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Conserved domains on  [gi|37221184|ref|NP_919438|]
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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 37221184    30 AKSYEILLHEVPIEGQKKKRKKVLLETKLQGNSEITQGILDYVVETTKPISPANQGIRGKRVVLMKKFPLDGEKMGREAS 109
Cdd:pfam16705   1 AKSYEILLLEVPIEGKKKKRKKVLLETKLRGSQEATKQILDYVYETTKPISPDNQGIKGKRVVHMKKFPLDGEESGREAS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37221184   110 LFIVPSVVKDNTKYTYTPGCPIFYCLQDIMRVCSESSTHFATLTARMLIALDKWLDERHAQSHFIPALFRPSPLERIKTN 189
Cdd:pfam16705  81 LFVVPVNVKDNTKPSYSPGSPSFYCLQDIMRVCSESSTHFPTLTSRMLIALDKWLKEQHAVPHAIPALFRPSALERIKTN 160


                  ....*....
gi 37221184   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 37221184 636 GAAFFTGQIFTKASPSNHKVIPVYVGVNIKGLHLLNMETKALLISLKYGCFMWQLGDTDTCFQIHSMENKMSFIVHTKQA 715
Cdd:cd13197   1 GAAFFTGQIFTKASSSNHKVIPVYVGVNIKGLHLLNMETKALLLSLKYGCFMWQLGDADTCFQIHSLENKMSFVVHTKQA 80

                        90       100
                ....*....|....*....|
gi 37221184 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 37221184    421 KVRIYRMDGSyrSVELKHGNNTTVQQIMEGMRLSQETqqyftiwICSENLSLQLKPYHKPLQHvrdWPEILAELTNLDPQ 500
Cdd:smart00295   1 VLKVYLLDGT--TLEFEVDSSTTAEELLETVCRKLGI-------RESEYFGLQFEDPDEDLRH---WLDPAKTLLDQDVK 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37221184    501 RETPQLFLRRDVRLPlEVEKQIEDPLAILILFDEARYNLLKGFYTAPDAKLITLASLLLQIVYGNYESKKHKQgfLNEEN 580
Cdd:smart00295  69 SEPLTLYFRVKFYPP-DPNQLKEDPTRLNLLYLQVRNDILEGRLPCPEEEALLLAALALQAEFGDYDEELHDL--RGELS 145

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 37221184    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 37221184 291 PLHRSACEGDSELLSRLLSERFSVNQLDSDHWAPIHYACWYGKVEATRILLEKGkCNPNLLNGQLSSPLHFAAGGGHAEI 370
Cdd:COG0666  90 LLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAG-ADVNAQDNDGNTPLHLAAANGNLEI 168

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 37221184 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 37221184    30 AKSYEILLHEVPIEGQKKKRKKVLLETKLQGNSEITQGILDYVVETTKPISPANQGIRGKRVVLMKKFPLDGEKMGREAS 109
Cdd:pfam16705   1 AKSYEILLLEVPIEGKKKKRKKVLLETKLRGSQEATKQILDYVYETTKPISPDNQGIKGKRVVHMKKFPLDGEESGREAS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37221184   110 LFIVPSVVKDNTKYTYTPGCPIFYCLQDIMRVCSESSTHFATLTARMLIALDKWLDERHAQSHFIPALFRPSPLERIKTN 189
Cdd:pfam16705  81 LFVVPVNVKDNTKPSYSPGSPSFYCLQDIMRVCSESSTHFPTLTSRMLIALDKWLKEQHAVPHAIPALFRPSALERIKTN 160


                  ....*....
gi 37221184   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 37221184 636 GAAFFTGQIFTKASPSNHKVIPVYVGVNIKGLHLLNMETKALLISLKYGCFMWQLGDTDTCFQIHSMENKMSFIVHTKQA 715
Cdd:cd13197   1 GAAFFTGQIFTKASSSNHKVIPVYVGVNIKGLHLLNMETKALLLSLKYGCFMWQLGDADTCFQIHSLENKMSFVVHTKQA 80

                        90       100
                ....*....|....*....|
gi 37221184 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 37221184    421 KVRIYRMDGSyrSVELKHGNNTTVQQIMEGMRLSQETqqyftiwICSENLSLQLKPYHKPLQHvrdWPEILAELTNLDPQ 500
Cdd:smart00295   1 VLKVYLLDGT--TLEFEVDSSTTAEELLETVCRKLGI-------RESEYFGLQFEDPDEDLRH---WLDPAKTLLDQDVK 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37221184    501 RETPQLFLRRDVRLPlEVEKQIEDPLAILILFDEARYNLLKGFYTAPDAKLITLASLLLQIVYGNYESKKHKQgfLNEEN 580
Cdd:smart00295  69 SEPLTLYFRVKFYPP-DPNQLKEDPTRLNLLYLQVRNDILEGRLPCPEEEALLLAALALQAEFGDYDEELHDL--RGELS 145

