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Conserved domains on  [gi|47086063|ref|NP_998408|]
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DNA polymerase lambda [Danio rerio]

Protein Classification

nucleotidyltransferase domain-containing protein( domain architecture ID 13026354)

nucleotidyltransferase domain-containing protein of family X DNA polymerases which includes eukaryotic Pol beta, Pol lambda, Pol mu, and terminal deoxyribonucleotidyl transferase (TdT).

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NT_POLXc cd00141
Nucleotidyltransferase (NT) domain of family X DNA Polymerases; X family polymerases fill in ...
 246-564 4.09e-148

Nucleotidyltransferase (NT) domain of family X DNA Polymerases; X family polymerases fill in short gaps during DNA repair. They are relatively inaccurate enzymes and play roles in base excision repair, in non-homologous end joining (NHEJ) which acts mainly to repair damage due to ionizing radiation, and in V(D)J recombination. This family includes eukaryotic Pol beta, Pol lambda, Pol mu, and terminal deoxyribonucleotidyl transferase (TdT). Pol beta and Pol lambda are primarily DNA template-dependent polymerases. TdT is a DNA template-independent polymerase. Pol mu has both template dependent and template independent activities. This subgroup belongs to the Pol beta-like NT superfamily. In the majority of enzymes in this superfamily, two carboxylates, Dx[D/E], together with a third more distal carboxylate, coordinate two divalent metal cations involved in a two-metal ion mechanism of nucleotide addition. These three carboxylate residues are fairly well conserved in this family.


:

Pssm-ID: 143386 [Multi-domain]  Cd Length: 307  Bit Score: 428.15  E-value: 4.09e-148
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086063 246 KHLTDKLEPLAKAYTHTG-DKWRALGYSKAINALKSYHKPITSYEEACKIPGIGKRMADKIMEIMESGHLRKLDHIGEEV 324
Cdd:cd00141   1 QEIADILEELADLLELLGgNPFRVRAYRKAARALESLPEPIESLEEAKKLPGIGKKIAEKIEEILETGKLRKLEELREDV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086063 325 P-VLEMFTNIWGAGAKTAQMWYQQGFRTLEDIRTKA--VLNHTLRIGLKHYDDLLERMPRSEANAIEKTVKDAAHSVDPQ 401
Cdd:cd00141  81 PpGLLLLLRVPGVGPKTARKLYELGIRTLEDLRKAAgaKLEQNILIGLEYYEDFQQRIPREEALAIAEIIKEALREVDPV 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086063 402 LLAMACGSYRRGRSTCGDVDVLITHPDGQShKGVFSKVLHLLHQSGFLTDDLVSHEengeqKKYMGICRLPGpSQLHRRL 481
Cdd:cd00141 161 LQVEIAGSYRRGKETVGDIDILVTHPDATS-RGLLEKVVDALVELGFVTEVLSKGD-----TKASGILKLPG-GWKGRRV 233

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086063 482 DIIVVPYSEFACALLYFTGSAHFNRSMRALAKTKNMSLSEHSLNcavirqrgvKLVAGTPLHTPTEKNVFQHLGIPYREP 561
Cdd:cd00141 234 DLRVVPPEEFGAALLYFTGSKQFNRALRRLAKEKGLKLNEYGLF---------DGVDGERLPGETEEEIFEALGLPYIEP 304


                ...
gi 47086063 562 HER 564
Cdd:cd00141 305 ELR 307
BRCT_polymerase_lambda cd17715
BRCT domain of DNA polymerase lambda and similar proteins; DNA polymerase lambda, also termed ...
 44-128 3.40e-36

BRCT domain of DNA polymerase lambda and similar proteins; DNA polymerase lambda, also termed Pol Lambda, or DNA polymerase beta-2 (Pol beta2), or DNA polymerase kappa, is involved in base excision repair (BER) and is responsible for repair of lesions that give rise to abasic (AP) sites in DNA. It also contributes to DNA double-strand break repair by non-homologous end joining and homologous recombination. DNA polymerase lambda has both template-dependent and template-independent (terminal transferase) DNA polymerase activities, as well as a 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity. DNA polymerase lambda contains one BRCT domain.


:

Pssm-ID: 349347  Cd Length: 80  Bit Score: 129.53  E-value: 3.40e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086063  44 FQGVTIYIVPAGIGKARCDIFHRQITQNGGQAVSTFAPSCTHVVVDDSVDFKRalrllKVDTLPSAVHLIKCTWLSACIS 123
Cdd:cd17715   1 FEGLTIHLVRTGIGRARAELFQRYIVQYGGQIVEDFGEGVTHVVVDDGMDAER-----KVDRDPPGAQLVKSGWLSACIQ 75


                ....*
gi 47086063 124 EKRLL 128
Cdd:cd17715  76 EKRLV 80
 
Name Accession Description Interval E-value
NT_POLXc cd00141
Nucleotidyltransferase (NT) domain of family X DNA Polymerases; X family polymerases fill in ...
 246-564 4.09e-148

Nucleotidyltransferase (NT) domain of family X DNA Polymerases; X family polymerases fill in short gaps during DNA repair. They are relatively inaccurate enzymes and play roles in base excision repair, in non-homologous end joining (NHEJ) which acts mainly to repair damage due to ionizing radiation, and in V(D)J recombination. This family includes eukaryotic Pol beta, Pol lambda, Pol mu, and terminal deoxyribonucleotidyl transferase (TdT). Pol beta and Pol lambda are primarily DNA template-dependent polymerases. TdT is a DNA template-independent polymerase. Pol mu has both template dependent and template independent activities. This subgroup belongs to the Pol beta-like NT superfamily. In the majority of enzymes in this superfamily, two carboxylates, Dx[D/E], together with a third more distal carboxylate, coordinate two divalent metal cations involved in a two-metal ion mechanism of nucleotide addition. These three carboxylate residues are fairly well conserved in this family.


