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Conserved domains on  [gi|1183596659|ref|NP_001337600|]
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krev interaction trapped protein 1 isoform 3 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FERM_C_CCM1 cd13197
FERM domain C-lobe of Cerebral cavernous malformation 1; CCM1 (also called KRIT-1/Krev ...
 398-497 3.89e-65

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: 3.89e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596659 398 GAAFFTGQIFTKASPSNHKVIPVYVGVNIKGLHLLNMETKALLISLKYGCFMWQLGDTDTCFQIHSMENKMSFIVHTKQA 477
Cdd:cd13197     1 GAAFFTGQIFTKASSSNHKVIPVYVGVNIKGLHLLNMETKALLLSLKYGCFMWQLGDADTCFQIHSLENKMSFVVHTKQA 80

                          90       100
                  ....*....|....*....|
gi 1183596659 478 GLVVKLLMKLNGQLMPTERN 497
Cdd:cd13197    81 GLIVKLLMKLSGQRKPNDRN 100
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 183-402 8.11e-38

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: 137.43  E-value: 8.11e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596659  183 KVRIYRMDGSyrSVELKHGNNTTVQQIMEGMRLSQETqqyftiwICSENLSLQLKPYHKPLQHvrdWPEILAELTNLDPQ 262
Cdd:smart00295   1 VLKVYLLDGT--TLEFEVDSSTTAEELLETVCRKLGI-------RESEYFGLQFEDPDEDLRH---WLDPAKTLLDQDVK 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596659  263 RETPQLFLRRDVRLPlEVEKQIEDPLAILILFDEARYNLLKGFYTAPDAKLITLASLLLQIVYGNYESKKHKQgfLNEEN 342
Cdd:smart00295  69 SEPLTLYFRVKFYPP-DPNQLKEDPTRLNLLYLQVRNDILEGRLPCPEEEALLLAALALQAEFGDYDEELHDL--RGELS 145

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1183596659  343 LKSIVPVTKLKS-KAPHWTNRILHEYKNLStsegvSKEMHHLQRMFLQNCWEIPTYGAAFF 402
Cdd:smart00295 146 LKRFLPKQLLDSrKLKEWRERIVELHKELI-----GLSPEEAKLKYLELARKLPTYGVELF 201
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
53-176 5.22e-22

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 96.18  E-value: 5.22e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596659  53 PLHRSACEGDSELLSRLLSERFSVNQLDSDHWAPIHYACWYGKVEATRILLEKGkCNPNLLNGQLSSPLHFAAGGGHAEI 132
Cdd:COG0666    90 LLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAG-ADVNAQDNDGNTPLHLAAANGNLEI 168

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1183596659 133 VQILLNHPeTDRHITDQQGRSPLNICEENKQnnwEEAAKLLKEA 176
Cdd:COG0666   169 VKLLLEAG-ADVNARDNDGETPLHLAAENGH---LEIVKLLLEA 208
 
Name Accession Description Interval E-value
FERM_C_CCM1 cd13197
FERM domain C-lobe of Cerebral cavernous malformation 1; CCM1 (also called KRIT-1/Krev ...
 398-497 3.89e-65

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: 3.89e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596659 398 GAAFFTGQIFTKASPSNHKVIPVYVGVNIKGLHLLNMETKALLISLKYGCFMWQLGDTDTCFQIHSMENKMSFIVHTKQA 477
Cdd:cd13197     1 GAAFFTGQIFTKASSSNHKVIPVYVGVNIKGLHLLNMETKALLLSLKYGCFMWQLGDADTCFQIHSLENKMSFVVHTKQA 80

                          90       100
                  ....*....|....*....|
gi 1183596659 478 GLVVKLLMKLNGQLMPTERN 497
Cdd:cd13197    81 GLIVKLLMKLSGQRKPNDRN 100
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 183-402 8.11e-38

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: 137.43  E-value: 8.11e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596659  183 KVRIYRMDGSyrSVELKHGNNTTVQQIMEGMRLSQETqqyftiwICSENLSLQLKPYHKPLQHvrdWPEILAELTNLDPQ 262
Cdd:smart00295   1 VLKVYLLDGT--TLEFEVDSSTTAEELLETVCRKLGI-------RESEYFGLQFEDPDEDLRH---WLDPAKTLLDQDVK 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596659  263 RETPQLFLRRDVRLPlEVEKQIEDPLAILILFDEARYNLLKGFYTAPDAKLITLASLLLQIVYGNYESKKHKQgfLNEEN 342
Cdd:smart00295  69 SEPLTLYFRVKFYPP-DPNQLKEDPTRLNLLYLQVRNDILEGRLPCPEEEALLLAALALQAEFGDYDEELHDL--RGELS 145

