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Conserved domains on  [gi|1183596667|ref|NP_001337605|]
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krev interaction trapped protein 1 isoform 1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NUDIX_5 pfam16705
NUDIX, or N-terminal NPxY motif-rich, region of KRIT; NUDIX_5 is found in higher eukaryotes at ...
 30-198 1.54e-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: 316.69  E-value: 1.54e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596667  30 AKSYEILLHEVPIEGQKKKRKKVLLETKLQGNSEITQGILDYVVETTKPISPANQGIRGKRVVLMKKFPLDGEKMGREAS 109
Cdd:pfam16705   1 AKSYEILLLEVPIEGKKKKRKKVLLETKLRGSQEATKQILDYVYETTKPISPDNQGIKGKRVVHMKKFPLDGEESGREAS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596667 110 LFIVPSVVKDNTKYTYTPGCPIFYCLQDIMRVCSESSTHFATLTARMLIALDKWLDERHAQSHFIPALFRPSPLERIKTN 189
Cdd:pfam16705  81 LFVVPVNVKDNTKPSYSPGSPSFYCLQDIMRVCSESSTHFPTLTSRMLIALDKWLKEQHAVPHAIPALFRPSALERIKTN 160


                  ....*....
gi 1183596667 190 VINPAYATE 198
Cdd:pfam16705 161 VSNPAYATE 169
FERM_C_CCM1 cd13197
FERM domain C-lobe of Cerebral cavernous malformation 1; CCM1 (also called KRIT-1/Krev ...
 636-735 1.15e-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: 207.08  E-value: 1.15e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596667 636 GAAFFTGQIFTKASPSNHKVIPVYVGVNIKGLHLLNMETKALLISLKYGCFMWQLGDTDTCFQIHSMENKMSFIVHTKQA 715
Cdd:cd13197     1 GAAFFTGQIFTKASSSNHKVIPVYVGVNIKGLHLLNMETKALLLSLKYGCFMWQLGDADTCFQIHSLENKMSFVVHTKQA 80

                          90       100
                  ....*....|....*....|
gi 1183596667 716 GLVVKLLMKLNGQLMPTERN 735
Cdd:cd13197    81 GLIVKLLMKLSGQRKPNDRN 100
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 421-640 1.05e-37

Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in myosins, ezrin, radixin, moesin, protein tyrosine phosphatases. Plasma membrane-binding domain. These proteins play structural and regulatory roles in the assembly and stabilization of specialized plasmamembrane domains. Some PDZ domain containing proteins bind one or more of this family. Now includes JAKs.


:

Pssm-ID: 214604 [Multi-domain]  Cd Length: 201  Bit Score: 139.35  E-value: 1.05e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596667  421 KVRIYRMDGSyrSVELKHGNNTTVQQIMEGMRLSQETqqyftiwICSENLSLQLKPYHKPLQHvrdWPEILAELTNLDPQ 500
Cdd:smart00295   1 VLKVYLLDGT--TLEFEVDSSTTAEELLETVCRKLGI-------RESEYFGLQFEDPDEDLRH---WLDPAKTLLDQDVK 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596667  501 RETPQLFLRRDVRLPlEVEKQIEDPLAILILFDEARYNLLKGFYTAPDAKLITLASLLLQIVYGNYESKKHKQgfLNEEN 580
Cdd:smart00295  69 SEPLTLYFRVKFYPP-DPNQLKEDPTRLNLLYLQVRNDILEGRLPCPEEEALLLAALALQAEFGDYDEELHDL--RGELS 145

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1183596667  581 LKSIVPVTKLKS-KAPHWTNRILHEYKNLStsegvSKEMHHLQRMFLQNCWEIPTYGAAFF 640
Cdd:smart00295 146 LKRFLPKQLLDSrKLKEWRERIVELHKELI-----GLSPEEAKLKYLELARKLPTYGVELF 201
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
291-414 5.45e-22

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 96.95  E-value: 5.45e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596667 291 PLHRSACEGDSELLSRLLSERFSVNQLDSDHWAPIHYACWYGKVEATRILLEKGkCNPNLLNGQLSSPLHFAAGGGHAEI 370
Cdd:COG0666    90 LLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAG-ADVNAQDNDGNTPLHLAAANGNLEI 168

