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Conserved domains on  [gi|612047297|ref|XP_007502005|]
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protein ECT2 isoform X1 [Monodelphis domestica]

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 ...
 628-801 5.04e-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: 5.04e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612047297 628 LKEVMTHINEDKRKTEAQKQIFDVVYEVDGCPANLLSSHRSLVQRVETISLG-EYPCDRGEQVTLFLFNDCLEIARKRHK 706
Cdd:cd01229    1 LKEVMTHINEDKRKTESQAQMFDIVNEIENCPPTLLSSHRSFVSRCEVVELGdSLKSGRGDSLTLFLFSDLIEICKKRSS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612047297 707 VIGTFKSPHGHTR-----PPAALKHIHLMPLSQIKKVLDIKETEDCHNAFALLVRPPTEQANVLLSFQMTSEDLPKDTWL 781
Cdd:cd01229   81 VKGTSKSPRGSTGsglreSKKKYKHVKLMPLSTIKRVIDIRETEDCQRVFALLFRHPTELKEKLYSFQILDEETDKESFL 160

                        170       180
                 ....*....|....*....|
gi 612047297 782 KMLCRHVANTICKADAENLI 801
Cdd:cd01229  161 KTLCKQVANTVCRADAENFL 180
BRCT_Ect2_rpt1 cd17733
first BRCT domain of epithelial cell-transforming sequence 2 protein (ECT2) and similar ...
 173-248 8.14e-50

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: 169.81  E-value: 8.14e-50
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 612047297 173 MLNLVLCFTGFRKKEELVKLVTLAHHMGGTIRKDFNSKVTHLVANCTQGEKFRVAVSLGTPIMKPEWIFKAWERRN 248
Cdd:cd17733    1 MENLVLCFTGFRKKEELSRLVNLVHHMGGSIRKDFSSKVTHLVANSTQGEKYRVAVSLGTPIMTEDWIYKAWEKRN 76
RhoGEF smart00325
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange ...
 453-637 1.83e-49

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: 172.87  E-value: 1.83e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612047297   453 VAKELYQTESNYVDILATIIQLFQIPLEEEGQrggpILAPEEIKAIFGSIPDIFDVHTKIKEDLEDLIINWDESK-SIGD 531
Cdd:smart00325   1 VLKELLQTERNYVRDLKLLVEVFLKPLKKELK----LLSPNELETLFGNIEEIYEFHRDFLDELEERIEEWDDSVeRIGD 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612047297   532 IFLKYSKDLvKIYPPFVNFFEMSKETIVKCeKQKPRFHAFLKINQAKPECGRQSLAELLIRPVQRLPSVALLLNDLKKHT 611
Cdd:smart00325  77 VFLKLEEFF-KIYSEYCSNHPDALELLKKL-KKNPRFQKFLKEIESSPQCRRLTLESLLLKPVQRLTKYPLLLKELLKHT 154

                          170       180
                   ....*....|....*....|....*.
gi 612047297   612 SDDNPDKNTLERAIGSLKEVMTHINE 637
Cdd:smart00325 155 PEDHEDREDLKKALKAIKELANQVNE 180
BRCT_Ect2_rpt2 cd17732
second BRCT domain of epithelial cell-transforming sequence 2 protein (ECT2) and similar ...
 267-346 8.64e-46

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: 158.59  E-value: 8.64e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612047297 267 PFQDCMLSFLGFSDEERANMEEMTEMQGGHCLPVGDEQCTHLIVEENAIKELPFEPSKKLYVVKQEWFWGSIQMDARAGE 346
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 ...
 628-801 5.04e-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: 5.04e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612047297 628 LKEVMTHINEDKRKTEAQKQIFDVVYEVDGCPANLLSSHRSLVQRVETISLG-EYPCDRGEQVTLFLFNDCLEIARKRHK 706
Cdd:cd01229    1 LKEVMTHINEDKRKTESQAQMFDIVNEIENCPPTLLSSHRSFVSRCEVVELGdSLKSGRGDSLTLFLFSDLIEICKKRSS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612047297 707 VIGTFKSPHGHTR-----PPAALKHIHLMPLSQIKKVLDIKETEDCHNAFALLVRPPTEQANVLLSFQMTSEDLPKDTWL 781
Cdd:cd01229   81 VKGTSKSPRGSTGsglreSKKKYKHVKLMPLSTIKRVIDIRETEDCQRVFALLFRHPTELKEKLYSFQILDEETDKESFL 160

                        170       180
                 ....*....|....*....|
gi 612047297 782 KMLCRHVANTICKADAENLI 801
Cdd:cd01229  161 KTLCKQVANTVCRADAENFL 180
BRCT_Ect2_rpt1 cd17733
first BRCT domain of epithelial cell-transforming sequence 2 protein (ECT2) and similar ...
 173-248 8.14e-50

