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Conserved domains on  [gi|387763004|ref|NP_001248698|]
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krev interaction trapped protein 1 [Macaca mulatta]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NUDIX_5 pfam16705
NUDIX, or N-terminal NPxY motif-rich, region of KRIT; NUDIX_5 is found in higher eukaryotes at ...
 30-198 7.03e-104

NUDIX, or N-terminal NPxY motif-rich, region of KRIT; NUDIX_5 is found in higher eukaryotes at the N-terminus of KRIT1 or Krev interaction trapped proteins. NUDIX_5 carries three NPxY-like motifs, and it is found to bind the integrin cytoplasmic-associated protein 1 ICAP1. In the absence of KRIT1 ICAP1 binds via its C-terminal PH/PTB fold domain to the integrin beta-1 cytoplasmic tail. Binding of KRIT1 to ICAP1 via NUDIX_5 out-competes the binding of ICAP1 to integrin cytoplasmic tails such that ICAP1 is sequestered in the nucleus. Integrin activation is thus prevented.


:

Pssm-ID: 465241  Cd Length: 169  Bit Score: 315.15  E-value: 7.03e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387763004   30 AKSYEILLHEVPIEGQKKKRKKVLLETKLQGNSEITQGILDYVVETTKPISPANQGIRGKRVVLMKKFPLDGEKMGREAS 109
Cdd:pfam16705   1 AKSYEILLLEVPIEGKKKKRKKVLLETKLRGSQEATKQILDYVYETTKPISPDNQGIKGKRVVHMKKFPLDGEESGREAS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387763004  110 LFIVPSVVKDNTKYTYTPGCPIFYCFQDIMRVCSESSTHFATLTARMLIALDKWLDERHAQSHFIPALFRPSPLERIKTN 189
Cdd:pfam16705  81 LFVVPVNVKDNTKPSYSPGSPSFYCLQDIMRVCSESSTHFPTLTSRMLIALDKWLKEQHAVPHAIPALFRPSALERIKTN 160


                  ....*....
gi 387763004  190 VINPAYATE 198
Cdd:pfam16705 161 VSNPAYATE 169
FERM_C_CCM1 cd13197
FERM domain C-lobe of Cerebral cavernous malformation 1; CCM1 (also called KRIT-1/Krev ...
 636-735 4.33e-63

FERM domain C-lobe of Cerebral cavernous malformation 1; CCM1 (also called KRIT-1/Krev interaction trapped 1;ankyrin repeat-containing protein Krit1; CAM), a Rap1-binding protein, is expressed in endothelial cells where it is present in cell-cell junctions and associated with junctional proteins. Together with CCM2/MGC4607 and CCM3/PDCD10, KRIT1 constitutes a set of proteins, mutations of which are found in cerebral cavernous malformations which are characterized by cerebral hemorrhages and vascular malformations in the central nervous system. KRIT-1 possesses four ankyrin repeats, a FERM domain, and multiple NPXY sequences, one of which is essential for integrin cytoplasmic domain-associated protein-1alpha (ICAP1alpha) binding and all of which mediate binding of CCM2. KRIT-1 localization is mediated by its FERM domain. 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: 270018  Cd Length: 100  Bit Score: 205.54  E-value: 4.33e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387763004 636 GAAFFTGQIFTKASPSNHKVIPVYVGVNIKGLHLLNMETKALLISLNYGCFMWQLGDADTCFQIHSMENKMSFIVHTKQA 715
Cdd:cd13197    1 GAAFFTGQIFTKASSSNHKVIPVYVGVNIKGLHLLNMETKALLLSLKYGCFMWQLGDADTCFQIHSLENKMSFVVHTKQA 80

                         90       100
                 ....*....|....*....|
gi 387763004 716 GLVVKLLMKLNGQLMPTERN 735
Cdd:cd13197   81 GLIVKLLMKLSGQRKPNDRN 100
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 421-640 3.51e-37

