NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|170932512|ref|NP_001116313|]
View 

FERM domain-containing protein 1 isoform 2 [Homo sapiens]

Protein Classification

FERM_B-lobe and PH-like domain-containing protein( domain architecture ID 13218810)

FERM_B-lobe and PH-like domain-containing protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Ubl1_cv_Nsp3_N-like super family cl28922
first ubiquitin-like (Ubl) domain located at the N-terminus of coronavirus SARS-CoV ...
 4-82 7.84e-49

first ubiquitin-like (Ubl) domain located at the N-terminus of coronavirus SARS-CoV non-structural protein 3 (Nsp3) and related proteins; This ubiquitin-like (Ubl) domain (Ubl1) is found at the N-terminus of coronavirus Nsp3, a large multi-functional multi-domain protein which is an essential component of the replication/transcription complex (RTC). The functions of Ubl1 in CoVs are related to single-stranded RNA (ssRNA) binding and to interacting with the nucleocapsid (N) protein. SARS-CoV Ubl1 has been shown to bind ssRNA having AUA patterns, and since the 5'-UTR of the SARS-CoV genome has a number of AUA repeats, it may bind there. In mouse hepatitis virus (MHV), this Ubl1 domain binds the cognate N protein. Adjacent to Ubl1 is a Glu-rich acidic region (also referred to as hypervariable region, HVR); Ubl1 together with HVR has been called Nsp3a. Currently, the function of HVR in CoVs is unknown. This model corresponds to one of two Ubl domains in Nsp3; the other is located N-terminal to the papain-like protease (PLpro) and is not represented by this model.


The actual alignment was detected with superfamily member cd17197:

Pssm-ID: 475130  Cd Length: 98  Bit Score: 162.66  E-value: 7.84e-49
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 170932512   4 VKATGRELFQQVCNVASIRDAQFFGLCVVRNNEYIFMDLEQKLSKYFSKDWKKERNEGNEKPRAPFVAFLRVQHYVENG 82
Cdd:cd17197   20 VKATGQELFQQVCELLKIKEAHFFGLSVVKNNEHIFMDLEQKLSKYFPKEWKKETGKGTEKFSIPFVACFRVQYYVENG 98
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
 80-196 8.76e-32

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


:

Pssm-ID: 459788 [Multi-domain]  Cd Length: 117  Bit Score: 117.76  E-value: 8.76e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170932512   80 ENGRVISDHRARHLYYCHLKERVLRSQCAHREEAYFLLAACALQADLGEHRESAHAGRYFEPHSYFPQWIITKRGIDYIL 159
Cdd:pfam00373   1 DLELLLQDEVTRHLLYLQAKDDILEGRLPCSEEEALLLAALQLQAEFGDYQPSSHTSEYLSLESFLPKQLLRKMKSKELE 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 170932512  160 RHMPTLHRERQGLSPKEAMLCFIQEACRLEDVPVHFF 196
Cdd:pfam00373  81 KRVLEAHKNLRGLSAEEAKLKYLQIAQSLPTYGVEFF 117
PH-like super family cl17171
Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like ...
 189-274 2.64e-26

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 cd13185:

Pssm-ID: 473070  Cd Length: 107  Bit Score: 102.39  E-value: 2.64e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170932512 189 EDVPVHFFRLHKDKKEGRPTVILGLALRGVHIYQ-----------------------GKKLEIQLDGlpAAQKLVYYTGC 245
Cdd:cd13185    1 EDLNAHLYRLRKSKKETPGSVLLGITAKGIQIYQesdgeqqllrtfpwsnigklsfdRKKFEIRPEG--SLRKLTYYTSS 78

                         90       100
                 ....*....|....*....|....*....
gi 170932512 246 TWRSRHLLHLLRASHQLHLRVRPTLQQLR 274
Cdd:cd13185   79 DEKSKYLLALCRETHQFSMAIQPRLSEIR 107
 
Name Accession Description Interval E-value
FERM_F1_FRMD1 cd17197
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM ...
 4-82 7.84e-49

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM domain-containing protein 1 (FRMD1); FRMD1 is an uncharacterized FERM domain-containing protein. 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).