Pssm-ID: 143386 [Multi-domain]  Cd Length: 307  Bit Score: 428.15  E-value: 4.09e-148
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086063 246 KHLTDKLEPLAKAYTHTG-DKWRALGYSKAINALKSYHKPITSYEEACKIPGIGKRMADKIMEIMESGHLRKLDHIGEEV 324
Cdd:cd00141   1 QEIADILEELADLLELLGgNPFRVRAYRKAARALESLPEPIESLEEAKKLPGIGKKIAEKIEEILETGKLRKLEELREDV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086063 325 P-VLEMFTNIWGAGAKTAQMWYQQGFRTLEDIRTKA--VLNHTLRIGLKHYDDLLERMPRSEANAIEKTVKDAAHSVDPQ 401
Cdd:cd00141  81 PpGLLLLLRVPGVGPKTARKLYELGIRTLEDLRKAAgaKLEQNILIGLEYYEDFQQRIPREEALAIAEIIKEALREVDPV 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086063 402 LLAMACGSYRRGRSTCGDVDVLITHPDGQShKGVFSKVLHLLHQSGFLTDDLVSHEengeqKKYMGICRLPGpSQLHRRL 481
Cdd:cd00141 161 LQVEIAGSYRRGKETVGDIDILVTHPDATS-RGLLEKVVDALVELGFVTEVLSKGD-----TKASGILKLPG-GWKGRRV 233

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086063 482 DIIVVPYSEFACALLYFTGSAHFNRSMRALAKTKNMSLSEHSLNcavirqrgvKLVAGTPLHTPTEKNVFQHLGIPYREP 561
Cdd:cd00141 234 DLRVVPPEEFGAALLYFTGSKQFNRALRRLAKEKGLKLNEYGLF---------DGVDGERLPGETEEEIFEALGLPYIEP 304


                ...
gi 47086063 562 HER 564
Cdd:cd00141 305 ELR 307
POLXc smart00483
DNA polymerase X family; includes vertebrate polymerase beta and terminal ...
 243-565 1.94e-88

DNA polymerase X family; includes vertebrate polymerase beta and terminal deoxynucleotidyltransferases


Pssm-ID: 214688  Cd Length: 334  Bit Score: 276.56  E-value: 1.94e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086063    243 NHNKHLTDKLEPLAKAYTHTGDKWRA-LGYSKAINALKSYHKPITSYEEACKIPGIGKRMADKIMEIMESGHLRKLDHI- 320
Cdd:smart00483   1 NLNRGIIDALEILAENYEVFGENKRKcSYFRKAASVLKSLPFPINSMKDLKGLPGIGDKIKKKIEEIIETGKSSKVLEIl 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086063    321 -GEEVPVLEMFTNIWGAGAKTAQMWYQQGFRTLEDIRTKA--VLNHTLRIGLKHYDDLLERMPRSEANAIEKTVKDAAHS 397
Cdd:smart00483  81 nDEVYKSLKLFTNVFGVGPKTAAKWYRKGIRTLEELKKNKelKLTKQQKAGLKYYEDILKKVSRAEAFAVEYIVKRAVRK 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086063    398 VDPQLLAMACGSYRRGRSTCGDVDVLITHPdgQSHKGVFSKVLH-LLHQSGFLTDDLVSHEEN---GEQKKYMGICRLP- 472
Cdd:smart00483 161 ILPDAIVTLTGSFRRGKETGHDVDFLITSP--HPAKEKELEVLDlLLLESTFEELQLPSIRVAtldHGQKKFMILKLSPs 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086063    473 -----------GPSQLHRRLDIIVVPYSEFACALLYFTGSAHFNRSMRALAKTK-NMSLSEHSLNcavirqrgvKLVAGT 540
Cdd:smart00483 239 redkeksgkpdEKGWKARRVDIVLCPEDQYPTALLGWTGSKQFNRDLRRYATSKfKLMLDGHELY---------DKTKEK 309

                          330       340
                   ....*....|....*....|....*
gi 47086063    541 PLHTPTEKNVFQHLGIPYREPHERD 565
Cdd:smart00483 310 FLKVESEEDIFDHLGLPYIEPEERN 334
DNA_pol_B_palm pfam14792
DNA polymerase beta palm; The catalytic region of DNA polymerase beta is split into three ...
 378-487 3.34e-52

DNA polymerase beta palm; The catalytic region of DNA polymerase beta is split into three domains. An N-terminal fingers domain, a central palm domain and a C-terminal thumb domain. This entry represents the palm domain.


