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Conserved domains on  [gi|385198079|ref|NP_001245244|]
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protein ECT2 isoform a [Homo sapiens]

Protein Classification

protein ECT2( domain architecture ID 13026830)

protein ECT2 acts as guanine nucleotide exchange factor (GEF) that catalyzes the exchange of GDP for GTP and is required for signal transduction pathways involved in the regulation of cytokinesis

Gene Ontology:  GO:0005085|GO:0005096|GO:0031267|GO:0090630

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PH_Ect2 cd01229
Epithelial cell transforming 2 (Ect2) pleckstrin homology (PH) domain; Ect2, a mammalian ...
 631-804 4.23e-88

Epithelial cell transforming 2 (Ect2) pleckstrin homology (PH) domain; Ect2, a mammalian ortholog of Drosophila pebble, plays a role in neuronal differentiation and brain development. Pebble and Ect2 have been identified as Rho-family guanine nucleotide exchange factors (GEF) that mediate activation of Rho during cytokinesis, but are proposed to play slightly different roles. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


:

Pssm-ID: 269936  Cd Length: 180  Bit Score: 278.00  E-value: 4.23e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198079 631 LKEVMTHINEDKRKTEAQKQIFDVVYEVDGCPANLLSSHRSLVQRVETISLG-EHPCDRGEQVTLFLFNDCLEIARKRHK 709
Cdd:cd01229    1 LKEVMTHINEDKRKTESQAQMFDIVNEIENCPPTLLSSHRSFVSRCEVVELGdSLKSGRGDSLTLFLFSDLIEICKKRSS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198079 710 VIGTFRSPHGQTR-----PPASLKHIHLMPLSQIKKVLDIRETEDCHNAFALLVRPPTEQANVLLSFQMTSDELPKENWL 784
Cdd:cd01229   81 VKGTSKSPRGSTGsglreSKKKYKHVKLMPLSTIKRVIDIRETEDCQRVFALLFRHPTELKEKLYSFQILDEETDKESFL 160

                        170       180
                 ....*....|....*....|
gi 385198079 785 KMLCRHVANTICKADAENLI 804
Cdd:cd01229  161 KTLCKQVANTVCRADAENFL 180
RhoGEF smart00325
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange ...
 456-640 6.27e-50

Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called Dbl-homologous (DH) domain. It appears that PH domains invariably occur C-terminal to RhoGEF/DH domains. Improved coverage.


:

Pssm-ID: 214619 [Multi-domain]  Cd Length: 180  Bit Score: 174.03  E-value: 6.27e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198079   456 VAKELYQTESNYVNILATIIQLFQVPLEEEGQrggpILAPEEIKTIFGSIPDIFDVHTKIKDDLEDLIVNWDESK-SIGD 534
Cdd:smart00325   1 VLKELLQTERNYVRDLKLLVEVFLKPLKKELK----LLSPNELETLFGNIEEIYEFHRDFLDELEERIEEWDDSVeRIGD 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198079   535 IFLKYSKDLvKTYPPFVNFFEMSKETIIKCeKQKPRFHAFLKINQAKPECGRQSLVELLIRPVQRLPSVALLLNDLKKHT 614
Cdd:smart00325  77 VFLKLEEFF-KIYSEYCSNHPDALELLKKL-KKNPRFQKFLKEIESSPQCRRLTLESLLLKPVQRLTKYPLLLKELLKHT 154

                          170       180
                   ....*....|....*....|....*.
gi 385198079   615 ADENPDKSTLEKAIGSLKEVMTHINE 640
Cdd:smart00325 155 PEDHEDREDLKKALKAIKELANQVNE 180
BRCT_Ect2_rpt1 cd17733
first BRCT domain of epithelial cell-transforming sequence 2 protein (ECT2) and similar ...
 176-251 2.69e-49

first BRCT domain of epithelial cell-transforming sequence 2 protein (ECT2) and similar proteins; ECT2 is a guanine nucleotide exchange factor (GEF) for Rho GTPases, phosphorylated in G2/M phases, and is involved in the regulation of cytokinesis. It contains two tandem BRCT domains. The family corresponds to the first BRCT domain.


:

Pssm-ID: 349365 [Multi-domain]  Cd Length: 76  Bit Score: 168.27  E-value: 2.69e-49
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 385198079 176 MMNLVLCFTGFRKKEELVRLVTLVHHMGGVIRKDFNSKVTHLVANCTQGEKFRVAVSLGTPIMKPEWIYKAWERRN 251
Cdd:cd17733    1 MENLVLCFTGFRKKEELSRLVNLVHHMGGSIRKDFSSKVTHLVANSTQGEKYRVAVSLGTPIMTEDWIYKAWEKRN 76
BRCT_Ect2_rpt2 cd17732
second BRCT domain of epithelial cell-transforming sequence 2 protein (ECT2) and similar ...
 270-349 1.20e-47

second BRCT domain of epithelial cell-transforming sequence 2 protein (ECT2) and similar proteins; ECT2 is a guanine nucleotide exchange factor (GEF) for Rho GTPases, phosphorylated in G2/M phases, and is involved in the regulation of cytokinesis. It contains two tandem BRCT domains. The family corresponds to the second BRCT domain.


:

Pssm-ID: 349364  Cd Length: 80  Bit Score: 163.59  E-value: 1.20e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198079 270 PFQDCILSFLGFSDEEKTNMEEMTEMQGGKYLPLGDERCTHLVVEENIVKDLPFEPSKKLYVVKQEWFWGSIQMDARAGE 349
Cdd:cd17732    1 PFEGCTLSFLGFSDEEKTHMEELTEENGGKVTPLGDPSCTHLVVDESTVKELPFEPSSKLHVVKQEWFWASIQMDACADE 80
 
Name Accession Description Interval E-value
PH_Ect2 cd01229
Epithelial cell transforming 2 (Ect2) pleckstrin homology (PH) domain; Ect2, a mammalian ...
 631-804 4.23e-88

Epithelial cell transforming 2 (Ect2) pleckstrin homology (PH) domain; Ect2, a mammalian ortholog of Drosophila pebble, plays a role in neuronal differentiation and brain development. Pebble and Ect2 have been identified as Rho-family guanine nucleotide exchange factors (GEF) that mediate activation of Rho during cytokinesis, but are proposed to play slightly different roles. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269936  Cd Length: 180  Bit Score: 278.00  E-value: 4.23e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198079 631 LKEVMTHINEDKRKTEAQKQIFDVVYEVDGCPANLLSSHRSLVQRVETISLG-EHPCDRGEQVTLFLFNDCLEIARKRHK 709
Cdd:cd01229    1 LKEVMTHINEDKRKTESQAQMFDIVNEIENCPPTLLSSHRSFVSRCEVVELGdSLKSGRGDSLTLFLFSDLIEICKKRSS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198079 710 VIGTFRSPHGQTR-----PPASLKHIHLMPLSQIKKVLDIRETEDCHNAFALLVRPPTEQANVLLSFQMTSDELPKENWL 784
Cdd:cd01229   81 VKGTSKSPRGSTGsglreSKKKYKHVKLMPLSTIKRVIDIRETEDCQRVFALLFRHPTELKEKLYSFQILDEETDKESFL 160

                        170       180
                 ....*....|....*....|
gi 385198079 785 KMLCRHVANTICKADAENLI 804
Cdd:cd01229  161 KTLCKQVANTVCRADAENFL 180
RhoGEF smart00325
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange ...
 456-640 6.27e-50

Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called Dbl-homologous (DH) domain. It appears that PH domains invariably occur C-terminal to RhoGEF/DH domains. Improved coverage.


