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Conserved domains on  [gi|17367126|sp|Q9UGP5|]
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RecName: Full=DNA polymerase lambda; Short=Pol Lambda; AltName: Full=DNA polymerase beta-2; Short=Pol beta2; AltName: Full=DNA polymerase kappa

Protein Classification

BRCT_polymerase_lambda and NT_POLXc domain-containing protein( domain architecture ID 13026354)

BRCT_polymerase_lambda and NT_POLXc domain-containing protein

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 ...
255-573 2.58e-145

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: 421.22  E-value: 2.58e-145
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17367126 255 HITEKLEVLAKAYSVQG-DKWRALGYAKAINALKSFHKPVTSYQEACSIPGIGKRMAEKIIEILESGHLRKLDHISESVP 333
Cdd:cd00141   2 EIADILEELADLLELLGgNPFRVRAYRKAARALESLPEPIESLEEAKKLPGIGKKIAEKIEEILETGKLRKLEELREDVP 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17367126 334 -VLELFSNIWGAGTKTAQMWYQQGFRSLEDIRSQAS--LTTQQAIGLKHYSDFLERMPREEATEIEQTVQKAAQAFNSGL 410
Cdd:cd00141  82 pGLLLLLRVPGVGPKTARKLYELGIRTLEDLRKAAGakLEQNILIGLEYYEDFQQRIPREEALAIAEIIKEALREVDPVL 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17367126 411 LCVACGSYRRGKATCGDVDVLITHPDGRShRGIFSRLLDSLRQEGFLTDDLvsqeeNGQQQKYLGVCRLPGpGRRHRRLD 490
Cdd:cd00141 162 QVEIAGSYRRGKETVGDIDILVTHPDATS-RGLLEKVVDALVELGFVTEVL-----SKGDTKASGILKLPG-GWKGRRVD 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17367126 491 IIVVPYSEFACALLYFTGSAHFNRSMRALAKTKGMSLSEHALStavvrnthgcKVGPGRVLPTPTEKDVFRLLGLPYREP 570
Cdd:cd00141 235 LRVVPPEEFGAALLYFTGSKQFNRALRRLAKEKGLKLNEYGLF----------DGVDGERLPGETEEEIFEALGLPYIEP 304

                ...
gi 17367126 571 AER 573
Cdd:cd00141 305 ELR 307
BRCT_polymerase_lambda cd17715
BRCT domain of DNA polymerase lambda and similar proteins; DNA polymerase lambda, also termed ...
41-125 1.10e-29

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: 111.81  E-value: 1.10e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17367126  41 LSSLRAHVVRTGIGRARAELFEKQIVQHGGQLCPAQGPGVTHIVVDEGMDYEralrlLRLPQLPPGAQLVKSAWLSLCLQ 120
Cdd:cd17715   1 FEGLTIHLVRTGIGRARAELFQRYIVQYGGQIVEDFGEGVTHVVVDDGMDAE-----RKVDRDPPGAQLVKSGWLSACIQ 75

                ....*
gi 17367126 121 ERRLV 125
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 ...
255-573 2.58e-145

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: 421.22  E-value: 2.58e-145
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17367126 255 HITEKLEVLAKAYSVQG-DKWRALGYAKAINALKSFHKPVTSYQEACSIPGIGKRMAEKIIEILESGHLRKLDHISESVP 333
Cdd:cd00141   2 EIADILEELADLLELLGgNPFRVRAYRKAARALESLPEPIESLEEAKKLPGIGKKIAEKIEEILETGKLRKLEELREDVP 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17367126 334 -VLELFSNIWGAGTKTAQMWYQQGFRSLEDIRSQAS--LTTQQAIGLKHYSDFLERMPREEATEIEQTVQKAAQAFNSGL 410
Cdd:cd00141  82 pGLLLLLRVPGVGPKTARKLYELGIRTLEDLRKAAGakLEQNILIGLEYYEDFQQRIPREEALAIAEIIKEALREVDPVL 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17367126 411 LCVACGSYRRGKATCGDVDVLITHPDGRShRGIFSRLLDSLRQEGFLTDDLvsqeeNGQQQKYLGVCRLPGpGRRHRRLD 490
Cdd:cd00141 162 QVEIAGSYRRGKETVGDIDILVTHPDATS-RGLLEKVVDALVELGFVTEVL-----SKGDTKASGILKLPG-GWKGRRVD 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17367126 491 IIVVPYSEFACALLYFTGSAHFNRSMRALAKTKGMSLSEHALStavvrnthgcKVGPGRVLPTPTEKDVFRLLGLPYREP 570
Cdd:cd00141 235 LRVVPPEEFGAALLYFTGSKQFNRALRRLAKEKGLKLNEYGLF----------DGVDGERLPGETEEEIFEALGLPYIEP 304