Pssm-ID: 340717  Cd Length: 98  Bit Score: 162.66  E-value: 7.84e-49
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 170932512   4 VKATGRELFQQVCNVASIRDAQFFGLCVVRNNEYIFMDLEQKLSKYFSKDWKKERNEGNEKPRAPFVAFLRVQHYVENG 82
Cdd:cd17197   20 VKATGQELFQQVCELLKIKEAHFFGLSVVKNNEHIFMDLEQKLSKYFPKEWKKETGKGTEKFSIPFVACFRVQYYVENG 98
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
 80-196 8.76e-32

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


Pssm-ID: 459788 [Multi-domain]  Cd Length: 117  Bit Score: 117.76  E-value: 8.76e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170932512   80 ENGRVISDHRARHLYYCHLKERVLRSQCAHREEAYFLLAACALQADLGEHRESAHAGRYFEPHSYFPQWIITKRGIDYIL 159
Cdd:pfam00373   1 DLELLLQDEVTRHLLYLQAKDDILEGRLPCSEEEALLLAALQLQAEFGDYQPSSHTSEYLSLESFLPKQLLRKMKSKELE 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 170932512  160 RHMPTLHRERQGLSPKEAMLCFIQEACRLEDVPVHFF 196
Cdd:pfam00373  81 KRVLEAHKNLRGLSAEEAKLKYLQIAQSLPTYGVEFF 117
FERM_C_FRMD1_FRMD6 cd13185
FERM domain C-lobe of FERM domain containing 1 and 6 proteins; FRMD6 (also called willin and ...
 189-274 2.64e-26

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: 102.39  E-value: 2.64e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170932512 189 EDVPVHFFRLHKDKKEGRPTVILGLALRGVHIYQ-----------------------GKKLEIQLDGlpAAQKLVYYTGC 245
Cdd:cd13185    1 EDLNAHLYRLRKSKKETPGSVLLGITAKGIQIYQesdgeqqllrtfpwsnigklsfdRKKFEIRPEG--SLRKLTYYTSS 78

                         90       100
                 ....*....|....*....|....*....
gi 170932512 246 TWRSRHLLHLLRASHQLHLRVRPTLQQLR 274
Cdd:cd13185   79 DEKSKYLLALCRETHQFSMAIQPRLSEIR 107
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 3-196 2.24e-22

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: 94.67  E-value: 2.24e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170932512     3 DVKATGRELFQQVCNVASIRDAQFFGLCVVR--NNEYIFMDLEQKLSKYFSKdwkkernegnekpRAPFVAFLRVQHYVE 80
Cdd:smart00295  17 DSSTTAEELLETVCRKLGIRESEYFGLQFEDpdEDLRHWLDPAKTLLDQDVK-------------SEPLTLYFRVKFYPP 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170932512    81 N-GRVISDHRARHLYYCHLKERVLRSQCAHREEAYFLLAACALQADLGEHRESAHAGRYFEPH-SYFPQWIITKRGIDYI 158
Cdd:smart00295  84 DpNQLKEDPTRLNLLYLQVRNDILEGRLPCPEEEALLLAALALQAEFGDYDEELHDLRGELSLkRFLPKQLLDSRKLKEW 163

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 170932512   159 LRHMPTLHRERQGLSPKEAMLCFIQEACRLEDVPVHFF 196
Cdd:smart00295 164 RERIVELHKELIGLSPEEAKLKYLELARKLPTYGVELF 201
FERM_B-lobe cd14473
FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C ...
 90-188 5.58e-19

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: 81.91  E-value: 5.58e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170932512  90 ARHLYYCHLKERVLRSQCAHREEAYFLLAACALQADLGEHRESAHAGRYFEPHSYFPQWIITKRGIDYILRHMPTLHRER 169
Cdd:cd14473    1 TRYLLYLQVKRDILEGRLPCSEETAALLAALALQAEYGDYDPSEHKPKYLSLKRFLPKQLLKQRKPEEWEKRIVELHKKL 80

                         90
                 ....*....|....*....
gi 170932512 170 QGLSPKEAMLCFIQEACRL 188
Cdd:cd14473   81 RGLSPAEAKLKYLKIARKL 99
FERM_N pfam09379
FERM N-terminal domain; This domain is the N-terminal ubiquitin-like structural domain of the ...
 3-51 1.43e-12

FERM N-terminal domain; This domain is the N-terminal ubiquitin-like structural domain of the FERM domain.