Pssm-ID: 214619 [Multi-domain]  Cd Length: 180  Bit Score: 174.03  E-value: 6.27e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198079   456 VAKELYQTESNYVNILATIIQLFQVPLEEEGQrggpILAPEEIKTIFGSIPDIFDVHTKIKDDLEDLIVNWDESK-SIGD 534
Cdd:smart00325   1 VLKELLQTERNYVRDLKLLVEVFLKPLKKELK----LLSPNELETLFGNIEEIYEFHRDFLDELEERIEEWDDSVeRIGD 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198079   535 IFLKYSKDLvKTYPPFVNFFEMSKETIIKCeKQKPRFHAFLKINQAKPECGRQSLVELLIRPVQRLPSVALLLNDLKKHT 614
Cdd:smart00325  77 VFLKLEEFF-KIYSEYCSNHPDALELLKKL-KKNPRFQKFLKEIESSPQCRRLTLESLLLKPVQRLTKYPLLLKELLKHT 154

                          170       180
                   ....*....|....*....|....*.
gi 385198079   615 ADENPDKSTLEKAIGSLKEVMTHINE 640
Cdd:smart00325 155 PEDHEDREDLKKALKAIKELANQVNE 180
BRCT_Ect2_rpt1 cd17733
first BRCT domain of epithelial cell-transforming sequence 2 protein (ECT2) and similar ...
 176-251 2.69e-49

first BRCT domain of epithelial cell-transforming sequence 2 protein (ECT2) and similar proteins; ECT2 is a guanine nucleotide exchange factor (GEF) for Rho GTPases, phosphorylated in G2/M phases, and is involved in the regulation of cytokinesis. It contains two tandem BRCT domains. The family corresponds to the first BRCT domain.


Pssm-ID: 349365 [Multi-domain]  Cd Length: 76  Bit Score: 168.27  E-value: 2.69e-49
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 385198079 176 MMNLVLCFTGFRKKEELVRLVTLVHHMGGVIRKDFNSKVTHLVANCTQGEKFRVAVSLGTPIMKPEWIYKAWERRN 251
Cdd:cd17733    1 MENLVLCFTGFRKKEELSRLVNLVHHMGGSIRKDFSSKVTHLVANSTQGEKYRVAVSLGTPIMTEDWIYKAWEKRN 76
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
 453-639 1.70e-48

Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous (DH) domain. It appears that PH domains invariably occur C-terminal to RhoGEF/DH domains.


Pssm-ID: 238091 [Multi-domain]  Cd Length: 181  Bit Score: 170.17  E-value: 1.70e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198079 453 RWQVAKELYQTESNYVNILATIIQLFQVPLEEEGQRggpiLAPEEIKTIFGSIPDIFDVHTKIKDDLEDLIVNWDESK-S 531
Cdd:cd00160    1 RQEVIKELLQTERNYVRDLKLLVEVFLKPLDKELLP----LSPEEVELLFGNIEEIYEFHRIFLKSLEERVEEWDKSGpR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198079 532 IGDIFLKYsKDLVKTYPPFVNFFEMSKETIIKCEKQKPRFHAFLKinQAKPECGRQSLVELLIRPVQRLPSVALLLNDLK 611
Cdd:cd00160   77 IGDVFLKL-APFFKIYSEYCSNHPDALELLKKLKKFNKFFQEFLE--KAESECGRLKLESLLLKPVQRLTKYPLLLKELL 153

                        170       180
                 ....*....|....*....|....*...
gi 385198079 612 KHTADENPDKSTLEKAIGSLKEVMTHIN 639
Cdd:cd00160  154 KHTPDGHEDREDLKKALEAIKEVASQVN 181
BRCT_Ect2_rpt2 cd17732
second BRCT domain of epithelial cell-transforming sequence 2 protein (ECT2) and similar ...
 270-349 1.20e-47

second BRCT domain of epithelial cell-transforming sequence 2 protein (ECT2) and similar proteins; ECT2 is a guanine nucleotide exchange factor (GEF) for Rho GTPases, phosphorylated in G2/M phases, and is involved in the regulation of cytokinesis. It contains two tandem BRCT domains. The family corresponds to the second BRCT domain.


Pssm-ID: 349364  Cd Length: 80  Bit Score: 163.59  E-value: 1.20e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198079 270 PFQDCILSFLGFSDEEKTNMEEMTEMQGGKYLPLGDERCTHLVVEENIVKDLPFEPSKKLYVVKQEWFWGSIQMDARAGE 349
Cdd:cd17732    1 PFEGCTLSFLGFSDEEKTHMEELTEENGGKVTPLGDPSCTHLVVDESTVKELPFEPSSKLHVVKQEWFWASIQMDACADE 80
RhoGEF pfam00621
RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called ...
 456-639 1.63e-47

RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called Dbl-homologous (DH) domain. It appears that pfam00169 domains invariably occur C-terminal to RhoGEF/DH domains.


Pssm-ID: 459876 [Multi-domain]  Cd Length: 176  Bit Score: 167.09  E-value: 1.63e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198079  456 VAKELYQTESNYVNILATIIQLFQVPLEEegqrggPI-LAPEEIKTIFGSIPDIFDVHTKIkdDLEDLIVNWDESKSIGD 534
Cdd:pfam00621   1 VIKELLQTERSYVRDLEILVEVFLPPNSK------PLsESEEEIKTIFSNIEEIYELHRQL--LLEELLKEWISIQRIGD 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198079  535 IFLKYSKDLvKTYPPFVNFFEMSKETIIKCEKQKPRFHAFLKINQAKPECGRQSLVELLIRPVQRLPSVALLLNDLKKHT 614
Cdd:pfam00621  73 IFLKFAPGF-KVYSTYCSNYPKALKLLKKLLKKNPKFRAFLEELEANPECRGLDLNSFLIKPVQRIPRYPLLLKELLKHT 151

                         170       180
                  ....*....|....*....|....*
gi 385198079  615 ADENPDKSTLEKAIGSLKEVMTHIN 639
Cdd:pfam00621 152 PPDHPDYEDLKKALEAIKEVAKQIN 176
PTCB-BRCT pfam12738
twin BRCT domain; This is a BRCT domain that appears in duplicate in most member sequences. ...
 179-242 1.56e-19

twin BRCT domain; This is a BRCT domain that appears in duplicate in most member sequences. BRCT domains are peptide- and phosphopeptide-binding modules. BRCT domains are present in a number of proteins involved in DNA checkpoint controls and DNA repair.