Pssm-ID: 464318  Cd Length: 110  Bit Score: 173.52  E-value: 3.34e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086063   378 RMPRSEANAIEKTVKDAAHSVDPQLLAMACGSYRRGRSTCGDVDVLITHPDGQSH---KGVFSKVLHLLHQSGFLTDDLV 454
Cdd:pfam14792   1 RIPREEVEALEAIVRKAAKTLDPDVEVIVCGSYRRGAESSGDVDILITHPDGTSEselKGLLDRLVARLKKSGFLTDDLA 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 47086063   455 SHEengEQKKYMGICRLPGPSQLHRRLDIIVVP 487
Cdd:pfam14792  81 VDS---GGSKWMGVCRLPGSERLHRRIDILVVP 110
PolX COG1796
DNA polymerase/3'-5' exonuclease PolX [Replication, recombination and repair];
264-561 2.33e-39

DNA polymerase/3'-5' exonuclease PolX [Replication, recombination and repair];


Pssm-ID: 441401 [Multi-domain]  Cd Length: 567  Bit Score: 151.50  E-value: 2.33e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086063 264 DKWRALGYSKAINALKSYHKPITSYEEAC---KIPGIGKRMADKIMEIMESGHLRKLDHIGEEVP--VLEMfTNIWGAGA 338
Cdd:COG1796  23 NPFKIRAYRRAARAIENLPEDIEELVAEGdltEIPGIGKAIAAKIEELLETGRLEELEELREEVPpgLLEL-LRIPGLGP 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086063 339 KTAQMWYQQ-GFRTLEDIRtKAVLNHTLR------------I--GLKHYDDLLERMPRSEANAIEKTVKDAAHSVDPQLL 403
Cdd:COG1796 102 KKVKKLYEElGITSLEELE-AAAEEGRIRelpgfgekteenIlkGIELLRKRGGRFLLGEALPLAEEILAYLRALPGVER 180

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086063 404 AMACGSYRRGRSTCGDVDVLITHPDGQShkgvfskvlhllhqsgfLTDDLVSHEE------NGEQKkymgiCRLpgpsQL 477
Cdd:COG1796 181 VEVAGSLRRRKETVGDIDILVASDDPEA-----------------VMDAFVKLPEvkevlaKGDTK-----ASV----RL 234

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086063 478 HR--RLDIIVVPYSEFACALLYFTGSAHFNRSMRALAKTKNMSLSEHslncavirqrGVKLVAGTPLHTPTEKNVFQHLG 555
Cdd:COG1796 235 KSglQVDLRVVPPESFGAALQYFTGSKEHNVALRQLAKERGLKLNEY----------GLFDVGGERIAGETEEEVYAALG 304


                ....*.
gi 47086063 556 IPYREP 561
Cdd:COG1796 305 LPYIPP 310
BRCT_polymerase_lambda cd17715
BRCT domain of DNA polymerase lambda and similar proteins; DNA polymerase lambda, also termed ...
 44-128 3.40e-36

BRCT domain of DNA polymerase lambda and similar proteins; DNA polymerase lambda, also termed Pol Lambda, or DNA polymerase beta-2 (Pol beta2), or DNA polymerase kappa, is involved in base excision repair (BER) and is responsible for repair of lesions that give rise to abasic (AP) sites in DNA. It also contributes to DNA double-strand break repair by non-homologous end joining and homologous recombination. DNA polymerase lambda has both template-dependent and template-independent (terminal transferase) DNA polymerase activities, as well as a 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity. DNA polymerase lambda contains one BRCT domain.


Pssm-ID: 349347  Cd Length: 80  Bit Score: 129.53  E-value: 3.40e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086063  44 FQGVTIYIVPAGIGKARCDIFHRQITQNGGQAVSTFAPSCTHVVVDDSVDFKRalrllKVDTLPSAVHLIKCTWLSACIS 123
Cdd:cd17715   1 FEGLTIHLVRTGIGRARAELFQRYIVQYGGQIVEDFGEGVTHVVVDDGMDAER-----KVDRDPPGAQLVKSGWLSACIQ 75


                ....*
gi 47086063 124 EKRLL 128
Cdd:cd17715  76 EKRLV 80
PRK08609 PRK08609
DNA polymerase/3'-5' exonuclease PolX;
271-564 4.16e-15

DNA polymerase/3'-5' exonuclease PolX;


Pssm-ID: 236311 [Multi-domain]  Cd Length: 570  Bit Score: 78.07  E-value: 4.16e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086063  271 YSKAINALKSYHKPITSYEEACKIPGIGKRMADKIMEIMESGHLRKLDHIGEEVP--VLEMFTnIWGAGAKTAQMWYQQ- 347
Cdd:PRK08609  30 FRKAAQALELDERSLSEIDDFTKLKGIGKGTAEVIQEYRETGESSVLQELKKEVPegLLPLLK-LPGLGGKKIAKLYKEl 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086063  348 GFRTLEDIRtKAVLNHTLR----IGLKHYDDLL----------ERMP----RSEANAIEKTVKDAaHSVDPQLLAmacGS 409
Cdd:PRK08609 109 GVVDKESLK-EACENGKVQalagFGKKTEEKILeavkelgkrpERLPiaqvLPIAQEIEEYLATI-DEIIRFSRA---GS 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086063  410 YRRGRSTCGDVDVLI--THPDgqshkgvfsKVLHLLHQSGFLTDDLVsheeNGEQKKYMgicrlpgpsQLHRRLDIIV-- 485
Cdd:PRK08609 184 LRRARETVKDLDFIIatDEPE---------AVREQLLQLPNIVEVIA----AGDTKVSV---------ELEYEYTISVdf 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086063  486 --VPYSEFACALLYFTGSAHFNRSMRALAKTKNMSLSEHslncavirqrGVKLV-AGTPLHTPTEKNVFQHLGIPYREPH 562
Cdd:PRK08609 242 rlVEPEAFATTLHHFTGSKDHNVRMRQLAKERGEKISEY----------GVEQAdTGEVKTFESEEAFFAHFGLPFIPPE 311