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1183596667 371 VQILLNHPeTDRHITDQQGRSPLNICEENKQnnwEEAAKLLKEA 414
Cdd:COG0666   169 VKLLLEAG-ADVNARDNDGETPLHLAAENGH---LEIVKLLLEA 208
 
Name Accession Description Interval E-value
NUDIX_5 pfam16705
NUDIX, or N-terminal NPxY motif-rich, region of KRIT; NUDIX_5 is found in higher eukaryotes at ...
 30-198 1.54e-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: 316.69  E-value: 1.54e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596667  30 AKSYEILLHEVPIEGQKKKRKKVLLETKLQGNSEITQGILDYVVETTKPISPANQGIRGKRVVLMKKFPLDGEKMGREAS 109
Cdd:pfam16705   1 AKSYEILLLEVPIEGKKKKRKKVLLETKLRGSQEATKQILDYVYETTKPISPDNQGIKGKRVVHMKKFPLDGEESGREAS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596667 110 LFIVPSVVKDNTKYTYTPGCPIFYCLQDIMRVCSESSTHFATLTARMLIALDKWLDERHAQSHFIPALFRPSPLERIKTN 189
Cdd:pfam16705  81 LFVVPVNVKDNTKPSYSPGSPSFYCLQDIMRVCSESSTHFPTLTSRMLIALDKWLKEQHAVPHAIPALFRPSALERIKTN 160


                  ....*....
gi 1183596667 190 VINPAYATE 198
Cdd:pfam16705 161 VSNPAYATE 169
FERM_C_CCM1 cd13197
FERM domain C-lobe of Cerebral cavernous malformation 1; CCM1 (also called KRIT-1/Krev ...
 636-735 1.15e-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: 207.08  E-value: 1.15e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596667 636 GAAFFTGQIFTKASPSNHKVIPVYVGVNIKGLHLLNMETKALLISLKYGCFMWQLGDTDTCFQIHSMENKMSFIVHTKQA 715
Cdd:cd13197     1 GAAFFTGQIFTKASSSNHKVIPVYVGVNIKGLHLLNMETKALLLSLKYGCFMWQLGDADTCFQIHSLENKMSFVVHTKQA 80

                          90       100
                  ....*....|....*....|
gi 1183596667 716 GLVVKLLMKLNGQLMPTERN 735
Cdd:cd13197    81 GLIVKLLMKLSGQRKPNDRN 100
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 421-640 1.05e-37

Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in myosins, ezrin, radixin, moesin, protein tyrosine phosphatases. Plasma membrane-binding domain. These proteins play structural and regulatory roles in the assembly and stabilization of specialized plasmamembrane domains. Some PDZ domain containing proteins bind one or more of this family. Now includes JAKs.


Pssm-ID: 214604 [Multi-domain]  Cd Length: 201  Bit Score: 139.35  E-value: 1.05e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596667  421 KVRIYRMDGSyrSVELKHGNNTTVQQIMEGMRLSQETqqyftiwICSENLSLQLKPYHKPLQHvrdWPEILAELTNLDPQ 500
Cdd:smart00295   1 VLKVYLLDGT--TLEFEVDSSTTAEELLETVCRKLGI-------RESEYFGLQFEDPDEDLRH---WLDPAKTLLDQDVK 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596667  501 RETPQLFLRRDVRLPlEVEKQIEDPLAILILFDEARYNLLKGFYTAPDAKLITLASLLLQIVYGNYESKKHKQgfLNEEN 580
Cdd:smart00295  69 SEPLTLYFRVKFYPP-DPNQLKEDPTRLNLLYLQVRNDILEGRLPCPEEEALLLAALALQAEFGDYDEELHDL--RGELS 145

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1183596667  581 LKSIVPVTKLKS-KAPHWTNRILHEYKNLStsegvSKEMHHLQRMFLQNCWEIPTYGAAFF 640
Cdd:smart00295 146 LKRFLPKQLLDSrKLKEWRERIVELHKELI-----GLSPEEAKLKYLELARKLPTYGVELF 201
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
 517-640 7.65e-28

