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Conserved domains on  [gi|1270540393|gb|ATO97604|]
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polymerase (DNA) lambda, partial [synthetic construct]

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 ...
 257-575 2.53e-147

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: 426.61  E-value: 2.53e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270540393 257 QFITDKLEVLAKAYSVQG-DRWRSLGYSKAINALKSYHKPVTSCEEAASIPGIGKKMAEKIEEILDSGHLRKLDHIS-DS 334
Cdd:cd00141     1 QEIADILEELADLLELLGgNPFRVRAYRKAARALESLPEPIESLEEAKKLPGIGKKIAEKIEEILETGKLRKLEELReDV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270540393 335 VAVLEIFSNIWGAGVKTAQSWYQQGFRTLDDIRTKGN--LTTQQAIGLKHYDDFLDRMPRDEAGKIEQTVREAAHAVNPE 412
Cdd:cd00141    81 PPGLLLLLRVPGVGPKTARKLYELGIRTLEDLRKAAGakLEQNILIGLEYYEDFQQRIPREEALAIAEIIKEALREVDPV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270540393 413 LICVACGSFRRGKATCGDVDVLVTHPDGKShRGVFSKLIDGLKAQGFLTDDLvnqevNGNQKKYLGVCSLPGeGQRHRRL 492
Cdd:cd00141   161 LQVEIAGSYRRGKETVGDIDILVTHPDATS-RGLLEKVVDALVELGFVTEVL-----SKGDTKASGILKLPG-GWKGRRV 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270540393 493 DIIVVPYGEFACAIMYFTGSAHFNRSMRALAKTKGMSLSEHSLNKNVvrnrsvkvsAGCPLPTPTEKEIFEILGLPFREP 572
Cdd:cd00141   234 DLRVVPPEEFGAALLYFTGSKQFNRALRRLAKEKGLKLNEYGLFDGV---------DGERLPGETEEEIFEALGLPYIEP 304


                  ...
gi 1270540393 573 HER 575
Cdd:cd00141   305 ELR 307
BRCT_polymerase_lambda cd17715
BRCT domain of DNA polymerase lambda and similar proteins; DNA polymerase lambda, also termed ...
 40-124 1.61e-35

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: 127.99  E-value: 1.61e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270540393  40 FEGVHAHILQAGIGLARSEIFQKQIIQNGGQVASQFSSEVTHIIVDEKMDCDRafrvlKLEKISHHVQLVKSAWLSLCIK 119
Cdd:cd17715     1 FEGLTIHLVRTGIGRARAELFQRYIVQYGGQIVEDFGEGVTHVVVDDGMDAER-----KVDRDPPGAQLVKSGWLSACIQ 75


                  ....*
gi 1270540393 120 EKQMV 124
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 ...
 257-575 2.53e-147

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: 426.61  E-value: 2.53e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270540393 257 QFITDKLEVLAKAYSVQG-DRWRSLGYSKAINALKSYHKPVTSCEEAASIPGIGKKMAEKIEEILDSGHLRKLDHIS-DS 334
Cdd:cd00141     1 QEIADILEELADLLELLGgNPFRVRAYRKAARALESLPEPIESLEEAKKLPGIGKKIAEKIEEILETGKLRKLEELReDV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270540393 335 VAVLEIFSNIWGAGVKTAQSWYQQGFRTLDDIRTKGN--LTTQQAIGLKHYDDFLDRMPRDEAGKIEQTVREAAHAVNPE 412
Cdd:cd00141    81 PPGLLLLLRVPGVGPKTARKLYELGIRTLEDLRKAAGakLEQNILIGLEYYEDFQQRIPREEALAIAEIIKEALREVDPV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270540393 413 LICVACGSFRRGKATCGDVDVLVTHPDGKShRGVFSKLIDGLKAQGFLTDDLvnqevNGNQKKYLGVCSLPGeGQRHRRL 492
Cdd:cd00141   161 LQVEIAGSYRRGKETVGDIDILVTHPDATS-RGLLEKVVDALVELGFVTEVL-----SKGDTKASGILKLPG-GWKGRRV 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270540393 493 DIIVVPYGEFACAIMYFTGSAHFNRSMRALAKTKGMSLSEHSLNKNVvrnrsvkvsAGCPLPTPTEKEIFEILGLPFREP 572
Cdd:cd00141   234 DLRVVPPEEFGAALLYFTGSKQFNRALRRLAKEKGLKLNEYGLFDGV---------DGERLPGETEEEIFEALGLPYIEP 304