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: 169.81  E-value: 8.14e-50
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 612047297 173 MLNLVLCFTGFRKKEELVKLVTLAHHMGGTIRKDFNSKVTHLVANCTQGEKFRVAVSLGTPIMKPEWIFKAWERRN 248
Cdd:cd17733    1 MENLVLCFTGFRKKEELSRLVNLVHHMGGSIRKDFSSKVTHLVANSTQGEKYRVAVSLGTPIMTEDWIYKAWEKRN 76
RhoGEF smart00325
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange ...
 453-637 1.83e-49

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: 172.87  E-value: 1.83e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612047297   453 VAKELYQTESNYVDILATIIQLFQIPLEEEGQrggpILAPEEIKAIFGSIPDIFDVHTKIKEDLEDLIINWDESK-SIGD 531
Cdd:smart00325   1 VLKELLQTERNYVRDLKLLVEVFLKPLKKELK----LLSPNELETLFGNIEEIYEFHRDFLDELEERIEEWDDSVeRIGD 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612047297   532 IFLKYSKDLvKIYPPFVNFFEMSKETIVKCeKQKPRFHAFLKINQAKPECGRQSLAELLIRPVQRLPSVALLLNDLKKHT 611
Cdd:smart00325  77 VFLKLEEFF-KIYSEYCSNHPDALELLKKL-KKNPRFQKFLKEIESSPQCRRLTLESLLLKPVQRLTKYPLLLKELLKHT 154

                          170       180
                   ....*....|....*....|....*.
gi 612047297   612 SDDNPDKNTLERAIGSLKEVMTHINE 637
Cdd:smart00325 155 PEDHEDREDLKKALKAIKELANQVNE 180
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
 450-636 6.21e-49

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: 171.33  E-value: 6.21e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612047297 450 RWQVAKELYQTESNYVDILATIIQLFQIPLEEEGQRggpiLAPEEIKAIFGSIPDIFDVHTKIKEDLEDLIINWDESK-S 528
Cdd:cd00160    1 RQEVIKELLQTERNYVRDLKLLVEVFLKPLDKELLP----LSPEEVELLFGNIEEIYEFHRIFLKSLEERVEEWDKSGpR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612047297 529 IGDIFLKYsKDLVKIYPPFVNFFEMSKETIVKCEKQKPRFHAFLKinQAKPECGRQSLAELLIRPVQRLPSVALLLNDLK 608
Cdd:cd00160   77 IGDVFLKL-APFFKIYSEYCSNHPDALELLKKLKKFNKFFQEFLE--KAESECGRLKLESLLLKPVQRLTKYPLLLKELL 153

                        170       180
                 ....*....|....*....|....*...
gi 612047297 609 KHTSDDNPDKNTLERAIGSLKEVMTHIN 636
Cdd:cd00160  154 KHTPDGHEDREDLKKALEAIKEVASQVN 181
RhoGEF pfam00621
RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called ...
 453-636 2.47e-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: 166.71  E-value: 2.47e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612047297  453 VAKELYQTESNYVDILATIIQLFQIPLEEegqrggPI-LAPEEIKAIFGSIPDIFDVHTKikEDLEDLIINWDESKSIGD 531
Cdd:pfam00621   1 VIKELLQTERSYVRDLEILVEVFLPPNSK------PLsESEEEIKTIFSNIEEIYELHRQ--LLLEELLKEWISIQRIGD 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612047297  532 IFLKYSKDLvKIYPPFVNFFEMSKETIVKCEKQKPRFHAFLKINQAKPECGRQSLAELLIRPVQRLPSVALLLNDLKKHT 611
Cdd:pfam00621  73 IFLKFAPGF-KVYSTYCSNYPKALKLLKKLLKKNPKFRAFLEELEANPECRGLDLNSFLIKPVQRIPRYPLLLKELLKHT 151

                         170       180
                  ....*....|....*....|....*
gi 612047297  612 SDDNPDKNTLERAIGSLKEVMTHIN 636
Cdd:pfam00621 152 PPDHPDYEDLKKALEAIKEVAKQIN 176
BRCT_Ect2_rpt2 cd17732
second BRCT domain of epithelial cell-transforming sequence 2 protein (ECT2) and similar ...
 267-346 8.64e-46

