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Conserved domains on  [gi|948549861|ref|NP_001303930|]
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krev interaction trapped protein 1 [Danio rerio]

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 ...
 30-197 4.83e-95

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: 292.03  E-value: 4.83e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549861   30 AKSYEILLIEVPLEGKEKKRKKVLLGTKIHADSDRTKSILEFVDETTKPIS-NNQGIIGKRVVHMRKFLLDGDSGGKEAS 108
Cdd:pfam16705   1 AKSYEILLLEVPIEGKKKKRKKVLLETKLRGSQEATKQILDYVYETTKPISpDNQGIKGKRVVHMKKFPLDGEESGREAS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549861  109 LFIVPINVKDNSKSVHHPGSPSFYCLQDIMRVCSETSAHFSSSTSKMLLALDKWLAEQHTVPHAIPALFRPAPVDRVKTN 188
Cdd:pfam16705  81 LFVVPVNVKDNTKPSYSPGSPSFYCLQDIMRVCSESSTHFPTLTSRMLIALDKWLKEQHAVPHAIPALFRPSALERIKTN 160


                  ....*....
gi 948549861  189 VSNPAYAVE 197
Cdd:pfam16705 161 VSNPAYATE 169
FERM_C_CCM1 cd13197
FERM domain C-lobe of Cerebral cavernous malformation 1; CCM1 (also called KRIT-1/Krev ...
 634-733 1.16e-56

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: 188.21  E-value: 1.16e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549861 634 GAAFFTGQVFTKASSSTHKVIRVYVGVNTKGLHLMNMETKVLHLSLEYGTFMWQLGQADQYVQIHSLENKKNFVVHTKQA 713
Cdd:cd13197    1 GAAFFTGQIFTKASSSNHKVIPVYVGVNIKGLHLLNMETKALLLSLKYGCFMWQLGDADTCFQIHSLENKMSFVVHTKQA 80

                         90       100
                 ....*....|....*....|
gi 948549861 714 GLIVKLLMKLSGQIAPNDRA 733
Cdd:cd13197   81 GLIVKLLMKLSGQRKPNDRN 100
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 419-638 6.37e-31

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: 120.09  E-value: 6.37e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549861   419 KVRIYRMDGSyrSVELKHGNNTTVQQIMEGMRLSQETqqyftiwICSENLSLQLKPYHKPLQH-LRMWSEIvtdlTALDP 497
Cdd:smart00295   1 VLKVYLLDGT--TLEFEVDSSTTAEELLETVCRKLGI-------RESEYFGLQFEDPDEDLRHwLDPAKTL----LDQDV 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549861   498 QRESPQLFLRRDVRLPlEVEKKVEDPLSILILFDEARHCLLKGFLSTSDNKLITLASLLLQIIYGNYDSKKHKQgfLNEE 577
Cdd:smart00295  68 KSEPLTLYFRVKFYPP-DPNQLKEDPTRLNLLYLQVRNDILEGRLPCPEEEALLLAALALQAEFGDYDEELHDL--RGEL 144

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 948549861   578 NLKSIVPISKVKSKAH-HWTNRILHEYKSLStsegvSKEMHHLQRLFLQNCWDIPTYGAAFF 638
Cdd:smart00295 145 SLKRFLPKQLLDSRKLkEWRERIVELHKELI-----GLSPEEAKLKYLELARKLPTYGVELF 201
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
289-409 1.32e-21

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 95.79  E-value: 1.32e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549861 289 PLHRSACEGDTELLSKLLDGGFSVKQLDSDHWAPIHYACWHGKVEATKLLLEKGnCNPNLLNGQLSSPLHFAAIGGHAEI 368
Cdd:COG0666   90 LLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAG-ADVNAQDNDGNTPLHLAAANGNLEI 168

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 948549861 369 VQLLLQHPeIDRHIEDQQKRSPLQVCEENKQnnwEETVNLL 409
Cdd:COG0666  169 VKLLLEAG-ADVNARDNDGETPLHLAAENGH---LEIVKLL 205
 