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1183596659  343 LKSIVPVTKLKS-KAPHWTNRILHEYKNLStsegvSKEMHHLQRMFLQNCWEIPTYGAAFF 402
Cdd:smart00295 146 LKRFLPKQLLDSrKLKEWRERIVELHKELI-----GLSPEEAKLKYLELARKLPTYGVELF 201
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
 279-402 1.76e-27

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


Pssm-ID: 459788 [Multi-domain]  Cd Length: 117  Bit Score: 106.20  E-value: 1.76e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596659 279 EVEKQIEDPLAILILFDEARYNLLKGFYTAPDAKLITLASLLLQIVYGNYESKKHKQGFLneeNLKSIVPVTKL-KSKAP 357
Cdd:pfam00373   1 DLELLLQDEVTRHLLYLQAKDDILEGRLPCSEEEALLLAALQLQAEFGDYQPSSHTSEYL---SLESFLPKQLLrKMKSK 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1183596659 358 HWTNRILHEYKNLStsegvSKEMHHLQRMFLQNCWEIPTYGAAFF 402
Cdd:pfam00373  78 ELEKRVLEAHKNLR-----GLSAEEAKLKYLQIAQSLPTYGVEFF 117
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
53-176 5.22e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 96.18  E-value: 5.22e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596659  53 PLHRSACEGDSELLSRLLSERFSVNQLDSDHWAPIHYACWYGKVEATRILLEKGkCNPNLLNGQLSSPLHFAAGGGHAEI 132
Cdd:COG0666    90 LLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAG-ADVNAQDNDGNTPLHLAAANGNLEI 168

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1183596659 133 VQILLNHPeTDRHITDQQGRSPLNICEENKQnnwEEAAKLLKEA 176
Cdd:COG0666   169 VKLLLEAG-ADVNARDNDGETPLHLAAENGH---LEIVKLLLEA 208
Ank_2 pfam12796
Ankyrin repeats (3 copies);
54-139 1.21e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.07  E-value: 1.21e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596659  54 LHRSACEGDSELLSRLLSERFSVNQLDSDHWAPIHYACWYGKVEATRILLEKGKCNpNLLNGQlsSPLHFAAGGGHAEIV 133
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVN-LKDNGR--TALHYAARSGHLEIV 77


                  ....*.
gi 1183596659 134 QILLNH 139
Cdd:pfam12796  78 KLLLEK 83
FERM_B-lobe cd14473
FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C ...
 293-393 5.55e-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: 59.18  E-value: 5.55e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596659 293 LFDEARYNLLKGFYTAPDAKLITLASLLLQIVYGNYESKKHKQGFLneeNLKSIVPVTKLKSKAPH-WTNRILHEYKNLS 371
Cdd:cd14473     5 LYLQVKRDILEGRLPCSEETAALLAALALQAEYGDYDPSEHKPKYL---SLKRFLPKQLLKQRKPEeWEKRIVELHKKLR 81

                          90       100
                  ....*....|....*....|..
gi 1183596659 372 tseGVSKemHHLQRMFLQNCWE 393
Cdd:cd14473    82 ---GLSP--AEAKLKYLKIARK 98
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 58-143 1.28e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.05  E-value: 1.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596659  58 ACEGDSELLSRLLSERFSVNQLDSDHWAPIHYACWYGKVEATRILLEKGkCNPNLLNGQLSSPLHFAAGGGHAEIVQILL 137
Cdd:PTZ00322   90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFG-ADPTLLDKDGKTPLELAEENGFREVVQLLS 168


                  ....*.
gi 1183596659 138 NHPETD 143
Cdd:PTZ00322  169 RHSQCH 174
 
Name Accession Description Interval E-value
FERM_C_CCM1 cd13197
FERM domain C-lobe of Cerebral cavernous malformation 1; CCM1 (also called KRIT-1/Krev ...
 398-497 3.89e-65

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: 3.89e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596659 398 GAAFFTGQIFTKASPSNHKVIPVYVGVNIKGLHLLNMETKALLISLKYGCFMWQLGDTDTCFQIHSMENKMSFIVHTKQA 477
Cdd:cd13197     1 GAAFFTGQIFTKASSSNHKVIPVYVGVNIKGLHLLNMETKALLLSLKYGCFMWQLGDADTCFQIHSLENKMSFVVHTKQA 80

                          90       100
                  ....*....|....*....|
gi 1183596659 478 GLVVKLLMKLNGQLMPTERN 497
Cdd:cd13197    81 GLIVKLLMKLSGQRKPNDRN 100
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 183-402 8.11e-38

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: 137.43  E-value: 8.11e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596659  183 KVRIYRMDGSyrSVELKHGNNTTVQQIMEGMRLSQETqqyftiwICSENLSLQLKPYHKPLQHvrdWPEILAELTNLDPQ 262
Cdd:smart00295   1 VLKVYLLDGT--TLEFEVDSSTTAEELLETVCRKLGI-------RESEYFGLQFEDPDEDLRH---WLDPAKTLLDQDVK 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596659  263 RETPQLFLRRDVRLPlEVEKQIEDPLAILILFDEARYNLLKGFYTAPDAKLITLASLLLQIVYGNYESKKHKQgfLNEEN 342
Cdd:smart00295  69 SEPLTLYFRVKFYPP-DPNQLKEDPTRLNLLYLQVRNDILEGRLPCPEEEALLLAALALQAEFGDYDEELHDL--RGELS 145

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1183596659  343 LKSIVPVTKLKS-KAPHWTNRILHEYKNLStsegvSKEMHHLQRMFLQNCWEIPTYGAAFF 402
Cdd:smart00295 146 LKRFLPKQLLDSrKLKEWRERIVELHKELI-----GLSPEEAKLKYLELARKLPTYGVELF 201
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
 279-402 1.76e-27

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


Pssm-ID: 459788 [Multi-domain]  Cd Length: 117  Bit Score: 106.20  E-value: 1.76e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596659 279 EVEKQIEDPLAILILFDEARYNLLKGFYTAPDAKLITLASLLLQIVYGNYESKKHKQGFLneeNLKSIVPVTKL-KSKAP 357
Cdd:pfam00373   1 DLELLLQDEVTRHLLYLQAKDDILEGRLPCSEEEALLLAALQLQAEFGDYQPSSHTSEYL---SLESFLPKQLLrKMKSK 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1183596659 358 HWTNRILHEYKNLStsegvSKEMHHLQRMFLQNCWEIPTYGAAFF 402
Cdd:pfam00373  78 ELEKRVLEAHKNLR-----GLSAEEAKLKYLQIAQSLPTYGVEFF 117
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
53-176 5.22e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 96.18  E-value: 5.22e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596659  53 PLHRSACEGDSELLSRLLSERFSVNQLDSDHWAPIHYACWYGKVEATRILLEKGkCNPNLLNGQLSSPLHFAAGGGHAEI 132
Cdd:COG0666    90 LLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAG-ADVNAQDNDGNTPLHLAAANGNLEI 168

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1183596659 133 VQILLNHPeTDRHITDQQGRSPLNICEENKQnnwEEAAKLLKEA 176
Cdd:COG0666   169 VKLLLEAG-ADVNARDNDGETPLHLAAENGH---LEIVKLLLEA 208
Ank_2 pfam12796
Ankyrin repeats (3 copies);
54-139 1.21e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.07  E-value: 1.21e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596659  54 LHRSACEGDSELLSRLLSERFSVNQLDSDHWAPIHYACWYGKVEATRILLEKGKCNpNLLNGQlsSPLHFAAGGGHAEIV 133
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVN-LKDNGR--TALHYAARSGHLEIV 77


                  ....*.
gi 1183596659 134 QILLNH 139
Cdd:pfam12796  78 KLLLEK 83
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
53-183 5.37e-15

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 75.38  E-value: 5.37e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596659  53 PLHRSACEGDSELLSRLLSERFSVNQLDSDHWAPIHYACWYGKVEATRILLEKGKcNPNLLNGQLSSPLHFAAGGGHAEI 132
Cdd:COG0666   156 PLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGA-DVNAKDNDGKTALDLAAENGNLEI 234

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1183596659 133 VQILLNHPETDRHITDQQGRSPLNICEENKQNNWEEAAKLLKEAINKPYEK 183
Cdd:COG0666   235 VKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDL 285
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
50-176 7.80e-14

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 71.91  E-value: 7.80e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596659  50 DDFPLHRSACEGDSELLSRLLSERFSVNQLDSDHWAPIHYACWYGKVEATRILLEKGKcNPNLLNGQLSSPLHFAAGGGH 129
Cdd:COG0666    54 GALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGA-DVNARDKDGETPLHLAAYNGN 132

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1183596659 130 AEIVQILLNHpETDRHITDQQGRSPLNI-CeenkQNNWEEAAKLLKEA 176
Cdd:COG0666   133 LEIVKLLLEA-GADVNAQDNDGNTPLHLaA----ANGNLEIVKLLLEA 175
Ank_2 pfam12796
Ankyrin repeats (3 copies);
87-173 3.53e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 65.14  E-value: 3.53e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596659  87 IHYACWYGKVEATRILLEKGkCNPNLLNGQLSSPLHFAAGGGHAEIVQILLNHPETDRhitDQQGRSPLNICEENKQnnw 166
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENG-ADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL---KDNGRTALHYAARSGH--- 73


                  ....*..
gi 1183596659 167 EEAAKLL 173
Cdd:pfam12796  74 LEIVKLL 80
FERM_B-lobe cd14473
FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C ...
 293-393 5.55e-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: 59.18  E-value: 5.55e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596659 293 LFDEARYNLLKGFYTAPDAKLITLASLLLQIVYGNYESKKHKQGFLneeNLKSIVPVTKLKSKAPH-WTNRILHEYKNLS 371
Cdd:cd14473     5 LYLQVKRDILEGRLPCSEETAALLAALALQAEYGDYDPSEHKPKYL---SLKRFLPKQLLKQRKPEeWEKRIVELHKKLR 81

                          90       100
                  ....*....|....*....|..
gi 1183596659 372 tseGVSKemHHLQRMFLQNCWE 393
Cdd:cd14473    82 ---GLSP--AEAKLKYLKIARK 98
FERM_C-lobe cd00836
FERM domain C-lobe; The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N ...
 398-492 1.01e-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: 55.46  E-value: 1.01e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596659 398 GAAFFTGQIFTKaspsnhKVIPVYVGVNIKGLHLLNMETKALLISLKYGC-FMWQLGDtDTCFQIHSM--ENKMSFIVHT 474
Cdd:cd00836     1 GVEFFPVKDKSK------KGSPIILGVNPEGISVYDELTGQPLVLFPWPNiKKISFSG-AKKFTIVVAdeDKQSKLLFQT 73

                          90       100
                  ....*....|....*....|
gi 1183596659 475 --KQAGLVVKLLMKLNGQLM 492
Cdd:cd00836    74 psRQAKEIWKLIVGYHRFLL 93
Ank_5 pfam13857
Ankyrin repeats (many copies);
102-158 2.30e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 53.12  E-value: 2.30e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1183596659 102 LLEKGKCNPNLLNGQLSSPLHFAAGGGHAEIVQILLNHPEtDRHITDQQGRSPLNIC 158
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGV-DLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
83-137 5.09e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.28  E-value: 5.09e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1183596659  83 HWAPIHYACWYGKVEATRILLEKGKcNPNLLNGQLSSPLHFAAGGGHAEIVQILL 137
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGA-DINAVDGNGETALHFAASNGNVEVLKLLL 54
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
50-176 3.75e-07

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 51.88  E-value: 3.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596659  50 DDFPLHRSACEGDSELLSRLLSERFSVNQLDSDHWAPIHYACWYGKVEATRILLEKGKCNPNLLNGQLSSPLHFAAGGGH 129
Cdd:COG0666    20 LLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGD 99

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1183596659 130 AEIVQILLNHPeTDRHITDQQGRSPLNICEENKQnnwEEAAKLLKEA 176
Cdd:COG0666   100 LEIVKLLLEAG-ADVNARDKDGETPLHLAAYNGN---LEIVKLLLEA 142
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 58-143 1.28e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.05  E-value: 1.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596659  58 ACEGDSELLSRLLSERFSVNQLDSDHWAPIHYACWYGKVEATRILLEKGkCNPNLLNGQLSSPLHFAAGGGHAEIVQILL 137
Cdd:PTZ00322   90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFG-ADPTLLDKDGKTPLELAEENGFREVVQLLS 168


                  ....*.
gi 1183596659 138 NHPETD 143
Cdd:PTZ00322  169 RHSQCH 174
Ank_2 pfam12796
Ankyrin repeats (3 copies);
53-114 7.47e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 44.34  E-value: 7.47e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1183596659  53 PLHRSACEGDSELLSRLLsERFSVNqLDSDHWAPIHYACWYGKVEATRILLEKGkCNPNLLN 114
Cdd:pfam12796  33 ALHLAAKNGHLEIVKLLL-EHADVN-LKDNGRTALHYAARSGHLEIVKLLLEKG-ADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 68-146 9.19e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 48.12  E-value: 9.19e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1183596659  68 RLLSERFSVNQLDSDHWAPIHYACWYGKVEATRILLEKGkCNPNLLNGQLSSPLHFAAGGGHAEIVQILLNHPETDRHI 146
Cdd:PHA03100  177 YLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLG-ANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTI 254
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 54-156 3.19e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 46.11  E-value: 3.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596659  54 LHRSACEGDSELLSRLLSERFSVNQLDSDHWAPIHYACWYGKVEATRILLEKGkCNPNLLNGQLSSPLHFAAGGGHAEIV 133
Cdd:PHA02874  128 LHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKG-AYANVKDNNGESPLHNAAEYGDYACI 206

                          90       100
                  ....*....|....*....|....*
gi 1183596659 134 QILLNHpetDRHITDQ--QGRSPLN 156
Cdd:PHA02874  207 KLLIDH---GNHIMNKckNGFTPLH 228
Ank_4 pfam13637
Ankyrin repeats (many copies);
53-103 5.04e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 40.72  E-value: 5.04e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1183596659  53 PLHRSACEGDSELLSRLLSERFSVNQLDSDHWAPIHYACWYGKVEATRILL 103
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 53-155 8.00e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 44.98  E-value: 8.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596659  53 PLHRSACEGDSELLSRLL-SERFSVNQLDSDHWAPIHYACWYGKVEATRILLEKGkCNPNLLNGQLSSPLHFAAGGGHAE 131
Cdd:PHA02875   71 ELHDAVEEGDVKAVEELLdLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARG-ADPDIPNTDKFSPLHLAVMMGDIK 149

                          90       100
                  ....*....|....*....|....
gi 1183596659 132 IVQILLNHPETdRHITDQQGRSPL 155
Cdd:PHA02875  150 GIELLIDHKAC-LDIEDCCGCTPL 172
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 100-173 1.30e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.50  E-value: 1.30e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1183596659 100 RILLEKGkCNPNLLNGQLSSPLHFAAGGGHAEIVQILLNHpETDRHITDQQGRSPLNICEEnkqNNWEEAAKLL 173
Cdd:PTZ00322   99 RILLTGG-ADPNCRDYDGRTPLHIACANGHVQVVRVLLEF-GADPTLLDKDGKTPLELAEE---NGFREVVQLL 167
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 49-178 2.53e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 43.70  E-value: 2.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596659  49 VDDFPLHRSACEGDSELLSRLLSERFSVNQLDSDHWAPIHYACWYGKVEATRILLEKGkCNPNLLNGQLSSPLHFAAGGG 128
Cdd:PLN03192  524 NMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHA-CNVHIRDANGNTALWNAISAK 602

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1183596659 129 HAEIVQILLNHPetdrHITDQQGRSPLnICEENKQNNWEEAAKLLKEAIN 178
Cdd:PLN03192  603 HHKIFRILYHFA----SISDPHAAGDL-LCTAAKRNDLTAMKELLKQGLN 647
Ank_5 pfam13857
Ankyrin repeats (many copies);
72-124 4.70e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.10  E-value: 4.70e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1183596659  72 ERFSVNQLDSDHWA--PIHYACWYGKVEATRILLEKGkCNPNLLNGQLSSPLHFA 124
Cdd:pfam13857   3 EHGPIDLNRLDGEGytPLHVAAKYGALEIVRVLLAYG-VDLNLKDEEGLTALDLA 56
 
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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