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: 158.59  E-value: 8.64e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612047297 267 PFQDCMLSFLGFSDEERANMEEMTEMQGGHCLPVGDEQCTHLIVEENAIKELPFEPSKKLYVVKQEWFWGSIQMDARAGE 346
Cdd:cd17732    1 PFEGCTLSFLGFSDEEKTHMEELTEENGGKVTPLGDPSCTHLVVDESTVKELPFEPSSKLHVVKQEWFWASIQMDACADE 80
PTCB-BRCT pfam12738
twin BRCT domain; This is a BRCT domain that appears in duplicate in most member sequences. ...
 176-239 6.26e-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: 81.48  E-value: 6.26e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 612047297  176 LVLCFTGFRKkEELVKLVTLAHHMGGTIRKDFNSKVTHLVANCTQGEKFRVAVSLGTPIMKPEW 239
Cdd:pfam12738   1 LVICVTGFDG-DDREGLQKLIEAMGAEYTKDLTKSVTHLICKSGEGEKYEKAKEWGIPVVSPLW 63
ROM1 COG5422
RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction ...
 443-649 1.42e-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: 65.30  E-value: 1.42e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612047297  443 VPPKQSARWQVAKELYQTESNYVDILATIIQLFQIPLEEEGqrggpiLAPEE-----IKAIFGSIPDIFDVHTKIKEDLE 517
Cdd:COG5422   478 LPKQEIKRQEAIYEVIYTERDFVKDLEYLRDTWIKPLEESN------IIPENarrnfIKHVFANINEIYAVNSKLLKALT 551

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612047297  518 DLIINWDESKSIGDIFLKYskdlVKIYPPFVNFFEMSKETIVKCEKQK---PRFHAFLKINQAKPECGRQSLAELLIRPV 594
Cdd:COG5422   552 NRQCLSPIVNGIADIFLDY----VPKFEPFIKYGASQPYAKYEFEREKsvnPNFARFDHEVERLDESRKLELDGYLTKPT 627

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 612047297  595 QRLPSVALLLNDLKKHTSDDNPDKNTLERAIGSLKEVMTHINEDKRKTEAQKQIF 649
Cdd:COG5422   628 TRLARYPLLLEEVLKFTDPDNPDTEDIPKVIDMLREFLSRLNFESGKAENRGDLF 682
BRCT pfam00533
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ...
 263-338 5.05e-10

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: 56.53  E-value: 5.05e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 612047297  263 FKVPPFQDCMLSFLGFSDEERANMEEMTEMQGGHCLPVGDEQCTHLIVEENAIKELpFEPSKKLYVVKQEWFWGSI 338
Cdd:pfam00533   1 PKEKLFSGKTFVITGLDGLERDELKELIEKLGGKVTDSLSKKTTHVIVEARTKKYL-KAKELGIPIVTEEWLLDCI 75
BRCT smart00292
breast cancer carboxy-terminal domain;
175-244 5.93e-10

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 56.23  E-value: 5.93e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 612047297   175 NLVLCFTGFRKKEELVKLVTLAHHMGGTIRKDFNSK-VTHLVANCTQGEK--FRVAVSLGTPIMKPEWIFKAW 244
Cdd:smart00292   6 GKTFYITGSFDKEERDELKELIEALGGKVTSSLSSKtTTHVIVGSPEGGKleLLKAIALGIPIVKEEWLLDCL 78
BRCT smart00292
breast cancer carboxy-terminal domain;
265-338 1.06e-08

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 52.76  E-value: 1.06e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 612047297   265 VPPFQDCMLSFLG-FSDEERANMEEMTEMQGGHCLP-VGDEQCTHLIVE--ENAIKELPFEPSKKLYVVKQEWFWGSI 338
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 ...
 628-801 5.04e-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: 5.04e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612047297 628 LKEVMTHINEDKRKTEAQKQIFDVVYEVDGCPANLLSSHRSLVQRVETISLG-EYPCDRGEQVTLFLFNDCLEIARKRHK 706
Cdd:cd01229    1 LKEVMTHINEDKRKTESQAQMFDIVNEIENCPPTLLSSHRSFVSRCEVVELGdSLKSGRGDSLTLFLFSDLIEICKKRSS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612047297 707 VIGTFKSPHGHTR-----PPAALKHIHLMPLSQIKKVLDIKETEDCHNAFALLVRPPTEQANVLLSFQMTSEDLPKDTWL 781
Cdd:cd01229   81 VKGTSKSPRGSTGsglreSKKKYKHVKLMPLSTIKRVIDIRETEDCQRVFALLFRHPTELKEKLYSFQILDEETDKESFL 160

                        170       180
                 ....*....|....*....|
gi 612047297 782 KMLCRHVANTICKADAENLI 801
Cdd:cd01229  161 KTLCKQVANTVCRADAENFL 180
BRCT_Ect2_rpt1 cd17733
first BRCT domain of epithelial cell-transforming sequence 2 protein (ECT2) and similar ...
 173-248 8.14e-50

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: 169.81  E-value: 8.14e-50
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 612047297 173 MLNLVLCFTGFRKKEELVKLVTLAHHMGGTIRKDFNSKVTHLVANCTQGEKFRVAVSLGTPIMKPEWIFKAWERRN 248
Cdd:cd17733    1 MENLVLCFTGFRKKEELSRLVNLVHHMGGSIRKDFSSKVTHLVANSTQGEKYRVAVSLGTPIMTEDWIYKAWEKRN 76
RhoGEF smart00325
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange ...
 453-637 1.83e-49