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: 137.81  E-value: 3.51e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387763004   421 KVRIYRMDGSyrSVELKHGNNTTVQQIMEGMRLSQETqqyftiwICSENLSLQLKPYHKPLQHvrdWPEILAELTNLDPQ 500
Cdd:smart00295   1 VLKVYLLDGT--TLEFEVDSSTTAEELLETVCRKLGI-------RESEYFGLQFEDPDEDLRH---WLDPAKTLLDQDVK 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387763004   501 RETSQLFLRRDVRLPlEVEKQIEDPLAILILFDEARYNLLKGFYTAPDAKLITLASLLLQIVYGNYESKKHKQgfLNEEN 580
Cdd:smart00295  69 SEPLTLYFRVKFYPP-DPNQLKEDPTRLNLLYLQVRNDILEGRLPCPEEEALLLAALALQAEFGDYDEELHDL--RGELS 145

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 387763004   581 LKSIVPVTKLKS-KAPHWTNRILHEYKNLStsegvSKEMHHLQRMFLQNCWEIPTYGAAFF 640
Cdd:smart00295 146 LKRFLPKQLLDSrKLKEWRERIVELHKELI-----GLSPEEAKLKYLELARKLPTYGVELF 201
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
291-414 5.30e-22

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 96.95  E-value: 5.30e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387763004 291 PLHRSACEGDSELLSRLLSERFSVNQLDSDHWAPIHYACWYGKVEATRILLEKGkCNPNLLNGQLSSPLHFAAGGGHAEI 370
Cdd:COG0666   90 LLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAG-ADVNAQDNDGNTPLHLAAANGNLEI 168

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 387763004 371 VQILLNHPeIDRHITDQQGRSPLNICEENKQnnwEEAAKLLKEA 414
Cdd:COG0666  169 VKLLLEAG-ADVNARDNDGETPLHLAAENGH---LEIVKLLLEA 208
 
Name Accession Description Interval E-value
NUDIX_5 pfam16705
NUDIX, or N-terminal NPxY motif-rich, region of KRIT; NUDIX_5 is found in higher eukaryotes at ...
 30-198 7.03e-104

NUDIX, or N-terminal NPxY motif-rich, region of KRIT; NUDIX_5 is found in higher eukaryotes at the N-terminus of KRIT1 or Krev interaction trapped proteins. NUDIX_5 carries three NPxY-like motifs, and it is found to bind the integrin cytoplasmic-associated protein 1 ICAP1. In the absence of KRIT1 ICAP1 binds via its C-terminal PH/PTB fold domain to the integrin beta-1 cytoplasmic tail. Binding of KRIT1 to ICAP1 via NUDIX_5 out-competes the binding of ICAP1 to integrin cytoplasmic tails such that ICAP1 is sequestered in the nucleus. Integrin activation is thus prevented.


Pssm-ID: 465241  Cd Length: 169  Bit Score: 315.15  E-value: 7.03e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387763004   30 AKSYEILLHEVPIEGQKKKRKKVLLETKLQGNSEITQGILDYVVETTKPISPANQGIRGKRVVLMKKFPLDGEKMGREAS 109
Cdd:pfam16705   1 AKSYEILLLEVPIEGKKKKRKKVLLETKLRGSQEATKQILDYVYETTKPISPDNQGIKGKRVVHMKKFPLDGEESGREAS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387763004  110 LFIVPSVVKDNTKYTYTPGCPIFYCFQDIMRVCSESSTHFATLTARMLIALDKWLDERHAQSHFIPALFRPSPLERIKTN 189
Cdd:pfam16705  81 LFVVPVNVKDNTKPSYSPGSPSFYCLQDIMRVCSESSTHFPTLTSRMLIALDKWLKEQHAVPHAIPALFRPSALERIKTN 160


                  ....*....
gi 387763004  190 VINPAYATE 198
Cdd:pfam16705 161 VSNPAYATE 169
FERM_C_CCM1 cd13197
FERM domain C-lobe of Cerebral cavernous malformation 1; CCM1 (also called KRIT-1/Krev ...
 636-735 4.33e-63

