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Conserved domains on  [gi|1911238500|ref|XP_036174066|]
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DNA polymerase zeta catalytic subunit isoform X12 [Myotis myotis]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DUF4683 pfam15735
Domain of unknown function (DUF4683); This domain family is found in eukaryotes, and is ...
753-1133 0e+00

Domain of unknown function (DUF4683); This domain family is found in eukaryotes, and is typically between 384 and 400 amino acids in length.


:

Pssm-ID: 464832  Cd Length: 391  Bit Score: 581.44  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911238500  753 NKTMVHSLDSIADESGLNKLKIRYEEFQEHKTEKPNLSQQAAHYMFFPSVVLSNCLSR---PQKLSPVTYKLQPS-NKQS 828
Cdd:pfam15735    1 VRNYVFDDDQSTDESDVGKLKIRYESFQENKAEKTSLSQQEAHYKFFPSVVLSNCLSRrsaLKKLGPVTYKLQQFkSRQS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911238500  829 RLKINKKK--LVGHQETYTKTSETGSTKDN-YIQNNSCNSN-SEKNNVLASDlTKVTRGVFENKTPTDS--FIDCHFGDG 902
Cdd:pfam15735   81 RLKLGKKKlnLDGKQEPEKKTHDKASTKEKcNLQGNALNKNiPETEVELDSD-VQVAHSAFKNKMSIDPanSDSCHFSDD 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911238500  903 TLETEQSFGLYGNKYTLRAKRKVNYETEDSESSFVTHNSKISLPHPMEIGESLDGTLKSRKRRKMSKKLPPVIIKYIIIN 982
Cdd:pfam15735  160 SEESYDASSLCGSKYTLRAKRKVNYETEDSESSEKIHNSKESLPQGSKEEDDDDGSPKSQKRRKVSKKEPPVIIKYIIIN 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911238500  983 RFRGRKNMLVKLGKIDSKEKQVILTEEKMELYKKLAPLKDFWPKVPDSPATKYPIYPPTPKKGHRRKTKHKSAKKKTG-K 1061
Cdd:pfam15735  240 RFKGRKNMLVKLGKVDSSETTVTLTEEKLEKYKKLAPLKDFWPKVPDSPATKYPVYPLTPKKSPKRKAKCKSTNKKRIqR 319
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1911238500 1062 QQRTNSENIKRTLSFRKKRSHAILSPPSPSYNAETEDCDLNYSDVMSKLGFLSERSTSPINSSPPRCWSPTD 1133
Cdd:pfam15735  320 LPNTESSNIKRTLSFKRKRSHASLSPPQPSYNAETEDCDLNYSDVMSKLGFLSERSLSPTASTPPRCWSPTD 391
DNA_polB_zeta_exo cd05778
inactive DEDDy 3'-5' exonuclease domain of eukaryotic DNA polymerase zeta, a family-B DNA ...
2294-2532 3.19e-100

inactive DEDDy 3'-5' exonuclease domain of eukaryotic DNA polymerase zeta, a family-B DNA polymerase; The 3'-5' exonuclease domain of eukaryotic DNA polymerase zeta. DNA polymerase zeta is a family-B DNA polymerase which is distantly related to DNA polymerase delta. It plays a major role in translesion replication and the production of either spontaneous or induced mutations. In addition, DNA polymerase zeta also appears to be involved in somatic hypermutability in B lymphocytes, an important element for the production of high affinity antibodies in response to an antigen. The catalytic subunit contains both polymerase and 3'-5' exonuclease domains, but only exhibits polymerase activity. The DnaQ-like 3'-5' exonuclease domain contains three sequence motifs termed ExoI, ExoII and ExoIII, without the four conserved acidic residues that are crucial for metal binding and catalysis.


:

Pssm-ID: 99821 [Multi-domain]  Cd Length: 231  Bit Score: 321.88  E-value: 3.19e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911238500 2294 IQNLTLISVELHARTRRDLEPDPEFDPICALFYCISSDTPLPNTDKTElTGVIVIDKDKTVSSQDiryqtplLIRSGITR 2373
Cdd:cd05778      1 HQHLTILSLEVHVNTRGDLLPDPEFDPISAIFYCIDDDVSPFILDANK-VGVIIVDELKSNASNG-------RIRSGLSG 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911238500 2374 LEVTYAADEKGLFQEIADIIKRYDPDILLGYEIQMHSWGYLLQRAAALSVDLC-QMISRVPDDKiENRFAAERDDYGSDT 2452
Cdd:cd05778     73 IPVEVVESELELFEELIDLVRRFDPDILSGYEIQRSSWGYLIERAAALGIDDLlDEISRVPSDS-NGKFGDRDDEWGYTH 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911238500 2453 MSEINIVGRITLNLWRIMRNEVALTNYTFENVSFHVLHQRFPLFTFRVLSDWFDNKTDLYRWKMVDHYISRVRGNLQMLE 2532
Cdd:cd05778    152 TSGIKIVGRHILNVWRLMRSELALTNYTLENVVYHVLHQRIPLYSNKTLTEWYKSGSASERWRVLEYYLKRVRLNLEILD 231
POLBc super family cl10023
DNA polymerase type-B family catalytic domain. DNA-directed DNA polymerases elongate DNA by ...
2558-2644 6.98e-51