Pssm-ID: 463687 [Multi-domain]  Cd Length: 63  Bit Score: 83.02  E-value: 1.56e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 385198079  179 LVLCFTGFRKkEELVRLVTLVHHMGGVIRKDFNSKVTHLVANCTQGEKFRVAVSLGTPIMKPEW 242
Cdd:pfam12738   1 LVICVTGFDG-DDREGLQKLIEAMGAEYTKDLTKSVTHLICKSGEGEKYEKAKEWGIPVVSPLW 63
BRCT pfam00533
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ...
 266-341 2.62e-11

BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in cell cycle checkpoint functions responsive to DNA damage. The BRCT domain of XRCC1 forms a homodimer in the crystal structure. This suggests that pairs of BRCT domains associate as homo- or heterodimers. BRCT domains are often found as tandem-repeat pairs. Structures of the BRCA1 BRCT domains revealed a basis for a widely utilized head-to-tail BRCT-BRCT oligomerization mode. This conserved tandem BRCT architecture facilitates formation of the canonical BRCT phospho-peptide interaction cleft at a groove between the BRCT domains. Disease associated missense and nonsense mutations in the BRCA1 BRCT domains disrupt peptide binding by directly occluding this peptide binding groove, or by disrupting key conserved BRCT core folding determinants.


Pssm-ID: 425736 [Multi-domain]  Cd Length: 75  Bit Score: 60.00  E-value: 2.62e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 385198079  266 FKVPPFQDCILSFLGFSDEEKTNMEEMTEMQGGKYLPLGDERCTHLVVEENIVKdLPFEPSKKLYVVKQEWFWGSI 341
Cdd:pfam00533   1 PKEKLFSGKTFVITGLDGLERDELKELIEKLGGKVTDSLSKKTTHVIVEARTKK-YLKAKELGIPIVTEEWLLDCI 75
ROM1 COG5422
RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction ...
 446-652 2.39e-10

RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction mechanisms];


Pssm-ID: 227709 [Multi-domain]  Cd Length: 1175  Bit Score: 64.53  E-value: 2.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198079  446 VPSKQSARWQVAKELYQTESNYVNILATIIQLFQVPLEEEGqrggpiLAPEE-----IKTIFGSIPDIFDVHTKIKDDLE 520
Cdd:COG5422   478 LPKQEIKRQEAIYEVIYTERDFVKDLEYLRDTWIKPLEESN------IIPENarrnfIKHVFANINEIYAVNSKLLKALT 551

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198079  521 DLIVNWDESKSIGDIFLKYskdlVKTYPPFVNFFEMSKETIIKCEKQK---PRFHAFLKINQAKPECGRQSLVELLIRPV 597
Cdd:COG5422   552 NRQCLSPIVNGIADIFLDY----VPKFEPFIKYGASQPYAKYEFEREKsvnPNFARFDHEVERLDESRKLELDGYLTKPT 627

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 385198079  598 QRLPSVALLLNDLKKHTADENPDKSTLEKAIGSLKEVMTHINEDKRKTEAQKQIF 652
Cdd:COG5422   628 TRLARYPLLLEEVLKFTDPDNPDTEDIPKVIDMLREFLSRLNFESGKAENRGDLF 682
BRCT smart00292
breast cancer carboxy-terminal domain;
178-247 2.06e-09

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 54.69  E-value: 2.06e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 385198079   178 NLVLCFTGFRKKEELVRLVTLVHHMGGVIRKDFNSK-VTHLVANCTQGEK--FRVAVSLGTPIMKPEWIYKAW 247
Cdd:smart00292   6 GKTFYITGSFDKEERDELKELIEALGGKVTSSLSSKtTTHVIVGSPEGGKleLLKAIALGIPIVKEEWLLDCL 78
BRCT smart00292
breast cancer carboxy-terminal domain;
268-341 4.13e-08

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 51.22  E-value: 4.13e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 385198079   268 VPPFQDCILSFLG-FSDEEKTNMEEMTEMQGGKYLP-LGDERCTHLVVE--ENIVKDLPFEPSKKLYVVKQEWFWGSI 341
Cdd:smart00292   1 PKLFKGKTFYITGsFDKEERDELKELIEALGGKVTSsLSSKTTTHVIVGspEGGKLELLKAIALGIPIVKEEWLLDCL 78
 
Name Accession Description Interval E-value
PH_Ect2 cd01229
Epithelial cell transforming 2 (Ect2) pleckstrin homology (PH) domain; Ect2, a mammalian ...
 631-804 4.23e-88

Epithelial cell transforming 2 (Ect2) pleckstrin homology (PH) domain; Ect2, a mammalian ortholog of Drosophila pebble, plays a role in neuronal differentiation and brain development. Pebble and Ect2 have been identified as Rho-family guanine nucleotide exchange factors (GEF) that mediate activation of Rho during cytokinesis, but are proposed to play slightly different roles. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269936  Cd Length: 180  Bit Score: 278.00  E-value: 4.23e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198079 631 LKEVMTHINEDKRKTEAQKQIFDVVYEVDGCPANLLSSHRSLVQRVETISLG-EHPCDRGEQVTLFLFNDCLEIARKRHK 709
Cdd:cd01229    1 LKEVMTHINEDKRKTESQAQMFDIVNEIENCPPTLLSSHRSFVSRCEVVELGdSLKSGRGDSLTLFLFSDLIEICKKRSS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198079 710 VIGTFRSPHGQTR-----PPASLKHIHLMPLSQIKKVLDIRETEDCHNAFALLVRPPTEQANVLLSFQMTSDELPKENWL 784
Cdd:cd01229   81 VKGTSKSPRGSTGsglreSKKKYKHVKLMPLSTIKRVIDIRETEDCQRVFALLFRHPTELKEKLYSFQILDEETDKESFL 160

                        170       180
                 ....*....|....*....|
gi 385198079 785 KMLCRHVANTICKADAENLI 804
Cdd:cd01229  161 KTLCKQVANTVCRADAENFL 180
RhoGEF smart00325
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange ...
 456-640 6.27e-50

Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called Dbl-homologous (DH) domain. It appears that PH domains invariably occur C-terminal to RhoGEF/DH domains. Improved coverage.


Pssm-ID: 214619 [Multi-domain]  Cd Length: 180  Bit Score: 174.03  E-value: 6.27e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198079   456 VAKELYQTESNYVNILATIIQLFQVPLEEEGQrggpILAPEEIKTIFGSIPDIFDVHTKIKDDLEDLIVNWDESK-SIGD 534
Cdd:smart00325   1 VLKELLQTERNYVRDLKLLVEVFLKPLKKELK----LLSPNELETLFGNIEEIYEFHRDFLDELEERIEEWDDSVeRIGD 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198079   535 IFLKYSKDLvKTYPPFVNFFEMSKETIIKCeKQKPRFHAFLKINQAKPECGRQSLVELLIRPVQRLPSVALLLNDLKKHT 614
Cdd:smart00325  77 VFLKLEEFF-KIYSEYCSNHPDALELLKKL-KKNPRFQKFLKEIESSPQCRRLTLESLLLKPVQRLTKYPLLLKELLKHT 154

                          170       180
                   ....*....|....*....|....*.
gi 385198079   615 ADENPDKSTLEKAIGSLKEVMTHINE 640
Cdd:smart00325 155 PEDHEDREDLKKALKAIKELANQVNE 180
BRCT_Ect2_rpt1 cd17733
first BRCT domain of epithelial cell-transforming sequence 2 protein (ECT2) and similar ...
 176-251 2.69e-49

first BRCT domain of epithelial cell-transforming sequence 2 protein (ECT2) and similar proteins; ECT2 is a guanine nucleotide exchange factor (GEF) for Rho GTPases, phosphorylated in G2/M phases, and is involved in the regulation of cytokinesis. It contains two tandem BRCT domains. The family corresponds to the first BRCT domain.


