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Conserved domains on  [gi|190684675|ref|NP_006288|]
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DNA repair protein XRCC1 [Homo sapiens]

Protein Classification

BRCT domain-containing protein( domain architecture ID 13667286)

BRCT (BRCA1 C-terminus) domain-containing protein may interact with DNA, and participate in DNA-damage checkpoint or DNA-repair pathways

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
XRCC1_N pfam01834
XRCC1 N terminal domain;
1-149 1.97e-92

XRCC1 N terminal domain;


:

Pssm-ID: 460356  Cd Length: 148  Bit Score: 281.82  E-value: 1.97e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684675    1 MPEIRLRHVVSCSSQDSTHCAENLLKADTYRKWRAAKAGEKTISVVLQLEKEEQIHSVDIGNDGSAFVEVLVGSSaGGAG 80
Cdd:pfam01834   1 MPPIKLKHVVSCSSEDPVHPAENLLKSDTYRKWKCAKPGEKQASVELQLERASQITSIDIGNEGSAFVEVLVGRS-SWPD 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 190684675   81 EQDYEVLLVTSSFMSPSESRSGSNPNRVRMFGPDKLVRAAAEKRWDRVKIVCSQPYSKDSPFGLSFVRF 149
Cdd:pfam01834  80 DQDFEVLLVTSSFMTPSESKNGTNRNRVRMFGKDKLNSSAAEEKWDRVKIVCTQPFNKTVQYGLSFIKF 148
BRCT_XRCC1_rpt2 cd17707
Second (C-terminal) BRCT domain in X-ray repair cross-complementing protein 1 (XRCC1) and ...
 538-631 3.94e-63

Second (C-terminal) 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 model corresponds to the second BRCT domain.


:

Pssm-ID: 349340  Cd Length: 94  Bit Score: 203.27  E-value: 3.94e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684675 538 ELPDFFQGKHFFLYGEFPGDERRKLIRYVTAFNGELEDYMSDRVQFVITAQEWDPSFEEALMDNPSLAFVRPRWIYSCNE 617
Cdd:cd17707    1 ELPDFFSGKHFFLYGDFPADERRLLKRYITAFNGEVEDYMSDKVTFVVTNQEWDDNFDEALAENPSLAFVRPRWIYACHE 80

                         90
                 ....*....|....
gi 190684675 618 KQKLLPHQLYGVVP 631
Cdd:cd17707   81 KQKLLPCQPYLVVP 94
BRCT_XRCC1_rpt1 cd17725
First (central) BRCT domain in X-ray repair cross-complementing protein 1 (XRCC1) and similar ...
 322-401 7.65e-53

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: 175.54  E-value: 7.65e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684675 322 GVVVVLSGFQNPFRSELRDKALELGAKYRPDWTRDSTHLICAFANTPKYSQVLGLGGRIVRKEWVLDCHRMRRRLPSQRY 401
Cdd:cd17725    1 GVVFVLSGFQNPFRGELRDKALEMGAKYRPDWTADCTHLICAFANTPKYKQVKGAGGIIVSKEWILDCYKKKKRLPWKRY 80
PRK13700 super family cl32925
conjugal transfer protein TraD; Provisional
 412-512 1.24e-03

conjugal transfer protein TraD; Provisional


The actual alignment was detected with superfamily member PRK13700:

Pssm-ID: 184256 [Multi-domain]  Cd Length: 732  Bit Score: 41.87  E-value: 1.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684675 412 EDEASHSGGSGDEAPKLPQKQPQTKTKPTQAAGPSSPQkPPTPEETKAASPVlqedidiegvqsegqdngAEDSGDTEDE 491
Cdd:PRK13700 604 EPDVPEVASGEDVTQAEQPQQPQQPQQPQQPQQPQQPV-SPVINDKKSDAGV------------------NVPAGGIEQE 664

                         90       100
                 ....*....|....*....|..
gi 190684675 492 LR-RVAEQKEHRLPPGQEENGE 512
Cdd:PRK13700 665 LKmKPEEEMEQQLPPGISESGE 686
PHA03307 super family cl33723
transcriptional regulator ICP4; Provisional
 94-321 8.38e-03

transcriptional regulator ICP4; Provisional


The actual alignment was detected with superfamily member PHA03307:

Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 39.38  E-value: 8.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684675   94 MSPSESRSGSNP---NRVRMFGPDKLVRAAAEKRWDRVKIVCSQPYS-KDSPFGLSFVRFHS--PPDKDEAEAPSQKVTV 167
Cdd:PHA03307  178 SPEETARAPSSPpaePPPSTPPAAASPRPPRRSSPISASASSPAPAPgRSAADDAGASSSDSssSESSGCGWGPENECPL 257

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684675  168 TKLGQFRVK-EEDESANSLRPGALFFSRINKTSPVTASDPAGPSYAAATLQASSAASSASPVSRAIGSTSKPQESPKGKR 246
Cdd:PHA03307  258 PRPAPITLPtRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSR 337

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 190684675  247 KLDlnqeekkTPSKPPAQLSPSvPKRPKLPAPTRTPATAPVPARAQGAvtgkPRGEGTEPRRPRAGPEELGKILQ 321
Cdd:PHA03307  338 GAA-------VSPGPSPSRSPS-PSRPPPPADPSSPRKRPRPSRAPSS----PAASAGRPTRRRARAAVAGRARR 400
 
Name Accession Description Interval E-value
XRCC1_N pfam01834
XRCC1 N terminal domain;
1-149 1.97e-92