                 ..
gi 47086063  563 ER 564
Cdd:PRK08609 312 VR 313
BRCT_2 pfam16589
BRCT domain, a BRCA1 C-terminus domain; This BRCT domain, a BRCA1 C-terminus region, is found ...
 40-133 1.39e-09

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: 55.06  E-value: 1.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086063    40 TGTVFQGVTIYIVpaGIGKARCDIFHRQITQNGGQAVSTFAPSCTHVVVDDSVDFKRAlrllkVDTLPSAVHLikcTWLS 119
Cdd:pfam16589   1 LPNLFEPLRFYIN--AIPSPSRSKLKRLIEANGGTVVDNINPAVYIVIAPYNKTDKLA-----ENTKLGVVSP---QWIF 70

                          90
                  ....*....|....
gi 47086063   120 ACISEKRLLDTEDY 133
Cdd:pfam16589  71 DCVKKGKLLPLENY 84
BRCT smart00292
breast cancer carboxy-terminal domain;
43-122 1.70e-04

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 40.44  E-value: 1.70e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086063     43 VFQGVTIYIVPAGIGKARcDIFHRQITQNGGQAVSTF-APSCTHVVVDDSVDFKRALRLLKvdtlPSAVHLIKCTWLSAC 121
Cdd:smart00292   3 LFKGKTFYITGSFDKEER-DELKELIEALGGKVTSSLsSKTTTHVIVGSPEGGKLELLKAI----ALGIPIVKEEWLLDC 77


                   .
gi 47086063    122 I 122
Cdd:smart00292  78 L 78
 
Name Accession Description Interval E-value
NT_POLXc cd00141
Nucleotidyltransferase (NT) domain of family X DNA Polymerases; X family polymerases fill in ...
 246-564 4.09e-148

Nucleotidyltransferase (NT) domain of family X DNA Polymerases; X family polymerases fill in short gaps during DNA repair. They are relatively inaccurate enzymes and play roles in base excision repair, in non-homologous end joining (NHEJ) which acts mainly to repair damage due to ionizing radiation, and in V(D)J recombination. This family includes eukaryotic Pol beta, Pol lambda, Pol mu, and terminal deoxyribonucleotidyl transferase (TdT). Pol beta and Pol lambda are primarily DNA template-dependent polymerases. TdT is a DNA template-independent polymerase. Pol mu has both template dependent and template independent activities. This subgroup belongs to the Pol beta-like NT superfamily. In the majority of enzymes in this superfamily, two carboxylates, Dx[D/E], together with a third more distal carboxylate, coordinate two divalent metal cations involved in a two-metal ion mechanism of nucleotide addition. These three carboxylate residues are fairly well conserved in this family.


Pssm-ID: 143386 [Multi-domain]  Cd Length: 307  Bit Score: 428.15  E-value: 4.09e-148
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086063 246 KHLTDKLEPLAKAYTHTG-DKWRALGYSKAINALKSYHKPITSYEEACKIPGIGKRMADKIMEIMESGHLRKLDHIGEEV 324
Cdd:cd00141   1 QEIADILEELADLLELLGgNPFRVRAYRKAARALESLPEPIESLEEAKKLPGIGKKIAEKIEEILETGKLRKLEELREDV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086063 325 P-VLEMFTNIWGAGAKTAQMWYQQGFRTLEDIRTKA--VLNHTLRIGLKHYDDLLERMPRSEANAIEKTVKDAAHSVDPQ 401
Cdd:cd00141  81 PpGLLLLLRVPGVGPKTARKLYELGIRTLEDLRKAAgaKLEQNILIGLEYYEDFQQRIPREEALAIAEIIKEALREVDPV 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086063 402 LLAMACGSYRRGRSTCGDVDVLITHPDGQShKGVFSKVLHLLHQSGFLTDDLVSHEengeqKKYMGICRLPGpSQLHRRL 481
Cdd:cd00141 161 LQVEIAGSYRRGKETVGDIDILVTHPDATS-RGLLEKVVDALVELGFVTEVLSKGD-----TKASGILKLPG-GWKGRRV 233

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086063 482 DIIVVPYSEFACALLYFTGSAHFNRSMRALAKTKNMSLSEHSLNcavirqrgvKLVAGTPLHTPTEKNVFQHLGIPYREP 561
Cdd:cd00141 234 DLRVVPPEEFGAALLYFTGSKQFNRALRRLAKEKGLKLNEYGLF---------DGVDGERLPGETEEEIFEALGLPYIEP 304


                ...
gi 47086063 562 HER 564
Cdd:cd00141 305 ELR 307
POLXc smart00483
DNA polymerase X family; includes vertebrate polymerase beta and terminal ...
 243-565 1.94e-88

DNA polymerase X family; includes vertebrate polymerase beta and terminal deoxynucleotidyltransferases