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 ...
 30-197 4.83e-95

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: 292.03  E-value: 4.83e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549861   30 AKSYEILLIEVPLEGKEKKRKKVLLGTKIHADSDRTKSILEFVDETTKPIS-NNQGIIGKRVVHMRKFLLDGDSGGKEAS 108
Cdd:pfam16705   1 AKSYEILLLEVPIEGKKKKRKKVLLETKLRGSQEATKQILDYVYETTKPISpDNQGIKGKRVVHMKKFPLDGEESGREAS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549861  109 LFIVPINVKDNSKSVHHPGSPSFYCLQDIMRVCSETSAHFSSSTSKMLLALDKWLAEQHTVPHAIPALFRPAPVDRVKTN 188
Cdd:pfam16705  81 LFVVPVNVKDNTKPSYSPGSPSFYCLQDIMRVCSESSTHFPTLTSRMLIALDKWLKEQHAVPHAIPALFRPSALERIKTN 160


                  ....*....
gi 948549861  189 VSNPAYAVE 197
Cdd:pfam16705 161 VSNPAYATE 169
FERM_C_CCM1 cd13197
FERM domain C-lobe of Cerebral cavernous malformation 1; CCM1 (also called KRIT-1/Krev ...
 634-733 1.16e-56

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: 188.21  E-value: 1.16e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549861 634 GAAFFTGQVFTKASSSTHKVIRVYVGVNTKGLHLMNMETKVLHLSLEYGTFMWQLGQADQYVQIHSLENKKNFVVHTKQA 713
Cdd:cd13197    1 GAAFFTGQIFTKASSSNHKVIPVYVGVNIKGLHLLNMETKALLLSLKYGCFMWQLGDADTCFQIHSLENKMSFVVHTKQA 80

                         90       100
                 ....*....|....*....|
gi 948549861 714 GLIVKLLMKLSGQIAPNDRA 733
Cdd:cd13197   81 GLIVKLLMKLSGQRKPNDRN 100
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 419-638 6.37e-31

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: 120.09  E-value: 6.37e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549861   419 KVRIYRMDGSyrSVELKHGNNTTVQQIMEGMRLSQETqqyftiwICSENLSLQLKPYHKPLQH-LRMWSEIvtdlTALDP 497
Cdd:smart00295   1 VLKVYLLDGT--TLEFEVDSSTTAEELLETVCRKLGI-------RESEYFGLQFEDPDEDLRHwLDPAKTL----LDQDV 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549861   498 QRESPQLFLRRDVRLPlEVEKKVEDPLSILILFDEARHCLLKGFLSTSDNKLITLASLLLQIIYGNYDSKKHKQgfLNEE 577
Cdd:smart00295  68 KSEPLTLYFRVKFYPP-DPNQLKEDPTRLNLLYLQVRNDILEGRLPCPEEEALLLAALALQAEFGDYDEELHDL--RGEL 144

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 948549861   578 NLKSIVPISKVKSKAH-HWTNRILHEYKSLStsegvSKEMHHLQRLFLQNCWDIPTYGAAFF 638
Cdd:smart00295 145 SLKRFLPKQLLDSRKLkEWRERIVELHKELI-----GLSPEEAKLKYLELARKLPTYGVELF 201
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
 515-638 8.44e-23

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


Pssm-ID: 459788 [Multi-domain]  Cd Length: 117  Bit Score: 93.87  E-value: 8.44e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549861  515 EVEKKVEDPLSILILFDEARHCLLKGFLSTSDNKLITLASLLLQIIYGNYDSKKHKQGFLneeNLKSIVPISKV-KSKAH 593
Cdd:pfam00373   1 DLELLLQDEVTRHLLYLQAKDDILEGRLPCSEEEALLLAALQLQAEFGDYQPSSHTSEYL---SLESFLPKQLLrKMKSK 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 948549861  594 HWTNRILHEYKSLStsegvSKEMHHLQRLFLQNCWDIPTYGAAFF 638
Cdd:pfam00373  78 ELEKRVLEAHKNLR-----GLSAEEAKLKYLQIAQSLPTYGVEFF 117
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
289-409 1.32e-21