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: 172.87  E-value: 1.83e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612047297   453 VAKELYQTESNYVDILATIIQLFQIPLEEEGQrggpILAPEEIKAIFGSIPDIFDVHTKIKEDLEDLIINWDESK-SIGD 531
Cdd:smart00325   1 VLKELLQTERNYVRDLKLLVEVFLKPLKKELK----LLSPNELETLFGNIEEIYEFHRDFLDELEERIEEWDDSVeRIGD 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612047297   532 IFLKYSKDLvKIYPPFVNFFEMSKETIVKCeKQKPRFHAFLKINQAKPECGRQSLAELLIRPVQRLPSVALLLNDLKKHT 611
Cdd:smart00325  77 VFLKLEEFF-KIYSEYCSNHPDALELLKKL-KKNPRFQKFLKEIESSPQCRRLTLESLLLKPVQRLTKYPLLLKELLKHT 154

                          170       180
                   ....*....|....*....|....*.
gi 612047297   612 SDDNPDKNTLERAIGSLKEVMTHINE 637
Cdd:smart00325 155 PEDHEDREDLKKALKAIKELANQVNE 180
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
 450-636 6.21e-49

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: 171.33  E-value: 6.21e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612047297 450 RWQVAKELYQTESNYVDILATIIQLFQIPLEEEGQRggpiLAPEEIKAIFGSIPDIFDVHTKIKEDLEDLIINWDESK-S 528
Cdd:cd00160    1 RQEVIKELLQTERNYVRDLKLLVEVFLKPLDKELLP----LSPEEVELLFGNIEEIYEFHRIFLKSLEERVEEWDKSGpR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612047297 529 IGDIFLKYsKDLVKIYPPFVNFFEMSKETIVKCEKQKPRFHAFLKinQAKPECGRQSLAELLIRPVQRLPSVALLLNDLK 608
Cdd:cd00160   77 IGDVFLKL-APFFKIYSEYCSNHPDALELLKKLKKFNKFFQEFLE--KAESECGRLKLESLLLKPVQRLTKYPLLLKELL 153

                        170       180
                 ....*....|....*....|....*...
gi 612047297 609 KHTSDDNPDKNTLERAIGSLKEVMTHIN 636
Cdd:cd00160  154 KHTPDGHEDREDLKKALEAIKEVASQVN 181
RhoGEF pfam00621
RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called ...
 453-636 2.47e-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: 166.71  E-value: 2.47e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612047297  453 VAKELYQTESNYVDILATIIQLFQIPLEEegqrggPI-LAPEEIKAIFGSIPDIFDVHTKikEDLEDLIINWDESKSIGD 531
Cdd:pfam00621   1 VIKELLQTERSYVRDLEILVEVFLPPNSK------PLsESEEEIKTIFSNIEEIYELHRQ--LLLEELLKEWISIQRIGD 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612047297  532 IFLKYSKDLvKIYPPFVNFFEMSKETIVKCEKQKPRFHAFLKINQAKPECGRQSLAELLIRPVQRLPSVALLLNDLKKHT 611
Cdd:pfam00621  73 IFLKFAPGF-KVYSTYCSNYPKALKLLKKLLKKNPKFRAFLEELEANPECRGLDLNSFLIKPVQRIPRYPLLLKELLKHT 151

                         170       180
                  ....*....|....*....|....*
gi 612047297  612 SDDNPDKNTLERAIGSLKEVMTHIN 636
Cdd:pfam00621 152 PPDHPDYEDLKKALEAIKEVAKQIN 176
BRCT_Ect2_rpt2 cd17732
second BRCT domain of epithelial cell-transforming sequence 2 protein (ECT2) and similar ...
 267-346 8.64e-46

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: 158.59  E-value: 8.64e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612047297 267 PFQDCMLSFLGFSDEERANMEEMTEMQGGHCLPVGDEQCTHLIVEENAIKELPFEPSKKLYVVKQEWFWGSIQMDARAGE 346
Cdd:cd17732    1 PFEGCTLSFLGFSDEEKTHMEELTEENGGKVTPLGDPSCTHLVVDESTVKELPFEPSSKLHVVKQEWFWASIQMDACADE 80
PTCB-BRCT pfam12738
twin BRCT domain; This is a BRCT domain that appears in duplicate in most member sequences. ...
 176-239 6.26e-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: 81.48  E-value: 6.26e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 612047297  176 LVLCFTGFRKkEELVKLVTLAHHMGGTIRKDFNSKVTHLVANCTQGEKFRVAVSLGTPIMKPEW 239
Cdd:pfam12738   1 LVICVTGFDG-DDREGLQKLIEAMGAEYTKDLTKSVTHLICKSGEGEKYEKAKEWGIPVVSPLW 63
BRCT_TopBP1_rpt1 cd17737
first BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins; ...
 175-246 2.37e-17