                ...
gi 17367126 571 AER 573
Cdd:cd00141 305 ELR 307
POLXc smart00483
DNA polymerase X family; includes vertebrate polymerase beta and terminal ...
251-574 9.44e-87

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


Pssm-ID: 214688  Cd Length: 334  Bit Score: 272.32  E-value: 9.44e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17367126    251 NHNLHITEKLEVLAKAYSVQGDKWRA-LGYAKAINALKSFHKPVTSYQEACSIPGIGKRMAEKIIEILESGHLRKLDHIS 329
Cdd:smart00483   1 NLNRGIIDALEILAENYEVFGENKRKcSYFRKAASVLKSLPFPINSMKDLKGLPGIGDKIKKKIEEIIETGKSSKVLEIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17367126    330 --ESVPVLELFSNIWGAGTKTAQMWYQQGFRSLEDIRSQA--SLTTQQAIGLKHYSDFLERMPREEATEIEQTVQKAAQA 405
Cdd:smart00483  81 ndEVYKSLKLFTNVFGVGPKTAAKWYRKGIRTLEELKKNKelKLTKQQKAGLKYYEDILKKVSRAEAFAVEYIVKRAVRK 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17367126    406 FNSGLLCVACGSYRRGKATCGDVDVLITHPDGRS-------HRGIFSRLLDSLRQEGFLTDDLVsqeenGQQQKYLGVCR 478
Cdd:smart00483 161 ILPDAIVTLTGSFRRGKETGHDVDFLITSPHPAKekelevlDLLLLESTFEELQLPSIRVATLD-----HGQKKFMILKL 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17367126    479 LP------------GPGRRHRRLDIIVVPYSEFACALLYFTGSAHFNRSMRALAKTKG-MSLSEHAlstavvRNTHGCKV 545
Cdd:smart00483 236 SPsredkeksgkpdEKGWKARRVDIVLCPEDQYPTALLGWTGSKQFNRDLRRYATSKFkLMLDGHE------LYDKTKEK 309
                          330       340
                   ....*....|....*....|....*....
gi 17367126    546 gpgrVLPTPTEKDVFRLLGLPYREPAERD 574
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 ...
386-495 2.85e-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: 434213  Cd Length: 110  Bit Score: 166.20  E-value: 2.85e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17367126   386 RMPREEATEIEQTVQKAAQAFNSGLLCVACGSYRRGKATCGDVDVLITHPDGRSHR---GIFSRLLDSLRQEGFLTDDLV 462
Cdd:pfam14792   1 RIPREEVEALEAIVRKAAKTLDPDVEVIVCGSYRRGAESSGDVDILITHPDGTSESelkGLLDRLVARLKKSGFLTDDLA 80
                          90       100       110
                  ....*....|....*....|....*....|...
gi 17367126   463 SQEengQQQKYLGVCRLPGPGRRHRRLDIIVVP 495
Cdd:pfam14792  81 VDS---GGSKWMGVCRLPGSERLHRRIDILVVP 110
PolX COG1796
DNA polymerase/3'-5' exonuclease PolX [Replication, recombination and repair];
252-573 1.45e-39

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


Pssm-ID: 224709 [Multi-domain]  Cd Length: 326  Bit Score: 147.10  E-value: 1.45e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17367126 252 HNLHITEKLEVLAKAYSVQGD-KWRALGYAKAINALKSFHKPVTSYQEA---CSIPGIGKRMAEKIIEILESGHLRKLDH 327
Cdd:COG1796   4 NNHDIARLLERIADYMELEGEnPFKIRAYRKAAQSLENLTEDLEEIEERgrlTELPGIGKGIAEKISEYLDTGEVKKLEA 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17367126 328 ISESVPV-LELFSNIWGAGTKT-AQMWYQQGFRSLEDIRSQASLTTQQAI---GLKHYSDFLERMPR-EEATE---IEQT 398
Cdd:COG1796  84 LKKEVPEgLEPLLKVPGLGPKKiVSLYKELGIKDLEELQEALENGKIRGLrgfGKKSEAKILENIEFaEESPEripLSFT 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17367126 399 VQKA-------AQAFNSGLLCVAcGSYRRGKATCGDVDVLIT--HPDgrshrgifsrlldSLRQEgFLTDDLVSQEENGQ 469
Cdd:COG1796 164 LPIAqeiegylEELTPIIQASIA-GSLRRGRETVGDIDILIStsHPE-------------SVLEE-LLEMPNVQEVIAKG 228
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17367126 470 QQKYLGVCRLpgpgRRHRRLDIIVVPYSEFACALLYFTGSAHFNRSMRALAKTKGMSLSEHALSTavvrnthgckvGPGR 549
Cdd:COG1796 229 ETKVSMLLIL----DEGTSVDFRVVPPEAFGAALQHFTGSKEHNIKIRQLAKAKGEKLSEYGLFR-----------DSGE 293
                       330       340
                ....*....|....*....|....
gi 17367126 550 VLPTPTEKDVFRLLGLPYREPAER 573
Cdd:COG1796 294 IIAGKTEEKIYEHLGLPYIPPELR 317
BRCT_polymerase_lambda cd17715
BRCT domain of DNA polymerase lambda and similar proteins; DNA polymerase lambda, also termed ...
41-125 1.10e-29

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: 111.81  E-value: 1.10e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17367126  41 LSSLRAHVVRTGIGRARAELFEKQIVQHGGQLCPAQGPGVTHIVVDEGMDYEralrlLRLPQLPPGAQLVKSAWLSLCLQ 120
Cdd:cd17715   1 FEGLTIHLVRTGIGRARAELFQRYIVQYGGQIVEDFGEGVTHVVVDDGMDAE-----RKVDRDPPGAQLVKSGWLSACIQ 75

                ....*
gi 17367126 121 ERRLV 125
Cdd:cd17715  76 EKRLV 80
PRK08609 PRK08609
DNA polymerase/3'-5' exonuclease PolX;
279-573 4.63e-12

DNA polymerase/3'-5' exonuclease PolX;


Pssm-ID: 236311 [Multi-domain]  Cd Length: 570  Bit Score: 68.44  E-value: 4.63e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17367126  279 YAKAINALKSFHKPVTSYQEACSIPGIGKRMAEKIIEILESGHLRKLDHISESVP--VLELFsNIWGAGTKTAQMWYQQ- 355
Cdd:PRK08609  30 FRKAAQALELDERSLSEIDDFTKLKGIGKGTAEVIQEYRETGESSVLQELKKEVPegLLPLL-KLPGLGGKKIAKLYKEl 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17367126  356 GFRSLEDIRsQASLT------------TQQAI--GLKHYSDFLERMP----REEATEIEQT------VQKAAQAfnsgll 411
Cdd:PRK08609 109 GVVDKESLK-EACENgkvqalagfgkkTEEKIleAVKELGKRPERLPiaqvLPIAQEIEEYlatideIIRFSRA------ 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17367126  412 cvacGSYRRGKATCGDVDVLI--THPDgrshrgifsrlldSLRQEGFLTDDLVSQEENG--------QQQKYLGVcrlpg 481
Cdd:PRK08609 182 ----GSLRRARETVKDLDFIIatDEPE-------------AVREQLLQLPNIVEVIAAGdtkvsvelEYEYTISV----- 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17367126  482 pgrrhrrlDIIVVPYSEFACALLYFTGSAHFNRSMRALAKTKGMSLSEHALSTAvvrnthgckvGPGRVLPTPTEKDVFR 561
Cdd:PRK08609 240 --------DFRLVEPEAFATTLHHFTGSKDHNVRMRQLAKERGEKISEYGVEQA----------DTGEVKTFESEEAFFA 301
                        330
                 ....*....|..
gi 17367126  562 LLGLPYREPAER 573
Cdd:PRK08609 302 HFGLPFIPPEVR 313
 
Name Accession Description Interval E-value
NT_POLXc cd00141
Nucleotidyltransferase (NT) domain of family X DNA Polymerases; X family polymerases fill in ...
255-573 2.58e-145

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: 421.22  E-value: 2.58e-145
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17367126 255 HITEKLEVLAKAYSVQG-DKWRALGYAKAINALKSFHKPVTSYQEACSIPGIGKRMAEKIIEILESGHLRKLDHISESVP 333
Cdd:cd00141   2 EIADILEELADLLELLGgNPFRVRAYRKAARALESLPEPIESLEEAKKLPGIGKKIAEKIEEILETGKLRKLEELREDVP 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17367126 334 -VLELFSNIWGAGTKTAQMWYQQGFRSLEDIRSQAS--LTTQQAIGLKHYSDFLERMPREEATEIEQTVQKAAQAFNSGL 410
Cdd:cd00141  82 pGLLLLLRVPGVGPKTARKLYELGIRTLEDLRKAAGakLEQNILIGLEYYEDFQQRIPREEALAIAEIIKEALREVDPVL 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17367126 411 LCVACGSYRRGKATCGDVDVLITHPDGRShRGIFSRLLDSLRQEGFLTDDLvsqeeNGQQQKYLGVCRLPGpGRRHRRLD 490
Cdd:cd00141 162 QVEIAGSYRRGKETVGDIDILVTHPDATS-RGLLEKVVDALVELGFVTEVL-----SKGDTKASGILKLPG-GWKGRRVD 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17367126 491 IIVVPYSEFACALLYFTGSAHFNRSMRALAKTKGMSLSEHALStavvrnthgcKVGPGRVLPTPTEKDVFRLLGLPYREP 570
Cdd:cd00141 235 LRVVPPEEFGAALLYFTGSKQFNRALRRLAKEKGLKLNEYGLF----------DGVDGERLPGETEEEIFEALGLPYIEP 304

                ...
gi 17367126 571 AER 573
Cdd:cd00141 305 ELR 307
POLXc smart00483
DNA polymerase X family; includes vertebrate polymerase beta and terminal ...
251-574 9.44e-87

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


Pssm-ID: 214688  Cd Length: 334  Bit Score: 272.32  E-value: 9.44e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17367126    251 NHNLHITEKLEVLAKAYSVQGDKWRA-LGYAKAINALKSFHKPVTSYQEACSIPGIGKRMAEKIIEILESGHLRKLDHIS 329
Cdd:smart00483   1 NLNRGIIDALEILAENYEVFGENKRKcSYFRKAASVLKSLPFPINSMKDLKGLPGIGDKIKKKIEEIIETGKSSKVLEIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17367126    330 --ESVPVLELFSNIWGAGTKTAQMWYQQGFRSLEDIRSQA--SLTTQQAIGLKHYSDFLERMPREEATEIEQTVQKAAQA 405
Cdd:smart00483  81 ndEVYKSLKLFTNVFGVGPKTAAKWYRKGIRTLEELKKNKelKLTKQQKAGLKYYEDILKKVSRAEAFAVEYIVKRAVRK 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17367126    406 FNSGLLCVACGSYRRGKATCGDVDVLITHPDGRS-------HRGIFSRLLDSLRQEGFLTDDLVsqeenGQQQKYLGVCR 478
Cdd:smart00483 161 ILPDAIVTLTGSFRRGKETGHDVDFLITSPHPAKekelevlDLLLLESTFEELQLPSIRVATLD-----HGQKKFMILKL 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17367126    479 LP------------GPGRRHRRLDIIVVPYSEFACALLYFTGSAHFNRSMRALAKTKG-MSLSEHAlstavvRNTHGCKV 545
Cdd:smart00483 236 SPsredkeksgkpdEKGWKARRVDIVLCPEDQYPTALLGWTGSKQFNRDLRRYATSKFkLMLDGHE------LYDKTKEK 309
                          330       340
                   ....*....|....*....|....*....
gi 17367126    546 gpgrVLPTPTEKDVFRLLGLPYREPAERD 574
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 ...
386-495 2.85e-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: 434213  Cd Length: 110  Bit Score: 166.20  E-value: 2.85e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17367126   386 RMPREEATEIEQTVQKAAQAFNSGLLCVACGSYRRGKATCGDVDVLITHPDGRSHR---GIFSRLLDSLRQEGFLTDDLV 462
Cdd:pfam14792   1 RIPREEVEALEAIVRKAAKTLDPDVEVIVCGSYRRGAESSGDVDILITHPDGTSESelkGLLDRLVARLKKSGFLTDDLA 80
                          90       100       110
                  ....*....|....*....|....*....|...
gi 17367126   463 SQEengQQQKYLGVCRLPGPGRRHRRLDIIVVP 495
Cdd:pfam14792  81 VDS---GGSKWMGVCRLPGSERLHRRIDILVVP 110
PolX COG1796
DNA polymerase/3'-5' exonuclease PolX [Replication, recombination and repair];
252-573 1.45e-39

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


Pssm-ID: 224709 [Multi-domain]  Cd Length: 326  Bit Score: 147.10  E-value: 1.45e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17367126 252 HNLHITEKLEVLAKAYSVQGD-KWRALGYAKAINALKSFHKPVTSYQEA---CSIPGIGKRMAEKIIEILESGHLRKLDH 327
Cdd:COG1796   4 NNHDIARLLERIADYMELEGEnPFKIRAYRKAAQSLENLTEDLEEIEERgrlTELPGIGKGIAEKISEYLDTGEVKKLEA 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17367126 328 ISESVPV-LELFSNIWGAGTKT-AQMWYQQGFRSLEDIRSQASLTTQQAI---GLKHYSDFLERMPR-EEATE---IEQT 398
Cdd:COG1796  84 LKKEVPEgLEPLLKVPGLGPKKiVSLYKELGIKDLEELQEALENGKIRGLrgfGKKSEAKILENIEFaEESPEripLSFT 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17367126 399 VQKA-------AQAFNSGLLCVAcGSYRRGKATCGDVDVLIT--HPDgrshrgifsrlldSLRQEgFLTDDLVSQEENGQ 469
Cdd:COG1796 164 LPIAqeiegylEELTPIIQASIA-GSLRRGRETVGDIDILIStsHPE-------------SVLEE-LLEMPNVQEVIAKG 228
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17367126 470 QQKYLGVCRLpgpgRRHRRLDIIVVPYSEFACALLYFTGSAHFNRSMRALAKTKGMSLSEHALSTavvrnthgckvGPGR 549
Cdd:COG1796 229 ETKVSMLLIL----DEGTSVDFRVVPPEAFGAALQHFTGSKEHNIKIRQLAKAKGEKLSEYGLFR-----------DSGE 293
                       330       340
                ....*....|....*....|....
gi 17367126 550 VLPTPTEKDVFRLLGLPYREPAER 573
Cdd:COG1796 294 IIAGKTEEKIYEHLGLPYIPPELR 317
BRCT_polymerase_lambda cd17715
BRCT domain of DNA polymerase lambda and similar proteins; DNA polymerase lambda, also termed ...
41-125 1.10e-29

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: 111.81  E-value: 1.10e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17367126  41 LSSLRAHVVRTGIGRARAELFEKQIVQHGGQLCPAQGPGVTHIVVDEGMDYEralrlLRLPQLPPGAQLVKSAWLSLCLQ 120
Cdd:cd17715   1 FEGLTIHLVRTGIGRARAELFQRYIVQYGGQIVEDFGEGVTHVVVDDGMDAE-----RKVDRDPPGAQLVKSGWLSACIQ 75

                ....*
gi 17367126 121 ERRLV 125
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 ...
502-574 5.44e-26

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: 434212 [Multi-domain]  Cd Length: 63  Bit Score: 100.53  E-value: 5.44e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17367126   502 ALLYFTGSAHFNRSMRALAKTKGMSLSEHALStavvrnthgcKVGPGRVLPTPTEKDVFRLLGLPYREPAERD 574
Cdd:pfam14791   1 ALLYFTGSKEFNRDLRLLAKKKGLKLNEYGLF----------DLKDGELLPGETEEDIFEALGLPYIPPELRE 63
HHH_8 pfam14716
Helix-hairpin-helix domain;
253-318 2.05e-20

Helix-hairpin-helix domain;


Pssm-ID: 434152 [Multi-domain]  Cd Length: 67  Bit Score: 84.86  E-value: 2.05e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17367126   253 NLHITEKLEVLAKAYSVQG-DKWRALGYAKAINALKSFHKPVTSYQEACSIPGIGKRMAEKIIEILE 318
Cdd:pfam14716   1 NQEIADALEELADLLELKGeDPFRVRAYRRAARALEALPEEITSLEELTKLPGIGKKIAAKIEEILE 67
DNA_pol_lambd_f pfam10391
Fingers domain of DNA polymerase lambda; DNA polymerases catalyze the addition of dNMPs onto ...
336-384 1.86e-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: 431250 [Multi-domain]  Cd Length: 51  Bit Score: 81.73  E-value: 1.86e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 17367126   336 ELFSNIWGAGTKTAQMWYQQGFRSLEDIR--SQASLTTQQAIGLKHYSDFL 384
Cdd:pfam10391   1 KLFTGIYGVGPTTARKWYAQGLRTLDDLRekKTAKLTRQQQIGLKYYDDFN 51
PRK08609 PRK08609
DNA polymerase/3'-5' exonuclease PolX;
279-573 4.63e-12

DNA polymerase/3'-5' exonuclease PolX;


Pssm-ID: 236311 [Multi-domain]  Cd Length: 570  Bit Score: 68.44  E-value: 4.63e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17367126  279 YAKAINALKSFHKPVTSYQEACSIPGIGKRMAEKIIEILESGHLRKLDHISESVP--VLELFsNIWGAGTKTAQMWYQQ- 355
Cdd:PRK08609  30 FRKAAQALELDERSLSEIDDFTKLKGIGKGTAEVIQEYRETGESSVLQELKKEVPegLLPLL-KLPGLGGKKIAKLYKEl 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17367126  356 GFRSLEDIRsQASLT------------TQQAI--GLKHYSDFLERMP----REEATEIEQT------VQKAAQAfnsgll 411
Cdd:PRK08609 109 GVVDKESLK-EACENgkvqalagfgkkTEEKIleAVKELGKRPERLPiaqvLPIAQEIEEYlatideIIRFSRA------ 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17367126  412 cvacGSYRRGKATCGDVDVLI--THPDgrshrgifsrlldSLRQEGFLTDDLVSQEENG--------QQQKYLGVcrlpg 481
Cdd:PRK08609 182 ----GSLRRARETVKDLDFIIatDEPE-------------AVREQLLQLPNIVEVIAAGdtkvsvelEYEYTISV----- 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17367126  482 pgrrhrrlDIIVVPYSEFACALLYFTGSAHFNRSMRALAKTKGMSLSEHALSTAvvrnthgckvGPGRVLPTPTEKDVFR 561
Cdd:PRK08609 240 --------DFRLVEPEAFATTLHHFTGSKDHNVRMRQLAKERGEKISEYGVEQA----------DTGEVKTFESEEAFFA 301
                        330
                 ....*....|..
gi 17367126  562 LLGLPYREPAER 573
Cdd:PRK08609 302 HFGLPFIPPEVR 313
PRK00254 PRK00254
ski2-like helicase; Provisional
267-401 3.69e-03

ski2-like helicase; Provisional


Pssm-ID: 234702 [Multi-domain]  Cd Length: 720  Bit Score: 40.19  E-value: 3.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17367126  267 YSVQ-GDKWRALGYAK-AINALKSFHKPVTSYQEacsipgigkrmaekIIEILESGHLRKLDHISES-VPVLELfSNIwg 343
Cdd:PRK00254 591 YNIDpGDLYRILELADwLMYSLIELYKLFEPKQE--------------VLDYLETLHLRVKHGVREElLELMRL-PMI-- 653
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17367126  344 aGTKTAQMWYQQGFRSLEDIRSQ--ASLTTQQAIGLKHYSDFLERMPREEATEIEQTVQK 401
Cdd:PRK00254 654 -GRKRARALYNAGFRSIEDIVNAkpSELLKVEGIGAKIVEGIFKHLGVEKEVKIKKKPRK 712
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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