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 95.79  E-value: 1.32e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549861 289 PLHRSACEGDTELLSKLLDGGFSVKQLDSDHWAPIHYACWHGKVEATKLLLEKGnCNPNLLNGQLSSPLHFAAIGGHAEI 368
Cdd:COG0666   90 LLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAG-ADVNAQDNDGNTPLHLAAANGNLEI 168

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 948549861 369 VQLLLQHPeIDRHIEDQQKRSPLQVCEENKQnnwEETVNLL 409
Cdd:COG0666  169 VKLLLEAG-ADVNARDNDGETPLHLAAENGH---LEIVKLL 205
Ank_2 pfam12796
Ankyrin repeats (3 copies);
290-375 1.15e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.54  E-value: 1.15e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549861  290 LHRSACEGDTELLSKLLDGGFSVKQLDSDHWAPIHYACWHGKVEATKLLLEKGNCNpNLLNGQlsSPLHFAAIGGHAEIV 369
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVN-LKDNGR--TALHYAARSGHLEIV 77


                  ....*.
gi 948549861  370 QLLLQH 375
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 ...
 529-629 2.29e-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: 60.72  E-value: 2.29e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549861 529 LFDEARHCLLKGFLSTSDNKLITLASLLLQIIYGNYDSKKHKQGFLneeNLKSIVPISKVKSKAHH-WTNRILHEYKSLS 607
Cdd:cd14473    5 LYLQVKRDILEGRLPCSEETAALLAALALQAEYGDYDPSEHKPKYL---SLKRFLPKQLLKQRKPEeWEKRIVELHKKLR 81

                         90       100
                 ....*....|....*....|..
gi 948549861 608 tseGVSKemHHLQRLFLQNCWD 629
Cdd:cd14473   82 ---GLSP--AEAKLKYLKIARK 98
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 294-379 3.69e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 53.75  E-value: 3.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549861 294 ACEGDTELLSKLLDGGFSVKQLDSDHWAPIHYACWHGKVEATKLLLEKGnCNPNLLNGQLSSPLHFAAIGGHAEIVQLLL 373
Cdd:PTZ00322  90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFG-ADPTLLDKDGKTPLELAEENGFREVVQLLS 168


                 ....*.
gi 948549861 374 QHPEID 379
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 ...
 30-197 4.83e-95

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: 292.03  E-value: 4.83e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549861   30 AKSYEILLIEVPLEGKEKKRKKVLLGTKIHADSDRTKSILEFVDETTKPIS-NNQGIIGKRVVHMRKFLLDGDSGGKEAS 108
Cdd:pfam16705   1 AKSYEILLLEVPIEGKKKKRKKVLLETKLRGSQEATKQILDYVYETTKPISpDNQGIKGKRVVHMKKFPLDGEESGREAS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549861  109 LFIVPINVKDNSKSVHHPGSPSFYCLQDIMRVCSETSAHFSSSTSKMLLALDKWLAEQHTVPHAIPALFRPAPVDRVKTN 188
Cdd:pfam16705  81 LFVVPVNVKDNTKPSYSPGSPSFYCLQDIMRVCSESSTHFPTLTSRMLIALDKWLKEQHAVPHAIPALFRPSALERIKTN 160


                  ....*....
gi 948549861  189 VSNPAYAVE 197
Cdd:pfam16705 161 VSNPAYATE 169
FERM_C_CCM1 cd13197
FERM domain C-lobe of Cerebral cavernous malformation 1; CCM1 (also called KRIT-1/Krev ...
 634-733 1.16e-56

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: 188.21  E-value: 1.16e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549861 634 GAAFFTGQVFTKASSSTHKVIRVYVGVNTKGLHLMNMETKVLHLSLEYGTFMWQLGQADQYVQIHSLENKKNFVVHTKQA 713
Cdd:cd13197    1 GAAFFTGQIFTKASSSNHKVIPVYVGVNIKGLHLLNMETKALLLSLKYGCFMWQLGDADTCFQIHSLENKMSFVVHTKQA 80

                         90       100
                 ....*....|....*....|
gi 948549861 714 GLIVKLLMKLSGQIAPNDRA 733
Cdd:cd13197   81 GLIVKLLMKLSGQRKPNDRN 100
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 419-638 6.37e-31