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: 77.06  E-value: 2.37e-17
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 612047297 175 NLVLCFTGFRKK--EELVKLVtlaHHMGGTIRKDFNSKVTHLVANCTQGEKFRVAVSLGTPIMKPEWIFKAWER 246
Cdd:cd17737    1 DVTISCTSLEKEerEEVHKYV---QLMGGRVSRDLTVSVTHLIAGEVGSKKYLVAASLKKPIMLPSWVKTLWEK 71
BRCT cd00027
C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The ...
 176-242 4.15e-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: 70.47  E-value: 4.15e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 612047297 176 LVLCFTGFRKKEELvKLVTLAHHMGGTIRKDFNSKVTHLVANCTQGEK-FRVAVSLGTPIMKPEWIFK 242
Cdd:cd00027    1 LVICFSGLDDEERE-ELKKLIEALGGKVSESLSSKVTHLIAKSPSGEKyYLAALAWGIPIVSPEWLLD 67
BRCT_Rad4_rpt1 cd17740
first BRCT domain of Schizosaccharomyces pombe S-M checkpoint control protein Rad4 and similar ...
 166-246 1.89e-13

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: 66.35  E-value: 1.89e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612047297 166 RPLYcasmlNLVLCFTGFRKKEElVKLVTLAHHMGGTIRKDFNSKVTHLVANCTQGEKFRVAVSLG--TPIMKPEWIFKA 243
Cdd:cd17740    1 KPLS-----GIVLCCTSIPAEQR-TEIATKASKMGAAYTADLTSDVTHLVAGQVNTTKYKFAARSRpdIKVMTVEWVEHL 74


                 ...
gi 612047297 244 WER 246
Cdd:cd17740   75 YES 77
BRCT_TopBP1_rpt2_like cd17731
second BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins; ...
 266-339 5.30e-12

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: 62.17  E-value: 5.30e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612047297 266 PPFQDCMLSFLGFSDEERANMEEMTEMQGGHCLPVGDEQCTHLIVEEN-------AIKElpfepsKKLYVVKQEWFWGSI 338
Cdd:cd17731    1 PPFKGLVICVTGFDSEERKEIQQLVEQNGGSYSPDLSKNCTHLIAGSPsgqkyefARKW------NSIHIVTPEWLYDSI 74


                 .
gi 612047297 339 Q 339
Cdd:cd17731   75 E 75
BRCT_TopBP1_rpt2_like cd17731
second BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins; ...
 173-247 7.85e-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: 58.71  E-value: 7.85e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 612047297 173 MLNLVLCFTGF--RKKEELVKLVTLahhMGGTIRKDFNSKVTHLVANCTQGEKFRVAVSLGT-PIMKPEWIFKAWERR 247
Cdd:cd17731    3 FKGLVICVTGFdsEERKEIQQLVEQ---NGGSYSPDLSKNCTHLIAGSPSGQKYEFARKWNSiHIVTPEWLYDSIEAG 77
ROM1 COG5422
RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction ...
 443-649 1.42e-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: 65.30  E-value: 1.42e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612047297  443 VPPKQSARWQVAKELYQTESNYVDILATIIQLFQIPLEEEGqrggpiLAPEE-----IKAIFGSIPDIFDVHTKIKEDLE 517
Cdd:COG5422   478 LPKQEIKRQEAIYEVIYTERDFVKDLEYLRDTWIKPLEESN------IIPENarrnfIKHVFANINEIYAVNSKLLKALT 551

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612047297  518 DLIINWDESKSIGDIFLKYskdlVKIYPPFVNFFEMSKETIVKCEKQK---PRFHAFLKINQAKPECGRQSLAELLIRPV 594
Cdd:COG5422   552 NRQCLSPIVNGIADIFLDY----VPKFEPFIKYGASQPYAKYEFEREKsvnPNFARFDHEVERLDESRKLELDGYLTKPT 627

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 612047297  595 QRLPSVALLLNDLKKHTSDDNPDKNTLERAIGSLKEVMTHINEDKRKTEAQKQIF 649
Cdd:COG5422   628 TRLARYPLLLEEVLKFTDPDNPDTEDIPKVIDMLREFLSRLNFESGKAENRGDLF 682
BRCT pfam00533
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ...
 263-338 5.05e-10

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: 56.53  E-value: 5.05e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 612047297  263 FKVPPFQDCMLSFLGFSDEERANMEEMTEMQGGHCLPVGDEQCTHLIVEENAIKELpFEPSKKLYVVKQEWFWGSI 338
Cdd:pfam00533   1 PKEKLFSGKTFVITGLDGLERDELKELIEKLGGKVTDSLSKKTTHVIVEARTKKYL-KAKELGIPIVTEEWLLDCI 75
BRCT smart00292
breast cancer carboxy-terminal domain;
175-244 5.93e-10