Pssm-ID: 349365 [Multi-domain]  Cd Length: 76  Bit Score: 168.27  E-value: 2.69e-49
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 385198079 176 MMNLVLCFTGFRKKEELVRLVTLVHHMGGVIRKDFNSKVTHLVANCTQGEKFRVAVSLGTPIMKPEWIYKAWERRN 251
Cdd:cd17733    1 MENLVLCFTGFRKKEELSRLVNLVHHMGGSIRKDFSSKVTHLVANSTQGEKYRVAVSLGTPIMTEDWIYKAWEKRN 76
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
 453-639 1.70e-48

Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous (DH) domain. It appears that PH domains invariably occur C-terminal to RhoGEF/DH domains.


Pssm-ID: 238091 [Multi-domain]  Cd Length: 181  Bit Score: 170.17  E-value: 1.70e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198079 453 RWQVAKELYQTESNYVNILATIIQLFQVPLEEEGQRggpiLAPEEIKTIFGSIPDIFDVHTKIKDDLEDLIVNWDESK-S 531
Cdd:cd00160    1 RQEVIKELLQTERNYVRDLKLLVEVFLKPLDKELLP----LSPEEVELLFGNIEEIYEFHRIFLKSLEERVEEWDKSGpR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198079 532 IGDIFLKYsKDLVKTYPPFVNFFEMSKETIIKCEKQKPRFHAFLKinQAKPECGRQSLVELLIRPVQRLPSVALLLNDLK 611
Cdd:cd00160   77 IGDVFLKL-APFFKIYSEYCSNHPDALELLKKLKKFNKFFQEFLE--KAESECGRLKLESLLLKPVQRLTKYPLLLKELL 153

                        170       180
                 ....*....|....*....|....*...
gi 385198079 612 KHTADENPDKSTLEKAIGSLKEVMTHIN 639
Cdd:cd00160  154 KHTPDGHEDREDLKKALEAIKEVASQVN 181
BRCT_Ect2_rpt2 cd17732
second BRCT domain of epithelial cell-transforming sequence 2 protein (ECT2) and similar ...
 270-349 1.20e-47

second BRCT domain of epithelial cell-transforming sequence 2 protein (ECT2) and similar proteins; ECT2 is a guanine nucleotide exchange factor (GEF) for Rho GTPases, phosphorylated in G2/M phases, and is involved in the regulation of cytokinesis. It contains two tandem BRCT domains. The family corresponds to the second BRCT domain.


Pssm-ID: 349364  Cd Length: 80  Bit Score: 163.59  E-value: 1.20e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198079 270 PFQDCILSFLGFSDEEKTNMEEMTEMQGGKYLPLGDERCTHLVVEENIVKDLPFEPSKKLYVVKQEWFWGSIQMDARAGE 349
Cdd:cd17732    1 PFEGCTLSFLGFSDEEKTHMEELTEENGGKVTPLGDPSCTHLVVDESTVKELPFEPSSKLHVVKQEWFWASIQMDACADE 80
RhoGEF pfam00621
RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called ...
 456-639 1.63e-47

RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called Dbl-homologous (DH) domain. It appears that pfam00169 domains invariably occur C-terminal to RhoGEF/DH domains.


Pssm-ID: 459876 [Multi-domain]  Cd Length: 176  Bit Score: 167.09  E-value: 1.63e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198079  456 VAKELYQTESNYVNILATIIQLFQVPLEEegqrggPI-LAPEEIKTIFGSIPDIFDVHTKIkdDLEDLIVNWDESKSIGD 534
Cdd:pfam00621   1 VIKELLQTERSYVRDLEILVEVFLPPNSK------PLsESEEEIKTIFSNIEEIYELHRQL--LLEELLKEWISIQRIGD 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198079  535 IFLKYSKDLvKTYPPFVNFFEMSKETIIKCEKQKPRFHAFLKINQAKPECGRQSLVELLIRPVQRLPSVALLLNDLKKHT 614
Cdd:pfam00621  73 IFLKFAPGF-KVYSTYCSNYPKALKLLKKLLKKNPKFRAFLEELEANPECRGLDLNSFLIKPVQRIPRYPLLLKELLKHT 151

                         170       180
                  ....*....|....*....|....*
gi 385198079  615 ADENPDKSTLEKAIGSLKEVMTHIN 639
Cdd:pfam00621 152 PPDHPDYEDLKKALEAIKEVAKQIN 176
PTCB-BRCT pfam12738
twin BRCT domain; This is a BRCT domain that appears in duplicate in most member sequences. ...
 179-242 1.56e-19

twin BRCT domain; This is a BRCT domain that appears in duplicate in most member sequences. BRCT domains are peptide- and phosphopeptide-binding modules. BRCT domains are present in a number of proteins involved in DNA checkpoint controls and DNA repair.


Pssm-ID: 463687 [Multi-domain]  Cd Length: 63  Bit Score: 83.02  E-value: 1.56e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 385198079  179 LVLCFTGFRKkEELVRLVTLVHHMGGVIRKDFNSKVTHLVANCTQGEKFRVAVSLGTPIMKPEW 242
Cdd:pfam12738   1 LVICVTGFDG-DDREGLQKLIEAMGAEYTKDLTKSVTHLICKSGEGEKYEKAKEWGIPVVSPLW 63
BRCT_TopBP1_rpt1 cd17737
first BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins; ...
 178-249 5.16e-16

first BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins; TopBP1, also termed DNA topoisomerase II-beta-binding protein 1, or DNA topoisomerase II-binding protein 1, functions in DNA replication and damage response. It binds double-stranded DNA breaks and nicks as well as single-stranded DNA. TopBP1 contains six copies of BRCT domain. The family corresponds to the first BRCT domain.


Pssm-ID: 349369 [Multi-domain]  Cd Length: 72  Bit Score: 73.21  E-value: 5.16e-16
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 385198079 178 NLVLCFTGFRKKEElVRLVTLVHHMGGVIRKDFNSKVTHLVANCTQGEKFRVAVSLGTPIMKPEWIYKAWER 249
Cdd:cd17737    1 DVTISCTSLEKEER-EEVHKYVQLMGGRVSRDLTVSVTHLIAGEVGSKKYLVAASLKKPIMLPSWVKTLWEK 71
BRCT cd00027
C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The ...
 179-245 3.20e-15

C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The BRCT (BRCA1 C-terminus) domain is found within many DNA damage repair and cell cycle checkpoint proteins. BRCT domains interact with each other forming homo/hetero BRCT multimers, but are also involved in BRCT-non-BRCT interactions and interactions within DNA strand breaks. BRCT tandem repeats bind to phosphopeptides; it has been shown that the repeats in human BRCA1 bind specifically to pS-X-X-F motifs, mediating the interaction between BRCA1 and the DNA helicase BACH1, or BRCA1 and CtIP, a transcriptional corepressor. It is assumed that BRCT repeats play similar roles in many signaling pathways associated with the response to DNA damage.