Pssm-ID: 430570  Cd Length: 63  Bit Score: 62.61  E-value: 1.43e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 170932512    3 DVKATGRELFQQVCNVASIRDAQFFGLCVVRNN-EYIFMDLEQKLSKYFS 51
Cdd:pfam09379  14 QPKATGQVLLDQVCNHLNLKEKDYFGLQFLDDNgEHRWLDLSKRLSKQAP 63
FERM_C pfam09380
FERM C-terminal PH-like domain;
201-267 1.15e-06

FERM C-terminal PH-like domain;


Pssm-ID: 462779 [Multi-domain]  Cd Length: 85  Bit Score: 46.48  E-value: 1.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170932512  201 DKKEGrpTVILGLALRGVHIYQ--------------------GKKLEIQLDGLPAAQKLVYYTGCTWRSRHLLHLLRASH 260
Cdd:pfam09380   1 DKEGT--DLWLGVSAKGILVYEdnnkilnlfpwreirkisfkRKKFLIKLRDKSSEETLGFYTESSRACKYLWKLCVEQH 78


                  ....*..
gi 170932512  261 QLHLRVR 267
Cdd:pfam09380  79 TFFRLRR 85
 
Name Accession Description Interval E-value
FERM_F1_FRMD1 cd17197
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM ...
 4-82 7.84e-49

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM domain-containing protein 1 (FRMD1); FRMD1 is an uncharacterized FERM domain-containing protein. 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).


Pssm-ID: 340717  Cd Length: 98  Bit Score: 162.66  E-value: 7.84e-49
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 170932512   4 VKATGRELFQQVCNVASIRDAQFFGLCVVRNNEYIFMDLEQKLSKYFSKDWKKERNEGNEKPRAPFVAFLRVQHYVENG 82
Cdd:cd17197   20 VKATGQELFQQVCELLKIKEAHFFGLSVVKNNEHIFMDLEQKLSKYFPKEWKKETGKGTEKFSIPFVACFRVQYYVENG 98
FERM_F1_PTPN13_like cd17101
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 3-81 1.73e-33

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein phosphatase non-receptor type 13 (PTPN13) and similar proteins; This family includes tyrosine-protein phosphatase non-receptor type 13 (PTPN13), FERM and PDZ domain-containing protein 2 (FRMPD2), and FERM domain-containing proteins FRMD1 and FRMD6. All family members contain a FERM domain that 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: 340621  Cd Length: 97  Bit Score: 121.90  E-value: 1.73e-33
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 170932512   3 DVKATGRELFQQVCNVASIRDAQFFGLCVVRNNEYIFMDLEQKLSKYFSKDWKKERNEGNEKPRAPFVAFLRVQHYVEN 81
Cdd:cd17101   19 DVKTTVQDLFDQVCDHLGLQETELFGLAVLKDGEYFFLDPDTKLSKYAPKGWKSEAKKGLKGGKPVFTLYFRVKFYVDN 97
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
 80-196 8.76e-32

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


Pssm-ID: 459788 [Multi-domain]  Cd Length: 117  Bit Score: 117.76  E-value: 8.76e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170932512   80 ENGRVISDHRARHLYYCHLKERVLRSQCAHREEAYFLLAACALQADLGEHRESAHAGRYFEPHSYFPQWIITKRGIDYIL 159
Cdd:pfam00373   1 DLELLLQDEVTRHLLYLQAKDDILEGRLPCSEEEALLLAALQLQAEFGDYQPSSHTSEYLSLESFLPKQLLRKMKSKELE 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 170932512  160 RHMPTLHRERQGLSPKEAMLCFIQEACRLEDVPVHFF 196
Cdd:pfam00373  81 KRVLEAHKNLRGLSAEEAKLKYLQIAQSLPTYGVEFF 117
FERM_C_FRMD1_FRMD6 cd13185
FERM domain C-lobe of FERM domain containing 1 and 6 proteins; FRMD6 (also called willin and ...
 189-274 2.64e-26

