEPNESlhnktidefqkdqEKCDRLKARKAELEMRLRQKMQELKDVCVEE 327
Cdd:pfam11819   5 EIISSSSGSLLSSG----------SDSSTSSEKQKK-------------EKTAALKKKQQALQERLELKLEELKKLCLRE 61
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 808356672  328 GDITGEMPVEINdvVLPGDDFPRLKRRVGTAYSIPDELIKADKAD-KMSQLETDVELHRRIVAAASRLATDKNTNKS 403
Cdd:pfam11819  62 AELTGKLPKEYP--LEPGEKPPQVRRRVGTAFKLDEQHVLQYAEDpELESLEREFALQQQIVEAARRLALEPNLSKT 136
FERM_C pfam09380
FERM C-terminal PH-like domain;
60-192 4.99e-17

FERM C-terminal PH-like domain;


Pssm-ID: 462779 [Multi-domain]  Cd Length: 85  Bit Score: 76.52  E-value: 4.99e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356672   60 NENNDKCILSIGYKGIYIYRrsrHQNLItpYLAYPWRVIDNLYYRDKKFSIEIRepkknessenvsddvilindrqlsea 139
Cdd:pfam09380   1 DKEGTDLWLGVSAKGILVYE---DNNKI--LNLFPWREIRKISFKRKKFLIKLR-------------------------- 49
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 808356672  140 fshpttqvscgrrrsnnQQPRVLLFPFTCQTPLVCRTVWMSAIAQHRFFLERK 192
Cdd:pfam09380  50 -----------------DKSSEETLGFYTESSRACKYLWKLCVEQHTFFRLRR 85
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
6-56 1.50e-07

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


Pssm-ID: 459788 [Multi-domain]  Cd Length: 117  Bit Score: 50.35  E-value: 1.50e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 808356672    6 PPYILLKTDQSEVERRVFEKFRYYRRLPVGTGMISFIKLAEKSESYGYRMY 56
Cdd:pfam00373  67 PKQLLRKMKSKELEKRVLEAHKNLRGLSAEEAKLKYLQIAQSLPTYGVEFF 117
 
Name Accession Description Interval E-value
FERM_C_FRMD4A_FRMD4B cd13191
FERM domain C-lobe of FERM domain-containing protein 4A and 4B (FRMD4A and 4B); FRMD4A is part ...
52-197 6.62e-47

FERM domain C-lobe of FERM domain-containing protein 4A and 4B (FRMD4A and 4B); FRMD4A is part of the Par-3/FRMD4A/cytohesin-1 complex that activates Arf6, a central player in actin cytoskeleton dynamics and membrane trafficking, during junctional remodeling and epithelial polarization. The Par-3/Par-6/aPKC/Cdc42 complex regulates the conversion of primordial adherens junctions (AJs) into belt-like AJs and the formation of linear actin cables. When primordial AJs are formed, Par-3 recruits scaffolding protein FRMD4A which connects Par-3 and the Arf6 guanine-nucleotide exchange factor (GEF), cytohesin-1. FRMD4B (also called GRP1-binding protein, GRSP1) is a novel member of GRP1 signaling complexes that are recruited to plasma membrane ruffles in response to insulin receptor signaling. The GRSP1/FRMD4B protein contains a FERM protein domain as well as two coiled coil domains and may function as a scaffolding protein. GRP1 and GRSP1 interact through the coiled coil domains in the two proteins. 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: 270012  Cd Length: 113  Bit Score: 162.13  E-value: 6.62e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356672  52 GYRMYEALNENNDKCILSIGYKGIYIYRrsrHQNLITPYLAYPWRVIDNLYYRDKKFSIEIREPKKNESsenvsddvili 131
Cdd:cd13191    1 GVHYYEVKDKNGIPWWLGVSYKGIGQYD---LQDKVKPRKFFQWKQLENLYFRDRKFSIEVRDPRRNSH----------- 66
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 808356672 132 ndrqlseafshpttqvscgRRRSNNQQPRVLLFPFTCQTPLVCRTVWMSAIAQHRFFLERKELKKK 197
Cdd:cd13191   67 -------------------RSRRTFQSSSVSVHVWYGQTPALCKTIWSMAIAQHQFYLDRKQSKKK 113
CUPID pfam11819
Cytohesin Ubiquitin Protein Inducing Domain; C1ORF106 also known as INAVA (Innate Immune ...
248-403 8.67e-21