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 37221184    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 37221184   517 EVEKQIEDPLAILILFDEARYNLLKGFYTAPDAKLITLASLLLQIVYGNYESKKHKQGFLneeNLKSIVPVTKL-KSKAP 595
Cdd:pfam00373   1 DLELLLQDEVTRHLLYLQAKDDILEGRLPCSEEEALLLAALQLQAEFGDYQPSSHTSEYL---SLESFLPKQLLrKMKSK 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 37221184   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 37221184 291 PLHRSACEGDSELLSRLLSERFSVNQLDSDHWAPIHYACWYGKVEATRILLEKGkCNPNLLNGQLSSPLHFAAGGGHAEI 370
Cdd:COG0666  90 LLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAG-ADVNAQDNDGNTPLHLAAANGNLEI 168

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 37221184 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 37221184   292 LHRSACEGDSELLSRLLSERFSVNQLDSDHWAPIHYACWYGKVEATRILLEKGKCNpNLLNGQlsSPLHFAAGGGHAEIV 371
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVN-LKDNGR--TALHYAARSGHLEIV 77


                  ....*.
gi 37221184   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 37221184 531 LFDEARYNLLKGFYTAPDAKLITLASLLLQIVYGNYESKKHKQGFLneeNLKSIVPVTKLKSKAPH-WTNRILHEYKNLS 609
Cdd:cd14473   5 LYLQVKRDILEGRLPCSEETAALLAALALQAEYGDYDPSEHKPKYL---SLKRFLPKQLLKQRKPEeWEKRIVELHKKLR 81

                        90       100
                ....*....|....*....|..
gi 37221184 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 37221184  296 ACEGDSELLSRLLSERFSVNQLDSDHWAPIHYACWYGKVEATRILLEKGkCNPNLLNGQLSSPLHFAAGGGHAEIVQILL 375
Cdd:PTZ00322  90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFG-ADPTLLDKDGKTPLELAEENGFREVVQLLS 168


                 ....*.
gi 37221184  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 37221184    30 AKSYEILLHEVPIEGQKKKRKKVLLETKLQGNSEITQGILDYVVETTKPISPANQGIRGKRVVLMKKFPLDGEKMGREAS 109
Cdd:pfam16705   1 AKSYEILLLEVPIEGKKKKRKKVLLETKLRGSQEATKQILDYVYETTKPISPDNQGIKGKRVVHMKKFPLDGEESGREAS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37221184   110 LFIVPSVVKDNTKYTYTPGCPIFYCLQDIMRVCSESSTHFATLTARMLIALDKWLDERHAQSHFIPALFRPSPLERIKTN 189
Cdd:pfam16705  81 LFVVPVNVKDNTKPSYSPGSPSFYCLQDIMRVCSESSTHFPTLTSRMLIALDKWLKEQHAVPHAIPALFRPSALERIKTN 160


                  ....*....
gi 37221184   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 37221184 636 GAAFFTGQIFTKASPSNHKVIPVYVGVNIKGLHLLNMETKALLISLKYGCFMWQLGDTDTCFQIHSMENKMSFIVHTKQA 715
Cdd:cd13197   1 GAAFFTGQIFTKASSSNHKVIPVYVGVNIKGLHLLNMETKALLLSLKYGCFMWQLGDADTCFQIHSLENKMSFVVHTKQA 80

                        90       100
                ....*....|....*....|
gi 37221184 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 37221184    421 KVRIYRMDGSyrSVELKHGNNTTVQQIMEGMRLSQETqqyftiwICSENLSLQLKPYHKPLQHvrdWPEILAELTNLDPQ 500
Cdd:smart00295   1 VLKVYLLDGT--TLEFEVDSSTTAEELLETVCRKLGI-------RESEYFGLQFEDPDEDLRH---WLDPAKTLLDQDVK 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37221184    501 RETPQLFLRRDVRLPlEVEKQIEDPLAILILFDEARYNLLKGFYTAPDAKLITLASLLLQIVYGNYESKKHKQgfLNEEN 580
Cdd:smart00295  69 SEPLTLYFRVKFYPP-DPNQLKEDPTRLNLLYLQVRNDILEGRLPCPEEEALLLAALALQAEFGDYDEELHDL--RGELS 145