FERM domain C-lobe of Cerebral cavernous malformation 1; CCM1 (also called KRIT-1/Krev interaction trapped 1;ankyrin repeat-containing protein Krit1; CAM), a Rap1-binding protein, is expressed in endothelial cells where it is present in cell-cell junctions and associated with junctional proteins. Together with CCM2/MGC4607 and CCM3/PDCD10, KRIT1 constitutes a set of proteins, mutations of which are found in cerebral cavernous malformations which are characterized by cerebral hemorrhages and vascular malformations in the central nervous system. KRIT-1 possesses four ankyrin repeats, a FERM domain, and multiple NPXY sequences, one of which is essential for integrin cytoplasmic domain-associated protein-1alpha (ICAP1alpha) binding and all of which mediate binding of CCM2. KRIT-1 localization is mediated by its FERM domain. 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: 270018  Cd Length: 100  Bit Score: 205.54  E-value: 4.33e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387763004 636 GAAFFTGQIFTKASPSNHKVIPVYVGVNIKGLHLLNMETKALLISLNYGCFMWQLGDADTCFQIHSMENKMSFIVHTKQA 715
Cdd:cd13197    1 GAAFFTGQIFTKASSSNHKVIPVYVGVNIKGLHLLNMETKALLLSLKYGCFMWQLGDADTCFQIHSLENKMSFVVHTKQA 80

                         90       100
                 ....*....|....*....|
gi 387763004 716 GLVVKLLMKLNGQLMPTERN 735
Cdd:cd13197   81 GLIVKLLMKLSGQRKPNDRN 100
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 421-640 3.51e-37

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: 137.81  E-value: 3.51e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387763004   421 KVRIYRMDGSyrSVELKHGNNTTVQQIMEGMRLSQETqqyftiwICSENLSLQLKPYHKPLQHvrdWPEILAELTNLDPQ 500
Cdd:smart00295   1 VLKVYLLDGT--TLEFEVDSSTTAEELLETVCRKLGI-------RESEYFGLQFEDPDEDLRH---WLDPAKTLLDQDVK 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387763004   501 RETSQLFLRRDVRLPlEVEKQIEDPLAILILFDEARYNLLKGFYTAPDAKLITLASLLLQIVYGNYESKKHKQgfLNEEN 580
Cdd:smart00295  69 SEPLTLYFRVKFYPP-DPNQLKEDPTRLNLLYLQVRNDILEGRLPCPEEEALLLAALALQAEFGDYDEELHDL--RGELS 145

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 387763004   581 LKSIVPVTKLKS-KAPHWTNRILHEYKNLStsegvSKEMHHLQRMFLQNCWEIPTYGAAFF 640
Cdd:smart00295 146 LKRFLPKQLLDSrKLKEWRERIVELHKELI-----GLSPEEAKLKYLELARKLPTYGVELF 201
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
 517-640 7.87e-28

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


Pssm-ID: 459788 [Multi-domain]  Cd Length: 117  Bit Score: 108.51  E-value: 7.87e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387763004  517 EVEKQIEDPLAILILFDEARYNLLKGFYTAPDAKLITLASLLLQIVYGNYESKKHKQGFLneeNLKSIVPVTKL-KSKAP 595
Cdd:pfam00373   1 DLELLLQDEVTRHLLYLQAKDDILEGRLPCSEEEALLLAALQLQAEFGDYQPSSHTSEYL---SLESFLPKQLLrKMKSK 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 387763004  596 HWTNRILHEYKNLStsegvSKEMHHLQRMFLQNCWEIPTYGAAFF 640
Cdd:pfam00373  78 ELEKRVLEAHKNLR-----GLSAEEAKLKYLQIAQSLPTYGVEFF 117
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
291-414 5.30e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 96.95  E-value: 5.30e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387763004 291 PLHRSACEGDSELLSRLLSERFSVNQLDSDHWAPIHYACWYGKVEATRILLEKGkCNPNLLNGQLSSPLHFAAGGGHAEI 370
Cdd:COG0666   90 LLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAG-ADVNAQDNDGNTPLHLAAANGNLEI 168

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 387763004 371 VQILLNHPeIDRHITDQQGRSPLNICEENKQnnwEEAAKLLKEA 414
Cdd:COG0666  169 VKLLLEAG-ADVNARDNDGETPLHLAAENGH---LEIVKLLLEA 208
Ank_2 pfam12796
Ankyrin repeats (3 copies);
292-386 1.07e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.84  E-value: 1.07e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387763004  292 LHRSACEGDSELLSRLLSERFSVNQLDSDHWAPIHYACWYGKVEATRILLEKGKCNpNLLNGQlsSPLHFAAGGGHAEIV 371
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVN-LKDNGR--TALHYAARSGHLEIV 77