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: 120.09  E-value: 6.37e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549861   419 KVRIYRMDGSyrSVELKHGNNTTVQQIMEGMRLSQETqqyftiwICSENLSLQLKPYHKPLQH-LRMWSEIvtdlTALDP 497
Cdd:smart00295   1 VLKVYLLDGT--TLEFEVDSSTTAEELLETVCRKLGI-------RESEYFGLQFEDPDEDLRHwLDPAKTL----LDQDV 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549861   498 QRESPQLFLRRDVRLPlEVEKKVEDPLSILILFDEARHCLLKGFLSTSDNKLITLASLLLQIIYGNYDSKKHKQgfLNEE 577
Cdd:smart00295  68 KSEPLTLYFRVKFYPP-DPNQLKEDPTRLNLLYLQVRNDILEGRLPCPEEEALLLAALALQAEFGDYDEELHDL--RGEL 144

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 948549861   578 NLKSIVPISKVKSKAH-HWTNRILHEYKSLStsegvSKEMHHLQRLFLQNCWDIPTYGAAFF 638
Cdd:smart00295 145 SLKRFLPKQLLDSRKLkEWRERIVELHKELI-----GLSPEEAKLKYLELARKLPTYGVELF 201
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
 515-638 8.44e-23

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


Pssm-ID: 459788 [Multi-domain]  Cd Length: 117  Bit Score: 93.87  E-value: 8.44e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549861  515 EVEKKVEDPLSILILFDEARHCLLKGFLSTSDNKLITLASLLLQIIYGNYDSKKHKQGFLneeNLKSIVPISKV-KSKAH 593
Cdd:pfam00373   1 DLELLLQDEVTRHLLYLQAKDDILEGRLPCSEEEALLLAALQLQAEFGDYQPSSHTSEYL---SLESFLPKQLLrKMKSK 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 948549861  594 HWTNRILHEYKSLStsegvSKEMHHLQRLFLQNCWDIPTYGAAFF 638
Cdd:pfam00373  78 ELEKRVLEAHKNLR-----GLSAEEAKLKYLQIAQSLPTYGVEFF 117
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
289-409 1.32e-21

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 95.79  E-value: 1.32e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549861 289 PLHRSACEGDTELLSKLLDGGFSVKQLDSDHWAPIHYACWHGKVEATKLLLEKGnCNPNLLNGQLSSPLHFAAIGGHAEI 368
Cdd:COG0666   90 LLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAG-ADVNAQDNDGNTPLHLAAANGNLEI 168

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 948549861 369 VQLLLQHPeIDRHIEDQQKRSPLQVCEENKQnnwEETVNLL 409
Cdd:COG0666  169 VKLLLEAG-ADVNARDNDGETPLHLAAENGH---LEIVKLL 205
Ank_2 pfam12796
Ankyrin repeats (3 copies);
290-375 1.15e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.54  E-value: 1.15e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549861  290 LHRSACEGDTELLSKLLDGGFSVKQLDSDHWAPIHYACWHGKVEATKLLLEKGNCNpNLLNGQlsSPLHFAAIGGHAEIV 369
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVN-LKDNGR--TALHYAARSGHLEIV 77


                  ....*.
gi 948549861  370 QLLLQH 375
Cdd:pfam12796  78 KLLLEK 83
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
289-384 6.11e-16

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 79.23  E-value: 6.11e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549861 289 PLHRSACEGDTELLSKLLDGGFSVKQLDSDHWAPIHYACWHGKVEATKLLLEKGNcNPNLLNGQLSSPLHFAAIGGHAEI 368
Cdd:COG0666  156 PLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGA-DVNAKDNDGKTALDLAAENGNLEI 234

                         90
                 ....*....|....*.
gi 948549861 369 VQLLLQHPEIDRHIED 384
Cdd:COG0666  235 VKLLLEAGADLNAKDK 250
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
286-409 3.57e-14

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 73.83  E-value: 3.57e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549861 286 DDFPLHRSACEGDTELLSKLLDGGFSVKQLDSDHWAPIHYACWHGKVEATKLLLEKGNcNPNLLNGQLSSPLHFAAIGGH 365
Cdd:COG0666   54 GALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGA-DVNARDKDGETPLHLAAYNGN 132