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: 102.39  E-value: 2.64e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170932512 189 EDVPVHFFRLHKDKKEGRPTVILGLALRGVHIYQ-----------------------GKKLEIQLDGlpAAQKLVYYTGC 245
Cdd:cd13185    1 EDLNAHLYRLRKSKKETPGSVLLGITAKGIQIYQesdgeqqllrtfpwsnigklsfdRKKFEIRPEG--SLRKLTYYTSS 78

                         90       100
                 ....*....|....*....|....*....
gi 170932512 246 TWRSRHLLHLLRASHQLHLRVRPTLQQLR 274
Cdd:cd13185   79 DEKSKYLLALCRETHQFSMAIQPRLSEIR 107
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 3-196 2.24e-22

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: 94.67  E-value: 2.24e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170932512     3 DVKATGRELFQQVCNVASIRDAQFFGLCVVR--NNEYIFMDLEQKLSKYFSKdwkkernegnekpRAPFVAFLRVQHYVE 80
Cdd:smart00295  17 DSSTTAEELLETVCRKLGIRESEYFGLQFEDpdEDLRHWLDPAKTLLDQDVK-------------SEPLTLYFRVKFYPP 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170932512    81 N-GRVISDHRARHLYYCHLKERVLRSQCAHREEAYFLLAACALQADLGEHRESAHAGRYFEPH-SYFPQWIITKRGIDYI 158
Cdd:smart00295  84 DpNQLKEDPTRLNLLYLQVRNDILEGRLPCPEEEALLLAALALQAEFGDYDEELHDLRGELSLkRFLPKQLLDSRKLKEW 163

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 170932512   159 LRHMPTLHRERQGLSPKEAMLCFIQEACRLEDVPVHFF 196
Cdd:smart00295 164 RERIVELHKELIGLSPEEAKLKYLELARKLPTYGVELF 201
FERM_F1_FRMD6 cd17198
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM ...
 3-82 3.48e-22

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM domain-containing protein 6 (FRMD6); FRMD6, also termed willin, expanded or expanded homolog, is a FERM domain-containing protein that plays a critical role in regulating both cell proliferation and apoptosis. It acts as a tumor suppressor of human breast cancer cells independently of the Hippo pathway. It also inhibits human glioblastoma growth and progression by negatively regulating activity of receptor tyrosine kinases. As an upstream component of the hippo signaling pathway, FRMD6 orchestrates mammalian peripheral nerve fibroblasts. FRMD6 contains a FERM domain that 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: 340718  Cd Length: 98  Bit Score: 90.74  E-value: 3.48e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170932512   3 DVKATGRELFQQVCNVASIRDAQFFGLCVVRNNEYIFMDLEQKLSKYFSKDWKKERNEGNEKPRAPFVAFLRVQHYVENG 82
Cdd:cd17198   19 NVKTLCQELLVQVCDLLRLKDCHLFGLSVIQNNEHVYMELSQKLYKYCPKEWKKEASKGIDQFGPPMIVHFRVQYYVENG 98
FERM_B-lobe cd14473
FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C ...
 90-188 5.58e-19

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: 81.91  E-value: 5.58e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170932512  90 ARHLYYCHLKERVLRSQCAHREEAYFLLAACALQADLGEHRESAHAGRYFEPHSYFPQWIITKRGIDYILRHMPTLHRER 169
Cdd:cd14473    1 TRYLLYLQVKRDILEGRLPCSEETAALLAALALQAEYGDYDPSEHKPKYLSLKRFLPKQLLKQRKPEEWEKRIVELHKKL 80

                         90
                 ....*....|....*....
gi 170932512 170 QGLSPKEAMLCFIQEACRL 188
Cdd:cd14473   81 RGLSPAEAKLKYLKIARKL 99
FERM_N pfam09379
FERM N-terminal domain; This domain is the N-terminal ubiquitin-like structural domain of the ...
 3-51 1.43e-12

FERM N-terminal domain; This domain is the N-terminal ubiquitin-like structural domain of the FERM domain.