                          90
                  ....*....|....*
gi 387763004  372 QILLNHpEIDRHITD 386
Cdd:pfam12796  78 KLLLEK-GADINVKD 91
FERM_B-lobe cd14473
FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C ...
 531-631 3.14e-11

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: 60.34  E-value: 3.14e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387763004 531 LFDEARYNLLKGFYTAPDAKLITLASLLLQIVYGNYESKKHKQGFLneeNLKSIVPVTKLKSKAPH-WTNRILHEYKNLS 609
Cdd:cd14473    5 LYLQVKRDILEGRLPCSEETAALLAALALQAEYGDYDPSEHKPKYL---SLKRFLPKQLLKQRKPEeWEKRIVELHKKLR 81

                         90       100
                 ....*....|....*....|..
gi 387763004 610 tseGVSKemHHLQRMFLQNCWE 631
Cdd:cd14473   82 ---GLSP--AEAKLKYLKIARK 98
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 296-381 2.82e-06

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 50.67  E-value: 2.82e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387763004 296 ACEGDSELLSRLLSERFSVNQLDSDHWAPIHYACWYGKVEATRILLEKGkCNPNLLNGQLSSPLHFAAGGGHAEIVQILL 375
Cdd:PTZ00322  90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFG-ADPTLLDKDGKTPLELAEENGFREVVQLLS 168


                 ....*.
gi 387763004 376 NHPEID 381
Cdd:PTZ00322 169 RHSQCH 174
 
Name Accession Description Interval E-value
NUDIX_5 pfam16705
NUDIX, or N-terminal NPxY motif-rich, region of KRIT; NUDIX_5 is found in higher eukaryotes at ...
 30-198 7.03e-104

NUDIX, or N-terminal NPxY motif-rich, region of KRIT; NUDIX_5 is found in higher eukaryotes at the N-terminus of KRIT1 or Krev interaction trapped proteins. NUDIX_5 carries three NPxY-like motifs, and it is found to bind the integrin cytoplasmic-associated protein 1 ICAP1. In the absence of KRIT1 ICAP1 binds via its C-terminal PH/PTB fold domain to the integrin beta-1 cytoplasmic tail. Binding of KRIT1 to ICAP1 via NUDIX_5 out-competes the binding of ICAP1 to integrin cytoplasmic tails such that ICAP1 is sequestered in the nucleus. Integrin activation is thus prevented.


Pssm-ID: 465241  Cd Length: 169  Bit Score: 315.15  E-value: 7.03e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387763004   30 AKSYEILLHEVPIEGQKKKRKKVLLETKLQGNSEITQGILDYVVETTKPISPANQGIRGKRVVLMKKFPLDGEKMGREAS 109
Cdd:pfam16705   1 AKSYEILLLEVPIEGKKKKRKKVLLETKLRGSQEATKQILDYVYETTKPISPDNQGIKGKRVVHMKKFPLDGEESGREAS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387763004  110 LFIVPSVVKDNTKYTYTPGCPIFYCFQDIMRVCSESSTHFATLTARMLIALDKWLDERHAQSHFIPALFRPSPLERIKTN 189
Cdd:pfam16705  81 LFVVPVNVKDNTKPSYSPGSPSFYCLQDIMRVCSESSTHFPTLTSRMLIALDKWLKEQHAVPHAIPALFRPSALERIKTN 160


                  ....*....
gi 387763004  190 VINPAYATE 198
Cdd:pfam16705 161 VSNPAYATE 169
FERM_C_CCM1 cd13197
FERM domain C-lobe of Cerebral cavernous malformation 1; CCM1 (also called KRIT-1/Krev ...
 636-735 4.33e-63

FERM domain C-lobe of Cerebral cavernous malformation 1; CCM1 (also called KRIT-1/Krev interaction trapped 1;ankyrin repeat-containing protein Krit1; CAM), a Rap1-binding protein, is expressed in endothelial cells where it is present in cell-cell junctions and associated with junctional proteins. Together with CCM2/MGC4607 and CCM3/PDCD10, KRIT1 constitutes a set of proteins, mutations of which are found in cerebral cavernous malformations which are characterized by cerebral hemorrhages and vascular malformations in the central nervous system. KRIT-1 possesses four ankyrin repeats, a FERM domain, and multiple NPXY sequences, one of which is essential for integrin cytoplasmic domain-associated protein-1alpha (ICAP1alpha) binding and all of which mediate binding of CCM2. KRIT-1 localization is mediated by its FERM domain. 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: 270018  Cd Length: 100  Bit Score: 205.54  E-value: 4.33e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387763004 636 GAAFFTGQIFTKASPSNHKVIPVYVGVNIKGLHLLNMETKALLISLNYGCFMWQLGDADTCFQIHSMENKMSFIVHTKQA 715
Cdd:cd13197    1 GAAFFTGQIFTKASSSNHKVIPVYVGVNIKGLHLLNMETKALLLSLKYGCFMWQLGDADTCFQIHSLENKMSFVVHTKQA 80