XRCC1 N terminal domain;


Pssm-ID: 460356  Cd Length: 148  Bit Score: 281.82  E-value: 1.97e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684675    1 MPEIRLRHVVSCSSQDSTHCAENLLKADTYRKWRAAKAGEKTISVVLQLEKEEQIHSVDIGNDGSAFVEVLVGSSaGGAG 80
Cdd:pfam01834   1 MPPIKLKHVVSCSSEDPVHPAENLLKSDTYRKWKCAKPGEKQASVELQLERASQITSIDIGNEGSAFVEVLVGRS-SWPD 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 190684675   81 EQDYEVLLVTSSFMSPSESRSGSNPNRVRMFGPDKLVRAAAEKRWDRVKIVCSQPYSKDSPFGLSFVRF 149
Cdd:pfam01834  80 DQDFEVLLVTSSFMTPSESKNGTNRNRVRMFGKDKLNSSAAEEKWDRVKIVCTQPFNKTVQYGLSFIKF 148
BRCT_XRCC1_rpt2 cd17707
Second (C-terminal) BRCT domain in X-ray repair cross-complementing protein 1 (XRCC1) and ...
 538-631 3.94e-63

Second (C-terminal) 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 model corresponds to the second BRCT domain.


Pssm-ID: 349340  Cd Length: 94  Bit Score: 203.27  E-value: 3.94e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684675 538 ELPDFFQGKHFFLYGEFPGDERRKLIRYVTAFNGELEDYMSDRVQFVITAQEWDPSFEEALMDNPSLAFVRPRWIYSCNE 617
Cdd:cd17707    1 ELPDFFSGKHFFLYGDFPADERRLLKRYITAFNGEVEDYMSDKVTFVVTNQEWDDNFDEALAENPSLAFVRPRWIYACHE 80

                         90
                 ....*....|....
gi 190684675 618 KQKLLPHQLYGVVP 631
Cdd:cd17707   81 KQKLLPCQPYLVVP 94
BRCT_XRCC1_rpt1 cd17725
First (central) BRCT domain in X-ray repair cross-complementing protein 1 (XRCC1) and similar ...
 322-401 7.65e-53

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: 175.54  E-value: 7.65e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684675 322 GVVVVLSGFQNPFRSELRDKALELGAKYRPDWTRDSTHLICAFANTPKYSQVLGLGGRIVRKEWVLDCHRMRRRLPSQRY 401
Cdd:cd17725    1 GVVFVLSGFQNPFRGELRDKALEMGAKYRPDWTADCTHLICAFANTPKYKQVKGAGGIIVSKEWILDCYKKKKRLPWKRY 80
BRCT_2 pfam16589
BRCT domain, a BRCA1 C-terminus domain; This BRCT domain, a BRCA1 C-terminus region, is found ...
 539-627 3.37e-21

BRCT domain, a BRCA1 C-terminus domain; This BRCT domain, a BRCA1 C-terminus region, is found on many RAP1 proteins, usually at the very N-terminus. The function in human at least of a BRCT is to contribute to the heterogeneity of the telomere DNA length, but that may not be its general function, which remains unknown.


Pssm-ID: 465186 [Multi-domain]  Cd Length: 84  Bit Score: 88.19  E-value: 3.37e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684675  539 LPDFFQGKHFFLyGEFPGDERRKLIRYVTAFNGELEDYMSDRVQFVITAQEWDPSfeeaLMDNPSLAFVRPRWIYSCNEK 618
Cdd:pfam16589   1 LPNLFEPLRFYI-NAIPSPSRSKLKRLIEANGGTVVDNINPAVYIVIAPYNKTDK----LAENTKLGVVSPQWIFDCVKK 75


                  ....*....
gi 190684675  619 QKLLPHQLY 627
Cdd:pfam16589  76 GKLLPLENY 84
BRCT pfam00533
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ...
 318-389 1.35e-15

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: 71.94  E-value: 1.35e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 190684675  318 KILQGVVVVLSGFQNPFRSELRDKALELGAKYRPDWTRDSTHLICAfANTPKYSQVLGLGGRIVRKEWVLDC 389
Cdd:pfam00533   4 KLFSGKTFVITGLDGLERDELKELIEKLGGKVTDSLSKKTTHVIVE-ARTKKYLKAKELGIPIVTEEWLLDC 74
BRCT smart00292
breast cancer carboxy-terminal domain;
318-389 1.06e-11

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 60.85  E-value: 1.06e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 190684675   318 KILQGVVVVLSG-FQNPFRSELRDKALELGAKYRPDWTRDS-THLICAFANTPKYS--QVLGLGGRIVRKEWVLDC 389
Cdd:smart00292   2 KLFKGKTFYITGsFDKEERDELKELIEALGGKVTSSLSSKTtTHVIVGSPEGGKLEllKAIALGIPIVKEEWLLDC 77
BRCT smart00292
breast cancer carboxy-terminal domain;
540-615 4.47e-08