Pssm-ID: 430570  Cd Length: 63  Bit Score: 62.61  E-value: 1.43e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 170932512    3 DVKATGRELFQQVCNVASIRDAQFFGLCVVRNN-EYIFMDLEQKLSKYFS 51
Cdd:pfam09379  14 QPKATGQVLLDQVCNHLNLKEKDYFGLQFLDDNgEHRWLDLSKRLSKQAP 63
FERM_F0_F1 cd01765
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0 sub-domain and F1 sub-domain, found ...
 3-77 2.78e-09

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: 53.75  E-value: 2.78e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 170932512   3 DVKATGRELFQQVCNVASIRDAQFFGLCVVRN-NEYIFMDLEQKLSKYFSKdwkkernegnekpRAPFVAFLRVQH 77
Cdd:cd01765   18 SKKATGQELFDKVCEKLNLLEKDYFGLFYEDNdGQKHWLDLDKKISKQLKR-------------SGPYQFYFRVKF 80
FERM_F1_PTPN13 cd17195
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 3-81 7.90e-09

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein phosphatase non-receptor type 13 (PTPN13); PTPN13, also termed Fas-associated protein-tyrosine phosphatase 1 (FAP-1), or PTP-BAS, or protein-tyrosine phosphatase 1E (PTP-E1 or PTPE1), or protein-tyrosine phosphatase PTPL1, belongs to the non-transmembrane FERM-containing protein-tyrosine phosphatase (PTP) subfamily characterized by a KIND domain, a FERM domain, five PDZ domains, and a C-terminal PTP catalytic 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). PTPN13 interacts with a variety of ligands, suggests an important role as a scaffolding protein. It is also involved in the regulation of apoptosis, cytokinesis and cell cycle progression.


Pssm-ID: 340715  Cd Length: 96  Bit Score: 52.89  E-value: 7.90e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 170932512   3 DVKATGRELFQQVCNVASIRDAQFFGLCVVRNNEYIFMDLEQKLSKYFSKDWKKERNEGNeKPRAPFVAFLRVQHYVEN 81
Cdd:cd17195   19 DTKSTCKDVFDMVVAHIGLVEHHLFALAYLKDNEFFFVDPDLKLSKVAPEGWKEEPKKKN-KMTVNFTLFFRIKFFVDD 96
FERM_F1_FRMPD2 cd17196
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM and PDZ ...
 3-81 5.15e-08

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM and PDZ domain-containing protein 2 (FRMPD2); FRMPD2, also termed PDZ domain-containing protein 4 (PDZK4), or PDZ domain-containing protein 5C (PDZD5C), is a potential scaffold protein involved in basolateral membrane targeting in epithelial cells. It interacts with nucleotide-binding oligomerization domain-2 (NOD2) through leucine-rich repeats and forms a complex with the membrane-associated protein ERBB2IP. FRMPD2 contains an N-terminal KIND domain, a FERM domain and three PDZ domains. 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).


Pssm-ID: 340716  Cd Length: 95  Bit Score: 50.59  E-value: 5.15e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 170932512   3 DVKATGRELFQQVCNVASIRDAQFFGLCVVRNNEYIFMDLEQKLSKYFSKDWKKERNEgnEKPRAPFVAFLRVQHYVEN 81
Cdd:cd17196   19 DIKSRVRDVFNMVVAFANLVEHFYFGLAYMKGKEFFFLDHETKLHKVAPEGWKDQSKK--KTSIVNFTLFLRIKFFVDN 95
FERM_F1_ERM_like cd17097
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in the ERM family ...
 3-80 5.31e-07

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in the ERM family proteins; The ezrin-radixin-moesin (ERM) family includes a group of closely related cytoskeletal proteins that play an essential role in microvilli formation, T-cell activation, and tumor metastasis through providing a regulated linkage between F-actin and membrane-associated proteins. These proteins may also function in signaling cascades that regulate the assembly of actin stress fibers. The ERM proteins consist of an N-terminal FERM domain, a coiled-coil (CC) domain and a C-terminal tail segment (C-tail) containing a well-defined actin-binding motif. They 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 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). Merlin, which is highly related to the members of the ezrin, radixin, and moesin (ERM) protein family that are directly attached to and functionally linked with NHE1, is included in this family.