DNA polymerase type-B family catalytic domain. DNA-directed DNA polymerases elongate DNA by adding nucleotide triphosphate (dNTP) residues to the 5'-end of the growing chain of DNA. DNA-directed DNA polymerases are multifunctional with both synthetic (polymerase) and degradative modes (exonucleases) and play roles in the processes of DNA replication, repair, and recombination. DNA-dependent DNA polymerases can be classified in six main groups based upon their phylogenetic relationships with E. coli polymerase I (class A), E. coli polymerase II (class B), E. coli polymerase III (class C), euryarchaeota polymerase II (class D), human polymerase beta (class x), E. coli UmuC/DinB, and eukaryotic RAP 30/Xeroderma pigmentosum variant (class Y). Family B DNA polymerases include E. coli DNA polymerase II, some eubacterial phage DNA polymerases, nuclear replicative DNA polymerases (alpha, delta, epsilon, and zeta), and eukaryotic viral and plasmid-borne enzymes. DNA polymerase is made up of distinct domains and sub-domains. The polymerase domain of DNA polymerase type B (Pol domain) is responsible for the template-directed polymerization of dNTPs onto the growing primer strand of duplex DNA that is usually magnesium dependent. In general, the architecture of the Pol domain has been likened to a right hand with fingers, thumb, and palm sub-domains with a deep groove to accommodate the nucleic acid substrate. There are a few conserved motifs in the Pol domain of family B DNA polymerases. The conserved aspartic acid residues in the DTDS motifs of the palm sub-domain is crucial for binding to divalent metal ion and is suggested to be important for polymerase catalysis.


The actual alignment was detected with superfamily member cd05534:

Pssm-ID: 353046  Cd Length: 451  Bit Score: 188.19  E-value: 6.98e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911238500 2558 GSQYRVESMMLRIAKPMNYIPVTPNVQQRSQMRAPQCVPLIMEPESRFYSNSVLVLDFQSLYPSIVIAYNYCFSTCLGHV 2637
Cdd:cd05534      1 GSQFRVESMLLRLAKPENYILPSPSRQQVAQQRALECLPLVMEPESGFYSDPVIVLDFQSLYPSIMIAYNYCYSTCLGRV 80

                   ....*..
gi 1911238500 2638 ENLGKSS 2644
Cdd:cd05534     81 EELNGGG 87
PTZ00166 super family cl36522
DNA polymerase delta catalytic subunit; Provisional
41-182 1.04e-11

DNA polymerase delta catalytic subunit; Provisional


The actual alignment was detected with superfamily member PTZ00166:

Pssm-ID: 240301 [Multi-domain]  Cd Length: 1054  Bit Score: 70.83  E-value: 1.04e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911238500   41 FGATPAGQKTCLHLHGIFPYLYVPydgygqQPESYLSQMAFSIDRALNVALGTPSS---TTQHVFKVSLVSGMPFYGYHE 117
Cdd:PTZ00166    80 YGVTKEGHSVLVNVHNFFPYFYIE------APPNFLPEDSQKLKRELNAQLSEQSQfkkYQNTVLDIEIVKKESLMYYKG 153
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1911238500  118 K-ERHFMKIYLYNPAMVKRICELLQSGAIMN-------KFYQPHEAHIPYLLQLFIDYNLYGMNLINLAAVKF 182
Cdd:PTZ00166   154 NgEKDFLKITVQLPKMVPRLRSLIESGVVVCgggwdgiRLFQTYESNVPFVLRFLIDNNITGGSWLTLPKGKY 226
REV3L_RBD cd22287
REV7 binding domain found in protein reversionless 3-like (REV3L) and similar proteins; REV3L, ...
1874-1896 6.56e-09

REV7 binding domain found in protein reversionless 3-like (REV3L) and similar proteins; REV3L, also called REV3-like, or REV3, or DNA polymerase zeta catalytic subunit (POLZ), is the catalytic subunit of the DNA polymerase zeta complex, an error-prone polymerase specialized in translesion DNA synthesis (TLS). REV3L lacks an intrinsic 3'-5' exonuclease activity and thus has no proofreading function. The model corresponds to a conserved region that is responsible for the binding of REV7.


:

Pssm-ID: 412083  Cd Length: 23  Bit Score: 53.33  E-value: 6.56e-09
                           10        20
                   ....*....|....*....|...
gi 1911238500 1874 RTAHILKPLMSPPSREEIMATLL 1896
Cdd:cd22287      1 RTAHILKPLMSPPSREEIMATLL 23
 
Name Accession Description Interval E-value
DUF4683 pfam15735
Domain of unknown function (DUF4683); This domain family is found in eukaryotes, and is ...
753-1133 0e+00

Domain of unknown function (DUF4683); This domain family is found in eukaryotes, and is typically between 384 and 400 amino acids in length.