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 56.23  E-value: 5.93e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 612047297   175 NLVLCFTGFRKKEELVKLVTLAHHMGGTIRKDFNSK-VTHLVANCTQGEK--FRVAVSLGTPIMKPEWIFKAW 244
Cdd:smart00292   6 GKTFYITGSFDKEERDELKELIEALGGKVTSSLSSKtTTHVIVGSPEGGKleLLKAIALGIPIVKEEWLLDCL 78
BRCT smart00292
breast cancer carboxy-terminal domain;
265-338 1.06e-08

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 52.76  E-value: 1.06e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 612047297   265 VPPFQDCMLSFLG-FSDEERANMEEMTEMQGGHCLP-VGDEQCTHLIVE--ENAIKELPFEPSKKLYVVKQEWFWGSI 338
Cdd:smart00292   1 PKLFKGKTFYITGsFDKEERDELKELIEALGGKVTSsLSSKTTTHVIVGspEGGKLELLKAIALGIPIVKEEWLLDCL 78
BRCT pfam00533
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ...
 173-241 1.53e-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: 49.21  E-value: 1.53e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 612047297  173 MLNLVLCFTGFR--KKEELVKLVTLahhMGGTIRKDFNSKVTHLVANCTQgEKFRVAVSLGTPIMKPEWIF 241
Cdd:pfam00533   6 FSGKTFVITGLDglERDELKELIEK---LGGKVTDSLSKKTTHVIVEART-KKYLKAKELGIPIVTEEWLL 72
BRCT_Rad4_rpt2 cd17746
second BRCT domain of Schizosaccharomyces pombe S-M checkpoint control protein Rad4 and ...
 265-342 2.57e-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: 2.57e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 612047297 265 VPPFQDCMLSFLGFSDEERANMEEMTEMQGGHCLPVGDEQCTHLIVEENAIKELPFEPSKKLYVVKQEWFWGSIQMDA 342
Cdd:cd17746    4 LPTLFKCRVCLTNIGQPERSRIENYVLKHGGTFCPDLTRDVTHLIAGTSSGRKYEYALKWKINVVCVEWLWQSIQRNA 81
BRCT_PAXIP1_rpt2 cd17710
second BRCT domain of PAX-interacting protein 1 (PAXIP1) and similar proteins; PAXIP1, also ...
 175-240 1.48e-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: 46.84  E-value: 1.48e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 612047297 175 NLVLCFTGFrKKEELVKLVTLAHHMGGTIRKDFNSKVTHLVANCTQGEKFRVAVSLGTP-IMKPEWI 240
Cdd:cd17710    4 GVVVCPSQI-SAEDRLKLWAMVTFHGGKCQLNLDKKCTHLVTGKASGAKYECALKHEGIkIVTPDWV 69
BRCT_PAXIP1_rpt4 cd17730
fourth BRCT domain of PAX-interacting protein 1 (PAXIP1) and similar proteins; PAXIP1, also ...
 176-240 2.05e-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: 46.08  E-value: 2.05e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 612047297 176 LVLCFTGFRKKEElVKLVTLAHHMGGTIRKDFNSKVTHLVANCTQGEKFRVAVSLGTPIMKPEWI 240
Cdd:cd17730    1 QVISVTGFDGSER-EDIKRMIELMGAKYTGYLTRSNTHLICKRPEGEKYEKAKEWRIPVVNAQWL 64
BRCT_CHS5_like cd17742
BRCT domain of yeast chitin biosynthesis protein CHS5 and similar proteins; CHS5, also termed ...
 179-241 2.40e-06

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: 46.17  E-value: 2.40e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 612047297 179 CFTGFRKKEELVKLVTLAHHMGGTIRKDFNSKVTHLVANCTQGEKFRVAVSLGTPIMKPEWIF 241
Cdd:cd17742    6 CLGPLDPPESVDELEQCLERIGAKPTDRVAIDTTHFVCTVPSGPEYEKAKEMNIPIVRPEWLR 68
BRCT cd00027
C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The ...
 273-337 3.04e-06

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: 45.43  E-value: 3.04e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 612047297 273 LSFLGFSDEERANMEEMTEMQGGHCLPVGDEQCTHLIVEENAIKELPFE-PSKKLYVVKQEWFWGS 337
Cdd:cd00027    3 ICFSGLDDEEREELKKLIEALGGKVSESLSSKVTHLIAKSPSGEKYYLAaLAWGIPIVSPEWLLDC 68
BRCT_Bard1_rpt1 cd17734
first BRCT domain of BRCA1-associated RING domain protein 1 (Bard1) and similar proteins; ...
 176-240 1.88e-05