Cytohesin Ubiquitin Protein Inducing Domain; C1ORF106 also known as INAVA (Innate Immune Activator), is identified as a risk factor for the chronic inflammatory bowel diseases (IBD). Mice lacking the protein show defects in intestinal barrier integrity at steady state and greater susceptibility to mucosal infection. INAVA carries CUPID (Cytohesin Ubiquitin Protein Inducing Domain). Three other human proteins contain CUPID: FRMD4A, FRMD4B, and CCDC120- proteins implicated in neurite outgrowth, and in human cancer, Alzheimer's, celiac, and heart disease. All appear to bind the ARF-GEF (guanine nucleotide-exchange factors) cytohesin family members, such as proteins (ARF 1-4), which regulate cell membrane and F-actin dynamics. INAVA-CUPID binds cytohesin 2 (also known as ARNO), targets the molecule to lateral membranes of epithelial monolayers, and enables ARNO to affect F-actin assembly that underlies cell-cell junctions and barrier function. In the case of inflammatory signalling, ARNO can coordinate CUPID function by binding and inhibiting CUPID activity of acting as an enhancer of TRAF6 dependent polyubiquitination. In other words, ARNO acts as a negative-regulator of inflammatory responses. In summary, INAVA-CUPID exhibits dual functions, coordinated directly by ARNO, that bridge epithelial barrier function with extracellular signals and inflammation.


Pssm-ID: 463360  Cd Length: 136  Bit Score: 88.91  E-value: 8.67e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356672  248 KIGDGSTSSLPMSSakpmstqtsePQLPDVPEPNESlhnktidefqkdqEKCDRLKARKAELEMRLRQKMQELKDVCVEE 327
Cdd:pfam11819   5 EIISSSSGSLLSSG----------SDSSTSSEKQKK-------------EKTAALKKKQQALQERLELKLEELKKLCLRE 61
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 808356672  328 GDITGEMPVEINdvVLPGDDFPRLKRRVGTAYSIPDELIKADKAD-KMSQLETDVELHRRIVAAASRLATDKNTNKS 403
Cdd:pfam11819  62 AELTGKLPKEYP--LEPGEKPPQVRRRVGTAFKLDEQHVLQYAEDpELESLEREFALQQQIVEAARRLALEPNLSKT 136
FERM_C pfam09380
FERM C-terminal PH-like domain;
60-192 4.99e-17

FERM C-terminal PH-like domain;


Pssm-ID: 462779 [Multi-domain]  Cd Length: 85  Bit Score: 76.52  E-value: 4.99e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356672   60 NENNDKCILSIGYKGIYIYRrsrHQNLItpYLAYPWRVIDNLYYRDKKFSIEIRepkknessenvsddvilindrqlsea 139
Cdd:pfam09380   1 DKEGTDLWLGVSAKGILVYE---DNNKI--LNLFPWREIRKISFKRKKFLIKLR-------------------------- 49
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 808356672  140 fshpttqvscgrrrsnnQQPRVLLFPFTCQTPLVCRTVWMSAIAQHRFFLERK 192
Cdd:pfam09380  50 -----------------DKSSEETLGFYTESSRACKYLWKLCVEQHTFFRLRR 85
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
6-56 1.50e-07

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


Pssm-ID: 459788 [Multi-domain]  Cd Length: 117  Bit Score: 50.35  E-value: 1.50e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 808356672    6 PPYILLKTDQSEVERRVFEKFRYYRRLPVGTGMISFIKLAEKSESYGYRMY 56
Cdd:pfam00373  67 PKQLLRKMKSKELEKRVLEAHKNLRGLSAEEAKLKYLQIAQSLPTYGVEFF 117
FERM_C_ERM cd13194
FERM domain C-lobe/F3 of the ERM family; The ERM family includes ezrin, radixin, moesin and ...
51-110 4.18e-06