                         90       100
                 ....*....|....*....|
gi 387763004 716 GLVVKLLMKLNGQLMPTERN 735
Cdd:cd13197   81 GLIVKLLMKLSGQRKPNDRN 100
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 421-640 3.51e-37

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: 137.81  E-value: 3.51e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387763004   421 KVRIYRMDGSyrSVELKHGNNTTVQQIMEGMRLSQETqqyftiwICSENLSLQLKPYHKPLQHvrdWPEILAELTNLDPQ 500
Cdd:smart00295   1 VLKVYLLDGT--TLEFEVDSSTTAEELLETVCRKLGI-------RESEYFGLQFEDPDEDLRH---WLDPAKTLLDQDVK 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387763004   501 RETSQLFLRRDVRLPlEVEKQIEDPLAILILFDEARYNLLKGFYTAPDAKLITLASLLLQIVYGNYESKKHKQgfLNEEN 580
Cdd:smart00295  69 SEPLTLYFRVKFYPP-DPNQLKEDPTRLNLLYLQVRNDILEGRLPCPEEEALLLAALALQAEFGDYDEELHDL--RGELS 145

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 387763004   581 LKSIVPVTKLKS-KAPHWTNRILHEYKNLStsegvSKEMHHLQRMFLQNCWEIPTYGAAFF 640
Cdd:smart00295 146 LKRFLPKQLLDSrKLKEWRERIVELHKELI-----GLSPEEAKLKYLELARKLPTYGVELF 201
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
 517-640 7.87e-28

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


Pssm-ID: 459788 [Multi-domain]  Cd Length: 117  Bit Score: 108.51  E-value: 7.87e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387763004  517 EVEKQIEDPLAILILFDEARYNLLKGFYTAPDAKLITLASLLLQIVYGNYESKKHKQGFLneeNLKSIVPVTKL-KSKAP 595
Cdd:pfam00373   1 DLELLLQDEVTRHLLYLQAKDDILEGRLPCSEEEALLLAALQLQAEFGDYQPSSHTSEYL---SLESFLPKQLLrKMKSK 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 387763004  596 HWTNRILHEYKNLStsegvSKEMHHLQRMFLQNCWEIPTYGAAFF 640
Cdd:pfam00373  78 ELEKRVLEAHKNLR-----GLSAEEAKLKYLQIAQSLPTYGVEFF 117
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
291-414 5.30e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 96.95  E-value: 5.30e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387763004 291 PLHRSACEGDSELLSRLLSERFSVNQLDSDHWAPIHYACWYGKVEATRILLEKGkCNPNLLNGQLSSPLHFAAGGGHAEI 370
Cdd:COG0666   90 LLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAG-ADVNAQDNDGNTPLHLAAANGNLEI 168

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 387763004 371 VQILLNHPeIDRHITDQQGRSPLNICEENKQnnwEEAAKLLKEA 414
Cdd:COG0666  169 VKLLLEAG-ADVNARDNDGETPLHLAAENGH---LEIVKLLLEA 208
Ank_2 pfam12796
Ankyrin repeats (3 copies);
292-386 1.07e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.84  E-value: 1.07e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387763004  292 LHRSACEGDSELLSRLLSERFSVNQLDSDHWAPIHYACWYGKVEATRILLEKGKCNpNLLNGQlsSPLHFAAGGGHAEIV 371
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVN-LKDNGR--TALHYAARSGHLEIV 77

                          90
                  ....*....|....*
gi 387763004  372 QILLNHpEIDRHITD 386
Cdd:pfam12796  78 KLLLEK-GADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
291-421 4.99e-15