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: 43.74  E-value: 1.88e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 612047297 176 LVLCFTGFrKKEELVKLVTLAHHMGGTIRKDFNSKVTHLVA------NCTQGEKFRVAVSLGTPIMKPEWI 240
Cdd:cd17734    1 LVLLGSGL-SSEQKKLLEKLAQLLKAKVVTEFSPEVTHVVVpadergVCPRTMKYLMGILAGKWIVSFEWV 70
BRCT_Rad4_rpt2 cd17746
second BRCT domain of Schizosaccharomyces pombe S-M checkpoint control protein Rad4 and ...
 172-246 2.96e-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: 43.38  E-value: 2.96e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 612047297 172 SMLNLVLCFT--GFRKKEELVKLVTlahHMGGTIRKDFNSKVTHLVANCTQGEKFRVAVSLGTPIMKPEWIFKAWER 246
Cdd:cd17746    6 TLFKCRVCLTniGQPERSRIENYVL---KHGGTFCPDLTRDVTHLIAGTSSGRKYEYALKWKINVVCVEWLWQSIQR 79
BRCT_MDC1_rpt1 cd17744
first BRCT domain of mediator of DNA damage checkpoint protein 1 (MDC1) and similar proteins; ...
 180-240 3.25e-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: 42.61  E-value: 3.25e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 612047297 180 FTGFRKKEELVKLVTLahhMGGTIRKDFNSKvTHLVAN---CTQgeKFRVAVSLGTPIMKPEWI 240
Cdd:cd17744    5 FTGVSDKEEGEKIIKK---LGGSVVDSVEDC-THLVTDkvrRTV--KFLCALARGIPIVSPDWL 62
BRCT_CTDP1 cd17729
BRCT domain of RNA polymerase II subunit A C-terminal domain phosphatase (CTDP1) and similar ...
 175-249 4.06e-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: 43.29  E-value: 4.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612047297 175 NLVLCFTGFRKKE---ELVKLVTLAHHMGGTIRKDFNSKVTHLVA--NCTqgEKFRVAVSLGT-PIMKPEWIFKA---WE 245
Cdd:cd17729   16 GCVIVFSGVIPTGidpERSRLWKLAESLGAKVVTDLSPRTTHLVAakLGT--EKVKQALKMPGiHVVHPDWLWACaerWE 93


                 ....
gi 612047297 246 RRNE 249
Cdd:cd17729   94 RVDE 97
BRCT_BRC1_like_rpt4 cd18438
fourth BRCT domain of Schizosaccharomyces pombe BRCT-containing protein 1 (BRC1) and similar ...
 189-242 3.57e-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: 39.67  E-value: 3.57e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 612047297 189 LVKLVTLahhMGGTIRKDFNSKVTHLVANCTQGEKFRVAVSLGTPIMKPEWIFK 242
Cdd:cd18438   16 LEKLILA---LGATYTKNLKPDNTHLITASPEGEKYEAAKEWNIPIVNHLWLYD 66
BRCT_PARP4_like cd17726
BRCT domain of poly [ADP-ribose] polymerase 4 (PARP-4) and similar proteins; PARP-4, also ...
 181-242 4.83e-04

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: 39.96  E-value: 4.83e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 612047297 181 TGFRKKEELVKLVTlahHMGGTIRKDFNSKVTHLV---ANCTQGEKFRVAVSLGTPIMKPEWIFK 242
Cdd:cd17726   15 PGFKEKKKLKKKIT---ENGGIISYIINKKCTHVVvnnAKALSSYKCRMAQKYGIPVVSLDYIWK 76
BRCT_TopBP1_rpt5 cd18434
fifth BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins; ...
 175-249 9.46e-04

fifth 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 fifth BRCT domain.


Pssm-ID: 349387  Cd Length: 89  Bit Score: 39.21  E-value: 9.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612047297 175 NLVLCFTGFRKKEELVkLVTLAHHMGGTI-----RKDFNSK----VTHLVANCTQGEKFRVAVSLGTPIMKPEWIFKA-- 243
Cdd:cd18434    4 GCVISVSQFTGTERDC-LTHLAELLGAKVqdyfvRKANPSKgllaSTHLVLKEPEGSKYEAAKKWNLPAVTKSWLFECar 82


                 ....*..
gi 612047297 244 -WERRNE 249
Cdd:cd18434   83 tGKKVPE 89
BRCT_XRCC1_rpt1 cd17725
First (central) BRCT domain in X-ray repair cross-complementing protein 1 (XRCC1) and similar ...
 192-247 1.36e-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: 38.41  E-value: 1.36e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 612047297 192 LVTLAHHMGGTIRKDFNSKVTHLVANCTQGEKFRVAVSLGTPIMKPEWIFKAWERR 247
Cdd:cd17725   17 LRDKALEMGAKYRPDWTADCTHLICAFANTPKYKQVKGAGGIIVSKEWILDCYKKK 72
BRCT_Rev1 cd17719
BRCT domain of DNA repair protein Rev1 and similar proteins; REV1, also termed alpha ...
 187-252 1.78e-03

BRCT domain of DNA repair protein Rev1 and similar proteins; REV1, also termed alpha integrin-binding protein 80, or AIBP80, or Rev1-like terminal deoxycytidyl transferase, is a DNA template-dependent dCMP transferase required for mutagenesis induced by UV light.