Pssm-ID: 340617  Cd Length: 83  Bit Score: 47.27  E-value: 5.31e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 170932512   3 DVKATGRELFQQVCNVASIRDAQFFGLC-VVRNNEYIFMDLEQKLSkyfskdwKKERNEGNekpraPFVAFLRVQHYVE 80
Cdd:cd17097   17 KPKAKGRELFDLVCRTIGLRETWYFGLQyENKKGRVAWLKPDKKVL-------TQDVSKNN-----TLKFFFLVKFYPE 83
FERM_C pfam09380
FERM C-terminal PH-like domain;
201-267 1.15e-06

FERM C-terminal PH-like domain;


Pssm-ID: 462779 [Multi-domain]  Cd Length: 85  Bit Score: 46.48  E-value: 1.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170932512  201 DKKEGrpTVILGLALRGVHIYQ--------------------GKKLEIQLDGLPAAQKLVYYTGCTWRSRHLLHLLRASH 260
Cdd:pfam09380   1 DKEGT--DLWLGVSAKGILVYEdnnkilnlfpwreirkisfkRKKFLIKLRDKSSEETLGFYTESSRACKYLWKLCVEQH 78


                  ....*..
gi 170932512  261 QLHLRVR 267
Cdd:pfam09380  79 TFFRLRR 85
FERM_C_PTPH13 cd13187
FERM domain C-lobe of Protein tyrosine phosphatase non-receptor 13 (PTPH13); There are many ...
 193-267 8.52e-04

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: 38.84  E-value: 8.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170932512 193 VHFFRLHKDKKEGRPTVILGLALRGVHIYQ-----------------------GKKLEIQLDGlPAAQKLVYYTGCTWRS 249
Cdd:cd13187    2 VHFHRVYREKKSSTLSLWLGICSRGIIIYEekngartpvlrfpwretqkisfdKKKFTIESRG-GSGIKHTFYTDSYKKS 80

                         90
                 ....*....|....*...
gi 170932512 250 RHLLHLLRASHQLHLRVR 267
Cdd:cd13187   81 QYLLQLCSAQHKFHIQMR 98
FERM_C-lobe cd00836
FERM domain C-lobe; The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N ...
 193-262 1.23e-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: 38.12  E-value: 1.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170932512 193 VHFFRLHKDKKEGRPtVILGLALRGVHIYQ----------------------GKKLEIQLDGLPAAQKLVYYTGCTwRSR 250
Cdd:cd00836    2 VEFFPVKDKSKKGSP-IILGVNPEGISVYDeltgqplvlfpwpnikkisfsgAKKFTIVVADEDKQSKLLFQTPSR-QAK 79

                         90
                 ....*....|..
gi 170932512 251 HLLHLLRASHQL 262
Cdd:cd00836   80 EIWKLIVGYHRF 91
FERM_F1_PTPN14_like cd17099
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 3-52 1.38e-03

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein phosphatase non-receptors PTPN14, PTPN21, and similar proteins; This family includes tyrosine-protein phosphatase non-receptors PTPN14 and PTPN21, both of which are protein-tyrosine phosphatase (PTP). They belong to the FERM family of PTPs characterized by a conserved N-terminal FERM domain and a C-terminal PTP catalytic domain with an intervening sequence containing an acidic region and a putative SH3 domain-binding sequence. 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). PTPN14 plays a role in the nucleus during cell proliferation. PTPN21 interacts with a Tec tyrosine kinase family member, the epithelial and endothelial tyrosine kinase (Etk, also known as Bmx), modulates Stat3 activation, and plays a role in the regulation of cell growth and differentiation.


Pssm-ID: 340619  Cd Length: 85  Bit Score: 37.60  E-value: 1.38e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 170932512   3 DVKATGRELFQQVCNVASIRDAQFFGL-CVVRNNEYIFMDLEQKLSKYFSK 52
Cdd:cd17099   21 SPESTGQDCLEYVAQRLELREIEYFGLrYVNKKGQLRWVDLEKPLKKQLDK 71
FERM_F1_Ezrin cd17239
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in Ezrin and ...
 7-69 1.73e-03