Pssm-ID: 464832  Cd Length: 391  Bit Score: 581.44  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911238500  753 NKTMVHSLDSIADESGLNKLKIRYEEFQEHKTEKPNLSQQAAHYMFFPSVVLSNCLSR---PQKLSPVTYKLQPS-NKQS 828
Cdd:pfam15735    1 VRNYVFDDDQSTDESDVGKLKIRYESFQENKAEKTSLSQQEAHYKFFPSVVLSNCLSRrsaLKKLGPVTYKLQQFkSRQS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911238500  829 RLKINKKK--LVGHQETYTKTSETGSTKDN-YIQNNSCNSN-SEKNNVLASDlTKVTRGVFENKTPTDS--FIDCHFGDG 902
Cdd:pfam15735   81 RLKLGKKKlnLDGKQEPEKKTHDKASTKEKcNLQGNALNKNiPETEVELDSD-VQVAHSAFKNKMSIDPanSDSCHFSDD 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911238500  903 TLETEQSFGLYGNKYTLRAKRKVNYETEDSESSFVTHNSKISLPHPMEIGESLDGTLKSRKRRKMSKKLPPVIIKYIIIN 982
Cdd:pfam15735  160 SEESYDASSLCGSKYTLRAKRKVNYETEDSESSEKIHNSKESLPQGSKEEDDDDGSPKSQKRRKVSKKEPPVIIKYIIIN 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911238500  983 RFRGRKNMLVKLGKIDSKEKQVILTEEKMELYKKLAPLKDFWPKVPDSPATKYPIYPPTPKKGHRRKTKHKSAKKKTG-K 1061
Cdd:pfam15735  240 RFKGRKNMLVKLGKVDSSETTVTLTEEKLEKYKKLAPLKDFWPKVPDSPATKYPVYPLTPKKSPKRKAKCKSTNKKRIqR 319
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1911238500 1062 QQRTNSENIKRTLSFRKKRSHAILSPPSPSYNAETEDCDLNYSDVMSKLGFLSERSTSPINSSPPRCWSPTD 1133
Cdd:pfam15735  320 LPNTESSNIKRTLSFKRKRSHASLSPPQPSYNAETEDCDLNYSDVMSKLGFLSERSLSPTASTPPRCWSPTD 391
DNA_polB_zeta_exo cd05778
inactive DEDDy 3'-5' exonuclease domain of eukaryotic DNA polymerase zeta, a family-B DNA ...
2294-2532 3.19e-100

inactive DEDDy 3'-5' exonuclease domain of eukaryotic DNA polymerase zeta, a family-B DNA polymerase; The 3'-5' exonuclease domain of eukaryotic DNA polymerase zeta. DNA polymerase zeta is a family-B DNA polymerase which is distantly related to DNA polymerase delta. It plays a major role in translesion replication and the production of either spontaneous or induced mutations. In addition, DNA polymerase zeta also appears to be involved in somatic hypermutability in B lymphocytes, an important element for the production of high affinity antibodies in response to an antigen. The catalytic subunit contains both polymerase and 3'-5' exonuclease domains, but only exhibits polymerase activity. The DnaQ-like 3'-5' exonuclease domain contains three sequence motifs termed ExoI, ExoII and ExoIII, without the four conserved acidic residues that are crucial for metal binding and catalysis.


Pssm-ID: 99821 [Multi-domain]  Cd Length: 231  Bit Score: 321.88  E-value: 3.19e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911238500 2294 IQNLTLISVELHARTRRDLEPDPEFDPICALFYCISSDTPLPNTDKTElTGVIVIDKDKTVSSQDiryqtplLIRSGITR 2373
Cdd:cd05778      1 HQHLTILSLEVHVNTRGDLLPDPEFDPISAIFYCIDDDVSPFILDANK-VGVIIVDELKSNASNG-------RIRSGLSG 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911238500 2374 LEVTYAADEKGLFQEIADIIKRYDPDILLGYEIQMHSWGYLLQRAAALSVDLC-QMISRVPDDKiENRFAAERDDYGSDT 2452
Cdd:cd05778     73 IPVEVVESELELFEELIDLVRRFDPDILSGYEIQRSSWGYLIERAAALGIDDLlDEISRVPSDS-NGKFGDRDDEWGYTH 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911238500 2453 MSEINIVGRITLNLWRIMRNEVALTNYTFENVSFHVLHQRFPLFTFRVLSDWFDNKTDLYRWKMVDHYISRVRGNLQMLE 2532
Cdd:cd05778    152 TSGIKIVGRHILNVWRLMRSELALTNYTLENVVYHVLHQRIPLYSNKTLTEWYKSGSASERWRVLEYYLKRVRLNLEILD 231
POLBc smart00486
DNA polymerase type-B family; DNA polymerase alpha, delta, epsilon and zeta chain (eukaryota), ...
2316-2642 5.61e-53

DNA polymerase type-B family; DNA polymerase alpha, delta, epsilon and zeta chain (eukaryota), DNA polymerases in archaea, DNA polymerase II in e. coli, mitochondrial DNA polymerases and and virus DNA polymerases


Pssm-ID: 214691 [Multi-domain]  Cd Length: 474  Bit Score: 194.67  E-value: 5.61e-53
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911238500  2316 PEFDPICALFYCISSDTPLPNTDKTELTgVIVID---KDKTVSSQDIRYQTPLLIRSGITRLEVTYAADEKGLFQEIADI 2392
Cdd:smart00486    1 PPLKILSFDIETYTDGGNFPDAEIFDDE-IIQISlviNDGDKKGANRRILFTLGTCKEIDGIEVYEFNNEKELLLAFFEF 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911238500  2393 IKRYDPDILLGYEIQMHSWGYLLQRAAALSVDLCQMISRVPD-DKIENRFAAERDDYGSDTMSEINIVGRITLNLWRIMR 2471
Cdd:smart00486   80 IKKYDPDIIYGHNISNFDLPYIISRLEKLKIDPLSKIGRLKIgLRIPNKKPLFGSKSFGLSDIKVYIKGRLVIDLYRLYK 159
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911238500  2472 NEVALTNYTFENVSFHVLHQRFPLFTFRVLSDWFDNKTDLYRWkMVDHYISRVRGNLQMLEQLDLIGKTSEMARLFGIQF 2551
Cdd:smart00486  160 NKLKLPSYKLDTVAEYLLGKEKDDLPYKDIPELYNGNYEERDE-LLRYCIQDAVLTLKLFNKLNVIPLIIELARIAGIPL 238
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911238500  2552 LHVLTRGSQYRVESMMLRIAKPMNYIPVTPNVQQRSQMRAPQCVP------LIMEPESRFYSNSVLVLDFQSLYPSIVIA 2625
Cdd:smart00486  239 RRTLYYGSQIRVESLLLREAKKNNYILPSKELYDFKGSEPDLKKKvkyeggKVLEPKKGFYDNPVLVLDFNSLYPSIIIA 318
                           330
                    ....*....|....*..
gi 1911238500  2626 YNYCFSTCLGHVENLGK 2642
Cdd:smart00486  319 HNLCYSTLVGVGEVVIK 335
POLBc_zeta cd05534
DNA polymerase type-B zeta subfamily catalytic domain. DNA polymerase (Pol) zeta is a member ...
2558-2644 6.98e-51