Pssm-ID: 214688  Cd Length: 334  Bit Score: 276.56  E-value: 1.94e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086063    243 NHNKHLTDKLEPLAKAYTHTGDKWRA-LGYSKAINALKSYHKPITSYEEACKIPGIGKRMADKIMEIMESGHLRKLDHI- 320
Cdd:smart00483   1 NLNRGIIDALEILAENYEVFGENKRKcSYFRKAASVLKSLPFPINSMKDLKGLPGIGDKIKKKIEEIIETGKSSKVLEIl 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086063    321 -GEEVPVLEMFTNIWGAGAKTAQMWYQQGFRTLEDIRTKA--VLNHTLRIGLKHYDDLLERMPRSEANAIEKTVKDAAHS 397
Cdd:smart00483  81 nDEVYKSLKLFTNVFGVGPKTAAKWYRKGIRTLEELKKNKelKLTKQQKAGLKYYEDILKKVSRAEAFAVEYIVKRAVRK 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086063    398 VDPQLLAMACGSYRRGRSTCGDVDVLITHPdgQSHKGVFSKVLH-LLHQSGFLTDDLVSHEEN---GEQKKYMGICRLP- 472
Cdd:smart00483 161 ILPDAIVTLTGSFRRGKETGHDVDFLITSP--HPAKEKELEVLDlLLLESTFEELQLPSIRVAtldHGQKKFMILKLSPs 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086063    473 -----------GPSQLHRRLDIIVVPYSEFACALLYFTGSAHFNRSMRALAKTK-NMSLSEHSLNcavirqrgvKLVAGT 540
Cdd:smart00483 239 redkeksgkpdEKGWKARRVDIVLCPEDQYPTALLGWTGSKQFNRDLRRYATSKfKLMLDGHELY---------DKTKEK 309

                          330       340
                   ....*....|....*....|....*
gi 47086063    541 PLHTPTEKNVFQHLGIPYREPHERD 565
Cdd:smart00483 310 FLKVESEEDIFDHLGLPYIEPEERN 334
DNA_pol_B_palm pfam14792
DNA polymerase beta palm; The catalytic region of DNA polymerase beta is split into three ...
 378-487 3.34e-52

DNA polymerase beta palm; The catalytic region of DNA polymerase beta is split into three domains. An N-terminal fingers domain, a central palm domain and a C-terminal thumb domain. This entry represents the palm domain.


Pssm-ID: 464318  Cd Length: 110  Bit Score: 173.52  E-value: 3.34e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086063   378 RMPRSEANAIEKTVKDAAHSVDPQLLAMACGSYRRGRSTCGDVDVLITHPDGQSH---KGVFSKVLHLLHQSGFLTDDLV 454
Cdd:pfam14792   1 RIPREEVEALEAIVRKAAKTLDPDVEVIVCGSYRRGAESSGDVDILITHPDGTSEselKGLLDRLVARLKKSGFLTDDLA 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 47086063   455 SHEengEQKKYMGICRLPGPSQLHRRLDIIVVP 487
Cdd:pfam14792  81 VDS---GGSKWMGVCRLPGSERLHRRIDILVVP 110
PolX COG1796
DNA polymerase/3'-5' exonuclease PolX [Replication, recombination and repair];
264-561 2.33e-39

DNA polymerase/3'-5' exonuclease PolX [Replication, recombination and repair];


Pssm-ID: 441401 [Multi-domain]  Cd Length: 567  Bit Score: 151.50  E-value: 2.33e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086063 264 DKWRALGYSKAINALKSYHKPITSYEEAC---KIPGIGKRMADKIMEIMESGHLRKLDHIGEEVP--VLEMfTNIWGAGA 338
Cdd:COG1796  23 NPFKIRAYRRAARAIENLPEDIEELVAEGdltEIPGIGKAIAAKIEELLETGRLEELEELREEVPpgLLEL-LRIPGLGP 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086063 339 KTAQMWYQQ-GFRTLEDIRtKAVLNHTLR------------I--GLKHYDDLLERMPRSEANAIEKTVKDAAHSVDPQLL 403
Cdd:COG1796 102 KKVKKLYEElGITSLEELE-AAAEEGRIRelpgfgekteenIlkGIELLRKRGGRFLLGEALPLAEEILAYLRALPGVER 180

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086063 404 AMACGSYRRGRSTCGDVDVLITHPDGQShkgvfskvlhllhqsgfLTDDLVSHEE------NGEQKkymgiCRLpgpsQL 477
Cdd:COG1796 181 VEVAGSLRRRKETVGDIDILVASDDPEA-----------------VMDAFVKLPEvkevlaKGDTK-----ASV----RL 234

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086063 478 HR--RLDIIVVPYSEFACALLYFTGSAHFNRSMRALAKTKNMSLSEHslncavirqrGVKLVAGTPLHTPTEKNVFQHLG 555
Cdd:COG1796 235 KSglQVDLRVVPPESFGAALQYFTGSKEHNVALRQLAKERGLKLNEY----------GLFDVGGERIAGETEEEVYAALG 304


                ....*.
gi 47086063 556 IPYREP 561
Cdd:COG1796 305 LPYIPP 310
BRCT_polymerase_lambda cd17715
BRCT domain of DNA polymerase lambda and similar proteins; DNA polymerase lambda, also termed ...
 44-128 3.40e-36

BRCT domain of DNA polymerase lambda and similar proteins; DNA polymerase lambda, also termed Pol Lambda, or DNA polymerase beta-2 (Pol beta2), or DNA polymerase kappa, is involved in base excision repair (BER) and is responsible for repair of lesions that give rise to abasic (AP) sites in DNA. It also contributes to DNA double-strand break repair by non-homologous end joining and homologous recombination. DNA polymerase lambda has both template-dependent and template-independent (terminal transferase) DNA polymerase activities, as well as a 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity. DNA polymerase lambda contains one BRCT domain.