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 50.45  E-value: 4.47e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 190684675   540 PDFFQGKHFFLYGEFPGDERRKLIRYVTAFNGELEDYMS-DRVQFVITAQEWDPSFEEALMDNPSLAFVRPRWIYSC 615
Cdd:smart00292   1 PKLFKGKTFYITGSFDKEERDELKELIEALGGKVTSSLSsKTTTHVIVGSPEGGKLELLKAIALGIPIVKEEWLLDC 77
PRK13700 PRK13700
conjugal transfer protein TraD; Provisional
 412-512 1.24e-03

conjugal transfer protein TraD; Provisional


Pssm-ID: 184256 [Multi-domain]  Cd Length: 732  Bit Score: 41.87  E-value: 1.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684675 412 EDEASHSGGSGDEAPKLPQKQPQTKTKPTQAAGPSSPQkPPTPEETKAASPVlqedidiegvqsegqdngAEDSGDTEDE 491
Cdd:PRK13700 604 EPDVPEVASGEDVTQAEQPQQPQQPQQPQQPQQPQQPV-SPVINDKKSDAGV------------------NVPAGGIEQE 664

                         90       100
                 ....*....|....*....|..
gi 190684675 492 LR-RVAEQKEHRLPPGQEENGE 512
Cdd:PRK13700 665 LKmKPEEEMEQQLPPGISESGE 686
PHA03247 PHA03247
large tegument protein UL36; Provisional
 258-473 1.98e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.46  E-value: 1.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684675  258 PSKPPAQLSPSVPKRPKLPAPTRTPATAPVPARAQGAVTGKPRGEGTEPRRPRAGPEELGKILQGVVVVLSGFQNPFRSE 337
Cdd:PHA03247 2733 PALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVL 2812

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684675  338 LRDKALELGAKYRPDWTRDSTHLICAFANTPKYSQ-VLGLGGrivrkeWVLDCHRMRRRLPSQ--------------RYL 402
Cdd:PHA03247 2813 APAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPpSLPLGG------SVAPGGDVRRRPPSRspaakpaaparppvRRL 2886

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 190684675  403 MAGPGSSSEEDEASHSggsgDEAPKLPQKQPQTKTKPtQAAGPSSPQKPPTPEETKAASPVLQEDIDIEGV 473
Cdd:PHA03247 2887 ARPAVSRSTESFALPP----DQPERPPQPQAPPPPQP-QPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGA 2952
NOP7 COG5163
Protein required for biogenesis of the 60S ribosomal subunit [Translation, ribosomal structure ...
 423-629 2.38e-03

Protein required for biogenesis of the 60S ribosomal subunit [Translation, ribosomal structure and biogenesis];


Pssm-ID: 227492 [Multi-domain]  Cd Length: 591  Bit Score: 40.83  E-value: 2.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684675 423 DEAPKLPQKQPQTKtkPTQAAGPSSPQkpptpEETKAASPVLQEdidiEGVQSEGQDNGAEDSGDTEDELRRVA--EQKE 500
Cdd:COG5163  239 EEGLDYPPKFDWSK--PNFLDGLSSYE-----LEESSSLPTEIE----EDVKVESLDSSTLKSAVCNDPGNIDVskEELS 307

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684675 501 HRLPPGQEENGEDPYAGSTDE-NTDSEEHQEPPDLPVPELPDFFQGKHFFLYGEFPGDERRKLIRyvtAFNGEL--EDYM 577
Cdd:COG5163  308 EKIPELMVECRLVEEKLDTFEdNNKNKDIMEMVSKPCSSLKSLFSGFKFYISREVPGDSLEFIIL---SCGGSVvgSPCE 384

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 190684675 578 SDrvqfVITAQEWDPSFEEALMDNPSLA-------FVRPRWIYSCNEKQKLLPHQLYGV 629
Cdd:COG5163  385 AD----IHVSEKVDEKVTHQIVDRPVMKnkvegrtYIQPQWLFDSINKGKLACVENYCV 439
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 94-321 8.38e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 39.38  E-value: 8.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684675   94 MSPSESRSGSNP---NRVRMFGPDKLVRAAAEKRWDRVKIVCSQPYS-KDSPFGLSFVRFHS--PPDKDEAEAPSQKVTV 167
Cdd:PHA03307  178 SPEETARAPSSPpaePPPSTPPAAASPRPPRRSSPISASASSPAPAPgRSAADDAGASSSDSssSESSGCGWGPENECPL 257

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684675  168 TKLGQFRVK-EEDESANSLRPGALFFSRINKTSPVTASDPAGPSYAAATLQASSAASSASPVSRAIGSTSKPQESPKGKR 246
Cdd:PHA03307  258 PRPAPITLPtRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSR 337

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 190684675  247 KLDlnqeekkTPSKPPAQLSPSvPKRPKLPAPTRTPATAPVPARAQGAvtgkPRGEGTEPRRPRAGPEELGKILQ 321
Cdd:PHA03307  338 GAA-------VSPGPSPSRSPS-PSRPPPPADPSSPRKRPRPSRAPSS----PAASAGRPTRRRARAAVAGRARR 400
 
Name Accession Description Interval E-value
XRCC1_N pfam01834
XRCC1 N terminal domain;
1-149 1.97e-92

XRCC1 N terminal domain;


Pssm-ID: 460356  Cd Length: 148  Bit Score: 281.82  E-value: 1.97e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684675    1 MPEIRLRHVVSCSSQDSTHCAENLLKADTYRKWRAAKAGEKTISVVLQLEKEEQIHSVDIGNDGSAFVEVLVGSSaGGAG 80
Cdd:pfam01834   1 MPPIKLKHVVSCSSEDPVHPAENLLKSDTYRKWKCAKPGEKQASVELQLERASQITSIDIGNEGSAFVEVLVGRS-SWPD 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 190684675   81 EQDYEVLLVTSSFMSPSESRSGSNPNRVRMFGPDKLVRAAAEKRWDRVKIVCSQPYSKDSPFGLSFVRF 149
Cdd:pfam01834  80 DQDFEVLLVTSSFMTPSESKNGTNRNRVRMFGKDKLNSSAAEEKWDRVKIVCTQPFNKTVQYGLSFIKF 148
BRCT_XRCC1_rpt2 cd17707
Second (C-terminal) BRCT domain in X-ray repair cross-complementing protein 1 (XRCC1) and ...
 538-631 3.94e-63

Second (C-terminal) 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 model corresponds to the second BRCT domain.