Pssm-ID: 349339 [Multi-domain]  Cd Length: 68  Bit Score: 70.85  E-value: 3.20e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 385198079 179 LVLCFTGFRKKEELvRLVTLVHHMGGVIRKDFNSKVTHLVANCTQGEK-FRVAVSLGTPIMKPEWIYK 245
Cdd:cd00027    1 LVICFSGLDDEERE-ELKKLIEALGGKVSESLSSKVTHLIAKSPSGEKyYLAALAWGIPIVSPEWLLD 67
BRCT_Rad4_rpt1 cd17740
first BRCT domain of Schizosaccharomyces pombe S-M checkpoint control protein Rad4 and similar ...
 169-249 5.48e-12

first BRCT domain of Schizosaccharomyces pombe S-M checkpoint control protein Rad4 and similar proteins; Rad4, also termed P74, or protein cut5, is an essential component for DNA replication and the checkpoint control system which couples the S and M phases. It may directly or indirectly interact with chromatin proteins to form the complex required for the initiation and/or progression of DNA synthesis. Rad4 contains four BRCT repeats. The family corresponds to the first one.


Pssm-ID: 349371  Cd Length: 82  Bit Score: 62.11  E-value: 5.48e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198079 169 RPLYctsmmNLVLCFTGFRKKEElVRLVTLVHHMGGVIRKDFNSKVTHLVANCTQGEKFRVAVSLG--TPIMKPEWIYKA 246
Cdd:cd17740    1 KPLS-----GIVLCCTSIPAEQR-TEIATKASKMGAAYTADLTSDVTHLVAGQVNTTKYKFAARSRpdIKVMTVEWVEHL 74


                 ...
gi 385198079 247 WER 249
Cdd:cd17740   75 YES 77
BRCT_TopBP1_rpt2_like cd17731
second BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins; ...
 269-342 2.37e-11

second BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins; TopBP1, also termed DNA topoisomerase II-beta-binding protein 1, or DNA topoisomerase II-binding protein 1, functions in DNA replication and damage response. It binds double-stranded DNA breaks and nicks as well as single-stranded DNA. TopBP1 contains six copies of BRCT domain. The family corresponds to the second BRCT domain.


Pssm-ID: 349363 [Multi-domain]  Cd Length: 77  Bit Score: 60.25  E-value: 2.37e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198079 269 PPFQDCILSFLGFSDEEKTNMEEMTEMQGGKYLPLGDERCTHLVVEENIvkdlpfepSKK---------LYVVKQEWFWG 339
Cdd:cd17731    1 PPFKGLVICVTGFDSEERKEIQQLVEQNGGSYSPDLSKNCTHLIAGSPS--------GQKyefarkwnsIHIVTPEWLYD 72


                 ...
gi 385198079 340 SIQ 342
Cdd:cd17731   73 SIE 75
BRCT pfam00533
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ...
 266-341 2.62e-11

BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in cell cycle checkpoint functions responsive to DNA damage. The BRCT domain of XRCC1 forms a homodimer in the crystal structure. This suggests that pairs of BRCT domains associate as homo- or heterodimers. BRCT domains are often found as tandem-repeat pairs. Structures of the BRCA1 BRCT domains revealed a basis for a widely utilized head-to-tail BRCT-BRCT oligomerization mode. This conserved tandem BRCT architecture facilitates formation of the canonical BRCT phospho-peptide interaction cleft at a groove between the BRCT domains. Disease associated missense and nonsense mutations in the BRCA1 BRCT domains disrupt peptide binding by directly occluding this peptide binding groove, or by disrupting key conserved BRCT core folding determinants.


Pssm-ID: 425736 [Multi-domain]  Cd Length: 75  Bit Score: 60.00  E-value: 2.62e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 385198079  266 FKVPPFQDCILSFLGFSDEEKTNMEEMTEMQGGKYLPLGDERCTHLVVEENIVKdLPFEPSKKLYVVKQEWFWGSI 341
Cdd:pfam00533   1 PKEKLFSGKTFVITGLDGLERDELKELIEKLGGKVTDSLSKKTTHVIVEARTKK-YLKAKELGIPIVTEEWLLDCI 75
BRCT_TopBP1_rpt2_like cd17731
second BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins; ...
 178-250 4.78e-11

second BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins; TopBP1, also termed DNA topoisomerase II-beta-binding protein 1, or DNA topoisomerase II-binding protein 1, functions in DNA replication and damage response. It binds double-stranded DNA breaks and nicks as well as single-stranded DNA. TopBP1 contains six copies of BRCT domain. The family corresponds to the second BRCT domain.


Pssm-ID: 349363 [Multi-domain]  Cd Length: 77  Bit Score: 59.48  E-value: 4.78e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 385198079 178 NLVLCFTGF--RKKEELVRLVTLvhhMGGVIRKDFNSKVTHLVANCTQGEKFRVAVSLGT-PIMKPEWIYKAWERR 250
Cdd:cd17731    5 GLVICVTGFdsEERKEIQQLVEQ---NGGSYSPDLSKNCTHLIAGSPSGQKYEFARKWNSiHIVTPEWLYDSIEAG 77
ROM1 COG5422
RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction ...
 446-652 2.39e-10

RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction mechanisms];


Pssm-ID: 227709 [Multi-domain]  Cd Length: 1175  Bit Score: 64.53  E-value: 2.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198079  446 VPSKQSARWQVAKELYQTESNYVNILATIIQLFQVPLEEEGqrggpiLAPEE-----IKTIFGSIPDIFDVHTKIKDDLE 520
Cdd:COG5422   478 LPKQEIKRQEAIYEVIYTERDFVKDLEYLRDTWIKPLEESN------IIPENarrnfIKHVFANINEIYAVNSKLLKALT 551

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198079  521 DLIVNWDESKSIGDIFLKYskdlVKTYPPFVNFFEMSKETIIKCEKQK---PRFHAFLKINQAKPECGRQSLVELLIRPV 597
Cdd:COG5422   552 NRQCLSPIVNGIADIFLDY----VPKFEPFIKYGASQPYAKYEFEREKsvnPNFARFDHEVERLDESRKLELDGYLTKPT 627

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 385198079  598 QRLPSVALLLNDLKKHTADENPDKSTLEKAIGSLKEVMTHINEDKRKTEAQKQIF 652
Cdd:COG5422   628 TRLARYPLLLEEVLKFTDPDNPDTEDIPKVIDMLREFLSRLNFESGKAENRGDLF 682
BRCT smart00292
breast cancer carboxy-terminal domain;
178-247 2.06e-09

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 54.69  E-value: 2.06e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 385198079   178 NLVLCFTGFRKKEELVRLVTLVHHMGGVIRKDFNSK-VTHLVANCTQGEK--FRVAVSLGTPIMKPEWIYKAW 247
Cdd:smart00292   6 GKTFYITGSFDKEERDELKELIEALGGKVTSSLSSKtTTHVIVGSPEGGKleLLKAIALGIPIVKEEWLLDCL 78
BRCT smart00292
breast cancer carboxy-terminal domain;
268-341 4.13e-08