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 948549861 366 AEIVQLLLQHpEIDRHIEDQQKRSPLQV-CeenkQNNWEETVNLL 409
Cdd:COG0666  133 LEIVKLLLEA-GADVNAQDNDGNTPLHLaA----ANGNLEIVKLL 172
Ank_2 pfam12796
Ankyrin repeats (3 copies);
323-409 3.26e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 65.91  E-value: 3.26e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549861  323 IHYACWHGKVEATKLLLEKGnCNPNLLNGQLSSPLHFAAIGGHAEIVQLLLQHPEIDrhiEDQQKRSPLQVCEENKQnnw 402
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENG-ADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVN---LKDNGRTALHYAARSGH--- 73


                  ....*..
gi 948549861  403 EETVNLL 409
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 ...
 529-629 2.29e-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: 60.72  E-value: 2.29e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549861 529 LFDEARHCLLKGFLSTSDNKLITLASLLLQIIYGNYDSKKHKQGFLneeNLKSIVPISKVKSKAHH-WTNRILHEYKSLS 607
Cdd:cd14473    5 LYLQVKRDILEGRLPCSEETAALLAALALQAEYGDYDPSEHKPKYL---SLKRFLPKQLLKQRKPEeWEKRIVELHKKLR 81

                         90       100
                 ....*....|....*....|..
gi 948549861 608 tseGVSKemHHLQRLFLQNCWD 629
Cdd:cd14473   82 ---GLSP--AEAKLKYLKIARK 98
Ank_4 pfam13637
Ankyrin repeats (many copies);
319-373 2.16e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 56.51  E-value: 2.16e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 948549861  319 HWAPIHYACWHGKVEATKLLLEKGNcNPNLLNGQLSSPLHFAAIGGHAEIVQLLL 373
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGA-DINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 294-379 3.69e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 53.75  E-value: 3.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549861 294 ACEGDTELLSKLLDGGFSVKQLDSDHWAPIHYACWHGKVEATKLLLEKGnCNPNLLNGQLSSPLHFAAIGGHAEIVQLLL 373
Cdd:PTZ00322  90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFG-ADPTLLDKDGKTPLELAEENGFREVVQLLS 168


                 ....*.
gi 948549861 374 QHPEID 379
Cdd:PTZ00322 169 RHSQCH 174
Ank_5 pfam13857
Ankyrin repeats (many copies);
338-394 4.19e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 47.34  E-value: 4.19e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 948549861  338 LLEKGNCNPNLLNGQLSSPLHFAAIGGHAEIVQLLLQHPEiDRHIEDQQKRSPLQVC 394
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGV-DLNLKDEEGLTALDLA 56
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
287-409 3.36e-06

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 49.57  E-value: 3.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549861 287 DFPLHRSACEGDTELLSKLLDGGFSVKQLDSDHWAPIHYACWHGKVEATKLLLEKGNcNPNLLNGQLSSPLHFAAIGGHA 366
Cdd:COG0666   22 ALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGA-DINAKDDGGNTLLHAAARNGDL 100

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 948549861 367 EIVQLLLQHPeIDRHIEDQQKRSPLQVCEENKQnnwEETVNLL 409
Cdd:COG0666  101 EIVKLLLEAG-ADVNARDKDGETPLHLAAYNGN---LEIVKLL 139
Ank_2 pfam12796
Ankyrin repeats (3 copies);
289-350 5.03e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 45.49  E-value: 5.03e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 948549861  289 PLHRSACEGDTELLSKLLDggFSVKQLDSDHWAPIHYACWHGKVEATKLLLEKGnCNPNLLN 350
Cdd:pfam12796  33 ALHLAAKNGHLEIVKLLLE--HADVNLKDNGRTALHYAARSGHLEIVKLLLEKG-ADINVKD 91
Ank_4 pfam13637
Ankyrin repeats (many copies);
289-339 9.78e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.42  E-value: 9.78e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 948549861  289 PLHRSACEGDTELLSKLLDGGFSVKQLDSDHWAPIHYACWHGKVEATKLLL 339
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 290-392 1.42e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 48.04  E-value: 1.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549861 290 LHRSACEGDTELLSKLLDGGFSVKQLDSDHWAPIHYACWHGKVEATKLLLEKGnCNPNLLNGQLSSPLHFAAIGGHAEIV 369
Cdd:PHA02874 128 LHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKG-AYANVKDNNGESPLHNAAEYGDYACI 206