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 37221184    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 37221184   517 EVEKQIEDPLAILILFDEARYNLLKGFYTAPDAKLITLASLLLQIVYGNYESKKHKQGFLneeNLKSIVPVTKL-KSKAP 595
Cdd:pfam00373   1 DLELLLQDEVTRHLLYLQAKDDILEGRLPCSEEEALLLAALQLQAEFGDYQPSSHTSEYL---SLESFLPKQLLrKMKSK 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 37221184   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 37221184 291 PLHRSACEGDSELLSRLLSERFSVNQLDSDHWAPIHYACWYGKVEATRILLEKGkCNPNLLNGQLSSPLHFAAGGGHAEI 370
Cdd:COG0666  90 LLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAG-ADVNAQDNDGNTPLHLAAANGNLEI 168

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 37221184 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 37221184   292 LHRSACEGDSELLSRLLSERFSVNQLDSDHWAPIHYACWYGKVEATRILLEKGKCNpNLLNGQlsSPLHFAAGGGHAEIV 371
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVN-LKDNGR--TALHYAARSGHLEIV 77


                  ....*.
gi 37221184   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 37221184 291 PLHRSACEGDSELLSRLLSERFSVNQLDSDHWAPIHYACWYGKVEATRILLEKGKcNPNLLNGQLSSPLHFAAGGGHAEI 370
Cdd:COG0666 156 PLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGA-DVNAKDNDGKTALDLAAENGNLEI 234

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 37221184 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 37221184 288 DDFPLHRSACEGDSELLSRLLSERFSVNQLDSDHWAPIHYACWYGKVEATRILLEKGKcNPNLLNGQLSSPLHFAAGGGH 367
Cdd:COG0666  54 GALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGA-DVNARDKDGETPLHLAAYNGN 132

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 37221184 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 37221184   325 IHYACWYGKVEATRILLEKGkCNPNLLNGQLSSPLHFAAGGGHAEIVQILLNHPETDRhitDQQGRSPLNICEENKQnnw 404
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENG-ADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL---KDNGRTALHYAARSGH--- 73


                  ....*..
gi 37221184   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 37221184 531 LFDEARYNLLKGFYTAPDAKLITLASLLLQIVYGNYESKKHKQGFLneeNLKSIVPVTKLKSKAPH-WTNRILHEYKNLS 609
Cdd:cd14473   5 LYLQVKRDILEGRLPCSEETAALLAALALQAEYGDYDPSEHKPKYL---SLKRFLPKQLLKQRKPEeWEKRIVELHKKLR 81

                        90       100
                ....*....|....*....|..
gi 37221184 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 37221184 636 GAAFFTGQIFTKaspsnhKVIPVYVGVNIKGLHLLNMETKALLISLKYGC-FMWQLGDtDTCFQIHSM--ENKMSFIVHT 712
Cdd:cd00836   1 GVEFFPVKDKSK------KGSPIILGVNPEGISVYDELTGQPLVLFPWPNiKKISFSG-AKKFTIVVAdeDKQSKLLFQT 73

                        90       100
                ....*....|....*....|
gi 37221184 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 37221184   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 37221184   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 37221184 288 DDFPLHRSACEGDSELLSRLLSERFSVNQLDSDHWAPIHYACWYGKVEATRILLEKGKCNPNLLNGQLSSPLHFAAGGGH 367
Cdd:COG0666  20 LLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGD 99

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 37221184 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 37221184  296 ACEGDSELLSRLLSERFSVNQLDSDHWAPIHYACWYGKVEATRILLEKGkCNPNLLNGQLSSPLHFAAGGGHAEIVQILL 375
Cdd:PTZ00322  90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFG-ADPTLLDKDGKTPLELAEENGFREVVQLLS 168


                 ....*.
gi 37221184  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 37221184   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 37221184  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 37221184   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 37221184  292 LHRSACEGDSELLSRLLSERFSVNQLDSDHWAPIHYACWYGKVEATRILLEKGkCNPNLLNGQLSSPLHFAAGGGHAEIV 371
Cdd:PHA02874 128 LHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKG-AYANVKDNNGESPLHNAAEYGDYACI 206

                         90       100
                 ....*....|....*....|....*
gi 37221184  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 37221184  291 PLHRSACEGDSELLSRLL-SERFSVNQLDSDHWAPIHYACWYGKVEATRILLEKGkCNPNLLNGQLSSPLHFAAGGGHAE 369
Cdd:PHA02875  71 ELHDAVEEGDVKAVEELLdLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARG-ADPDIPNTDKFSPLHLAVMMGDIK 149

                         90       100
                 ....*....|....*....|....
gi 37221184  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 37221184  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 37221184  287 VDDFPLHRSACEGDSELLSRLLSERFSVNQLDSDHWAPIHYACWYGKVEATRILLEKGkCNPNLLNGQLSSPLHFAAGGG 366
Cdd:PLN03192 524 NMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHA-CNVHIRDANGNTALWNAISAK 602

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 37221184  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 37221184   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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