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 51.22  E-value: 4.13e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 385198079   268 VPPFQDCILSFLG-FSDEEKTNMEEMTEMQGGKYLP-LGDERCTHLVVE--ENIVKDLPFEPSKKLYVVKQEWFWGSI 341
Cdd:smart00292   1 PKLFKGKTFYITGsFDKEERDELKELIEALGGKVTSsLSSKTTTHVIVGspEGGKLELLKAIALGIPIVKEEWLLDCL 78
BRCT cd00027
C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The ...
 274-340 9.41e-08

C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The BRCT (BRCA1 C-terminus) domain is found within many DNA damage repair and cell cycle checkpoint proteins. BRCT domains interact with each other forming homo/hetero BRCT multimers, but are also involved in BRCT-non-BRCT interactions and interactions within DNA strand breaks. BRCT tandem repeats bind to phosphopeptides; it has been shown that the repeats in human BRCA1 bind specifically to pS-X-X-F motifs, mediating the interaction between BRCA1 and the DNA helicase BACH1, or BRCA1 and CtIP, a transcriptional corepressor. It is assumed that BRCT repeats play similar roles in many signaling pathways associated with the response to DNA damage.


Pssm-ID: 349339 [Multi-domain]  Cd Length: 68  Bit Score: 49.67  E-value: 9.41e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 385198079 274 CILSFLGFSDEEKTNMEEMTEMQGGKYLPLGDERCTHLVVEENIV-KDLPFEPSKKLYVVKQEWFWGS 340
Cdd:cd00027    1 LVICFSGLDDEEREELKKLIEALGGKVSESLSSKVTHLIAKSPSGeKYYLAALAWGIPIVSPEWLLDC 68
BRCT_Rad4_rpt2 cd17746
second BRCT domain of Schizosaccharomyces pombe S-M checkpoint control protein Rad4 and ...
 268-345 2.55e-07

second BRCT domain of Schizosaccharomyces pombe S-M checkpoint control protein Rad4 and similar proteins; Rad4, also termed P74, or protein cut5, is an essential component for DNA replication and the checkpoint control system which couples S and M phases. It may directly or indirectly interact with chromatin proteins to form the complex required for the initiation and/or progression of DNA synthesis. Rad4 contains four BRCT repeats. The family corresponds to the second one.


Pssm-ID: 349377 [Multi-domain]  Cd Length: 91  Bit Score: 49.16  E-value: 2.55e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 385198079 268 VPPFQDCILSFLGFSDEEKTNMEEMTEMQGGKYLPLGDERCTHLVVEENIVKDLPFEPSKKLYVVKQEWFWGSIQMDA 345
Cdd:cd17746    4 LPTLFKCRVCLTNIGQPERSRIENYVLKHGGTFCPDLTRDVTHLIAGTSSGRKYEYALKWKINVVCVEWLWQSIQRNA 81
BRCT pfam00533
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ...
 178-244 6.20e-07

BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in cell cycle checkpoint functions responsive to DNA damage. The BRCT domain of XRCC1 forms a homodimer in the crystal structure. This suggests that pairs of BRCT domains associate as homo- or heterodimers. BRCT domains are often found as tandem-repeat pairs. Structures of the BRCA1 BRCT domains revealed a basis for a widely utilized head-to-tail BRCT-BRCT oligomerization mode. This conserved tandem BRCT architecture facilitates formation of the canonical BRCT phospho-peptide interaction cleft at a groove between the BRCT domains. Disease associated missense and nonsense mutations in the BRCA1 BRCT domains disrupt peptide binding by directly occluding this peptide binding groove, or by disrupting key conserved BRCT core folding determinants.


Pssm-ID: 425736 [Multi-domain]  Cd Length: 75  Bit Score: 47.67  E-value: 6.20e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 385198079  178 NLVLCFTGFR--KKEELVRLVTLvhhMGGVIRKDFNSKVTHLVANCTQgEKFRVAVSLGTPIMKPEWIY 244
Cdd:pfam00533   8 GKTFVITGLDglERDELKELIEK---LGGKVTDSLSKKTTHVIVEART-KKYLKAKELGIPIVTEEWLL 72
BRCT_PAXIP1_rpt2 cd17710
second BRCT domain of PAX-interacting protein 1 (PAXIP1) and similar proteins; PAXIP1, also ...
 178-243 1.19e-06

second BRCT domain of PAX-interacting protein 1 (PAXIP1) and similar proteins; PAXIP1, also termed PAX transactivation activation domain-interacting protein (PTIP), is involved in DNA damage response and in transcriptional regulation through histone methyltransferase (HMT) complexes. It also facilitates ATM-mediated activation of p53 and promotes cellular resistance to ionizing radiation. PAXIP1 contains six BRCT repeats. This family corresponds to the second BRCT domain.


Pssm-ID: 349342 [Multi-domain]  Cd Length: 81  Bit Score: 47.23  E-value: 1.19e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 385198079 178 NLVLCFTGFrKKEELVRLVTLVHHMGGVIRKDFNSKVTHLVANCTQGEKFRVAVSLGTP-IMKPEWI 243
Cdd:cd17710    4 GVVVCPSQI-SAEDRLKLWAMVTFHGGKCQLNLDKKCTHLVTGKASGAKYECALKHEGIkIVTPDWV 69
BRCT_PAXIP1_rpt4 cd17730
fourth BRCT domain of PAX-interacting protein 1 (PAXIP1) and similar proteins; PAXIP1, also ...
 179-249 1.79e-06

fourth BRCT domain of PAX-interacting protein 1 (PAXIP1) and similar proteins; PAXIP1, also termed PAX transactivation activation domain-interacting protein (PTIP), is involved in DNA damage response and in transcriptional regulation through histone methyltransferase (HMT) complexes. It also facilitates ATM-mediated activation of p53 and promotes cellular resistance to ionizing radiation. PAXIP1 contains six BRCT repeats. This family corresponds to the fourth BRCT domain.


Pssm-ID: 349362 [Multi-domain]  Cd Length: 73  Bit Score: 46.47  E-value: 1.79e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 385198079 179 LVLCFTGFRKKEElVRLVTLVHHMGGVIRKDFNSKVTHLVANCTQGEKFRVAVSLGTPIMKPEW---IYKAWER 249
Cdd:cd17730    1 QVISVTGFDGSER-EDIKRMIELMGAKYTGYLTRSNTHLICKRPEGEKYEKAKEWRIPVVNAQWledILLGGRL 73
BRCT_Rad4_rpt2 cd17746
second BRCT domain of Schizosaccharomyces pombe S-M checkpoint control protein Rad4 and ...
 175-249 1.14e-05

second BRCT domain of Schizosaccharomyces pombe S-M checkpoint control protein Rad4 and similar proteins; Rad4, also termed P74, or protein cut5, is an essential component for DNA replication and the checkpoint control system which couples S and M phases. It may directly or indirectly interact with chromatin proteins to form the complex required for the initiation and/or progression of DNA synthesis. Rad4 contains four BRCT repeats. The family corresponds to the second one.