DNA polymerase type-B zeta subfamily catalytic domain. DNA polymerase (Pol) zeta is a member of the eukaryotic B-family of DNA polymerases and distantly related to DNA Pol delta. Pol zeta plays a major role in translesion replication and the production of either spontaneous or induced mutations. Apart from its role in translesion replication, Pol zeta also appears to be involved in somatic hypermutability in B lymphocytes, an important element for the production of high affinity antibodies in response to an antigen.


Pssm-ID: 99917  Cd Length: 451  Bit Score: 188.19  E-value: 6.98e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911238500 2558 GSQYRVESMMLRIAKPMNYIPVTPNVQQRSQMRAPQCVPLIMEPESRFYSNSVLVLDFQSLYPSIVIAYNYCFSTCLGHV 2637
Cdd:cd05534      1 GSQFRVESMLLRLAKPENYILPSPSRQQVAQQRALECLPLVMEPESGFYSDPVIVLDFQSLYPSIMIAYNYCYSTCLGRV 80

                   ....*..
gi 1911238500 2638 ENLGKSS 2644
Cdd:cd05534     81 EELNGGG 87
PTZ00166 PTZ00166
DNA polymerase delta catalytic subunit; Provisional
2381-2634 1.81e-33

DNA polymerase delta catalytic subunit; Provisional


Pssm-ID: 240301 [Multi-domain]  Cd Length: 1054  Bit Score: 142.09  E-value: 1.81e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911238500 2381 DEKGLFQEIADIIKRYDPDILLGYEIQMHSWGYLLQRAAALSVDLCQMISRVPDDKI---ENRFAAERddYGSDTMSEIN 2457
Cdd:PTZ00166   329 TEKELLLAWAEFVIAVDPDFLTGYNIINFDLPYLLNRAKALKLNDFKYLGRIKSTRSvikDSKFSSKQ--MGTRESKEIN 406
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911238500 2458 IVGRITLNLWRIMRNEVALTNYTFENVSFHVLHQRFPLFTFRVLSDWFdNKTDLYRWKMVDHYISRVRGNLQMLEQLDLI 2537
Cdd:PTZ00166   407 IEGRIQFDVMDLIRRDYKLKSYSLNYVSFEFLKEQKEDVHYSIISDLQ-NGSPETRRRIAVYCLKDAILPLRLLDKLLLI 485
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911238500 2538 GKTSEMARLFGIQFLHVLTRGSQYRVESMMLRIAKPMNY-IPVTPNVQQRSQMRAPQCVplIMEPESRFYSNSVLVLDFQ 2616
Cdd:PTZ00166   486 YNYVEMARVTGTPIGWLLTRGQQIKVTSQLLRKCKKLNYvIPTVKYSGGGSEEKYEGAT--VLEPKKGFYDEPIATLDFA 563
                          250
                   ....*....|....*...
gi 1911238500 2617 SLYPSIVIAYNYCFSTCL 2634
Cdd:PTZ00166   564 SLYPSIMIAHNLCYSTLV 581
PolB COG0417
DNA polymerase B elongation subunit [Replication, recombination and repair];
2345-2632 4.40e-25

DNA polymerase B elongation subunit [Replication, recombination and repair];


Pssm-ID: 440186 [Multi-domain]  Cd Length: 794  Bit Score: 114.15  E-value: 4.40e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911238500 2345 VIVIdkdkTVSSQDIRYQTPLLIRSGItRLEVTYAADEKGLFQEIADIIKRYDPDILLGYEIQMHSWGYLLQRAAALSVD 2424
Cdd:COG0417    184 IISI----GLAGSDGEKKVLMLGREGV-DFEVEYFDDEKALLEAFFEIIREYDPDIIIGWNVDNFDLPYLQKRAERLGIP 258
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911238500 2425 LcqMISRvpddkieNRFAAERDDYGSDTMseINIVGRITLNLWRIMRN-EVALTNYTFENVSFHVLHqrfplftfrvlsd 2503
Cdd:COG0417    259 L--DLGR-------DGSEPSWREHGGQGF--ASIPGRVVIDLYDALKSaTYKFKSYSLDAVAEELLG------------- 314
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911238500 2504 wfDNKTDLYRWKMVDHYISR----VRGNLQ-------MLEQLDLIGKTSEMARLFGIQFLHVLTRGSQYRVESMMLRIAK 2572
Cdd:COG0417    315 --EGKLIVDGGEIERLWDDDkpalAEYNLRdaeltlrIFEKTLLLPFLIELSRITGLPLDDVGRAGSSAAFENLLLPEAH 392
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911238500 2573 PMNYipVTPNVQQRSQMRAPQCVplIMEPESRFYSNsVLVLDFQSLYPSIVIAYNYCFST 2632
Cdd:COG0417    393 RRGY--LAPNKGEIKGEAYPGGY--VLDPKPGLYEN-VLVLDFKSLYPSIIRTFNISPET 447
DNA_pol_B pfam00136
DNA polymerase family B; This region of DNA polymerase B appears to consist of more than one ...
2554-2639 3.12e-18

DNA polymerase family B; This region of DNA polymerase B appears to consist of more than one structural domain, possibly including elongation, DNA-binding and dNTP binding activities.