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


Pssm-ID: 459788 [Multi-domain]  Cd Length: 117  Bit Score: 108.51  E-value: 7.65e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596667 517 EVEKQIEDPLAILILFDEARYNLLKGFYTAPDAKLITLASLLLQIVYGNYESKKHKQGFLneeNLKSIVPVTKL-KSKAP 595
Cdd:pfam00373   1 DLELLLQDEVTRHLLYLQAKDDILEGRLPCSEEEALLLAALQLQAEFGDYQPSSHTSEYL---SLESFLPKQLLrKMKSK 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1183596667 596 HWTNRILHEYKNLStsegvSKEMHHLQRMFLQNCWEIPTYGAAFF 640
Cdd:pfam00373  78 ELEKRVLEAHKNLR-----GLSAEEAKLKYLQIAQSLPTYGVEFF 117
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
291-414 5.45e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 96.95  E-value: 5.45e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596667 291 PLHRSACEGDSELLSRLLSERFSVNQLDSDHWAPIHYACWYGKVEATRILLEKGkCNPNLLNGQLSSPLHFAAGGGHAEI 370
Cdd:COG0666    90 LLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAG-ADVNAQDNDGNTPLHLAAANGNLEI 168

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1183596667 371 VQILLNHPeTDRHITDQQGRSPLNICEENKQnnwEEAAKLLKEA 414
Cdd:COG0666   169 VKLLLEAG-ADVNARDNDGETPLHLAAENGH---LEIVKLLLEA 208
Ank_2 pfam12796
Ankyrin repeats (3 copies);
292-377 9.92e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.84  E-value: 9.92e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596667 292 LHRSACEGDSELLSRLLSERFSVNQLDSDHWAPIHYACWYGKVEATRILLEKGKCNpNLLNGQlsSPLHFAAGGGHAEIV 371
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVN-LKDNGR--TALHYAARSGHLEIV 77


                  ....*.
gi 1183596667 372 QILLNH 377
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 ...
 531-631 3.17e-11

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


Pssm-ID: 271216  Cd Length: 99  Bit Score: 60.34  E-value: 3.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596667 531 LFDEARYNLLKGFYTAPDAKLITLASLLLQIVYGNYESKKHKQGFLneeNLKSIVPVTKLKSKAPH-WTNRILHEYKNLS 609
Cdd:cd14473     5 LYLQVKRDILEGRLPCSEETAALLAALALQAEYGDYDPSEHKPKYL---SLKRFLPKQLLKQRKPEeWEKRIVELHKKLR 81

                          90       100
                  ....*....|....*....|..
gi 1183596667 610 tseGVSKemHHLQRMFLQNCWE 631
Cdd:cd14473    82 ---GLSP--AEAKLKYLKIARK 98
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 296-381 2.29e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.05  E-value: 2.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596667 296 ACEGDSELLSRLLSERFSVNQLDSDHWAPIHYACWYGKVEATRILLEKGkCNPNLLNGQLSSPLHFAAGGGHAEIVQILL 375
Cdd:PTZ00322   90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFG-ADPTLLDKDGKTPLELAEENGFREVVQLLS 168


                  ....*.
gi 1183596667 376 NHPETD 381
Cdd:PTZ00322  169 RHSQCH 174
 
Name Accession Description Interval E-value
NUDIX_5 pfam16705
NUDIX, or N-terminal NPxY motif-rich, region of KRIT; NUDIX_5 is found in higher eukaryotes at ...
 30-198 1.54e-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: 316.69  E-value: 1.54e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596667  30 AKSYEILLHEVPIEGQKKKRKKVLLETKLQGNSEITQGILDYVVETTKPISPANQGIRGKRVVLMKKFPLDGEKMGREAS 109
Cdd:pfam16705   1 AKSYEILLLEVPIEGKKKKRKKVLLETKLRGSQEATKQILDYVYETTKPISPDNQGIKGKRVVHMKKFPLDGEESGREAS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596667 110 LFIVPSVVKDNTKYTYTPGCPIFYCLQDIMRVCSESSTHFATLTARMLIALDKWLDERHAQSHFIPALFRPSPLERIKTN 189
Cdd:pfam16705  81 LFVVPVNVKDNTKPSYSPGSPSFYCLQDIMRVCSESSTHFPTLTSRMLIALDKWLKEQHAVPHAIPALFRPSALERIKTN 160