                  ...
gi 1270540393 573 HER 575
Cdd:cd00141   305 ELR 307
POLXc smart00483
DNA polymerase X family; includes vertebrate polymerase beta and terminal ...
 254-576 1.61e-86

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


Pssm-ID: 214688  Cd Length: 334  Bit Score: 271.93  E-value: 1.61e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270540393  254 NYNQFITDKLEVLAKAYSVQGDRWRS-LGYSKAINALKSYHKPVTSCEEAASIPGIGKKMAEKIEEILDSGHLRKLDHIS 332
Cdd:smart00483   1 NLNRGIIDALEILAENYEVFGENKRKcSYFRKAASVLKSLPFPINSMKDLKGLPGIGDKIKKKIEEIIETGKSSKVLEIL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270540393  333 --DSVAVLEIFSNIWGAGVKTAQSWYQQGFRTLDDIRTKGN--LTTQQAIGLKHYDDFLDRMPRDEAGKIEQTVREAAHA 408
Cdd:smart00483  81 ndEVYKSLKLFTNVFGVGPKTAAKWYRKGIRTLEELKKNKElkLTKQQKAGLKYYEDILKKVSRAEAFAVEYIVKRAVRK 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270540393  409 VNPELICVACGSFRRGKATCGDVDVLVTHP-DGKS------HRGVFSKLIDGLKAQGFLTDDLVnqevnGNQKKYLGVCS 481
Cdd:smart00483 161 ILPDAIVTLTGSFRRGKETGHDVDFLITSPhPAKEkelevlDLLLLESTFEELQLPSIRVATLD-----HGQKKFMILKL 235

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270540393  482 LPGE------------GQRHRRLDIIVVPYGEFACAIMYFTGSAHFNRSMRALAKTKG-MSLSEHSLNknvvrnrsvKVS 548
Cdd:smart00483 236 SPSRedkeksgkpdekGWKARRVDIVLCPEDQYPTALLGWTGSKQFNRDLRRYATSKFkLMLDGHELY---------DKT 306

                          330       340
                   ....*....|....*....|....*...
gi 1270540393  549 AGCPLPTPTEKEIFEILGLPFREPHERD 576
Cdd:smart00483 307 KEKFLKVESEEDIFDHLGLPYIEPEERN 334
DNA_pol_B_palm pfam14792
DNA polymerase beta palm; The catalytic region of DNA polymerase beta is split into three ...
 389-498 9.51e-49

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: 164.66  E-value: 9.51e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270540393 389 RMPRDEAGKIEQTVREAAHAVNPELICVACGSFRRGKATCGDVDVLVTHPDGKSHR---GVFSKLIDGLKAQGFLTDDLV 465
Cdd:pfam14792   1 RIPREEVEALEAIVRKAAKTLDPDVEVIVCGSYRRGAESSGDVDILITHPDGTSESelkGLLDRLVARLKKSGFLTDDLA 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1270540393 466 nqeVNGNQKKYLGVCSLPGEGQRHRRLDIIVVP 498
Cdd:pfam14792  81 ---VDSGGSKWMGVCRLPGSERLHRRIDILVVP 110
PolX COG1796
DNA polymerase/3'-5' exonuclease PolX [Replication, recombination and repair];
256-572 5.44e-37

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


Pssm-ID: 441401 [Multi-domain]  Cd Length: 567  Bit Score: 144.95  E-value: 5.44e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270540393 256 NQFITDKLEVLAKAYSVQG-DRWRSLGYSKAINALKSYHKPVTSCEEA---ASIPGIGKKMAEKIEEILDSGHLRKLDHI 331
Cdd:COG1796     3 NKEIARILEEIADLLELKGeNPFKIRAYRRAARAIENLPEDIEELVAEgdlTEIPGIGKAIAAKIEELLETGRLEELEEL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270540393 332 SDSV--AVLEIFSnIWGAGVKTAQSWYQQ-GFRTLDD---------IRT-KG-NLTTQQAI--GLKHYDDFLDRMPRDEA 395
Cdd:COG1796    83 REEVppGLLELLR-IPGLGPKKVKKLYEElGITSLEEleaaaeegrIRElPGfGEKTEENIlkGIELLRKRGGRFLLGEA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270540393 396 ----GKIEQTVREAAHAVNpeliCVACGSFRRGKATCGDVDVLVTHPDGkshrgvfSKLIDGLKAQGFLTDDLVNQEvng 471
Cdd:COG1796   162 lplaEEILAYLRALPGVER----VEVAGSLRRRKETVGDIDILVASDDP-------EAVMDAFVKLPEVKEVLAKGD--- 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270540393 472 nqKKylgvCSLpgegqRHR---RLDIIVVPYGEFACAIMYFTGSAHFNRSMRALAKTKGMSLSEHSlnknvVRNRSVKVS 548
Cdd:COG1796   228 --TK----ASV-----RLKsglQVDLRVVPPESFGAALQYFTGSKEHNVALRQLAKERGLKLNEYG-----LFDVGGERI 291

                         330       340
                  ....*....|....*....|....
gi 1270540393 549 AGcplptPTEKEIFEILGLPFREP 572
Cdd:COG1796   292 AG-----ETEEEVYAALGLPYIPP 310
BRCT_polymerase_lambda cd17715
BRCT domain of DNA polymerase lambda and similar proteins; DNA polymerase lambda, also termed ...
 40-124 1.61e-35

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: 127.99  E-value: 1.61e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270540393  40 FEGVHAHILQAGIGLARSEIFQKQIIQNGGQVASQFSSEVTHIIVDEKMDCDRafrvlKLEKISHHVQLVKSAWLSLCIK 119
Cdd:cd17715     1 FEGLTIHLVRTGIGRARAELFQRYIVQYGGQIVEDFGEGVTHVVVDDGMDAER-----KVDRDPPGAQLVKSGWLSACIQ 75


                  ....*
gi 1270540393 120 EKQMV 124
Cdd:cd17715    76 EKRLV 80
PRK08609 PRK08609
DNA polymerase/3'-5' exonuclease PolX;
282-575 2.96e-10

DNA polymerase/3'-5' exonuclease PolX;


Pssm-ID: 236311 [Multi-domain]  Cd Length: 570  Bit Score: 63.05  E-value: 2.96e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270540393 282 YSKAINALKSYHKPVTSCEEAASIPGIGKKMAEKIEEILDSGHLRKLDHISDSV-AVLEIFSNIWGAGVKTAQSWYQQ-G 359
Cdd:PRK08609   30 FRKAAQALELDERSLSEIDDFTKLKGIGKGTAEVIQEYRETGESSVLQELKKEVpEGLLPLLKLPGLGGKKIAKLYKElG 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270540393 360 FRTLDDIRTK---GNLTTQQAIGLKHYDDFL----------DRMP----RDEAGKIEQTVREAAHAVNPElicVAcGSFR 422
Cdd:PRK08609  110 VVDKESLKEAcenGKVQALAGFGKKTEEKILeavkelgkrpERLPiaqvLPIAQEIEEYLATIDEIIRFS---RA-GSLR 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270540393 423 RGKATCGDVDVLV--THPDGkshrgvfsklidgLKAQGFLTDDLVNQEVNGNQKkylgvCSLPGEGQRHRRLDIIVVPYG 500
Cdd:PRK08609  186 RARETVKDLDFIIatDEPEA-------------VREQLLQLPNIVEVIAAGDTK-----VSVELEYEYTISVDFRLVEPE 247

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1270540393 501 EFACAIMYFTGSAHFNRSMRALAKTKGMSLSEHSlnknvVRNrsvkVSAGCPLPTPTEKEIFEILGLPFREPHER 575
Cdd:PRK08609  248 AFATTLHHFTGSKDHNVRMRQLAKERGEKISEYG-----VEQ----ADTGEVKTFESEEAFFAHFGLPFIPPEVR 313
BRCT smart00292
breast cancer carboxy-terminal domain;
39-118 5.10e-05

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 41.59  E-value: 5.10e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270540393   39 FFEGVHAHILQAGIGLARSEIfQKQIIQNGGQVASQFSS-EVTHIIVDEkmdcDRAFRVLKLEKISHHVQLVKSAWLSLC 117
Cdd:smart00292   3 LFKGKTFYITGSFDKEERDEL-KELIEALGGKVTSSLSSkTTTHVIVGS----PEGGKLELLKAIALGIPIVKEEWLLDC 77


                   .
gi 1270540393  118 I 118
Cdd:smart00292  78 L 78
BRCT pfam00533
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ...
 39-118 1.59e-04

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: 40.35  E-value: 1.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270540393  39 FFEGVHAHILQaGIGLARSEIfQKQIIQNGGQVASQFSSEVTHIIVDEkmdcdrafRVLKLEK-ISHHVQLVKSAWLSLC 117
Cdd:pfam00533   5 LFSGKTFVITG-LDGLERDEL-KELIEKLGGKVTDSLSKKTTHVIVEA--------RTKKYLKaKELGIPIVTEEWLLDC 74


                  .
gi 1270540393 118 I 118
Cdd:pfam00533  75 I 75
 
Name Accession Description Interval E-value
NT_POLXc cd00141
Nucleotidyltransferase (NT) domain of family X DNA Polymerases; X family polymerases fill in ...
 257-575 2.53e-147

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: 426.61  E-value: 2.53e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270540393 257 QFITDKLEVLAKAYSVQG-DRWRSLGYSKAINALKSYHKPVTSCEEAASIPGIGKKMAEKIEEILDSGHLRKLDHIS-DS 334
Cdd:cd00141     1 QEIADILEELADLLELLGgNPFRVRAYRKAARALESLPEPIESLEEAKKLPGIGKKIAEKIEEILETGKLRKLEELReDV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270540393 335 VAVLEIFSNIWGAGVKTAQSWYQQGFRTLDDIRTKGN--LTTQQAIGLKHYDDFLDRMPRDEAGKIEQTVREAAHAVNPE 412
Cdd:cd00141    81 PPGLLLLLRVPGVGPKTARKLYELGIRTLEDLRKAAGakLEQNILIGLEYYEDFQQRIPREEALAIAEIIKEALREVDPV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270540393 413 LICVACGSFRRGKATCGDVDVLVTHPDGKShRGVFSKLIDGLKAQGFLTDDLvnqevNGNQKKYLGVCSLPGeGQRHRRL 492
Cdd:cd00141   161 LQVEIAGSYRRGKETVGDIDILVTHPDATS-RGLLEKVVDALVELGFVTEVL-----SKGDTKASGILKLPG-GWKGRRV 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270540393 493 DIIVVPYGEFACAIMYFTGSAHFNRSMRALAKTKGMSLSEHSLNKNVvrnrsvkvsAGCPLPTPTEKEIFEILGLPFREP 572
Cdd:cd00141   234 DLRVVPPEEFGAALLYFTGSKQFNRALRRLAKEKGLKLNEYGLFDGV---------DGERLPGETEEEIFEALGLPYIEP 304


                  ...
gi 1270540393 573 HER 575
Cdd:cd00141   305 ELR 307
POLXc smart00483
DNA polymerase X family; includes vertebrate polymerase beta and terminal ...
 254-576 1.61e-86

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


Pssm-ID: 214688  Cd Length: 334  Bit Score: 271.93  E-value: 1.61e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270540393  254 NYNQFITDKLEVLAKAYSVQGDRWRS-LGYSKAINALKSYHKPVTSCEEAASIPGIGKKMAEKIEEILDSGHLRKLDHIS 332
Cdd:smart00483   1 NLNRGIIDALEILAENYEVFGENKRKcSYFRKAASVLKSLPFPINSMKDLKGLPGIGDKIKKKIEEIIETGKSSKVLEIL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270540393  333 --DSVAVLEIFSNIWGAGVKTAQSWYQQGFRTLDDIRTKGN--LTTQQAIGLKHYDDFLDRMPRDEAGKIEQTVREAAHA 408
Cdd:smart00483  81 ndEVYKSLKLFTNVFGVGPKTAAKWYRKGIRTLEELKKNKElkLTKQQKAGLKYYEDILKKVSRAEAFAVEYIVKRAVRK 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270540393  409 VNPELICVACGSFRRGKATCGDVDVLVTHP-DGKS------HRGVFSKLIDGLKAQGFLTDDLVnqevnGNQKKYLGVCS 481
Cdd:smart00483 161 ILPDAIVTLTGSFRRGKETGHDVDFLITSPhPAKEkelevlDLLLLESTFEELQLPSIRVATLD-----HGQKKFMILKL 235

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270540393  482 LPGE------------GQRHRRLDIIVVPYGEFACAIMYFTGSAHFNRSMRALAKTKG-MSLSEHSLNknvvrnrsvKVS 548
Cdd:smart00483 236 SPSRedkeksgkpdekGWKARRVDIVLCPEDQYPTALLGWTGSKQFNRDLRRYATSKFkLMLDGHELY---------DKT 306

                          330       340
                   ....*....|....*....|....*...
gi 1270540393  549 AGCPLPTPTEKEIFEILGLPFREPHERD 576
Cdd:smart00483 307 KEKFLKVESEEDIFDHLGLPYIEPEERN 334
DNA_pol_B_palm pfam14792
DNA polymerase beta palm; The catalytic region of DNA polymerase beta is split into three ...
 389-498 9.51e-49

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: 164.66  E-value: 9.51e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270540393 389 RMPRDEAGKIEQTVREAAHAVNPELICVACGSFRRGKATCGDVDVLVTHPDGKSHR---GVFSKLIDGLKAQGFLTDDLV 465
Cdd:pfam14792   1 RIPREEVEALEAIVRKAAKTLDPDVEVIVCGSYRRGAESSGDVDILITHPDGTSESelkGLLDRLVARLKKSGFLTDDLA 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1270540393 466 nqeVNGNQKKYLGVCSLPGEGQRHRRLDIIVVP 498
Cdd:pfam14792  81 ---VDSGGSKWMGVCRLPGSERLHRRIDILVVP 110
PolX COG1796
DNA polymerase/3'-5' exonuclease PolX [Replication, recombination and repair];
256-572 5.44e-37

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


Pssm-ID: 441401 [Multi-domain]  Cd Length: 567  Bit Score: 144.95  E-value: 5.44e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270540393 256 NQFITDKLEVLAKAYSVQG-DRWRSLGYSKAINALKSYHKPVTSCEEA---ASIPGIGKKMAEKIEEILDSGHLRKLDHI 331
Cdd:COG1796     3 NKEIARILEEIADLLELKGeNPFKIRAYRRAARAIENLPEDIEELVAEgdlTEIPGIGKAIAAKIEELLETGRLEELEEL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270540393 332 SDSV--AVLEIFSnIWGAGVKTAQSWYQQ-GFRTLDD---------IRT-KG-NLTTQQAI--GLKHYDDFLDRMPRDEA 395
Cdd:COG1796    83 REEVppGLLELLR-IPGLGPKKVKKLYEElGITSLEEleaaaeegrIRElPGfGEKTEENIlkGIELLRKRGGRFLLGEA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270540393 396 ----GKIEQTVREAAHAVNpeliCVACGSFRRGKATCGDVDVLVTHPDGkshrgvfSKLIDGLKAQGFLTDDLVNQEvng 471
Cdd:COG1796   162 lplaEEILAYLRALPGVER----VEVAGSLRRRKETVGDIDILVASDDP-------EAVMDAFVKLPEVKEVLAKGD--- 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270540393 472 nqKKylgvCSLpgegqRHR---RLDIIVVPYGEFACAIMYFTGSAHFNRSMRALAKTKGMSLSEHSlnknvVRNRSVKVS 548
Cdd:COG1796   228 --TK----ASV-----RLKsglQVDLRVVPPESFGAALQYFTGSKEHNVALRQLAKERGLKLNEYG-----LFDVGGERI 291

                         330       340
                  ....*....|....*....|....
gi 1270540393 549 AGcplptPTEKEIFEILGLPFREP 572
Cdd:COG1796   292 AG-----ETEEEVYAALGLPYIPP 310
BRCT_polymerase_lambda cd17715
BRCT domain of DNA polymerase lambda and similar proteins; DNA polymerase lambda, also termed ...
 40-124 1.61e-35

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: 127.99  E-value: 1.61e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270540393  40 FEGVHAHILQAGIGLARSEIFQKQIIQNGGQVASQFSSEVTHIIVDEKMDCDRafrvlKLEKISHHVQLVKSAWLSLCIK 119
Cdd:cd17715     1 FEGLTIHLVRTGIGRARAELFQRYIVQYGGQIVEDFGEGVTHVVVDDGMDAER-----KVDRDPPGAQLVKSGWLSACIQ 75


                  ....*
gi 1270540393 120 EKQMV 124
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 ...
 505-576 1.54e-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: 99.37  E-value: 1.54e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1270540393 505 AIMYFTGSAHFNRSMRALAKTKGMSLSEHSLNknvvrnrsvKVSAGCPLPTPTEKEIFEILGLPFREPHERD 576
Cdd:pfam14791   1 ALLYFTGSKEFNRDLRLLAKKKGLKLNEYGLF---------DLKDGELLEGETEEDIFEALGLPYIPPELRE 63
HHH_8 pfam14716
Helix-hairpin-helix domain;
256-321 9.16e-22

Helix-hairpin-helix domain;


Pssm-ID: 434152 [Multi-domain]  Cd Length: 67  Bit Score: 89.10  E-value: 9.16e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1270540393 256 NQFITDKLEVLAKAYSVQG-DRWRSLGYSKAINALKSYHKPVTSCEEAASIPGIGKKMAEKIEEILD 321
Cdd:pfam14716   1 NQEIADALEELADLLELKGeDPFRVRAYRRAARALEALPEEITSLEELTKLPGIGKKIAAKIEEILE 67
DNA_pol_lambd_f pfam10391
Fingers domain of DNA polymerase lambda; DNA polymerases catalyze the addition of dNMPs onto ...
 339-387 1.46e-20

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: 84.81  E-value: 1.46e-20
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1270540393 339 EIFSNIWGAGVKTAQSWYQQGFRTLDDIRTKGN--LTTQQAIGLKHYDDFL 387
Cdd:pfam10391   1 KLFTGIYGVGPTTARKWYAQGYRTLDDLREKKTakLTRQQQIGLKYYDDFN 51
PRK08609 PRK08609
DNA polymerase/3'-5' exonuclease PolX;
282-575 2.96e-10

DNA polymerase/3'-5' exonuclease PolX;


Pssm-ID: 236311 [Multi-domain]  Cd Length: 570  Bit Score: 63.05  E-value: 2.96e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270540393 282 YSKAINALKSYHKPVTSCEEAASIPGIGKKMAEKIEEILDSGHLRKLDHISDSV-AVLEIFSNIWGAGVKTAQSWYQQ-G 359
Cdd:PRK08609   30 FRKAAQALELDERSLSEIDDFTKLKGIGKGTAEVIQEYRETGESSVLQELKKEVpEGLLPLLKLPGLGGKKIAKLYKElG 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270540393 360 FRTLDDIRTK---GNLTTQQAIGLKHYDDFL----------DRMP----RDEAGKIEQTVREAAHAVNPElicVAcGSFR 422
Cdd:PRK08609  110 VVDKESLKEAcenGKVQALAGFGKKTEEKILeavkelgkrpERLPiaqvLPIAQEIEEYLATIDEIIRFS---RA-GSLR 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270540393 423 RGKATCGDVDVLV--THPDGkshrgvfsklidgLKAQGFLTDDLVNQEVNGNQKkylgvCSLPGEGQRHRRLDIIVVPYG 500
Cdd:PRK08609  186 RARETVKDLDFIIatDEPEA-------------VREQLLQLPNIVEVIAAGDTK-----VSVELEYEYTISVDFRLVEPE 247

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1270540393 501 EFACAIMYFTGSAHFNRSMRALAKTKGMSLSEHSlnknvVRNrsvkVSAGCPLPTPTEKEIFEILGLPFREPHER 575
Cdd:PRK08609  248 AFATTLHHFTGSKDHNVRMRQLAKERGEKISEYG-----VEQ----ADTGEVKTFESEEAFFAHFGLPFIPPEVR 313
BRCT_PAXIP1_rpt3 cd17711
third BRCT domain of PAX-interacting protein 1 (PAXIP1) and similar proteins; PAXIP1, also ...
 64-125 8.70e-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: 44.18  E-value: 8.70e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1270540393  64 IIQNGGQVASQFSSEVTHIIVDEKMDCDRAfRVLKLEKishhvQLVKSAWLSLCIKEKQMVN 125
Cdd:cd17711    25 IEEHGGEVVDEYSPRVTHVICESQDSPEYQ-QALRDGK-----RVVTAYWLNDVLKRGKLLP 80
BRCT_Bard1_rpt1 cd17734
first BRCT domain of BRCA1-associated RING domain protein 1 (Bard1) and similar proteins; ...
 68-124 1.32e-05

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


Pssm-ID: 349366  Cd Length: 80  Bit Score: 43.36  E-value: 1.32e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1270540393  68 GGQVASQFSSEVTHIIV--DEKMDCDRAFRVLKleKISHHVQLVKSAWLSLCIKEKQMV 124
Cdd:cd17734    24 KAKVVTEFSPEVTHVVVpaDERGVCPRTMKYLM--GILAGKWIVSFEWVEACLKAKKLV 80
BRCT_TopBP1_rpt3 cd17718
third BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins; ...
 51-122 1.39e-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: 43.35  E-value: 1.39e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1270540393  51 GIGLARSEIFQKQIIQNGGQVASQFSSEVTHIIVDEKMDCDRAFrvlkLEKISHHVQLVKSAWLSLCIKEKQ 122
Cdd:cd17718    16 GFSGAELDKLRRIINAGGGTRFNQLNESVTHVVVGESSEELLKE----LAKLAGRPHVVTPSWLLECFKQGK 83
BRCT_BRCA1_rpt1 cd17735
first BRCT domain of breast cancer type 1 susceptibility protein (BRCA1) and similar proteins; ...
 53-131 2.91e-05

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: 43.10  E-value: 2.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270540393  53 GLARSEI--FQKQIIQNGGQVASQFSSEVTHIIV--DEKMDCDrafRVLK-LEKISHHVQLVKSAWLSLCIKEKQMVNTA 127
Cdd:cd17735     7 GLTPEELmlVQKFARKTGSTLTSQFTEETTHVIMktDAELVCE---RTLKyFLGIAGRKWVVSYQWITQSIKEGKILPEH 83


                  ....
gi 1270540393 128 GYRI 131
Cdd:cd17735    84 DFEV 87
BRCT cd00027
C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The ...
 51-117 4.21e-05

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: 41.58  E-value: 4.21e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1270540393  51 GIGLARSEIFQKQIIQNGGQVASQFSSEVTHIIVDEKMDcdrafRVLKLEKISHHVQLVKSAWLSLC 117
Cdd:cd00027     7 GLDDEEREELKKLIEALGGKVSESLSSKVTHLIAKSPSG-----EKYYLAALAWGIPIVSPEWLLDC 68
BRCT smart00292
breast cancer carboxy-terminal domain;
39-118 5.10e-05

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 41.59  E-value: 5.10e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270540393   39 FFEGVHAHILQAGIGLARSEIfQKQIIQNGGQVASQFSS-EVTHIIVDEkmdcDRAFRVLKLEKISHHVQLVKSAWLSLC 117
Cdd:smart00292   3 LFKGKTFYITGSFDKEERDEL-KELIEALGGKVTSSLSSkTTTHVIVGS----PEGGKLELLKAIALGIPIVKEEWLLDC 77


                   .
gi 1270540393  118 I 118
Cdd:smart00292  78 L 78
BRCT pfam00533
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ...
 39-118 1.59e-04

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: 40.35  E-value: 1.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270540393  39 FFEGVHAHILQaGIGLARSEIfQKQIIQNGGQVASQFSSEVTHIIVDEkmdcdrafRVLKLEK-ISHHVQLVKSAWLSLC 117
Cdd:pfam00533   5 LFSGKTFVITG-LDGLERDEL-KELIEKLGGKVTDSLSKKTTHVIVEA--------RTKKYLKaKELGIPIVTEEWLLDC 74


                  .
gi 1270540393 118 I 118
Cdd:pfam00533  75 I 75
BRCT_TopBP1_rpt2_like cd17731
second BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins; ...
 56-119 6.79e-04

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: 38.68  E-value: 6.79e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1270540393  56 RSEIfQKQIIQNGGQVASQFSSEVTHIIVD----EKMDCDRAFRvlklekishHVQLVKSAWLSLCIK 119
Cdd:cd17731    18 RKEI-QQLVEQNGGSYSPDLSKNCTHLIAGspsgQKYEFARKWN---------SIHIVTPEWLYDSIE 75
BRCT_BRC1_like_rpt1 cd18435
first (N-terminal) BRCT domain of Schizosaccharomyces pombe BRCT-containing protein 1 (BRC1) ...
 61-129 1.66e-03

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: 38.46  E-value: 1.66e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270540393  61 QKQIIQNGGQVAS-QFSSEVTHIIVDeKMDCDRAFRVLKLEKISHHVQLVKSAWLSLCIKEKQMVNTAGY 129
Cdd:cd18435    37 EKLFIDNGGKILDlPYDPKLTHVILD-DFDSPRVVELMKRTGKPRRLHLVKTKWIEDCVDENTLLDEEEY 105
BRCT_Ect2_rpt2 cd17732
second BRCT domain of epithelial cell-transforming sequence 2 protein (ECT2) and similar ...
 65-113 2.14e-03

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: 37.25  E-value: 2.14e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1270540393  65 IQNGGQVASQFSSEVTHIIVDEKmdcdrafRVLKL-EKISHHVQLVKSAW 113
Cdd:cd17732    25 EENGGKVTPLGDPSCTHLVVDES-------TVKELpFEPSSKLHVVKQEW 67
BRCT_Rev1 cd17719
BRCT domain of DNA repair protein Rev1 and similar proteins; REV1, also termed alpha ...
 64-131 3.42e-03

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


Pssm-ID: 349351 [Multi-domain]  Cd Length: 87  Bit Score: 36.78  E-value: 3.42e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1270540393  64 IIQNGGQVASQFS-SEVTHIIV----DEKMdcdRAFRVLKLEKIshhvqlVKSAWLSLCIKEKQMVNTAGYRI 131
Cdd:cd17719    24 ILLHGGQYEHYYSrSRVTHIIAtnlpGSKI---KKLKKARNYKV------VRPEWIVDSIKAGRLLPEAPYLL 87
BRCT_2 pfam16589
BRCT domain, a BRCA1 C-terminus domain; This BRCT domain, a BRCA1 C-terminus region, is found ...
 39-129 5.48e-03

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: 36.19  E-value: 5.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270540393  39 FFEGVHAHILQAGiGLARSEIfQKQIIQNGGQVASQFSSEVTHIIVDEKMDcdrafrvlKLEKISHHVQLVKSAWLSLCI 118
Cdd:pfam16589   4 LFEPLRFYINAIP-SPSRSKL-KRLIEANGGTVVDNINPAVYIVIAPYNKT--------DKLAENTKLGVVSPQWIFDCV 73

                          90
                  ....*....|.
gi 1270540393 119 KEKQMVNTAGY 129
Cdd:pfam16589  74 KKGKLLPLENY 84
 
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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