Pssm-ID: 395085  Cd Length: 439  Bit Score: 90.36  E-value: 3.12e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911238500 2554 VLTRGSQYRVESMMLRIAKPMNYIpvTPNVQQRSQMRAPQCVPLIMEPESRFYSNSVLVLDFQSLYPSIVIAYNYCFSTC 2633
Cdd:pfam00136    6 VLEGGQQIRVESCLLRLALEEGFI--LPDRPSAKGDEDGYQGATVIEPKKGFYDKPVLVLDFNSLYPSIIQAHNLCYTTL 83

                   ....*.
gi 1911238500 2634 LGHVEN 2639
Cdd:pfam00136   84 VRSVDE 89
PTZ00166 PTZ00166
DNA polymerase delta catalytic subunit; Provisional
41-182 1.04e-11

DNA polymerase delta catalytic subunit; Provisional


Pssm-ID: 240301 [Multi-domain]  Cd Length: 1054  Bit Score: 70.83  E-value: 1.04e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911238500   41 FGATPAGQKTCLHLHGIFPYLYVPydgygqQPESYLSQMAFSIDRALNVALGTPSS---TTQHVFKVSLVSGMPFYGYHE 117
Cdd:PTZ00166    80 YGVTKEGHSVLVNVHNFFPYFYIE------APPNFLPEDSQKLKRELNAQLSEQSQfkkYQNTVLDIEIVKKESLMYYKG 153
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1911238500  118 K-ERHFMKIYLYNPAMVKRICELLQSGAIMN-------KFYQPHEAHIPYLLQLFIDYNLYGMNLINLAAVKF 182
Cdd:PTZ00166   154 NgEKDFLKITVQLPKMVPRLRSLIESGVVVCgggwdgiRLFQTYESNVPFVLRFLIDNNITGGSWLTLPKGKY 226
DNA_pol_B_exo1 pfam03104
DNA polymerase family B, exonuclease domain; This domain has 3' to 5' exonuclease activity and ...
2314-2484 2.42e-11

DNA polymerase family B, exonuclease domain; This domain has 3' to 5' exonuclease activity and adopts a ribonuclease H type fold.


Pssm-ID: 397292  Cd Length: 333  Bit Score: 67.83  E-value: 2.42e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911238500 2314 PDPEF--DP---ICALFYCISSDTPLPNTdkteltgVIVIdkdKTVSSQDIrYQTPLLIRSGITRLEVTYAADEKGLFQE 2388
Cdd:pfam03104  172 PDAENvkDPiiqISCMLDGQGEPEPEPRF-------LFTL---RECDSEDI-EDFEYTPKPIYPGVKVFEFPSEKELLRR 240
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911238500 2389 IADIIKRYDPDILLGYEIQMHSWGYLLQRAAALSVDLCQMISRVPDDkieNRFAAERDDYGSDTMSEINIVGRITLNLWR 2468
Cdd:pfam03104  241 FFEFIRQYDPDIITGYNGDNFDWPYILNRAKELYIVKLSSIGRLNRG---GRSKVREIGFGTRSYEKVKISGRLHLDLYR 317
                          170
                   ....*....|....*.
gi 1911238500 2469 IMRNEVALTNYTFENV 2484
Cdd:pfam03104  318 VIKRDYKLPSYKLNAV 333
pol2 TIGR00592
DNA polymerase (pol2); All proteins in this superfamily for which functions are known are DNA ...
2379-2632 2.84e-09

DNA polymerase (pol2); All proteins in this superfamily for which functions are known are DNA polymerases.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273159 [Multi-domain]  Cd Length: 1172  Bit Score: 63.15  E-value: 2.84e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911238500 2379 AADEKGLFQEIADIIKRYDPDILLGYEIQMHSWGYLLQRAAALSVDLCQMISRVPDDKIENRFAAERddygsdtmseinI 2458
Cdd:TIGR00592  581 LATERALIKKFMAKVKKIDPDEIVGHDYQQRALKVLANRINDLKIPTWSKIGRLRRSPKFGRRFGER------------T 648
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911238500 2459 VGRITLNLWRIMRNEVALTNYTFENVSFHVLH-QRFPLFTFRVLSDWFDNKTDLYrwkMVDHYISRVRGNLQMLEQLDLI 2537
Cdd:TIGR00592  649 CGRMICDVEISAKELIRCKSYDLSELVQQILKtERKVIPIDNINNMYSESSSLTY---LLEHTWKDAMFILQIMCELNVL 725
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911238500 2538 GKTSEMARLFGIQFLHVLTRGSQYRVESMMLRIAKPMNYI-PVTPNVQQRSQMR--------------APQCVPLIMEPE 2602
Cdd:TIGR00592  726 PLALQITNIAGNIMSRTLMGGRSERNEFLLLHAFYENNYIvPDKQIFRKQQKLGdedeeidgykkgkkAAYAGGLVLEPK 805
                          250       260       270
                   ....*....|....*....|....*....|
gi 1911238500 2603 SRFYSNSVLVLDFQSLYPSIVIAYNYCFST 2632
Cdd:TIGR00592  806 VGLYDKYVLLMDFNSLYPSIIQEFNICFTT 835
REV3L_RBD cd22287
REV7 binding domain found in protein reversionless 3-like (REV3L) and similar proteins; REV3L, ...
1874-1896 6.56e-09