                  ....*....
gi 1183596667 190 VINPAYATE 198
Cdd:pfam16705 161 VSNPAYATE 169
FERM_C_CCM1 cd13197
FERM domain C-lobe of Cerebral cavernous malformation 1; CCM1 (also called KRIT-1/Krev ...
 636-735 1.15e-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: 207.08  E-value: 1.15e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596667 636 GAAFFTGQIFTKASPSNHKVIPVYVGVNIKGLHLLNMETKALLISLKYGCFMWQLGDTDTCFQIHSMENKMSFIVHTKQA 715
Cdd:cd13197     1 GAAFFTGQIFTKASSSNHKVIPVYVGVNIKGLHLLNMETKALLLSLKYGCFMWQLGDADTCFQIHSLENKMSFVVHTKQA 80

                          90       100
                  ....*....|....*....|
gi 1183596667 716 GLVVKLLMKLNGQLMPTERN 735
Cdd:cd13197    81 GLIVKLLMKLSGQRKPNDRN 100
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 421-640 1.05e-37

Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in myosins, ezrin, radixin, moesin, protein tyrosine phosphatases. Plasma membrane-binding domain. These proteins play structural and regulatory roles in the assembly and stabilization of specialized plasmamembrane domains. Some PDZ domain containing proteins bind one or more of this family. Now includes JAKs.


Pssm-ID: 214604 [Multi-domain]  Cd Length: 201  Bit Score: 139.35  E-value: 1.05e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596667  421 KVRIYRMDGSyrSVELKHGNNTTVQQIMEGMRLSQETqqyftiwICSENLSLQLKPYHKPLQHvrdWPEILAELTNLDPQ 500
Cdd:smart00295   1 VLKVYLLDGT--TLEFEVDSSTTAEELLETVCRKLGI-------RESEYFGLQFEDPDEDLRH---WLDPAKTLLDQDVK 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596667  501 RETPQLFLRRDVRLPlEVEKQIEDPLAILILFDEARYNLLKGFYTAPDAKLITLASLLLQIVYGNYESKKHKQgfLNEEN 580
Cdd:smart00295  69 SEPLTLYFRVKFYPP-DPNQLKEDPTRLNLLYLQVRNDILEGRLPCPEEEALLLAALALQAEFGDYDEELHDL--RGELS 145

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1183596667  581 LKSIVPVTKLKS-KAPHWTNRILHEYKNLStsegvSKEMHHLQRMFLQNCWEIPTYGAAFF 640
Cdd:smart00295 146 LKRFLPKQLLDSrKLKEWRERIVELHKELI-----GLSPEEAKLKYLELARKLPTYGVELF 201
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
 517-640 7.65e-28

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


Pssm-ID: 459788 [Multi-domain]  Cd Length: 117  Bit Score: 108.51  E-value: 7.65e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596667 517 EVEKQIEDPLAILILFDEARYNLLKGFYTAPDAKLITLASLLLQIVYGNYESKKHKQGFLneeNLKSIVPVTKL-KSKAP 595
Cdd:pfam00373   1 DLELLLQDEVTRHLLYLQAKDDILEGRLPCSEEEALLLAALQLQAEFGDYQPSSHTSEYL---SLESFLPKQLLrKMKSK 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1183596667 596 HWTNRILHEYKNLStsegvSKEMHHLQRMFLQNCWEIPTYGAAFF 640
Cdd:pfam00373  78 ELEKRVLEAHKNLR-----GLSAEEAKLKYLQIAQSLPTYGVEFF 117
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
291-414 5.45e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 96.95  E-value: 5.45e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596667 291 PLHRSACEGDSELLSRLLSERFSVNQLDSDHWAPIHYACWYGKVEATRILLEKGkCNPNLLNGQLSSPLHFAAGGGHAEI 370
Cdd:COG0666    90 LLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAG-ADVNAQDNDGNTPLHLAAANGNLEI 168

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1183596667 371 VQILLNHPeTDRHITDQQGRSPLNICEENKQnnwEEAAKLLKEA 414
Cdd:COG0666   169 VKLLLEAG-ADVNARDNDGETPLHLAAENGH---LEIVKLLLEA 208
Ank_2 pfam12796
Ankyrin repeats (3 copies);
292-377 9.92e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.84  E-value: 9.92e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596667 292 LHRSACEGDSELLSRLLSERFSVNQLDSDHWAPIHYACWYGKVEATRILLEKGKCNpNLLNGQlsSPLHFAAGGGHAEIV 371
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVN-LKDNGR--TALHYAARSGHLEIV 77