Pssm-ID: 349347  Cd Length: 80  Bit Score: 129.53  E-value: 3.40e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086063  44 FQGVTIYIVPAGIGKARCDIFHRQITQNGGQAVSTFAPSCTHVVVDDSVDFKRalrllKVDTLPSAVHLIKCTWLSACIS 123
Cdd:cd17715   1 FEGLTIHLVRTGIGRARAELFQRYIVQYGGQIVEDFGEGVTHVVVDDGMDAER-----KVDRDPPGAQLVKSGWLSACIQ 75


                ....*
gi 47086063 124 EKRLL 128
Cdd:cd17715  76 EKRLV 80
DNA_pol_B_thumb pfam14791
DNA polymerase beta thumb; The catalytic region of DNA polymerase beta is split into three ...
 494-565 3.61e-25

DNA polymerase beta thumb; The catalytic region of DNA polymerase beta is split into three domains. An N-terminal fingers domain, a central palm domain and a C-terminal thumb domain. This entry represents the thumb domain.


Pssm-ID: 464317 [Multi-domain]  Cd Length: 63  Bit Score: 98.21  E-value: 3.61e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 47086063   494 ALLYFTGSAHFNRSMRALAKTKNMSLSEHSLNcavirqrgvKLVAGTPLHTPTEKNVFQHLGIPYREPHERD 565
Cdd:pfam14791   1 ALLYFTGSKEFNRDLRLLAKKKGLKLNEYGLF---------DLKDGELLEGETEEDIFEALGLPYIPPELRE 63
HHH_8 pfam14716
Helix-hairpin-helix domain;
245-310 1.70e-22

Helix-hairpin-helix domain;


Pssm-ID: 434152 [Multi-domain]  Cd Length: 67  Bit Score: 91.03  E-value: 1.70e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 47086063   245 NKHLTDKLEPLAKAYT-HTGDKWRALGYSKAINALKSYHKPITSYEEACKIPGIGKRMADKIMEIME 310
Cdd:pfam14716   1 NQEIADALEELADLLElKGEDPFRVRAYRRAARALEALPEEITSLEELTKLPGIGKKIAAKIEEILE 67
DNA_pol_lambd_f pfam10391
Fingers domain of DNA polymerase lambda; DNA polymerases catalyze the addition of dNMPs onto ...
 330-376 7.94e-19

Fingers domain of DNA polymerase lambda; DNA polymerases catalyze the addition of dNMPs onto the 3-prime ends of DNA chains. There is a general polymerase fold consisting of three subdomains that have been likened to the fingers, palm, and thumb of a right hand. DNA_pol_lambd_f is the central three-helical region of DNA polymerase lambda referred to as the F and G helices of the fingers domain. Contacts with DNA involve this conserved helix-hairpin-helix motif in the fingers region which interacts with the primer strand. This motif is common to several DNA binding proteins and confers a sequence-independent interaction with the DNA backbone.


Pssm-ID: 463069 [Multi-domain]  Cd Length: 51  Bit Score: 80.19  E-value: 7.94e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 47086063   330 FTNIWGAGAKTAQMWYQQGFRTLEDIRTK--AVLNHTLRIGLKHYDDLL 376
Cdd:pfam10391   3 FTGIYGVGPTTARKWYAQGYRTLDDLREKktAKLTRQQQIGLKYYDDFN 51
PRK08609 PRK08609
DNA polymerase/3'-5' exonuclease PolX;
271-564 4.16e-15

DNA polymerase/3'-5' exonuclease PolX;


Pssm-ID: 236311 [Multi-domain]  Cd Length: 570  Bit Score: 78.07  E-value: 4.16e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086063  271 YSKAINALKSYHKPITSYEEACKIPGIGKRMADKIMEIMESGHLRKLDHIGEEVP--VLEMFTnIWGAGAKTAQMWYQQ- 347
Cdd:PRK08609  30 FRKAAQALELDERSLSEIDDFTKLKGIGKGTAEVIQEYRETGESSVLQELKKEVPegLLPLLK-LPGLGGKKIAKLYKEl 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086063  348 GFRTLEDIRtKAVLNHTLR----IGLKHYDDLL----------ERMP----RSEANAIEKTVKDAaHSVDPQLLAmacGS 409
Cdd:PRK08609 109 GVVDKESLK-EACENGKVQalagFGKKTEEKILeavkelgkrpERLPiaqvLPIAQEIEEYLATI-DEIIRFSRA---GS 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086063  410 YRRGRSTCGDVDVLI--THPDgqshkgvfsKVLHLLHQSGFLTDDLVsheeNGEQKKYMgicrlpgpsQLHRRLDIIV-- 485
Cdd:PRK08609 184 LRRARETVKDLDFIIatDEPE---------AVREQLLQLPNIVEVIA----AGDTKVSV---------ELEYEYTISVdf 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086063  486 --VPYSEFACALLYFTGSAHFNRSMRALAKTKNMSLSEHslncavirqrGVKLV-AGTPLHTPTEKNVFQHLGIPYREPH 562
Cdd:PRK08609 242 rlVEPEAFATTLHHFTGSKDHNVRMRQLAKERGEKISEY----------GVEQAdTGEVKTFESEEAFFAHFGLPFIPPE 311