REV7 binding domain found in protein reversionless 3-like (REV3L) and similar proteins; REV3L, also called REV3-like, or REV3, or DNA polymerase zeta catalytic subunit (POLZ), is the catalytic subunit of the DNA polymerase zeta complex, an error-prone polymerase specialized in translesion DNA synthesis (TLS). REV3L lacks an intrinsic 3'-5' exonuclease activity and thus has no proofreading function. The model corresponds to a conserved region that is responsible for the binding of REV7.


Pssm-ID: 412083  Cd Length: 23  Bit Score: 53.33  E-value: 6.56e-09
                           10        20
                   ....*....|....*....|...
gi 1911238500 1874 RTAHILKPLMSPPSREEIMATLL 1896
Cdd:cd22287      1 RTAHILKPLMSPPSREEIMATLL 23
DNA_pol_B_exo1 pfam03104
DNA polymerase family B, exonuclease domain; This domain has 3' to 5' exonuclease activity and ...
51-189 3.72e-07

DNA polymerase family B, exonuclease domain; This domain has 3' to 5' exonuclease activity and adopts a ribonuclease H type fold.


Pssm-ID: 397292  Cd Length: 333  Bit Score: 54.73  E-value: 3.72e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911238500   51 CLHLHGIFPYLYVPYDGYGQQPE--SYLSQMAFSIDRALNVALGTPSSttqhvfkvslvsgmpFYGYHEKERHFMKIYLY 128
Cdd:pfam03104    9 CVNVFGFKPYFYCLAPDGKELEEviEEIKELYEGLDKIEKIELKLKKS---------------LYGYEEDPVPYLKVSFA 73
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1911238500  129 NPAMVKRICELLQSGAIMNKFyqphEAHIPYLLQLFIDYNLYGMNLINLAAVKFRKARRKS 189
Cdd:pfam03104   74 NPRPLLKIRKYLSPENISDVY----EYDVDYLERFLIDNDIVGFGWYKVKVYPFRAEGRIS 130
 
Name Accession Description Interval E-value
DUF4683 pfam15735
Domain of unknown function (DUF4683); This domain family is found in eukaryotes, and is ...
753-1133 0e+00

Domain of unknown function (DUF4683); This domain family is found in eukaryotes, and is typically between 384 and 400 amino acids in length.


Pssm-ID: 464832  Cd Length: 391  Bit Score: 581.44  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911238500  753 NKTMVHSLDSIADESGLNKLKIRYEEFQEHKTEKPNLSQQAAHYMFFPSVVLSNCLSR---PQKLSPVTYKLQPS-NKQS 828
Cdd:pfam15735    1 VRNYVFDDDQSTDESDVGKLKIRYESFQENKAEKTSLSQQEAHYKFFPSVVLSNCLSRrsaLKKLGPVTYKLQQFkSRQS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911238500  829 RLKINKKK--LVGHQETYTKTSETGSTKDN-YIQNNSCNSN-SEKNNVLASDlTKVTRGVFENKTPTDS--FIDCHFGDG 902
Cdd:pfam15735   81 RLKLGKKKlnLDGKQEPEKKTHDKASTKEKcNLQGNALNKNiPETEVELDSD-VQVAHSAFKNKMSIDPanSDSCHFSDD 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911238500  903 TLETEQSFGLYGNKYTLRAKRKVNYETEDSESSFVTHNSKISLPHPMEIGESLDGTLKSRKRRKMSKKLPPVIIKYIIIN 982
Cdd:pfam15735  160 SEESYDASSLCGSKYTLRAKRKVNYETEDSESSEKIHNSKESLPQGSKEEDDDDGSPKSQKRRKVSKKEPPVIIKYIIIN 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911238500  983 RFRGRKNMLVKLGKIDSKEKQVILTEEKMELYKKLAPLKDFWPKVPDSPATKYPIYPPTPKKGHRRKTKHKSAKKKTG-K 1061
Cdd:pfam15735  240 RFKGRKNMLVKLGKVDSSETTVTLTEEKLEKYKKLAPLKDFWPKVPDSPATKYPVYPLTPKKSPKRKAKCKSTNKKRIqR 319
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1911238500 1062 QQRTNSENIKRTLSFRKKRSHAILSPPSPSYNAETEDCDLNYSDVMSKLGFLSERSTSPINSSPPRCWSPTD 1133
Cdd:pfam15735  320 LPNTESSNIKRTLSFKRKRSHASLSPPQPSYNAETEDCDLNYSDVMSKLGFLSERSLSPTASTPPRCWSPTD 391
DNA_polB_zeta_exo cd05778
inactive DEDDy 3'-5' exonuclease domain of eukaryotic DNA polymerase zeta, a family-B DNA ...
2294-2532 3.19e-100

inactive DEDDy 3'-5' exonuclease domain of eukaryotic DNA polymerase zeta, a family-B DNA polymerase; The 3'-5' exonuclease domain of eukaryotic DNA polymerase zeta. DNA polymerase zeta is a family-B DNA polymerase which is distantly related to DNA polymerase delta. It plays a major role in translesion replication and the production of either spontaneous or induced mutations. In addition, DNA polymerase zeta also appears to be involved in somatic hypermutability in B lymphocytes, an important element for the production of high affinity antibodies in response to an antigen. The catalytic subunit contains both polymerase and 3'-5' exonuclease domains, but only exhibits polymerase activity. The DnaQ-like 3'-5' exonuclease domain contains three sequence motifs termed ExoI, ExoII and ExoIII, without the four conserved acidic residues that are crucial for metal binding and catalysis.