Pssm-ID: 349340  Cd Length: 94  Bit Score: 203.27  E-value: 3.94e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684675 538 ELPDFFQGKHFFLYGEFPGDERRKLIRYVTAFNGELEDYMSDRVQFVITAQEWDPSFEEALMDNPSLAFVRPRWIYSCNE 617
Cdd:cd17707    1 ELPDFFSGKHFFLYGDFPADERRLLKRYITAFNGEVEDYMSDKVTFVVTNQEWDDNFDEALAENPSLAFVRPRWIYACHE 80

                         90
                 ....*....|....
gi 190684675 618 KQKLLPHQLYGVVP 631
Cdd:cd17707   81 KQKLLPCQPYLVVP 94
BRCT_XRCC1_rpt1 cd17725
First (central) BRCT domain in X-ray repair cross-complementing protein 1 (XRCC1) and similar ...
 322-401 7.65e-53

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: 175.54  E-value: 7.65e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684675 322 GVVVVLSGFQNPFRSELRDKALELGAKYRPDWTRDSTHLICAFANTPKYSQVLGLGGRIVRKEWVLDCHRMRRRLPSQRY 401
Cdd:cd17725    1 GVVFVLSGFQNPFRGELRDKALEMGAKYRPDWTADCTHLICAFANTPKYKQVKGAGGIIVSKEWILDCYKKKKRLPWKRY 80
BRCT_2 pfam16589
BRCT domain, a BRCA1 C-terminus domain; This BRCT domain, a BRCA1 C-terminus region, is found ...
 539-627 3.37e-21

BRCT domain, a BRCA1 C-terminus domain; This BRCT domain, a BRCA1 C-terminus region, is found on many RAP1 proteins, usually at the very N-terminus. The function in human at least of a BRCT is to contribute to the heterogeneity of the telomere DNA length, but that may not be its general function, which remains unknown.


Pssm-ID: 465186 [Multi-domain]  Cd Length: 84  Bit Score: 88.19  E-value: 3.37e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684675  539 LPDFFQGKHFFLyGEFPGDERRKLIRYVTAFNGELEDYMSDRVQFVITAQEWDPSfeeaLMDNPSLAFVRPRWIYSCNEK 618
Cdd:pfam16589   1 LPNLFEPLRFYI-NAIPSPSRSKLKRLIEANGGTVVDNINPAVYIVIAPYNKTDK----LAENTKLGVVSPQWIFDCVKK 75


                  ....*....
gi 190684675  619 QKLLPHQLY 627
Cdd:pfam16589  76 GKLLPLENY 84
BRCT pfam00533
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ...
 318-389 1.35e-15

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: 71.94  E-value: 1.35e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 190684675  318 KILQGVVVVLSGFQNPFRSELRDKALELGAKYRPDWTRDSTHLICAfANTPKYSQVLGLGGRIVRKEWVLDC 389
Cdd:pfam00533   4 KLFSGKTFVITGLDGLERDELKELIEKLGGKVTDSLSKKTTHVIVE-ARTKKYLKAKELGIPIVTEEWLLDC 74
BRCT cd00027
C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The ...
 323-389 1.61e-14

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: 68.54  E-value: 1.61e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 190684675 323 VVVVLSGFQNPFRSELRDKALELGAKYRPDWTRDSTHLICAFANTPKY-SQVLGLGGRIVRKEWVLDC 389
Cdd:cd00027    1 LVICFSGLDDEEREELKKLIEALGGKVSESLSSKVTHLIAKSPSGEKYyLAALAWGIPIVSPEWLLDC 68
BRCT_DNA_ligase_III cd18431
BRCT domain of DNA ligase 3 (LIG3) and similar proteins; LIG3 (EC 6.5.1.1), also termed DNA ...
 539-623 3.06e-13

BRCT domain of DNA ligase 3 (LIG3) and similar proteins; LIG3 (EC 6.5.1.1), also termed DNA ligase III, or polydeoxyribonucleotide synthase [ATP] 3, functions as heterodimer with DNA-repair protein XRCC1 in the nucleus and can correct defective DNA strand-break repair and sister chromatid exchange following treatment with ionizing radiation and alkylating agents.


Pssm-ID: 349384 [Multi-domain]  Cd Length: 78  Bit Score: 65.03  E-value: 3.06e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684675 539 LPDFFQGKHFFLYGEFPgDERRKLIRYVTAFNGELEDYMSDR-VQFVITAQEWDpsfeealMDNPSLAFVRPRWIYSCNE 617
Cdd:cd18431    1 LPDIFTGVKVYLPGSVE-DDYKKLKRYFIAYDGDVVEEYDEEdATHVVVDRDDK-------LGNPSAKVVSPEWLWDCIK 72


                 ....*.
gi 190684675 618 KQKLLP 623
Cdd:cd18431   73 KQKLVP 78
BRCT smart00292
breast cancer carboxy-terminal domain;
318-389 1.06e-11

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 60.85  E-value: 1.06e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 190684675   318 KILQGVVVVLSG-FQNPFRSELRDKALELGAKYRPDWTRDS-THLICAFANTPKYS--QVLGLGGRIVRKEWVLDC 389
Cdd:smart00292   2 KLFKGKTFYITGsFDKEERDELKELIEALGGKVTSSLSSKTtTHVIVGSPEGGKLEllKAIALGIPIVKEEWLLDC 77
BRCT_TopBP1_rpt2_like cd17731
second BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins; ...
 318-389 1.07e-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: 60.63  E-value: 1.07e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 190684675 318 KILQGVVVVLSGFQNPFRSELRDKALELGAKYRPDWTRDSTHLICAFANTPKYSQVLGLGG-RIVRKEWVLDC 389
Cdd:cd17731    1 PPFKGLVICVTGFDSEERKEIQQLVEQNGGSYSPDLSKNCTHLIAGSPSGQKYEFARKWNSiHIVTPEWLYDS 73
BRCT_CTDP1 cd17729
BRCT domain of RNA polymerase II subunit A C-terminal domain phosphatase (CTDP1) and similar ...
 313-394 1.06e-10

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: 58.70  E-value: 1.06e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684675 313 PEELGKILQGVVVVLSGF----QNPFRSELRDKALELGAKYRPDWTRDSTHLICAFANTPKYSQVLGLGGR-IVRKEWVL 387
Cdd:cd17729    7 PELRSKVLKGCVIVFSGViptgIDPERSRLWKLAESLGAKVVTDLSPRTTHLVAAKLGTEKVKQALKMPGIhVVHPDWLW 86


                 ....*...
gi 190684675 388 DC-HRMRR 394
Cdd:cd17729   87 ACaERWER 94
PTCB-BRCT pfam12738
twin BRCT domain; This is a BRCT domain that appears in duplicate in most member sequences. ...
 323-385 5.13e-10

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: 55.67  E-value: 5.13e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 190684675  323 VVVVLSGFQNPFRSELRDKALELGAKYRPDWTRDSTHLICAFANTPKYSQVLGLGGRIVRKEW 385
Cdd:pfam12738   1 LVICVTGFDGDDREGLQKLIEAMGAEYTKDLTKSVTHLICKSGEGEKYEKAKEWGIPVVSPLW 63
BRCT_Rev1 cd17719
BRCT domain of DNA repair protein Rev1 and similar proteins; REV1, also termed alpha ...
 319-403 2.83e-09

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: 54.11  E-value: 2.83e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684675 319 ILQGVVVVLSGFQNPFRSELRDKALELGAKYRPDWTRDS-THLICAFANTPKYSQVLGLGG-RIVRKEWVLDCHRMRRRL 396
Cdd:cd17719    1 IFKGVVIYVNGYTDPSADELKRLILLHGGQYEHYYSRSRvTHIIATNLPGSKIKKLKKARNyKVVRPEWIVDSIKAGRLL 80


                 ....*..
gi 190684675 397 PSQRYLM 403
Cdd:cd17719   81 PEAPYLL 87
BRCT_Rad4_rpt2 cd17746
second BRCT domain of Schizosaccharomyces pombe S-M checkpoint control protein Rad4 and ...
 325-385 1.17e-08

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: 52.62  E-value: 1.17e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 190684675 325 VVLSGFQNPFRSELRDKALELGAKYRPDWTRDSTHLICAFANTPKYSQVLGLGGRIVRKEW 385
Cdd:cd17746   12 VCLTNIGQPERSRIENYVLKHGGTFCPDLTRDVTHLIAGTSSGRKYEYALKWKINVVCVEW 72
BRCT smart00292
breast cancer carboxy-terminal domain;
540-615 4.47e-08

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 50.45  E-value: 4.47e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 190684675   540 PDFFQGKHFFLYGEFPGDERRKLIRYVTAFNGELEDYMS-DRVQFVITAQEWDPSFEEALMDNPSLAFVRPRWIYSC 615
Cdd:smart00292   1 PKLFKGKTFYITGSFDKEERDELKELIEALGGKVTSSLSsKTTTHVIVGSPEGGKLELLKAIALGIPIVKEEWLLDC 77
BRCT pfam00533
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ...
 540-615 1.37e-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: 1.37e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 190684675  540 PDFFQGKHFFLYGeFPGDERRKLIRYVTAFNGELEDYMSDRVQFVITaqeWDPSFEEALMDNPSLAFVRPRWIYSC 615
Cdd:pfam00533   3 EKLFSGKTFVITG-LDGLERDELKELIEKLGGKVTDSLSKKTTHVIV---EARTKKYLKAKELGIPIVTEEWLLDC 74
BRCT_Rad4_rpt1 cd17740
first BRCT domain of Schizosaccharomyces pombe S-M checkpoint control protein Rad4 and similar ...
 318-390 1.46e-07

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: 49.40  E-value: 1.46e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 190684675 318 KILQGVVVVLSGFQNPFRSELRDKALELGAKYRPDWTRDSTHLICAFANTPKYSQVLGLGG--RIVRKEWVLDCH 390
Cdd:cd17740    1 KPLSGIVLCCTSIPAEQRTEIATKASKMGAAYTADLTSDVTHLVAGQVNTTKYKFAARSRPdiKVMTVEWVEHLY 75
BRCT_PAXIP1_rpt4 cd17730
fourth BRCT domain of PAX-interacting protein 1 (PAXIP1) and similar proteins; PAXIP1, also ...
 323-389 1.14e-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: 1.14e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 190684675 323 VVVVLSGFQNPFRSELRDKALELGAKYRPDWTRDSTHLICAFANTPKYSQVLGLGGRIVRKEWVLDC 389
Cdd:cd17730    1 QVISVTGFDGSEREDIKRMIELMGAKYTGYLTRSNTHLICKRPEGEKYEKAKEWRIPVVNAQWLEDI 67
BRCT_BRC1_like_rpt4 cd18438
fourth BRCT domain of Schizosaccharomyces pombe BRCT-containing protein 1 (BRC1) and similar ...
 324-389 2.18e-06

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: 45.45  E-value: 2.18e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 190684675 324 VVVLSGFQNPFRSELRDKALELGAKYRPDWTRDSTHLICAFANTPKYSQVLGLGGRIVRKEWVLDC 389
Cdd:cd18438    2 KITITNYTGAARQYLEKLILALGATYTKNLKPDNTHLITASPEGEKYEAAKEWNIPIVNHLWLYDS 67
BRCT_BRC1_like_rpt2 cd18436
second BRCT domain of Schizosaccharomyces pombe BRCT-containing protein 1 (BRC1) and similar ...
 321-391 2.99e-06

second 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. The family also includes Cryptococcus neoformans DNA ligase 4 (LIG4, also known as DNA ligase IV or polydeoxyribonucleotide synthase [ATP] 4), which is involved in dsDNA break repair, and plays a role in non-homologous integration (NHI) pathways where it is required in the final step of non-homologus end-joining. Members in this family contains six BRCT domains. This family corresponds to the second repeat.


Pssm-ID: 349389 [Multi-domain]  Cd Length: 75  Bit Score: 45.30  E-value: 2.99e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 190684675 321 QGVVVVLSGFqNPFRSELRDKALE-LGAKYRPDWTRDSTHLICAFANTPKYSQVL---GLGGRIVRKEWVLDCHR 391
Cdd:cd18436    2 SGVVITCSDL-PSGDKEAIYGGVLaLGGQYSDELTRDVTHLIALSPDGDKYKTALkrpELNIKIVLPHWFDDCFK 75
BRCT_CHS5_like cd17742
BRCT domain of yeast chitin biosynthesis protein CHS5 and similar proteins; CHS5, also termed ...
 335-394 6.41e-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: 44.25  E-value: 6.41e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684675 335 RSELRDKALELGAKYRPDWTRDSTHLICAFANTPKYSQVLGLGGRIVRKEWVLDCHRMRR 394
Cdd:cd17742   16 VDELEQCLERIGAKPTDRVAIDTTHFVCTVPSGPEYEKAKEMNIPIVRPEWLRACEVEKK 75
BRCT_TopBP1_rpt6 cd17727
sixth BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins; ...
 320-391 6.76e-06

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: 44.12  E-value: 6.76e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 190684675 320 LQGVVVVLSGFQNPFRSELRDKALELGAKYRpdWTRDS--THLIC---AFANTPKYSQVLGLGGRIVRKEWVLDCHR 391
Cdd:cd17727    1 LKGVVICVSKKLSKRQGELNKIAASLGAEYR--WTYDEscTHFIYqgkANDTNREYKSAKEQGKFIVSPHWLYACKE 75
LIG3_BRCT pfam16759
DNA ligase 3 BRCT domain; The BRCT domain of DNA ligase 3 (LIG3) binds to the C-terminal BRCT ...
 539-615 1.34e-05

DNA ligase 3 BRCT domain; The BRCT domain of DNA ligase 3 (LIG3) binds to the C-terminal BRCT domain of the scaffolding protein X-ray repair cross-complementing protein 1 (XRCC1) and mediates homo- and heterodimerization.


Pssm-ID: 465260  Cd Length: 77  Bit Score: 43.51  E-value: 1.34e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 190684675  539 LPDFFQGKHFFLYGEFPgdERRKLIRYVTAFNGEL-EDYMSDRVQFVITAQEWDPSFEealmDNPSLAFVRPRWIYSC 615
Cdd:pfam16759   2 LPDIFTGVRLFLPPSVP--DFSKLRRYFIAYDGDLvQEYDLDSATHVVVPKDSAKEKE----ESSGAKHVTASWIWEC 73
BRCT_2 pfam16589
BRCT domain, a BRCA1 C-terminus domain; This BRCT domain, a BRCA1 C-terminus region, is found ...
 316-401 2.77e-05

BRCT domain, a BRCA1 C-terminus domain; This BRCT domain, a BRCA1 C-terminus region, is found on many RAP1 proteins, usually at the very N-terminus. The function in human at least of a BRCT is to contribute to the heterogeneity of the telomere DNA length, but that may not be its general function, which remains unknown.


Pssm-ID: 465186 [Multi-domain]  Cd Length: 84  Bit Score: 42.74  E-value: 2.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684675  316 LGKILQGVVVVLSGFQNPFRSELRDKALELGAKYRPDWTRDSTHLICAFANTPKysQVLGLGGRIVRKEWVLDCHRMRRR 395
Cdd:pfam16589   1 LPNLFEPLRFYINAIPSPSRSKLKRLIEANGGTVVDNINPAVYIVIAPYNKTDK--LAENTKLGVVSPQWIFDCVKKGKL 78


                  ....*.
gi 190684675  396 LPSQRY 401
Cdd:pfam16589  79 LPLENY 84
BRCT_TopBP1_rpt5 cd18434
fifth BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins; ...
 319-397 4.17e-05