Pssm-ID: 349377 [Multi-domain]  Cd Length: 91  Bit Score: 44.53  E-value: 1.14e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 385198079 175 SMMNLVLCFTGFrKKEELVRLVTLVHHMGGVIRKDFNSKVTHLVANCTQGEKFRVAVSLGTPIMKPEWIYKAWER 249
Cdd:cd17746    6 TLFKCRVCLTNI-GQPERSRIENYVLKHGGTFCPDLTRDVTHLIAGTSSGRKYEYALKWKINVVCVEWLWQSIQR 79
BRCT_CHS5_like cd17742
BRCT domain of yeast chitin biosynthesis protein CHS5 and similar proteins; CHS5, also termed ...
 182-243 3.63e-05

BRCT domain of yeast chitin biosynthesis protein CHS5 and similar proteins; CHS5, also termed protein CAL3, is a component of the CHS5/6 complex which mediates export of specific cargo proteins, including chitin synthase CHS3. It is also involved in targeting FUS1 to sites of polarized growth.


Pssm-ID: 349373 [Multi-domain]  Cd Length: 77  Bit Score: 42.71  E-value: 3.63e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 385198079 182 CFTGFRKKEELVRLVTLVHHMGGVIRKDFNSKVTHLVANCTQGEKFRVAVSLGTPIMKPEWI 243
Cdd:cd17742    6 CLGPLDPPESVDELEQCLERIGAKPTDRVAIDTTHFVCTVPSGPEYEKAKEMNIPIVRPEWL 67
BRCT_MDC1_rpt1 cd17744
first BRCT domain of mediator of DNA damage checkpoint protein 1 (MDC1) and similar proteins; ...
 183-251 4.46e-05

first BRCT domain of mediator of DNA damage checkpoint protein 1 (MDC1) and similar proteins; MDC1, also termed nuclear factor with BRCT domains 1 (NFBD1), is a nuclear chromatin-associated protein that is required for checkpoint mediated cell cycle arrest in response to DNA damage within both the S phase and G2/M phases of the cell cycle. It directly binds phosphorylated histone H2AX to regulate cellular responses to DNA double-strand breaks. MDC1 contains a forkhead-associated (FHA) domain and two BRCT domains, as well as an internal 41-amino acid repeat sequence. The family corresponds to the first BRCT domain.


Pssm-ID: 349375 [Multi-domain]  Cd Length: 72  Bit Score: 42.22  E-value: 4.46e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 385198079 183 FTGFRKKEELVRLVTLvhhMGGVIRKDFNSKvTHLVAN---CTQgeKFRVAVSLGTPIMKPEWIYKAWERRN 251
Cdd:cd17744    5 FTGVSDKEEGEKIIKK---LGGSVVDSVEDC-THLVTDkvrRTV--KFLCALARGIPIVSPDWLEASIKANK 70
BRCT_CTDP1 cd17729
BRCT domain of RNA polymerase II subunit A C-terminal domain phosphatase (CTDP1) and similar ...
 178-252 9.98e-05

BRCT domain of RNA polymerase II subunit A C-terminal domain phosphatase (CTDP1) and similar proteins; CTDP1 (EC 3.1.3.16), also termed TFIIF-associating CTD phosphatase, or TFIIF- associating RNA polymerase C-terminal domain phosphatase (FCP1), promotes the activity of RNA polymerase II through processively dephosphorylating 'Ser-2' and 'Ser-5' of the heptad repeats YSPTSPS in the C-terminal domain of the largest RNA polymerase II subunit. It plays a role in the exit from mitosis by dephosphorylating crucial mitotic substrates (USP44, CDC20 and WEE1) that are required for M-phase-promoting factor (MPF)/CDK1 inactivation.


Pssm-ID: 349361 [Multi-domain]  Cd Length: 97  Bit Score: 42.13  E-value: 9.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198079 178 NLVLCFTGFRKKE---ELVRLVTLVHHMGGVIRKDFNSKVTHLVA--NCTqgEKFRVAVSLGT-PIMKPEWIYKA---WE 248
Cdd:cd17729   16 GCVIVFSGVIPTGidpERSRLWKLAESLGAKVVTDLSPRTTHLVAakLGT--EKVKQALKMPGiHVVHPDWLWACaerWE 93


                 ....
gi 385198079 249 RRNE 252
Cdd:cd17729   94 RVDE 97
BRCT_BRC1_like_rpt4 cd18438
fourth BRCT domain of Schizosaccharomyces pombe BRCT-containing protein 1 (BRC1) and similar ...
 186-245 1.78e-04

fourth BRCT domain of Schizosaccharomyces pombe BRCT-containing protein 1 (BRC1) and similar proteins; Schizosaccharomyces pombe BRC1 is required for mitotic fidelity, specifically in the G2 phase of the cell cycle. It plays a role in chromatin organization. Members in this family contains six BRCT domains. This family corresponds to the fourth repeat.


Pssm-ID: 349391 [Multi-domain]  Cd Length: 68  Bit Score: 40.45  E-value: 1.78e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198079 186 FRKKEELVRLVTLVHHMGGVIRKDFNSKVTHLVANCTQGEKFRVAVSLGTPIMKPEWIYK 245
Cdd:cd18438    7 NYTGAARQYLEKLILALGATYTKNLKPDNTHLITASPEGEKYEAAKEWNIPIVNHLWLYD 66
BRCT_TopBP1_rpt7 cd17738
seventh BRCT domain of DNA topoisomerase 2-binding protein 1; TopBP1, also termed DNA ...
 183-244 5.85e-04

seventh BRCT domain of DNA topoisomerase 2-binding protein 1; TopBP1, also termed DNA topoisomerase II-beta-binding protein 1, or DNA topoisomerase II-binding protein 1, functions in DNA replication and damage response. It binds double-stranded DNA breaks and nicks as well as single-stranded DNA. TopBP1 contains six copies of BRCT domain. The family corresponds to the seventh BRCT domain. The Trp-X-X-X-Cys/Ser signature motif of the BRCT family is missing in this group.


Pssm-ID: 349370 [Multi-domain]  Cd Length: 75  Bit Score: 39.09  E-value: 5.85e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 385198079 183 FTGFrKKEELVRLVTLVHHMGGVI--RKDFNSKVTHLVA-NCTQGEKFRVAVSLGTPIMKPEWIY 244
Cdd:cd17738    6 LSGF-SEDEKKELISIIEKLGGKVldSDEFDPKCTHLICgKPSRSEKFLAACAAGKWILHPSYIE 69
BRCT_Bard1_rpt1 cd17734
first BRCT domain of BRCA1-associated RING domain protein 1 (Bard1) and similar proteins; ...
 179-243 8.27e-04

first BRCT domain of BRCA1-associated RING domain protein 1 (Bard1) and similar proteins; Bard1, also termed BARD-1, or RING-type E3 ubiquitin transferase BARD1, is a critical factor in BRCA1-mediated tumor suppression and may also serve as a target for tumorigenic lesions in some human cancers. It associates with BRCA1 (breast cancer-1) to form a heterodimeric BRCA1/BARD1 complex that is responsible for maintaining genomic stability through nuclear functions involving DNA damage signaling and repair, transcriptional regulation, and cell cycle control. The BRCA1/BARD1 complex catalyzes autoubiquitination of BRCA1 and trans ubiquitination of other protein substrates. Its E3 ligase activity is dramatically reduced in the presence of UBX domain protein 1 (UBXN1). BARD-1 contains an N-terminal C3HC4-type RING-HC finger that binds BRCA1, and a C-terminal region with three ankyrin repeats and tandem BRCT domains that bind CstF-50 (cleavage stimulation factor) to modulate mRNA processing and RNAP II stability in response to DNA damage. The family corresponds to the first BRCT domain.