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 76.15  E-value: 4.99e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387763004 291 PLHRSACEGDSELLSRLLSERFSVNQLDSDHWAPIHYACWYGKVEATRILLEKGKcNPNLLNGQLSSPLHFAAGGGHAEI 370
Cdd:COG0666  156 PLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGA-DVNAKDNDGKTALDLAAENGNLEI 234

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 387763004 371 VQILLNHPEIDRHITDQQGRSPLNICEENKQNNWEEAAKLLKEAINKPYEK 421
Cdd:COG0666  235 VKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDL 285
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
288-414 2.73e-14

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 74.22  E-value: 2.73e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387763004 288 DDFPLHRSACEGDSELLSRLLSERFSVNQLDSDHWAPIHYACWYGKVEATRILLEKGKcNPNLLNGQLSSPLHFAAGGGH 367
Cdd:COG0666   54 GALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGA-DVNARDKDGETPLHLAAYNGN 132

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 387763004 368 AEIVQILLNHpEIDRHITDQQGRSPLNI-CeenkQNNWEEAAKLLKEA 414
Cdd:COG0666  133 LEIVKLLLEA-GADVNAQDNDGNTPLHLaA----ANGNLEIVKLLLEA 175
FERM_B-lobe cd14473
FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C ...
 531-631 3.14e-11

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: 60.34  E-value: 3.14e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387763004 531 LFDEARYNLLKGFYTAPDAKLITLASLLLQIVYGNYESKKHKQGFLneeNLKSIVPVTKLKSKAPH-WTNRILHEYKNLS 609
Cdd:cd14473    5 LYLQVKRDILEGRLPCSEETAALLAALALQAEYGDYDPSEHKPKYL---SLKRFLPKQLLKQRKPEeWEKRIVELHKKLR 81

                         90       100
                 ....*....|....*....|..
gi 387763004 610 tseGVSKemHHLQRMFLQNCWE 631
Cdd:cd14473   82 ---GLSP--AEAKLKYLKIARK 98
Ank_5 pfam13857
Ankyrin repeats (many copies);
340-396 2.32e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 53.50  E-value: 2.32e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 387763004  340 LLEKGKCNPNLLNGQLSSPLHFAAGGGHAEIVQILLNHPEiDRHITDQQGRSPLNIC 396
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGV-DLNLKDEEGLTALDLA 56
FERM_C-lobe cd00836
FERM domain C-lobe; The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N ...
 636-730 2.32e-09

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: 54.69  E-value: 2.32e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387763004 636 GAAFFTGQIFTKaspsnhKVIPVYVGVNIKGLHLLNMETKALLISLNYGC-FMWQLGDaDTCFQIHSM--ENKMSFIVHT 712
Cdd:cd00836    1 GVEFFPVKDKSK------KGSPIILGVNPEGISVYDELTGQPLVLFPWPNiKKISFSG-AKKFTIVVAdeDKQSKLLFQT 73

                         90       100
                 ....*....|....*....|
gi 387763004 713 --KQAGLVVKLLMKLNGQLM 730
Cdd:cd00836   74 psRQAKEIWKLIVGYHRFLL 93
Ank_4 pfam13637
Ankyrin repeats (many copies);
321-375 3.81e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.05  E-value: 3.81e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 387763004  321 HWAPIHYACWYGKVEATRILLEKGKcNPNLLNGQLSSPLHFAAGGGHAEIVQILL 375
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGA-DINAVDGNGETALHFAASNGNVEVLKLLL 54
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
288-414 3.08e-07

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 52.65  E-value: 3.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387763004 288 DDFPLHRSACEGDSELLSRLLSERFSVNQLDSDHWAPIHYACWYGKVEATRILLEKGKCNPNLLNGQLSSPLHFAAGGGH 367
Cdd:COG0666   20 LLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGD 99

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 387763004 368 AEIVQILLNHPeIDRHITDQQGRSPLNICEENKQnnwEEAAKLLKEA 414
Cdd:COG0666  100 LEIVKLLLEAG-ADVNARDKDGETPLHLAAYNGN---LEIVKLLLEA 142
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 296-381 2.82e-06

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 50.67  E-value: 2.82e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387763004 296 ACEGDSELLSRLLSERFSVNQLDSDHWAPIHYACWYGKVEATRILLEKGkCNPNLLNGQLSSPLHFAAGGGHAEIVQILL 375
Cdd:PTZ00322  90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFG-ADPTLLDKDGKTPLELAEENGFREVVQLLS 168