Pssm-ID: 349351 [Multi-domain]  Cd Length: 87  Bit Score: 38.32  E-value: 1.78e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 612047297 187 EELVKLVTLahHmGGTIRKDFN-SKVTHLVANCTQGEKFR-VAVSLGTPIMKPEWIF---KAWERRNEQDF 252
Cdd:cd17719   18 DELKRLILL--H-GGQYEHYYSrSRVTHIIATNLPGSKIKkLKKARNYKVVRPEWIVdsiKAGRLLPEAPY 85
BRCT_nibrin cd17741
BRCT domain of nibrin and similar proteins; Nibrin (NBN), also termed Nijmegen breakage ...
 176-240 2.22e-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: 37.58  E-value: 2.22e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 612047297 176 LVLCFTGFRKkEELVKLVTLAHHMGGTIRKDFNSKVTHLV-ANCTQGEKFRVAVSLGTPIMKPEWI 240
Cdd:cd17741    3 LVVCSSCLDS-EEKKKLKQIIAKLGGKVVNEWTEECTHLVmSKIKVTVKVICALISGKPIVTPEYL 67
PH_RalBD_exo84 cd01226
Exocyst complex 84-kDa subunit Ral-binding domain/Pleckstrin Homology (PH) domain; The Sec6/8 ...
 689-781 4.49e-03

Exocyst complex 84-kDa subunit Ral-binding domain/Pleckstrin Homology (PH) domain; The Sec6/8 complex, also called the exocyst complex, forms an octameric protein (Sec3, Sec5, Sec6, Sec8, Sec10, Sec15, Exo70 and Exo84) involved in the tethering of secretory vesicles to specific regions on the plasma membrane. The regulation of Sec6/8 complex differs between mammals and yeast. Mamalian Exo84 and Sec5 are effector targets for active Ral GTPases which are not present in yeast. Ral GTPases are members of the Ras superfamily, and as such cycle between an active GTP-bound state and an inactive GDP-bound state. The Exo84 Ral-binding domain adopts a PH domain fold. Mammalian Exo84 and Sec5 competitively bind to active RalA. 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: 269933  Cd Length: 115  Bit Score: 38.02  E-value: 4.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612047297 689 VTLFLFNDCLEIArkrhkvigtfkSPHGHTRPPAALKHIHLMPLSQIkKVLDIKETEDCHNAFALLVRPPTEQanvllsF 768
Cdd:cd01226   28 VHLFLLNDVLLIA-----------SWLPNRRGPVRYKFQALYPLEDL-AVVNVKDLGPVKNAFKLLTFPETRV------F 89

                         90
                 ....*....|...
gi 612047297 769 QMTSEDLPKDtWL 781
Cdd:cd01226   90 QCENAKIKKE-WL 101
BRCT_TopBP1_rpt6 cd17727
sixth BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins; ...
 184-242 5.01e-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: 36.81  E-value: 5.01e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 612047297 184 RKKEELVKLVTlahHMGGTIRKDFNSKVTHLVANCTQGEK---FRVAVSLGTPIMKPEWIFK 242
Cdd:cd17727   14 KRQGELNKIAA---SLGAEYRWTYDESCTHFIYQGKANDTnreYKSAKEQGKFIVSPHWLYA 72
BRCT_PAXIP1_rpt5 cd17712
fifth BRCT domain of PAX-interacting protein 1 (PAXIP1) and similar proteins; PAXIP1, also ...
 177-240 5.54e-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: 36.45  E-value: 5.54e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 612047297 177 VLCFTGFRKKE--ELVKLVTLahhMGGTIRKDfNSKVTHLVAN-CTQGEKFRVAVSLGTPIMKPEWI 240
Cdd:cd17712    3 RVLFTGFDPVQvrKLTKKVTI---LGGEVVES-PQECTHLVAPkVSRTVKFLTAISVCKHIVTPEWL 65
BRCT_TopBP1_rpt7 cd17738
seventh BRCT domain of DNA topoisomerase 2-binding protein 1; TopBP1, also termed DNA ...
 272-312 5.98e-03

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: 36.39  E-value: 5.98e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 612047297 272 MLSflGFSDEERANMEEMTEMQGGHCL--PVGDEQCTHLIVEE 312
Cdd:cd17738    5 LLS--GFSEDEKKELISIIEKLGGKVLdsDEFDPKCTHLICGK 45
BRCT_TopBP1_rpt7 cd17738
seventh BRCT domain of DNA topoisomerase 2-binding protein 1; TopBP1, also termed DNA ...
 180-240 8.12e-03

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: 36.01  E-value: 8.12e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 612047297 180 FTGFRK--KEELVKLVTLahhMGGTI--RKDFNSKVTHLVA-NCTQGEKFRVAVSLGTPIMKPEWI 240
Cdd:cd17738    6 LSGFSEdeKKELISIIEK---LGGKVldSDEFDPKCTHLICgKPSRSEKFLAACAAGKWILHPSYI 68
 
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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