Pssm-ID: 349366  Cd Length: 80  Bit Score: 39.12  E-value: 8.27e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 385198079 179 LVLCFTGFRK--KEELVRLVTLvhhMGGVIRKDFNSKVTHLVA------NCTQGEKFRVAVSLGTPIMKPEWI 243
Cdd:cd17734    1 LVLLGSGLSSeqKKLLEKLAQL---LKAKVVTEFSPEVTHVVVpadergVCPRTMKYLMGILAGKWIVSFEWV 70
BRCT_TopBP1_rpt6 cd17727
sixth BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins; ...
 187-245 1.26e-03

sixth BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins; TopBP1, also termed DNA topoisomerase II-beta-binding protein 1, or DNA topoisomerase II-binding protein 1, functions in DNA replication and damage response. It binds double-stranded DNA breaks and nicks as well as single-stranded DNA. TopBP1 contains six copies of BRCT domain. The family corresponds to the sixth BRCT domain.


Pssm-ID: 349359 [Multi-domain]  Cd Length: 75  Bit Score: 38.35  E-value: 1.26e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 385198079 187 RKKEELVRLVTlvhHMGGVIRKDFNSKVTHLVANCTQGEK---FRVAVSLGTPIMKPEWIYK 245
Cdd:cd17727   14 KRQGELNKIAA---SLGAEYRWTYDESCTHFIYQGKANDTnreYKSAKEQGKFIVSPHWLYA 72
BRCT_PARP4_like cd17726
BRCT domain of poly [ADP-ribose] polymerase 4 (PARP-4) and similar proteins; PARP-4, also ...
 184-245 1.55e-03

BRCT domain of poly [ADP-ribose] polymerase 4 (PARP-4) and similar proteins; PARP-4, also termed 193 kDa vault protein, or ADP-ribosyltransferase diphtheria toxin-like 4 (ARTD4), or PARP-related/IalphaI-related H5/proline-rich (PH5P), or vault poly(ADP-ribose) polymerase (VPARP), shows poly(ADP-ribosyl)ation activity that catalyzes the formation of ADP-ribose polymers in response to DNA damage. PARP-4 is a component of the vault ribonucleoprotein particle, at least composed of MVP, PARP4 and one or more vault RNAs (vRNAs). The Trp-X-X-X-Cys/Ser signature motif of the BRCT family is not conserved in this group.


Pssm-ID: 349358 [Multi-domain]  Cd Length: 85  Bit Score: 38.42  E-value: 1.55e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 385198079 184 TGFRKKEELVRLVTlvhHMGGVIRKDFNSKVTHLV---ANCTQGEKFRVAVSLGTPIMKPEWIYK 245
Cdd:cd17726   15 PGFKEKKKLKKKIT---ENGGIISYIINKKCTHVVvnnAKALSSYKCRMAQKYGIPVVSLDYIWK 76
BRCT_PAXIP1_rpt5 cd17712
fifth BRCT domain of PAX-interacting protein 1 (PAXIP1) and similar proteins; PAXIP1, also ...
 180-250 3.23e-03

fifth BRCT domain of PAX-interacting protein 1 (PAXIP1) and similar proteins; PAXIP1, also termed PAX transactivation activation domain-interacting protein (PTIP), is involved in DNA damage response and in transcriptional regulation through histone methyltransferase (HMT) complexes. It also facilitates ATM-mediated activation of p53 and promotes cellular resistance to ionizing radiation. PAXIP1 contains six BRCT repeats. This family corresponds to the fifth BRCT domain.


Pssm-ID: 349344  Cd Length: 75  Bit Score: 37.22  E-value: 3.23e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 385198079 180 VLCFTGFRKKEElVRLVTLVHHMGGVIRKDfNSKVTHLVAN-CTQGEKFRVAVSLGTPIMKPEWIYKAWERR 250
Cdd:cd17712    3 RVLFTGFDPVQV-RKLTKKVTILGGEVVES-PQECTHLVAPkVSRTVKFLTAISVCKHIVTPEWLEESFKQG 72
BRCT_nibrin cd17741
BRCT domain of nibrin and similar proteins; Nibrin (NBN), also termed Nijmegen breakage ...
 179-244 4.93e-03

BRCT domain of nibrin and similar proteins; Nibrin (NBN), also termed Nijmegen breakage syndrome protein 1 (NBS1), or cell cycle regulatory protein p95, is a novel DNA double-strand break repair protein that is mutated in Nijmegen breakage syndrome. It is a component of the MRE11-RAD50-NBN (MRN complex) which plays a critical role in the cellular response to DNA damage and the maintenance of chromosome integrity. The BRCT (Breast Cancer Suppressor Protein BRCA1, carboxy-terminal) domain is found within many DNA damage repair and cell cycle checkpoint proteins. The unique diversity of this domain superfamily allows BRCT modules to interact forming homo/hetero BRCT multimers, BRCT-non-BRCT interactions, and interactions within DNA strand breaks. The Trp-X-X-X-Cys/Ser signature motif of the BRCT family is absent in this group.


Pssm-ID: 349372 [Multi-domain]  Cd Length: 74  Bit Score: 36.43  E-value: 4.93e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 385198079 179 LVLCFTGFRKkEELVRLVTLVHHMGGVIRKDFNSKVTHLV-ANCTQGEKFRVAVSLGTPIMKPEWIY 244
Cdd:cd17741    3 LVVCSSCLDS-EEKKKLKQIIAKLGGKVVNEWTEECTHLVmSKIKVTVKVICALISGKPIVTPEYLD 68
BRCT_XRCC1_rpt1 cd17725
First (central) BRCT domain in X-ray repair cross-complementing protein 1 (XRCC1) and similar ...
 202-255 5.16e-03

First (central) BRCT domain in X-ray repair cross-complementing protein 1 (XRCC1) and similar proteins; XRCC1 is a DNA repair protein that corrects defective DNA strand-break repair and sister chromatid exchange following treatment with ionizing radiation and alkylating agents. It forms homodimers and interacts with polynucleotide kinase (PNK), DNA polymerase-beta (POLB), DNA ligase III (LIG3), APTX, APLF, and APEX1. XRCC1 contains an N-terminal XRCC1-specific domain and two BRCT domains. This family corresponds to the first one.


Pssm-ID: 349357 [Multi-domain]  Cd Length: 80  Bit Score: 36.87  E-value: 5.16e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 385198079 202 MGGVIRKDFNSKVTHLVANCTQGEKFRVAVSLGTPIMKPEWI---YKAWERRNEQDF 255
Cdd:cd17725   24 MGAKYRPDWTADCTHLICAFANTPKYKQVKGAGGIIVSKEWIldcYKKKKRLPWKRY 80
 
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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