                 ..
gi 47086063  563 ER 564
Cdd:PRK08609 312 VR 313
BRCT_2 pfam16589
BRCT domain, a BRCA1 C-terminus domain; This BRCT domain, a BRCA1 C-terminus region, is found ...
 40-133 1.39e-09

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: 55.06  E-value: 1.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086063    40 TGTVFQGVTIYIVpaGIGKARCDIFHRQITQNGGQAVSTFAPSCTHVVVDDSVDFKRAlrllkVDTLPSAVHLikcTWLS 119
Cdd:pfam16589   1 LPNLFEPLRFYIN--AIPSPSRSKLKRLIEANGGTVVDNINPAVYIVIAPYNKTDKLA-----ENTKLGVVSP---QWIF 70

                          90
                  ....*....|....
gi 47086063   120 ACISEKRLLDTEDY 133
Cdd:pfam16589  71 DCVKKGKLLPLENY 84
BRCT_BRC1_like_rpt1 cd18435
first (N-terminal) BRCT domain of Schizosaccharomyces pombe BRCT-containing protein 1 (BRC1) ...
 68-134 8.04e-08

first (N-terminal) 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: 349388  Cd Length: 107  Bit Score: 50.79  E-value: 8.04e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 47086063  68 ITQNGGQAVST-FAPSCTHVVVDDSvDFKRALRLLKVDTLPSAVHLIKCTWLSACISEKRLLDTEDYS 134
Cdd:cd18435  40 FIDNGGKILDLpYDPKLTHVILDDF-DSPRVVELMKRTGKPRRLHLVKTKWIEDCVDENTLLDEEEYS 106
BRCT_Rev1 cd17719
BRCT domain of DNA repair protein Rev1 and similar proteins; REV1, also termed alpha ...
 43-135 3.66e-07

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: 47.95  E-value: 3.66e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086063  43 VFQGVTIYIvpAGIGKARCDIFHRQITQNGGQAVSTFAPS-CTHVVVDDSVDFKRAlRLLKVDTLPsavhLIKCTWLSAC 121
Cdd:cd17719   1 IFKGVVIYV--NGYTDPSADELKRLILLHGGQYEHYYSRSrVTHIIATNLPGSKIK-KLKKARNYK----VVRPEWIVDS 73

                        90
                ....*....|....
gi 47086063 122 ISEKRLLDTEDYSL 135
Cdd:cd17719  74 IKAGRLLPEAPYLL 87
BRCT_PAXIP1_rpt3 cd17711
third BRCT domain of PAX-interacting protein 1 (PAXIP1) and similar proteins; PAXIP1, also ...
 68-129 4.83e-06

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: 44.56  E-value: 4.83e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47086063  68 ITQNGGQAVSTFAPSCTHVVVDDSVD--FKRALRLLKVdtlpsavhLIKCTWLSACISEKRLLD 129
Cdd:cd17711  25 IEEHGGEVVDEYSPRVTHVICESQDSpeYQQALRDGKR--------VVTAYWLNDVLKRGKLLP 80
BRCT_TopBP1_rpt3 cd17718
third BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins; ...
 41-126 3.95e-05

third 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 third BRCT domain.


Pssm-ID: 349350  Cd Length: 83  Bit Score: 42.20  E-value: 3.95e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086063  41 GTVFQGVTIYIvpAGIGKARCDIFHRQITQNGGQAVSTFAPSCTHVVVDDSVDfkralRLLK-VDTLPSAVHLIKCTWLS 119
Cdd:cd17718   4 GDFLDGCKIYL--SGFSGAELDKLRRIINAGGGTRFNQLNESVTHVVVGESSE-----ELLKeLAKLAGRPHVVTPSWLL 76


                ....*..
gi 47086063 120 ACISEKR 126
Cdd:cd17718  77 ECFKQGK 83
BRCT smart00292
breast cancer carboxy-terminal domain;
43-122 1.70e-04

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 40.44  E-value: 1.70e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086063     43 VFQGVTIYIVPAGIGKARcDIFHRQITQNGGQAVSTF-APSCTHVVVDDSVDFKRALRLLKvdtlPSAVHLIKCTWLSAC 121
Cdd:smart00292   3 LFKGKTFYITGSFDKEER-DELKELIEALGGKVTSSLsSKTTTHVIVGSPEGGKLELLKAI----ALGIPIVKEEWLLDC 77


                   .
gi 47086063    122 I 122
Cdd:smart00292  78 L 78
BRCT_Ect2_rpt2 cd17732
second BRCT domain of epithelial cell-transforming sequence 2 protein (ECT2) and similar ...
 70-122 7.01e-04

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: 38.40  E-value: 7.01e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 47086063  70 QNGGQAVSTFAPSCTHVVVDDSVDfkralrlLKVDTLPSA-VHLIKCTWLSACI 122
Cdd:cd17732  26 ENGGKVTPLGDPSCTHLVVDESTV-------KELPFEPSSkLHVVKQEWFWASI 72
BRCT_PAXIP1_rpt2 cd17710
second BRCT domain of PAX-interacting protein 1 (PAXIP1) and similar proteins; PAXIP1, also ...
 43-129 1.96e-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: 37.21  E-value: 1.96e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086063  43 VFQGVTIyiVPAGIGKARCDIFHRQITQNGGQAVSTFAPSCTHVVVDD--SVDFKRALRLLKvdtlpsavhlIKCT---W 117
Cdd:cd17710   1 LFSGVVV--CPSQISAEDRLKLWAMVTFHGGKCQLNLDKKCTHLVTGKasGAKYECALKHEG----------IKIVtpdW 68