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in Ezrin and similar proteins; Ezrin, also termed cytovillin, or villin-2, or p81, is a member of the ezrin/radixin/moesin (ERM) family of cytoskeletal proteins that plays an essential role in microvilli formation, T-cell activation, and tumor metastasis through providing a regulated linkage between F-actin and membrane-associated proteins. These proteins may also function in signaling cascades that regulate the assembly of actin stress fibers. The ERM proteins consist of an N-terminal FERM domain, a coiled-coil (CC) domain and a C-terminal tail segment (C-tail) containing a well-defined actin-binding motif. The C-terminal domain can fold back to bind to the FERM domain forming an autoinhibited conformation. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N). Ezrin is a tyrosine kinase substrate that functions as a cross-linker between actin cytoskeleton and plasma membrane. It has been implicated in the regulation of the proliferation, apoptosis, adhesion, invasion, metastasis and angiogenesis of cancer cells.


Pssm-ID: 340759  Cd Length: 85  Bit Score: 37.28  E-value: 1.73e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 170932512   7 TGRELFQQVCNVASIRDAQFFGLCVVRNNEYI-FMDLEQKLSkyfSKDWKKErNEGNEKPRAPF 69
Cdd:cd17239   23 TGKQLFDQVVKTIGLREVWYFGLQYVDNKGFPtWLKLDKKVS---AQEVRKE-NPLQFKFRAKF 82
FERM_F1_ERM cd17187
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in the ERM family ...
 7-57 2.69e-03

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in the ERM family proteins, Ezrin, Radixin, and Moesin; The ezrin-radixin-moesin (ERM) family includes a group of closely related cytoskeletal proteins that plays an essential role in microvilli formation, T-cell activation, and tumor metastasis through providing a regulated linkage between F-actin and membrane-associated proteins. These proteins may also function in signaling cascades that regulate the assembly of actin stress fibers. The ERM proteins consist of an N-terminal FERM domain, a coiled-coil (CC) domain and a C-terminal tail segment (C-tail) containing a well-defined actin-binding motif. They 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 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: 340707 [Multi-domain]  Cd Length: 83  Bit Score: 36.68  E-value: 2.69e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 170932512   7 TGRELFQQVCNVASIRDAQFFGLCVVRNNEYI-FMDLEQKLSkyfSKDWKKE 57
Cdd:cd17187   21 TGKQLFDQVVKTIGLREIWFFGLQYVDSKGYStWLKLNKKVL---SQDVKKE 69
FERM_F1_Merlin cd17186
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in merlin and ...
 3-48 2.74e-03

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in merlin and similar proteins; Merlin, also termed moesin-ezrin-radixin-like protein, or neurofibromin-2 (NF2), or Schwannomerlin, or Schwannomin, is a member of the ezrin/radixin/moesin (ERM) family of cytoskeletal proteins that plays an essential role in microvilli formation, T-cell activation, and tumor metastasis through providing a regulated linkage between F-actin and membrane-associated proteins. These proteins may also function in signaling cascades that regulate the assembly of actin stress fibers. The ERM proteins consist of an N-terminal FERM domain, a coiled-coil (CC) domain and a C-terminal tail segment (C-tail) containing a well-defined actin-binding motif, merlin however lacks the typical actin-binding motif in the C-tail. 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). Merlin plays vital roles in controlling proper development of organ sizes by specifically binding to a large number of target proteins localized both in cytoplasm and nuclei. Merlin may function as a tumor suppressor that functions upstream of the core Hippo pathway kinases Lats1/2 (Wts in Drosophila) and Mst1/2 (Hpo in Drosophila), as well as the nuclear E3 ubiquitin ligase DDB1-and-Cullin 4-associated Factor 1 (DCAF1)-associated cullin 4-Roc1 ligase, CRL4(DCAF1). Merlin may also has a tumor suppressor function in melanoma cells, the inhibition of the proto-oncogenic Na(+)/H(+) exchanger isoform 1 (NHE1) activity.


Pssm-ID: 340706  Cd Length: 85  Bit Score: 36.98  E-value: 2.74e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 170932512   3 DVKATGRELFQQVCNVASIRDAQFFGLCVVRNNEYIF---MD---LEQKLSK 48
Cdd:cd17186   19 EMKWKGKDLFDLVCRTIGLRETWYFGLQYTDSKGTVAwlkMDkkvLDQDVPK 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH