NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1183596639|ref|NP_001337598|]
View 

krev interaction trapped protein 1 isoform 2 [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 1.28e-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: 315.53  E-value: 1.28e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596639  30 AKSYEILLHEVPIEGQKKKRKKVLLETKLQGNSEITQGILDYVVETTKPISPANQGIRGKRVVLMKKFPLDGEKMGREAS 109
Cdd:pfam16705   1 AKSYEILLLEVPIEGKKKKRKKVLLETKLRGSQEATKQILDYVYETTKPISPDNQGIKGKRVVHMKKFPLDGEESGREAS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596639 110 LFIVPSVVKDNTKYTYTPGCPIFYCLQDIMRVCSESSTHFATLTARMLIALDKWLDERHAQSHFIPALFRPSPLERIKTN 189
Cdd:pfam16705  81 LFVVPVNVKDNTKPSYSPGSPSFYCLQDIMRVCSESSTHFPTLTSRMLIALDKWLKEQHAVPHAIPALFRPSALERIKTN 160


                  ....*....
gi 1183596639 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 ...
 588-687 1.33e-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: 205.93  E-value: 1.33e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596639 588 GAAFFTGQIFTKASPSNHKVIPVYVGVNIKGLHLLNMETKALLISLKYGCFMWQLGDTDTCFQIHSMENKMSFIVHTKQA 667
Cdd:cd13197     1 GAAFFTGQIFTKASSSNHKVIPVYVGVNIKGLHLLNMETKALLLSLKYGCFMWQLGDADTCFQIHSLENKMSFVVHTKQA 80

                          90       100
                  ....*....|....*....|
gi 1183596639 668 GLVVKLLMKLNGQLMPTERN 687
Cdd:cd13197    81 GLIVKLLMKLSGQRKPNDRN 100
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 373-592 5.41e-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: 140.12  E-value: 5.41e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596639  373 KVRIYRMDGSyrSVELKHGNNTTVQQIMEGMRLSQETqqyftiwICSENLSLQLKPYHKPLQHvrdWPEILAELTNLDPQ 452
Cdd:smart00295   1 VLKVYLLDGT--TLEFEVDSSTTAEELLETVCRKLGI-------RESEYFGLQFEDPDEDLRH---WLDPAKTLLDQDVK 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596639  453 RETPQLFLRRDVRLPlEVEKQIEDPLAILILFDEARYNLLKGFYTAPDAKLITLASLLLQIVYGNYESKKHKQgfLNEEN 532
Cdd:smart00295  69 SEPLTLYFRVKFYPP-DPNQLKEDPTRLNLLYLQVRNDILEGRLPCPEEEALLLAALALQAEFGDYDEELHDL--RGELS 145

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1183596639  533 LKSIVPVTKLKS-KAPHWTNRILHEYKNLStsegvSKEMHHLQRMFLQNCWEIPTYGAAFF 592
Cdd:smart00295 146 LKRFLPKQLLDSrKLKEWRERIVELHKELI-----GLSPEEAKLKYLELARKLPTYGVELF 201
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
282-373 1.90e-11

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 65.36  E-value: 1.90e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596639 282 KYGKVEATRILLEKGkCNPNLLNGQLSSPLHFAAGGGHAEIVQILLNHpETDRHITDQQGRSPLNICEENKQNnweEAAK 361
Cdd:COG0666   162 ANGNLEIVKLLLEAG-ADVNARDNDGETPLHLAAENGHLEIVKLLLEA-GADVNAKDNDGKTALDLAAENGNL---EIVK 236

                          90
                  ....*....|..
gi 1183596639 362 LLKEAINKPYEK 373
Cdd:COG0666   237 LLLEAGADLNAK 248
 
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 1.28e-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: 315.53  E-value: 1.28e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596639  30 AKSYEILLHEVPIEGQKKKRKKVLLETKLQGNSEITQGILDYVVETTKPISPANQGIRGKRVVLMKKFPLDGEKMGREAS 109
Cdd:pfam16705   1 AKSYEILLLEVPIEGKKKKRKKVLLETKLRGSQEATKQILDYVYETTKPISPDNQGIKGKRVVHMKKFPLDGEESGREAS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596639 110 LFIVPSVVKDNTKYTYTPGCPIFYCLQDIMRVCSESSTHFATLTARMLIALDKWLDERHAQSHFIPALFRPSPLERIKTN 189
Cdd:pfam16705  81 LFVVPVNVKDNTKPSYSPGSPSFYCLQDIMRVCSESSTHFPTLTSRMLIALDKWLKEQHAVPHAIPALFRPSALERIKTN 160


                  ....*....
gi 1183596639 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 ...
 588-687 1.33e-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: 205.93  E-value: 1.33e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596639 588 GAAFFTGQIFTKASPSNHKVIPVYVGVNIKGLHLLNMETKALLISLKYGCFMWQLGDTDTCFQIHSMENKMSFIVHTKQA 667
Cdd:cd13197     1 GAAFFTGQIFTKASSSNHKVIPVYVGVNIKGLHLLNMETKALLLSLKYGCFMWQLGDADTCFQIHSLENKMSFVVHTKQA 80

                          90       100
                  ....*....|....*....|
gi 1183596639 668 GLVVKLLMKLNGQLMPTERN 687
Cdd:cd13197    81 GLIVKLLMKLSGQRKPNDRN 100
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 373-592 5.41e-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: 140.12  E-value: 5.41e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596639  373 KVRIYRMDGSyrSVELKHGNNTTVQQIMEGMRLSQETqqyftiwICSENLSLQLKPYHKPLQHvrdWPEILAELTNLDPQ 452
Cdd:smart00295   1 VLKVYLLDGT--TLEFEVDSSTTAEELLETVCRKLGI-------RESEYFGLQFEDPDEDLRH---WLDPAKTLLDQDVK 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596639  453 RETPQLFLRRDVRLPlEVEKQIEDPLAILILFDEARYNLLKGFYTAPDAKLITLASLLLQIVYGNYESKKHKQgfLNEEN 532
Cdd:smart00295  69 SEPLTLYFRVKFYPP-DPNQLKEDPTRLNLLYLQVRNDILEGRLPCPEEEALLLAALALQAEFGDYDEELHDL--RGELS 145

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1183596639  533 LKSIVPVTKLKS-KAPHWTNRILHEYKNLStsegvSKEMHHLQRMFLQNCWEIPTYGAAFF 592
Cdd:smart00295 146 LKRFLPKQLLDSrKLKEWRERIVELHKELI-----GLSPEEAKLKYLELARKLPTYGVELF 201
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
 469-592 4.99e-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: 108.90  E-value: 4.99e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596639 469 EVEKQIEDPLAILILFDEARYNLLKGFYTAPDAKLITLASLLLQIVYGNYESKKHKQGFLneeNLKSIVPVTKL-KSKAP 547
Cdd:pfam00373   1 DLELLLQDEVTRHLLYLQAKDDILEGRLPCSEEEALLLAALQLQAEFGDYQPSSHTSEYL---SLESFLPKQLLrKMKSK 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1183596639 548 HWTNRILHEYKNLStsegvSKEMHHLQRMFLQNCWEIPTYGAAFF 592
Cdd:pfam00373  78 ELEKRVLEAHKNLR-----GLSAEEAKLKYLQIAQSLPTYGVEFF 117
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
282-373 1.90e-11

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 65.36  E-value: 1.90e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596639 282 KYGKVEATRILLEKGkCNPNLLNGQLSSPLHFAAGGGHAEIVQILLNHpETDRHITDQQGRSPLNICEENKQNnweEAAK 361
Cdd:COG0666   162 ANGNLEIVKLLLEAG-ADVNARDNDGETPLHLAAENGHLEIVKLLLEA-GADVNAKDNDGKTALDLAAENGNL---EIVK 236

                          90
                  ....*....|..
gi 1183596639 362 LLKEAINKPYEK 373
Cdd:COG0666   237 LLLEAGADLNAK 248
FERM_B-lobe cd14473
FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C ...
 483-583 2.78e-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: 2.78e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596639 483 LFDEARYNLLKGFYTAPDAKLITLASLLLQIVYGNYESKKHKQGFLneeNLKSIVPVTKLKSKAPH-WTNRILHEYKNLS 561
Cdd:cd14473     5 LYLQVKRDILEGRLPCSEETAALLAALALQAEYGDYDPSEHKPKYL---SLKRFLPKQLLKQRKPEeWEKRIVELHKKLR 81

                          90       100
                  ....*....|....*....|..
gi 1183596639 562 tseGVSKemHHLQRMFLQNCWE 583
Cdd:cd14473    82 ---GLSP--AEAKLKYLKIARK 98
Ank_2 pfam12796
Ankyrin repeats (3 copies);
282-363 1.53e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 58.20  E-value: 1.53e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596639 282 KYGKVEATRILLEKGkCNPNLLNGQLSSPLHFAAGGGHAEIVQILLNHPETDRhitDQQGRSPLNICEENKQnnwEEAAK 361
Cdd:pfam12796   6 KNGNLELVKLLLENG-ADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL---KDNGRTALHYAARSGH---LEIVK 78


                  ..
gi 1183596639 362 LL 363
Cdd:pfam12796  79 LL 80
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 290-363 2.04e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.50  E-value: 2.04e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1183596639 290 RILLEKGkCNPNLLNGQLSSPLHFAAGGGHAEIVQILLNHpETDRHITDQQGRSPLNICEEnkqNNWEEAAKLL 363
Cdd:PTZ00322   99 RILLTGG-ADPNCRDYDGRTPLHIACANGHVQVVRVLLEF-GADPTLLDKDGKTPLELAEE---NGFREVVQLL 167
 
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 1.28e-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: 315.53  E-value: 1.28e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596639  30 AKSYEILLHEVPIEGQKKKRKKVLLETKLQGNSEITQGILDYVVETTKPISPANQGIRGKRVVLMKKFPLDGEKMGREAS 109
Cdd:pfam16705   1 AKSYEILLLEVPIEGKKKKRKKVLLETKLRGSQEATKQILDYVYETTKPISPDNQGIKGKRVVHMKKFPLDGEESGREAS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596639 110 LFIVPSVVKDNTKYTYTPGCPIFYCLQDIMRVCSESSTHFATLTARMLIALDKWLDERHAQSHFIPALFRPSPLERIKTN 189
Cdd:pfam16705  81 LFVVPVNVKDNTKPSYSPGSPSFYCLQDIMRVCSESSTHFPTLTSRMLIALDKWLKEQHAVPHAIPALFRPSALERIKTN 160


                  ....*....
gi 1183596639 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 ...
 588-687 1.33e-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: 205.93  E-value: 1.33e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596639 588 GAAFFTGQIFTKASPSNHKVIPVYVGVNIKGLHLLNMETKALLISLKYGCFMWQLGDTDTCFQIHSMENKMSFIVHTKQA 667
Cdd:cd13197     1 GAAFFTGQIFTKASSSNHKVIPVYVGVNIKGLHLLNMETKALLLSLKYGCFMWQLGDADTCFQIHSLENKMSFVVHTKQA 80

                          90       100
                  ....*....|....*....|
gi 1183596639 668 GLVVKLLMKLNGQLMPTERN 687
Cdd:cd13197    81 GLIVKLLMKLSGQRKPNDRN 100
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 373-592 5.41e-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: 140.12  E-value: 5.41e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596639  373 KVRIYRMDGSyrSVELKHGNNTTVQQIMEGMRLSQETqqyftiwICSENLSLQLKPYHKPLQHvrdWPEILAELTNLDPQ 452
Cdd:smart00295   1 VLKVYLLDGT--TLEFEVDSSTTAEELLETVCRKLGI-------RESEYFGLQFEDPDEDLRH---WLDPAKTLLDQDVK 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596639  453 RETPQLFLRRDVRLPlEVEKQIEDPLAILILFDEARYNLLKGFYTAPDAKLITLASLLLQIVYGNYESKKHKQgfLNEEN 532
Cdd:smart00295  69 SEPLTLYFRVKFYPP-DPNQLKEDPTRLNLLYLQVRNDILEGRLPCPEEEALLLAALALQAEFGDYDEELHDL--RGELS 145

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1183596639  533 LKSIVPVTKLKS-KAPHWTNRILHEYKNLStsegvSKEMHHLQRMFLQNCWEIPTYGAAFF 592
Cdd:smart00295 146 LKRFLPKQLLDSrKLKEWRERIVELHKELI-----GLSPEEAKLKYLELARKLPTYGVELF 201
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
 469-592 4.99e-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: 108.90  E-value: 4.99e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596639 469 EVEKQIEDPLAILILFDEARYNLLKGFYTAPDAKLITLASLLLQIVYGNYESKKHKQGFLneeNLKSIVPVTKL-KSKAP 547
Cdd:pfam00373   1 DLELLLQDEVTRHLLYLQAKDDILEGRLPCSEEEALLLAALQLQAEFGDYQPSSHTSEYL---SLESFLPKQLLrKMKSK 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1183596639 548 HWTNRILHEYKNLStsegvSKEMHHLQRMFLQNCWEIPTYGAAFF 592
Cdd:pfam00373  78 ELEKRVLEAHKNLR-----GLSAEEAKLKYLQIAQSLPTYGVEFF 117
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
282-373 1.90e-11

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 65.36  E-value: 1.90e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596639 282 KYGKVEATRILLEKGkCNPNLLNGQLSSPLHFAAGGGHAEIVQILLNHpETDRHITDQQGRSPLNICEENKQNnweEAAK 361
Cdd:COG0666   162 ANGNLEIVKLLLEAG-ADVNARDNDGETPLHLAAENGHLEIVKLLLEA-GADVNAKDNDGKTALDLAAENGNL---EIVK 236

                          90
                  ....*....|..
gi 1183596639 362 LLKEAINKPYEK 373
Cdd:COG0666   237 LLLEAGADLNAK 248
FERM_B-lobe cd14473
FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C ...
 483-583 2.78e-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: 2.78e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596639 483 LFDEARYNLLKGFYTAPDAKLITLASLLLQIVYGNYESKKHKQGFLneeNLKSIVPVTKLKSKAPH-WTNRILHEYKNLS 561
Cdd:cd14473     5 LYLQVKRDILEGRLPCSEETAALLAALALQAEYGDYDPSEHKPKYL---SLKRFLPKQLLKQRKPEeWEKRIVELHKKLR 81

                          90       100
                  ....*....|....*....|..
gi 1183596639 562 tseGVSKemHHLQRMFLQNCWE 583
Cdd:cd14473    82 ---GLSP--AEAKLKYLKIARK 98
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
282-366 4.23e-11

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 64.20  E-value: 4.23e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596639 282 KYGKVEATRILLEKGkCNPNLLNGQLSSPLHFAAGGGHAEIVQILLNHPeTDRHITDQQGRSPLNICEENKQnnwEEAAK 361
Cdd:COG0666   129 YNGNLEIVKLLLEAG-ADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAG-ADVNARDNDGETPLHLAAENGH---LEIVK 203


                  ....*
gi 1183596639 362 LLKEA 366
Cdd:COG0666   204 LLLEA 208
Ank_2 pfam12796
Ankyrin repeats (3 copies);
282-363 1.53e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 58.20  E-value: 1.53e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596639 282 KYGKVEATRILLEKGkCNPNLLNGQLSSPLHFAAGGGHAEIVQILLNHPETDRhitDQQGRSPLNICEENKQnnwEEAAK 361
Cdd:pfam12796   6 KNGNLELVKLLLENG-ADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL---KDNGRTALHYAARSGH---LEIVK 78


                  ..
gi 1183596639 362 LL 363
Cdd:pfam12796  79 LL 80
FERM_C-lobe cd00836
FERM domain C-lobe; The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N ...
 588-682 1.03e-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: 55.84  E-value: 1.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596639 588 GAAFFTGQIFTKaspsnhKVIPVYVGVNIKGLHLLNMETKALLISLKYGC-FMWQLGDtDTCFQIHSM--ENKMSFIVHT 664
Cdd:cd00836     1 GVEFFPVKDKSK------KGSPIILGVNPEGISVYDELTGQPLVLFPWPNiKKISFSG-AKKFTIVVAdeDKQSKLLFQT 73

                          90       100
                  ....*....|....*....|
gi 1183596639 665 --KQAGLVVKLLMKLNGQLM 682
Cdd:cd00836    74 psRQAKEIWKLIVGYHRFLL 93
Ank_5 pfam13857
Ankyrin repeats (many copies);
292-348 1.89e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 53.89  E-value: 1.89e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1183596639 292 LLEKGKCNPNLLNGQLSSPLHFAAGGGHAEIVQILLNHPEtDRHITDQQGRSPLNIC 348
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGV-DLNLKDEEGLTALDLA 56
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
282-366 1.39e-08

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 56.89  E-value: 1.39e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596639 282 KYGKVEATRILLEKGKcNPNLLNGQLSSPLHFAAGGGHAEIVQILLNHpETDRHITDQQGRSPLNI-CeenkQNNWEEAA 360
Cdd:COG0666    96 RNGDLEIVKLLLEAGA-DVNARDKDGETPLHLAAYNGNLEIVKLLLEA-GADVNAQDNDGNTPLHLaA----ANGNLEIV 169


                  ....*.
gi 1183596639 361 KLLKEA 366
Cdd:COG0666   170 KLLLEA 175
Ank_4 pfam13637
Ankyrin repeats (many copies);
282-327 3.33e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.57  E-value: 3.33e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1183596639 282 KYGKVEATRILLEKGKcNPNLLNGQLSSPLHFAAGGGHAEIVQILL 327
Cdd:pfam13637  10 ASGHLELLRLLLEKGA-DINAVDGNGETALHFAASNGNVEVLKLLL 54
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
282-366 7.54e-06

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 48.41  E-value: 7.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596639 282 KYGKVEATRILLEKGKCNPNLLNGQLSSPLHFAAGGGHAEIVQILLNHPeTDRHITDQQGRSPLNICEENKQnnwEEAAK 361
Cdd:COG0666    62 ALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAG-ADVNARDKDGETPLHLAAYNGN---LEIVK 137


                  ....*
gi 1183596639 362 LLKEA 366
Cdd:COG0666   138 LLLEA 142
Ank_2 pfam12796
Ankyrin repeats (3 copies);
311-368 9.04e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 44.72  E-value: 9.04e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1183596639 311 LHFAAGGGHAEIVQILLNHPeTDRHITDQQGRSPLNICeenKQNNWEEAAKLLKEAIN 368
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENG-ADANLQDKNGRTALHLA---AKNGHLEIVKLLLEHAD 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
282-329 4.76e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 42.41  E-value: 4.76e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1183596639 282 KYGKVEATRILLEKGKCNpNLLNGQlsSPLHFAAGGGHAEIVQILLNH 329
Cdd:pfam12796  39 KNGHLEIVKLLLEHADVN-LKDNGR--TALHYAARSGHLEIVKLLLEK 83
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
282-373 7.68e-05

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 45.33  E-value: 7.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596639 282 KYGKVEATRILLEKGKcNPNLLNGQLSSPLHFAAGGGHAEIVQILLNHPETDRHITDQQGRSPLNICEENKQNNWEEAAK 361
Cdd:COG0666   195 ENGHLEIVKLLLEAGA-DVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLL 273

                          90
                  ....*....|..
gi 1183596639 362 LLKEAINKPYEK 373
Cdd:COG0666   274 ALLLLAAALLDL 285
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 290-363 2.04e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.50  E-value: 2.04e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1183596639 290 RILLEKGkCNPNLLNGQLSSPLHFAAGGGHAEIVQILLNHpETDRHITDQQGRSPLNICEEnkqNNWEEAAKLL 363
Cdd:PTZ00322   99 RILLTGG-ADPNCRDYDGRTPLHIACANGHVQVVRVLLEF-GADPTLLDKDGKTPLELAEE---NGFREVVQLL 167
 
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