                 ....*.
gi 387763004 376 NHPEID 381
Cdd:PTZ00322 169 RHSQCH 174
Ank_2 pfam12796
Ankyrin repeats (3 copies);
291-352 8.06e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 44.72  E-value: 8.06e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 387763004  291 PLHRSACEGDSELLSRLLsERFSVNqLDSDHWAPIHYACWYGKVEATRILLEKGkCNPNLLN 352
Cdd:pfam12796  33 ALHLAAKNGHLEIVKLLL-EHADVN-LKDNGRTALHYAARSGHLEIVKLLLEKG-ADINVKD 91
Ank_4 pfam13637
Ankyrin repeats (many copies);
291-341 4.77e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.49  E-value: 4.77e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 387763004  291 PLHRSACEGDSELLSRLLSERFSVNQLDSDHWAPIHYACWYGKVEATRILL 341
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 306-395 5.76e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 46.20  E-value: 5.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387763004 306 RLLSERFSVNQLDSDHWAPIHYACWYGKVEATRILLEKGkCNPNLLNGQLSSPLHFAAGGGHAEIVQILLNHPE----ID 381
Cdd:PHA03100 177 YLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLG-ANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPsiktII 255

                         90
                 ....*....|....
gi 387763004 382 RHITDQQGRSPLNI 395
Cdd:PHA03100 256 ETLLYFKDKDLNTI 269
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 292-394 6.58e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 46.11  E-value: 6.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387763004 292 LHRSACEGDSELLSRLLSERFSVNQLDSDHWAPIHYACWYGKVEATRILLEKGkCNPNLLNGQLSSPLHFAAGGGHAEIV 371
Cdd:PHA02874 128 LHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKG-AYANVKDNNGESPLHNAAEYGDYACI 206

                         90       100
                 ....*....|....*....|....*
gi 387763004 372 QILLNHpeiDRHITDQ--QGRSPLN 394
Cdd:PHA02874 207 KLLIDH---GNHIMNKckNGFTPLH 228
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 338-411 2.88e-04

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.12  E-value: 2.88e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 387763004 338 RILLEKGkCNPNLLNGQLSSPLHFAAGGGHAEIVQILLNHPEiDRHITDQQGRSPLNICEEnkqNNWEEAAKLL 411
Cdd:PTZ00322  99 RILLTGG-ADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGA-DPTLLDKDGKTPLELAEE---NGFREVVQLL 167
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 287-416 4.25e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 43.70  E-value: 4.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387763004 287 VDDFPLHRSACEGDSELLSRLLSERFSVNQLDSDHWAPIHYACWYGKVEATRILLEKGkCNPNLLNGQLSSPLHFAAGGG 366
Cdd:PLN03192 524 NMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHA-CNVHIRDANGNTALWNAISAK 602

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 387763004 367 HAEIVQILLNHPeidrHITDQQGRSPLnICEENKQNNWEEAAKLLKEAIN 416
Cdd:PLN03192 603 HHKIFRILYHFA----SISDPHAAGDL-LCTAAKRNDLTAMKELLKQGLN 647
Ank_5 pfam13857
Ankyrin repeats (many copies);
310-362 5.11e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.48  E-value: 5.11e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 387763004  310 ERFSVNQLDSDHWA--PIHYACWYGKVEATRILLEKGkCNPNLLNGQLSSPLHFA 362
Cdd:pfam13857   3 EHGPIDLNRLDGEGytPLHVAAKYGALEIVRVLLAYG-VDLNLKDEEGLTALDLA 56
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 291-393 6.60e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 42.67  E-value: 6.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387763004 291 PLHRSACEGDSELLSRLL-SERFSVNQLDSDHWAPIHYACWYGKVEATRILLEKGkCNPNLLNGQLSSPLHFAAGGGHAE 369
Cdd:PHA02875  71 ELHDAVEEGDVKAVEELLdLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARG-ADPDIPNTDKFSPLHLAVMMGDIK 149

                         90       100
                 ....*....|....*....|....
gi 387763004 370 IVQILLNHpEIDRHITDQQGRSPL 393
Cdd:PHA02875 150 GIELLIDH-KACLDIEDCCGCTPL 172
 
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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