FERM domain C-lobe/F3 of the ERM family; The ERM family includes ezrin, radixin, moesin and merlin. They are composed of a N-terminal FERM (ERM) domain (also called N-ERMAD (N-terminal ERM association domain)), a coiled coil region (CRR), and a C-terminal domain CERMAD (C-terminal ERM association domain) which has an F-actin-binding site (ABD). Two actin-binding sites have been identified in the middle and N-terminal domains. Merlin is structurally similar to the ERM proteins, but instead of an actin-binding domain (ABD), it contains a C-terminal domain (CTD), just like the proteins from the 4.1 family. Activated ezrin, radixin and moesin are thought to be involved in the linking of actin filaments to CD43, CD44, ICAM1-3 cell adhesion molecules, various membrane channels and receptors, such as the Na+/H+ exchanger-3 (NHE3), cystic fibrosis transmembrane conductance regulator (CFTR), and the beta2-adrenergic receptor. The ERM proteins exist in two states, a dormant state in which the FERM domain binds to its own C-terminal tail and thereby precludes binding of some partner proteins, and an activated state, in which the FERM domain binds to one of many membrane binding proteins and the C-terminal tail binds to F-actin. 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 of ERM 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: 270015  Cd Length: 97  Bit Score: 45.73  E-value: 4.18e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356672  51 YGYRMYEALNENNDKCILSIGYKGIYIYRrsrHQNLITPYLAYPWRVIDNLYYRDKKFSI 110
Cdd:cd13194    2 YGVNYFEIKNKKGTDLWLGVDALGLNIYE---PDNKLTPKIGFPWSEIRNISFNDKKFVI 58
FERM_C_4_1_family cd13184
FERM domain C-lobe of Protein 4.1 family; The protein 4.1 family includes four well-defined ...
51-122 2.05e-04

FERM domain C-lobe of Protein 4.1 family; The protein 4.1 family includes four well-defined members: erythroid protein 4.1 (4.1R), the best known and characterized member, 4.1G (general), 4.1N (neuronal), and 4.1 B (brain). The less well understood 4.1O/FRMD3 is not a true member of this family and is not included in this hierarchy. Besides three highly conserved domains, FERM, SAB (spectrin and actin binding domain) and CTD (C-terminal domain), the proteins from this family contain several unique domains: U1, U2 and U3. FERM domains like other members of the FERM domain superfamily have a cloverleaf architecture with three distinct lobes: (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 brain is a particularly rich source of protein 4.1 isoforms. The various 4.1R, 4.1G, 4.1N, and 4.1B mRNAs are all expressed in distinct patterns within the brain. It is likely that 4.1 proteins play important functional roles in the brain including motor coordination and spatial learning, postmitotic differentiation, and synaptic architecture and function. In addition they are found in nonerythroid, nonneuronal cells where they may play a general structural role in nuclear architecture and/or may interact with splicing factors. The FERM C domain is the third structural domain within the FERM domain. 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: 270005  Cd Length: 94  Bit Score: 40.77  E-value: 2.05e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 808356672  51 YGYRMYEALNENNDKCILSIGYKGIYIYRRSRHQNlitpylAYPWRVIDNLYYRDKKFSIEIRePKKNESSE 122
Cdd:cd13184    1 YGVDLHPAKDSEGVDIMLGVCSSGLLVYRDRLRIN------RFAWPKVLKISYKRNNFYIKIR-PGEFEQYE 65
FERM_C-lobe cd00836
FERM domain C-lobe; The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N ...
52-120 1.18e-03

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: 38.51  E-value: 1.18e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 808356672  52 GYRMYEALNENNDKC--ILSIGYKGIYIYRRSRHQNLITpylaYPWRVIDNLYY-RDKKFSIEIREPKKNES 120
Cdd:cd00836    1 GVEFFPVKDKSKKGSpiILGVNPEGISVYDELTGQPLVL----FPWPNIKKISFsGAKKFTIVVADEDKQSK 68
FERM_C_PTPN4_PTPN3_like cd13189
FERM domain C-lobe of Protein tyrosine phosphatase non-receptor proteins 3 and 4 (PTPN4 and ...
51-188 1.23e-03

FERM domain C-lobe of Protein tyrosine phosphatase non-receptor proteins 3 and 4 (PTPN4 and PTPN3); PTPN4 (also called PTPMEG, protein tyrosine phosphatase, megakaryocyte) is a cytoplasmic protein-tyrosine phosphatase (PTP) thought to play a role in cerebellar function. PTPMEG-knockout mice have impaired memory formation and cerebellar long-term depression. PTPN3/PTPH1 is a membrane-associated PTP that is implicated in regulating tyrosine phosphorylation of growth factor receptors, p97 VCP (valosin-containing protein, or Cdc48 in Saccharomyces cerevisiae), and HBV (Hepatitis B Virus) gene expression; it is mutated in a subset of colon cancers. PTPMEG and PTPN3/PTPH1 contains a N-terminal FERM domain, a middle PDZ domain, and a C-terminal phosphatase domain. PTP1/Tyrosine-protein phosphatase 1 from nematodes and a FERM_C repeat 1 from Tetraodon nigroviridis are also included in this cd. 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 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: 270010  Cd Length: 95  Bit Score: 38.83  E-value: 1.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356672  51 YGYRMYEALNENNDKCILSIGYKGIYIYRRSRHQNLitpylaYPWRVIDNLYYRDKKFSIEIRePKKNESSENvsddvIL 130
Cdd:cd13189    2 YGVELHSARDSNNLELQIGVSSAGILVFQNGIRINT------FPWSKIVKISFKRKQFFIQLR-REPNESRDT-----IL 69
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 808356672 131 IndrqlseafshpttqvscgrrrsnnqqprvllfpFTCQTPLVCRTVWMSAIAQHRFF 188
Cdd:cd13189   70 G----------------------------------FNMLSYRACKNLWKSCVEHHTFF 93
FERM_C_FRMD1_FRMD6 cd13185
FERM domain C-lobe of FERM domain containing 1 and 6 proteins; FRMD6 (also called willin and ...
53-110 5.06e-03

FERM domain C-lobe of FERM domain containing 1 and 6 proteins; FRMD6 (also called willin and hEx/human expanded) is localized throughout the cytoplasm or along the plasma membrane. The Drosophilla protein Ex is a regulator of the Hippo/SWH (Sav/Wts/Hpo) signaling pathway, a signaling pathway that plays a pivotal role in organ size control and is tumor suppression by restricting proliferation and promoting apoptosis. Surprisingly, hEx is thought to function independently of the Hippo pathway. Instead it is hypothesized that hEx inhibits progression through the S phase of the cell cycle by upregulating p21(Cip1) and downregulating Cyclin A. It is also implicated in the progression of Alzheimer disease. Not much is known about FRMD1 to date. Both FRMD1 and FRMD6 contains a single FERM domain which 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 is a member of the PH superfamily. 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: 270006  Cd Length: 107  Bit Score: 37.29  E-value: 5.06e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 808356672  53 YRMYEALNENNDKCILSIGYKGIYIYRRSRHQNlITPYLaYPWRVIDNLYYRDKKFSI 110
Cdd:cd13185    8 YRLRKSKKETPGSVLLGITAKGIQIYQESDGEQ-QLLRT-FPWSNIGKLSFDRKKFEI 63
FERM_C_PTPH13 cd13187
FERM domain C-lobe of Protein tyrosine phosphatase non-receptor 13 (PTPH13); There are many ...
68-120 8.59e-03

FERM domain C-lobe of Protein tyrosine phosphatase non-receptor 13 (PTPH13); There are many functions of PTPN13 (also called PTPL1, PTP-BAS, hPTP1E, FAP1, or PTPL1). Mice lacking PTPN13 activity have abnormal regulation of signal transducer and activator of transcription signaling in their T cells, mild impairment of motor nerve repair, and a significant reduction in the growth of retinal glia cultures. It also plays a role in adipocyte differentiation. PTPN13 contains a kinase non-catalytic C-lobe domain (KIND), a FERM domain with two potential phosphatidylinositol 4,5-biphosphate [PtdIns(4,5)P2]-binding motifs, 5 PDZ domains, and a carboxy-terminal catalytic domain. There is an nteraction between the FERM domain of PTPL1 and PtdIns(4,5)P2 which is thought to regulate the membrane localization of PTPN13. PDZ are protein/protein interaction domains so there is the potential for numerous partners that can actively participate in the regulation of its phosphatase activity or can permit direct or indirect recruitment of tyrosine phosphorylated PTPL1 substrates. 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: 270008  Cd Length: 103  Bit Score: 36.53  E-value: 8.59e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 808356672  68 LSIGYKGIYIYRRSRHQNliTPYLAYPWRVIDNLYYRDKKFSIEIREPKKNES 120
Cdd:cd13187   20 LGICSRGIIIYEEKNGAR--TPVLRFPWRETQKISFDKKKFTIESRGGSGIKH 70
 
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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