                         90       100
                 ....*....|....*....|....*
gi 948549861 370 QLLLQHpeiDRHIEDQQKR--SPLQ 392
Cdd:PHA02874 207 KLLIDH---GNHIMNKCKNgfTPLH 228
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 289-391 1.57e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 48.06  E-value: 1.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549861 289 PLHRSACEGDTELLSKLLDGG-FSVKQLDSDHWAPIHYACWHGKVEATKLLLEKGnCNPNLLNGQLSSPLHFAAIGGHAE 367
Cdd:PHA02875  71 ELHDAVEEGDVKAVEELLDLGkFADDVFYKDGMTPLHLATILKKLDIMKLLIARG-ADPDIPNTDKFSPLHLAVMMGDIK 149

                         90       100
                 ....*....|....*....|....
gi 948549861 368 IVQLLLQHpEIDRHIEDQQKRSPL 391
Cdd:PHA02875 150 GIELLIDH-KACLDIEDCCGCTPL 172
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 322-375 2.03e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 47.74  E-value: 2.03e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 948549861 322 PIHYACWHGKVEATKLLLEKGnCNPNLLNGQLSSPLHFAAIGGHAEIVQLLLQH 375
Cdd:PHA03100 195 PLHYAVYNNNPEFVKYLLDLG-ANPNLVNKYGDTPLHIAILNNNKEIFKLLLNN 247
FERM_C-lobe cd00836
FERM domain C-lobe; The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N ...
 634-721 9.19e-04

FERM domain C-lobe; The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 275389  Cd Length: 93  Bit Score: 38.90  E-value: 9.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549861 634 GAAFFTGQVFTKasssthKVIRVYVGVNTKGLHLMNMETKVLHLSLEYG-TFMWQLGQADQ-YVQIHSLENKKNFVVHT- 710
Cdd:cd00836    1 GVEFFPVKDKSK------KGSPIILGVNPEGISVYDELTGQPLVLFPWPnIKKISFSGAKKfTIVVADEDKQSKLLFQTp 74

                         90
                 ....*....|..
gi 948549861 711 -KQAGLIVKLLM 721
Cdd:cd00836   75 sRQAKEIWKLIV 86
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 282-375 1.01e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 42.36  E-value: 1.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549861 282 RQWVDDFPLHRSACEGDTELLSKLLDGGFSVKQLDSDHWAPIHYA-CWHGKVEATKLLLEKGnCNPNLLNGQLSSPLHFA 360
Cdd:PHA02876 371 RDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRG-ANVNSKNKDLSTPLHYA 449

                         90
                 ....*....|....*.
gi 948549861 361 AIGG-HAEIVQLLLQH 375
Cdd:PHA02876 450 CKKNcKLDVIEMLLDN 465
Ank_5 pfam13857
Ankyrin repeats (many copies);
322-360 4.03e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.17  E-value: 4.03e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 948549861  322 PIHYACWHGKVEATKLLLEKGnCNPNLLNGQLSSPLHFA 360
Cdd:pfam13857  19 PLHVAAKYGALEIVRVLLAYG-VDLNLKDEEGLTALDLA 56
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 285-414 7.87e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 39.85  E-value: 7.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948549861 285 VDDFPLHRSACEGDTELLSKLLDGGFSVKQLDSDHWAPIHYACWHGKVEATKLLLeKGNCNPNLLNGQLSSPLHFAAIGG 364
Cdd:PLN03192 524 NMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLL-KHACNVHIRDANGNTALWNAISAK 602

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 948549861 365 HAEIVQLLLQHPeidrHIEDQQKRSPLqVCEENKQNNWEETVNLLQQASN 414
Cdd:PLN03192 603 HHKIFRILYHFA----SISDPHAAGDL-LCTAAKRNDLTAMKELLKQGLN 647
 
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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