                  ....*.
gi 1183596667 372 QILLNH 377
Cdd:pfam12796  78 KLLLEK 83
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
291-421 6.07e-15

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 76.15  E-value: 6.07e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596667 291 PLHRSACEGDSELLSRLLSERFSVNQLDSDHWAPIHYACWYGKVEATRILLEKGKcNPNLLNGQLSSPLHFAAGGGHAEI 370
Cdd:COG0666   156 PLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGA-DVNAKDNDGKTALDLAAENGNLEI 234

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1183596667 371 VQILLNHPETDRHITDQQGRSPLNICEENKQNNWEEAAKLLKEAINKPYEK 421
Cdd:COG0666   235 VKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDL 285
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
288-414 7.77e-14

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 72.68  E-value: 7.77e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596667 288 DDFPLHRSACEGDSELLSRLLSERFSVNQLDSDHWAPIHYACWYGKVEATRILLEKGKcNPNLLNGQLSSPLHFAAGGGH 367
Cdd:COG0666    54 GALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGA-DVNARDKDGETPLHLAAYNGN 132

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1183596667 368 AEIVQILLNHpETDRHITDQQGRSPLNI-CeenkQNNWEEAAKLLKEA 414
Cdd:COG0666   133 LEIVKLLLEA-GADVNAQDNDGNTPLHLaA----ANGNLEIVKLLLEA 175
Ank_2 pfam12796
Ankyrin repeats (3 copies);
325-411 2.74e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 65.91  E-value: 2.74e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596667 325 IHYACWYGKVEATRILLEKGkCNPNLLNGQLSSPLHFAAGGGHAEIVQILLNHPETDRhitDQQGRSPLNICEENKQnnw 404
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENG-ADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL---KDNGRTALHYAARSGH--- 73


                  ....*..
gi 1183596667 405 EEAAKLL 411
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 ...
 531-631 3.17e-11

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


Pssm-ID: 271216  Cd Length: 99  Bit Score: 60.34  E-value: 3.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596667 531 LFDEARYNLLKGFYTAPDAKLITLASLLLQIVYGNYESKKHKQGFLneeNLKSIVPVTKLKSKAPH-WTNRILHEYKNLS 609
Cdd:cd14473     5 LYLQVKRDILEGRLPCSEETAALLAALALQAEYGDYDPSEHKPKYL---SLKRFLPKQLLKQRKPEeWEKRIVELHKKLR 81

                          90       100
                  ....*....|....*....|..
gi 1183596667 610 tseGVSKemHHLQRMFLQNCWE 631
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 ...
 636-730 9.95e-10

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: 9.95e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596667 636 GAAFFTGQIFTKaspsnhKVIPVYVGVNIKGLHLLNMETKALLISLKYGC-FMWQLGDtDTCFQIHSM--ENKMSFIVHT 712
Cdd:cd00836     1 GVEFFPVKDKSK------KGSPIILGVNPEGISVYDELTGQPLVLFPWPNiKKISFSG-AKKFTIVVAdeDKQSKLLFQT 73

                          90       100
                  ....*....|....*....|
gi 1183596667 713 --KQAGLVVKLLMKLNGQLM 730
Cdd:cd00836    74 psRQAKEIWKLIVGYHRFLL 93
Ank_5 pfam13857
Ankyrin repeats (many copies);
340-396 2.14e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 53.89  E-value: 2.14e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1183596667 340 LLEKGKCNPNLLNGQLSSPLHFAAGGGHAEIVQILLNHPEtDRHITDQQGRSPLNIC 396
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGV-DLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
321-375 3.49e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.05  E-value: 3.49e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1183596667 321 HWAPIHYACWYGKVEATRILLEKGKcNPNLLNGQLSSPLHFAAGGGHAEIVQILL 375
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGA-DINAVDGNGETALHFAASNGNVEVLKLLL 54
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
288-414 4.22e-07

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 52.26  E-value: 4.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596667 288 DDFPLHRSACEGDSELLSRLLSERFSVNQLDSDHWAPIHYACWYGKVEATRILLEKGKCNPNLLNGQLSSPLHFAAGGGH 367
Cdd:COG0666    20 LLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGD 99