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: 42.29  E-value: 4.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684675 319 ILQGVVVVLSGFQNPFRSELRDKALELGAK------YRPDWTRD---STHLICAFANTPKYSQVLGLGGRIVRKEWVLDC 389
Cdd:cd18434    1 PLNGCVISVSQFTGTERDCLTHLAELLGAKvqdyfvRKANPSKGllaSTHLVLKEPEGSKYEAAKKWNLPAVTKSWLFEC 80


                 ....*...
gi 190684675 390 HRMRRRLP 397
Cdd:cd18434   81 ARTGKKVP 88
BRCT_nibrin cd17741
BRCT domain of nibrin and similar proteins; Nibrin (NBN), also termed Nijmegen breakage ...
 323-385 5.10e-05

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: 41.82  E-value: 5.10e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 190684675 323 VVVVLSGFQNPFRSELRDKALELGAKYRPDWTRDSTHLICAFAN-TPKYSQVLGLGGRIVRKEW 385
Cdd:cd17741    3 LVVCSSCLDSEEKKKLKQIIAKLGGKVVNEWTEECTHLVMSKIKvTVKVICALISGKPIVTPEY 66
BRCT_PAXIP1_rpt3 cd17711
third BRCT domain of PAX-interacting protein 1 (PAXIP1) and similar proteins; PAXIP1, also ...
 322-397 1.05e-04

third 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 third BRCT domain.


Pssm-ID: 349343  Cd Length: 81  Bit Score: 41.10  E-value: 1.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684675 322 GVVVVLSGFQN----PFRSELRDKALELGAKYRPDWTRDSTHLICAFANTPKYSQVLGLGGRIVRKEWVLDCHRMRRRLP 397
Cdd:cd17711    1 GCVFFIADYPEqmgdQEIATWKKVIEEHGGEVVDEYSPRVTHVICESQDSPEYQQALRDGKRVVTAYWLNDVLKRGKLLP 80
BRCT cd00027
C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The ...
 548-615 5.00e-04

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: 38.88  E-value: 5.00e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 190684675 548 FFLYGeFPGDERRKLIRYVTAFNGELEDYMSDRVQFVITAQEWDPSFEEALMdNPSLAFVRPRWIYSC 615
Cdd:cd00027    3 ICFSG-LDDEEREELKKLIEALGGKVSESLSSKVTHLIAKSPSGEKYYLAAL-AWGIPIVSPEWLLDC 68
BRCT_microcephalin_rpt1 cd17716
first (N-terminal) BRCT domain of microcephalin and similar proteins; Microcephalin is a DNA ...
 322-396 5.04e-04

first (N-terminal) BRCT domain of microcephalin and similar proteins; Microcephalin is a DNA damage response protein involved in regulation of CHK1 and BRCA1. It has been implicated in chromosome condensation and DNA damage induced cellular responses. It may play a role in neurogenesis and regulation of the size of the cerebral cortex. Microcephalin contains three BRCT repeats. This family corresponds to the first repeat.


Pssm-ID: 349348 [Multi-domain]  Cd Length: 78  Bit Score: 39.10  E-value: 5.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684675 322 GVVVVL----SGFQN---PFRSELRdkalELGAKYRPDWTRDSTHLICAFANTPKYSQVLGLGGRIVRKEWVLDCHRMRR 394
Cdd:cd17716    1 GVVAYVdvrsGDGADrssAFRSILE----ELGAKVVKRLTKTVTHVVFKDGSQSTLEKAKKRNVKLVSPLWVEACKETGK 76


                 ..
gi 190684675 395 RL 396
Cdd:cd17716   77 RV 78
BRCT_PAXIP1_rpt2 cd17710
second BRCT domain of PAX-interacting protein 1 (PAXIP1) and similar proteins; PAXIP1, also ...
 346-397 1.09e-03

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: 38.37  E-value: 1.09e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 190684675 346 GAKYRPDWTRDSTHLICAFANTPKYSQVLGLGG-RIVRKEWVLDCHRMRRRLP 397
Cdd:cd17710   28 GGKCQLNLDKKCTHLVTGKASGAKYECALKHEGiKIVTPDWVTDCIKAKTLLD 80
PRK13700 PRK13700
conjugal transfer protein TraD; Provisional
 412-512 1.24e-03

conjugal transfer protein TraD; Provisional


Pssm-ID: 184256 [Multi-domain]  Cd Length: 732  Bit Score: 41.87  E-value: 1.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684675 412 EDEASHSGGSGDEAPKLPQKQPQTKTKPTQAAGPSSPQkPPTPEETKAASPVlqedidiegvqsegqdngAEDSGDTEDE 491
Cdd:PRK13700 604 EPDVPEVASGEDVTQAEQPQQPQQPQQPQQPQQPQQPV-SPVINDKKSDAGV------------------NVPAGGIEQE 664

                         90       100
                 ....*....|....*....|..
gi 190684675 492 LR-RVAEQKEHRLPPGQEENGE 512
Cdd:PRK13700 665 LKmKPEEEMEQQLPPGISESGE 686
PHA03247 PHA03247
large tegument protein UL36; Provisional
 258-473 1.98e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.46  E-value: 1.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684675  258 PSKPPAQLSPSVPKRPKLPAPTRTPATAPVPARAQGAVTGKPRGEGTEPRRPRAGPEELGKILQGVVVVLSGFQNPFRSE 337
Cdd:PHA03247 2733 PALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVL 2812

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684675  338 LRDKALELGAKYRPDWTRDSTHLICAFANTPKYSQ-VLGLGGrivrkeWVLDCHRMRRRLPSQ--------------RYL 402
Cdd:PHA03247 2813 APAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPpSLPLGG------SVAPGGDVRRRPPSRspaakpaaparppvRRL 2886

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 190684675  403 MAGPGSSSEEDEASHSggsgDEAPKLPQKQPQTKTKPtQAAGPSSPQKPPTPEETKAASPVLQEDIDIEGV 473
Cdd:PHA03247 2887 ARPAVSRSTESFALPP----DQPERPPQPQAPPPPQP-QPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGA 2952
BRCT_PAXIP1_rpt1 cd17714
first (N-terminal) BRCT domain of PAX-interacting protein 1 (PAXIP1) and similar proteins; ...
 543-623 2.27e-03

first (N-terminal) 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 first BRCT domain.