Pssm-ID: 99821 [Multi-domain]  Cd Length: 231  Bit Score: 321.88  E-value: 3.19e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911238500 2294 IQNLTLISVELHARTRRDLEPDPEFDPICALFYCISSDTPLPNTDKTElTGVIVIDKDKTVSSQDiryqtplLIRSGITR 2373
Cdd:cd05778      1 HQHLTILSLEVHVNTRGDLLPDPEFDPISAIFYCIDDDVSPFILDANK-VGVIIVDELKSNASNG-------RIRSGLSG 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911238500 2374 LEVTYAADEKGLFQEIADIIKRYDPDILLGYEIQMHSWGYLLQRAAALSVDLC-QMISRVPDDKiENRFAAERDDYGSDT 2452
Cdd:cd05778     73 IPVEVVESELELFEELIDLVRRFDPDILSGYEIQRSSWGYLIERAAALGIDDLlDEISRVPSDS-NGKFGDRDDEWGYTH 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911238500 2453 MSEINIVGRITLNLWRIMRNEVALTNYTFENVSFHVLHQRFPLFTFRVLSDWFDNKTDLYRWKMVDHYISRVRGNLQMLE 2532
Cdd:cd05778    152 TSGIKIVGRHILNVWRLMRSELALTNYTLENVVYHVLHQRIPLYSNKTLTEWYKSGSASERWRVLEYYLKRVRLNLEILD 231
POLBc smart00486
DNA polymerase type-B family; DNA polymerase alpha, delta, epsilon and zeta chain (eukaryota), ...
2316-2642 5.61e-53

DNA polymerase type-B family; DNA polymerase alpha, delta, epsilon and zeta chain (eukaryota), DNA polymerases in archaea, DNA polymerase II in e. coli, mitochondrial DNA polymerases and and virus DNA polymerases


Pssm-ID: 214691 [Multi-domain]  Cd Length: 474  Bit Score: 194.67  E-value: 5.61e-53
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911238500  2316 PEFDPICALFYCISSDTPLPNTDKTELTgVIVID---KDKTVSSQDIRYQTPLLIRSGITRLEVTYAADEKGLFQEIADI 2392
Cdd:smart00486    1 PPLKILSFDIETYTDGGNFPDAEIFDDE-IIQISlviNDGDKKGANRRILFTLGTCKEIDGIEVYEFNNEKELLLAFFEF 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911238500  2393 IKRYDPDILLGYEIQMHSWGYLLQRAAALSVDLCQMISRVPD-DKIENRFAAERDDYGSDTMSEINIVGRITLNLWRIMR 2471
Cdd:smart00486   80 IKKYDPDIIYGHNISNFDLPYIISRLEKLKIDPLSKIGRLKIgLRIPNKKPLFGSKSFGLSDIKVYIKGRLVIDLYRLYK 159
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911238500  2472 NEVALTNYTFENVSFHVLHQRFPLFTFRVLSDWFDNKTDLYRWkMVDHYISRVRGNLQMLEQLDLIGKTSEMARLFGIQF 2551
Cdd:smart00486  160 NKLKLPSYKLDTVAEYLLGKEKDDLPYKDIPELYNGNYEERDE-LLRYCIQDAVLTLKLFNKLNVIPLIIELARIAGIPL 238
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911238500  2552 LHVLTRGSQYRVESMMLRIAKPMNYIPVTPNVQQRSQMRAPQCVP------LIMEPESRFYSNSVLVLDFQSLYPSIVIA 2625
Cdd:smart00486  239 RRTLYYGSQIRVESLLLREAKKNNYILPSKELYDFKGSEPDLKKKvkyeggKVLEPKKGFYDNPVLVLDFNSLYPSIIIA 318
                           330
                    ....*....|....*..
gi 1911238500  2626 YNYCFSTCLGHVENLGK 2642
Cdd:smart00486  319 HNLCYSTLVGVGEVVIK 335
DEDDy_DNA_polB_exo cd05160
DEDDy 3'-5' exonuclease domain of family-B DNA polymerases; The 3'-5' exonuclease domain of ...
2308-2532 1.51e-52

DEDDy 3'-5' exonuclease domain of family-B DNA polymerases; The 3'-5' exonuclease domain of family-B DNA polymerases. This domain has a fundamental role in reducing polymerase errors and is involved in proofreading activity. Family-B DNA polymerases contain an N-terminal DEDDy DnaQ-like exonuclease domain in the same polypeptide chain as the polymerase domain, similar to family-A DNA polymerases. This domain contains three sequence motifs termed ExoI, ExoII and ExoIII, with a specific YX(3)D pattern at ExoIII. These motifs are clustered around the active site and contain four conserved acidic residues that serve as ligands for the two metal ions required for catalysis. The exonuclease domain of family B polymerase also contains a beta hairpin structure that plays an important role in active site switching in the event of nucleotide misincorporation. Members include Escherichia coli DNA polymerase II, some eubacterial phage DNA polymerases, nuclear replicative DNA polymerases (alpha, delta, epsilon and zeta), and eukaryotic viral and plasmid-borne enzymes. Nuclear DNA polymerases alpha and zeta lack the four conserved acidic metal-binding residues. Family-B DNA polymerases are predominantly involved in DNA replication and DNA repair.