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1183596667 368 AEIVQILLNHPeTDRHITDQQGRSPLNICEENKQnnwEEAAKLLKEA 414
Cdd:COG0666   100 LEIVKLLLEAG-ADVNARDKDGETPLHLAAYNGN---LEIVKLLLEA 142
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 296-381 2.29e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.05  E-value: 2.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596667 296 ACEGDSELLSRLLSERFSVNQLDSDHWAPIHYACWYGKVEATRILLEKGkCNPNLLNGQLSSPLHFAAGGGHAEIVQILL 375
Cdd:PTZ00322   90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFG-ADPTLLDKDGKTPLELAEENGFREVVQLLS 168


                  ....*.
gi 1183596667 376 NHPETD 381
Cdd:PTZ00322  169 RHSQCH 174
Ank_2 pfam12796
Ankyrin repeats (3 copies);
291-352 7.31e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 44.72  E-value: 7.31e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1183596667 291 PLHRSACEGDSELLSRLLsERFSVNqLDSDHWAPIHYACWYGKVEATRILLEKGkCNPNLLN 352
Cdd:pfam12796  33 ALHLAAKNGHLEIVKLLL-EHADVN-LKDNGRTALHYAARSGHLEIVKLLLEKG-ADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 306-384 1.86e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 47.74  E-value: 1.86e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1183596667 306 RLLSERFSVNQLDSDHWAPIHYACWYGKVEATRILLEKGkCNPNLLNGQLSSPLHFAAGGGHAEIVQILLNHPETDRHI 384
Cdd:PHA03100  177 YLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLG-ANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTI 254
Ank_4 pfam13637
Ankyrin repeats (many copies);
291-341 4.28e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.49  E-value: 4.28e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1183596667 291 PLHRSACEGDSELLSRLLSERFSVNQLDSDHWAPIHYACWYGKVEATRILL 341
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 292-394 6.08e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 46.11  E-value: 6.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596667 292 LHRSACEGDSELLSRLLSERFSVNQLDSDHWAPIHYACWYGKVEATRILLEKGkCNPNLLNGQLSSPLHFAAGGGHAEIV 371
Cdd:PHA02874  128 LHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKG-AYANVKDNNGESPLHNAAEYGDYACI 206

                          90       100
                  ....*....|....*....|....*
gi 1183596667 372 QILLNHpetDRHITDQ--QGRSPLN 394
Cdd:PHA02874  207 KLLIDH---GNHIMNKckNGFTPLH 228
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 291-393 1.77e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 44.60  E-value: 1.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596667 291 PLHRSACEGDSELLSRLL-SERFSVNQLDSDHWAPIHYACWYGKVEATRILLEKGkCNPNLLNGQLSSPLHFAAGGGHAE 369
Cdd:PHA02875   71 ELHDAVEEGDVKAVEELLdLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARG-ADPDIPNTDKFSPLHLAVMMGDIK 149

                          90       100
                  ....*....|....*....|....
gi 1183596667 370 IVQILLNHPETdRHITDQQGRSPL 393
Cdd:PHA02875  150 GIELLIDHKAC-LDIEDCCGCTPL 172
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 338-411 2.23e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.50  E-value: 2.23e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1183596667 338 RILLEKGkCNPNLLNGQLSSPLHFAAGGGHAEIVQILLNHpETDRHITDQQGRSPLNICEEnkqNNWEEAAKLL 411
Cdd:PTZ00322   99 RILLTGG-ADPNCRDYDGRTPLHIACANGHVQVVRVLLEF-GADPTLLDKDGKTPLELAEE---NGFREVVQLL 167
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 287-416 4.11e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 43.70  E-value: 4.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596667 287 VDDFPLHRSACEGDSELLSRLLSERFSVNQLDSDHWAPIHYACWYGKVEATRILLEKGkCNPNLLNGQLSSPLHFAAGGG 366
Cdd:PLN03192  524 NMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHA-CNVHIRDANGNTALWNAISAK 602

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1183596667 367 HAEIVQILLNHPetdrHITDQQGRSPLnICEENKQNNWEEAAKLLKEAIN 416
Cdd:PLN03192  603 HHKIFRILYHFA----SISDPHAAGDL-LCTAAKRNDLTAMKELLKQGLN 647
Ank_5 pfam13857
Ankyrin repeats (many copies);
310-362 4.96e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.48  E-value: 4.96e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1183596667 310 ERFSVNQLDSDHWA--PIHYACWYGKVEATRILLEKGkCNPNLLNGQLSSPLHFA 362
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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