Pssm-ID: 349346  Cd Length: 76  Bit Score: 37.30  E-value: 2.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684675 543 FQGKHFFLYGEFPGderrKLIRYVTAFNGELEDYMSDRVQFVITAQEWDPSFEEA--LMDNPSlafVRPRWIYSCNEKQK 620
Cdd:cd17714    1 FKDVKYFVVGNLDE----KVEQLLKNGGAKEVSYLSDMATHVIVDDNDNPEVGEArdLFELPV---VTSSWVILSIKAGK 73


                 ...
gi 190684675 621 LLP 623
Cdd:cd17714   74 LLP 76
NOP7 COG5163
Protein required for biogenesis of the 60S ribosomal subunit [Translation, ribosomal structure ...
 423-629 2.38e-03

Protein required for biogenesis of the 60S ribosomal subunit [Translation, ribosomal structure and biogenesis];


Pssm-ID: 227492 [Multi-domain]  Cd Length: 591  Bit Score: 40.83  E-value: 2.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684675 423 DEAPKLPQKQPQTKtkPTQAAGPSSPQkpptpEETKAASPVLQEdidiEGVQSEGQDNGAEDSGDTEDELRRVA--EQKE 500
Cdd:COG5163  239 EEGLDYPPKFDWSK--PNFLDGLSSYE-----LEESSSLPTEIE----EDVKVESLDSSTLKSAVCNDPGNIDVskEELS 307

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684675 501 HRLPPGQEENGEDPYAGSTDE-NTDSEEHQEPPDLPVPELPDFFQGKHFFLYGEFPGDERRKLIRyvtAFNGEL--EDYM 577
Cdd:COG5163  308 EKIPELMVECRLVEEKLDTFEdNNKNKDIMEMVSKPCSSLKSLFSGFKFYISREVPGDSLEFIIL---SCGGSVvgSPCE 384

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 190684675 578 SDrvqfVITAQEWDPSFEEALMDNPSLA-------FVRPRWIYSCNEKQKLLPHQLYGV 629
Cdd:COG5163  385 AD----IHVSEKVDEKVTHQIVDRPVMKnkvegrtYIQPQWLFDSINKGKLACVENYCV 439
BRCT_TopBP1_rpt7 cd17738
seventh BRCT domain of DNA topoisomerase 2-binding protein 1; TopBP1, also termed DNA ...
 324-391 3.68e-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: 3.68e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 190684675 324 VVVLSGFQNPFRSELRDKALELGAKY--RPDWTRDSTHLICAFAN-TPKYSQVLGLGGRIVRKEWVLDCHR 391
Cdd:cd17738    3 VFLLSGFSEDEKKELISIIEKLGGKVldSDEFDPKCTHLICGKPSrSEKFLAACAAGKWILHPSYIEASAK 73
PHA03169 PHA03169
hypothetical protein; Provisional
 405-538 6.90e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 39.18  E-value: 6.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684675 405 GPGSSSEEDEASHSGGSGDEAPKLPQKQPQTKTKPTQAAGPSSPQKPPTPE-ETKAASPVLQEDIDiegvQSEGQDNGAE 483
Cdd:PHA03169  91 GPSGSGSESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPsHPGPHEPAPPESHN----PSPNQQPSSF 166

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 190684675 484 DSGDTEDElrrvAEQKEhrlPPGQEENGEDPYAGSTDENTDSEEHQEPPDLPVPE 538
Cdd:PHA03169 167 LQPSHEDS----PEEPE---PPTSEPEPDSPGPPQSETPTSSPPPQSPPDEPGEP 214
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 94-321 8.38e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 39.38  E-value: 8.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684675   94 MSPSESRSGSNP---NRVRMFGPDKLVRAAAEKRWDRVKIVCSQPYS-KDSPFGLSFVRFHS--PPDKDEAEAPSQKVTV 167
Cdd:PHA03307  178 SPEETARAPSSPpaePPPSTPPAAASPRPPRRSSPISASASSPAPAPgRSAADDAGASSSDSssSESSGCGWGPENECPL 257

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684675  168 TKLGQFRVK-EEDESANSLRPGALFFSRINKTSPVTASDPAGPSYAAATLQASSAASSASPVSRAIGSTSKPQESPKGKR 246
Cdd:PHA03307  258 PRPAPITLPtRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSR 337

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 190684675  247 KLDlnqeekkTPSKPPAQLSPSvPKRPKLPAPTRTPATAPVPARAQGAvtgkPRGEGTEPRRPRAGPEELGKILQ 321
Cdd:PHA03307  338 GAA-------VSPGPSPSRSPS-PSRPPPPADPSSPRKRPRPSRAPSS----PAASAGRPTRRRARAAVAGRARR 400
 
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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