                        90
                ....*....|..
gi 47086063 118 LSACISEKRLLD 129
Cdd:cd17710  69 VTDCIKAKTLLD 80
BRCT_BRCA1_rpt1 cd17735
first BRCT domain of breast cancer type 1 susceptibility protein (BRCA1) and similar proteins; ...
 51-136 2.14e-03

first BRCT domain of breast cancer type 1 susceptibility protein (BRCA1) and similar proteins; BRCA1, also termed RING finger protein 53 (RNF53), is a RING finger protein encoded by BRCA1, a tumor suppressor gene that regulates all DNA double-strand break (DSB) repair pathways. BRCA1 is frequently mutated in patients with hereditary breast and ovarian cancer (HBOC). Its mutation is also associated with an increased risk of pancreatic, stomach, laryngeal, fallopian tube, and prostate cancer. It plays an important role in the DNA damage response signaling, and has been implicated in various cellular processes such as cell cycle regulation, transcriptional regulation, chromatin remodeling, DNA DSBs, and apoptosis. BRCA1 contains an N-terminal C3HC4-type RING-HC finger, and two BRCT (BRCA1 C-terminus domain) repeats at the C-terminus. The family corresponds to the first BRCT domain.


Pssm-ID: 349367  Cd Length: 97  Bit Score: 37.71  E-value: 2.14e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086063  51 IVPAGIGKARCDIFHRQITQNGGQAVSTFAPSCTHVVVDDSVDF--KRALRLLKvdTLPSAVHLIKCTWLSACISEKRLL 128
Cdd:cd17735   3 MVASGLTPEELMLVQKFARKTGSTLTSQFTEETTHVIMKTDAELvcERTLKYFL--GIAGRKWVVSYQWITQSIKEGKIL 80


                ....*...
gi 47086063 129 DTEDYSLR 136
Cdd:cd17735  81 PEHDFEVR 88
BRCT_TopBP1_rpt2_like cd17731
second BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins; ...
 43-122 2.68e-03

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: 36.75  E-value: 2.68e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086063  43 VFQGVTIYIvpAGIGKARCDIFHRQITQNGGQAVSTFAPSCTHVVVDD--SVDFKRALRLlkvdtlpSAVHLIKCTWLSA 120
Cdd:cd17731   2 PFKGLVICV--TGFDSEERKEIQQLVEQNGGSYSPDLSKNCTHLIAGSpsGQKYEFARKW-------NSIHIVTPEWLYD 72


                ..
gi 47086063 121 CI 122
Cdd:cd17731  73 SI 74
BRCT pfam00533
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ...
 42-122 2.69e-03

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: 36.89  E-value: 2.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086063    42 TVFQGVTIYIvpAGIGKARCDIFHRQITQNGGQAVSTFAPSCTHVVVDDsvdfkralRLLKVDTLPSA-VHLIKCTWLSA 120
Cdd:pfam00533   4 KLFSGKTFVI--TGLDGLERDELKELIEKLGGKVTDSLSKKTTHVIVEA--------RTKKYLKAKELgIPIVTEEWLLD 73


                  ..
gi 47086063   121 CI 122
Cdd:pfam00533  74 CI 75
BRCT cd00027
C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The ...
 62-121 3.18e-03

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: 36.57  E-value: 3.18e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086063  62 DIFHRQITQNGGQAVSTFAPSCTHVVVDDSVDFKRALRLLKvdtlpSAVHLIKCTWLSAC 121
Cdd:cd00027  14 EELKKLIEALGGKVSESLSSKVTHLIAKSPSGEKYYLAALA-----WGIPIVSPEWLLDC 68
BRCT_PARP4_like cd17726
BRCT domain of poly [ADP-ribose] polymerase 4 (PARP-4) and similar proteins; PARP-4, also ...
 68-129 5.10e-03

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


Pssm-ID: 349358 [Multi-domain]  Cd Length: 85  Bit Score: 36.11  E-value: 5.10e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 47086063  68 ITQNGGQAVSTFAPSCTHVVVDD-----SVDFKRALRLlkvdtlpsAVHLIKCTWLSACISEKRLLD 129
Cdd:cd17726  27 ITENGGIISYIINKKCTHVVVNNakalsSYKCRMAQKY--------GIPVVSLDYIWKCVEAGKLLD 85
RTT107_BRCT_5 pfam16770
Regulator of Ty1 transposition protein 107 BRCT domain; This is the fifth BRCT domain of ...
 67-135 5.24e-03

Regulator of Ty1 transposition protein 107 BRCT domain; This is the fifth BRCT domain of regulator of Ty1 transposition protein 107 (RTT107). It is involved in binding phosphorylated histone H2A.


Pssm-ID: 465266  Cd Length: 91  Bit Score: 36.34  E-value: 5.24e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086063    67 QITQNGGQavstfapsCTHVVVDdsvdfkRALRLLK-VDTLPSAVHLIKCTWLSACISEKRLLDTEDYSL 135
Cdd:pfam16770  36 KIVQDPSK--------CNHLIAP------KILRTEKfLCALAFAPYILSPDFITDCLKEGKLPDEEDYLL 91
 
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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