Pssm-ID: 176646 [Multi-domain]  Cd Length: 199  Bit Score: 184.10  E-value: 1.51e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911238500 2308 TRRDLEPDPEFDPICALFYCISSDtplpntdkteltGVIVIDKDKTVSSQDIRYqtpllirsGITRLEVTYAADEKGLFQ 2387
Cdd:cd05160      9 TPPVGGPEPDRDPIICITYADSFD------------GVKVVFLLKTSTVGDDIE--------FIDGIEVEYFADEKELLK 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911238500 2388 EIADIIKRYDPDILLGYEIQMHSWGYLLQRAAALSVDLCQMISRVPDDKIENRFaaerddygsdtMSEINIVGRITLNLW 2467
Cdd:cd05160     69 RFFDIIREYDPDILTGYNIDDFDLPYLLKRAEALGIKLTDGIYRRSGGEKSSGS-----------TERIAVKGRVVFDLL 137
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1911238500 2468 RIMRNEVALTNYTFENVSFHVLHQRFPLFTFRvlsDWFDNKTDLYRWKMVDHYISRVRGNLQMLE 2532
Cdd:cd05160    138 AAYKRDFKLKSYTLDAVAEELLGEGKEKVDGE---IIEDAEWEEDPERLIEYNLKDAELTLQILE 199
POLBc_zeta cd05534
DNA polymerase type-B zeta subfamily catalytic domain. DNA polymerase (Pol) zeta is a member ...
2558-2644 6.98e-51

DNA polymerase type-B zeta subfamily catalytic domain. DNA polymerase (Pol) zeta is a member of the eukaryotic B-family of DNA polymerases and distantly related to DNA Pol delta. Pol zeta plays a major role in translesion replication and the production of either spontaneous or induced mutations. Apart from its role in translesion replication, Pol zeta also appears to be involved in somatic hypermutability in B lymphocytes, an important element for the production of high affinity antibodies in response to an antigen.


Pssm-ID: 99917  Cd Length: 451  Bit Score: 188.19  E-value: 6.98e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911238500 2558 GSQYRVESMMLRIAKPMNYIPVTPNVQQRSQMRAPQCVPLIMEPESRFYSNSVLVLDFQSLYPSIVIAYNYCFSTCLGHV 2637
Cdd:cd05534      1 GSQFRVESMLLRLAKPENYILPSPSRQQVAQQRALECLPLVMEPESGFYSDPVIVLDFQSLYPSIMIAYNYCYSTCLGRV 80

                   ....*..
gi 1911238500 2638 ENLGKSS 2644
Cdd:cd05534     81 EELNGGG 87
PTZ00166 PTZ00166
DNA polymerase delta catalytic subunit; Provisional
2381-2634 1.81e-33

DNA polymerase delta catalytic subunit; Provisional


Pssm-ID: 240301 [Multi-domain]  Cd Length: 1054  Bit Score: 142.09  E-value: 1.81e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911238500 2381 DEKGLFQEIADIIKRYDPDILLGYEIQMHSWGYLLQRAAALSVDLCQMISRVPDDKI---ENRFAAERddYGSDTMSEIN 2457
Cdd:PTZ00166   329 TEKELLLAWAEFVIAVDPDFLTGYNIINFDLPYLLNRAKALKLNDFKYLGRIKSTRSvikDSKFSSKQ--MGTRESKEIN 406
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911238500 2458 IVGRITLNLWRIMRNEVALTNYTFENVSFHVLHQRFPLFTFRVLSDWFdNKTDLYRWKMVDHYISRVRGNLQMLEQLDLI 2537
Cdd:PTZ00166   407 IEGRIQFDVMDLIRRDYKLKSYSLNYVSFEFLKEQKEDVHYSIISDLQ-NGSPETRRRIAVYCLKDAILPLRLLDKLLLI 485
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911238500 2538 GKTSEMARLFGIQFLHVLTRGSQYRVESMMLRIAKPMNY-IPVTPNVQQRSQMRAPQCVplIMEPESRFYSNSVLVLDFQ 2616
Cdd:PTZ00166   486 YNYVEMARVTGTPIGWLLTRGQQIKVTSQLLRKCKKLNYvIPTVKYSGGGSEEKYEGAT--VLEPKKGFYDEPIATLDFA 563
                          250
                   ....*....|....*...
gi 1911238500 2617 SLYPSIVIAYNYCFSTCL 2634
Cdd:PTZ00166   564 SLYPSIMIAHNLCYSTLV 581
PolB COG0417
DNA polymerase B elongation subunit [Replication, recombination and repair];
2345-2632 4.40e-25

DNA polymerase B elongation subunit [Replication, recombination and repair];


Pssm-ID: 440186 [Multi-domain]  Cd Length: 794  Bit Score: 114.15  E-value: 4.40e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911238500 2345 VIVIdkdkTVSSQDIRYQTPLLIRSGItRLEVTYAADEKGLFQEIADIIKRYDPDILLGYEIQMHSWGYLLQRAAALSVD 2424
Cdd:COG0417    184 IISI----GLAGSDGEKKVLMLGREGV-DFEVEYFDDEKALLEAFFEIIREYDPDIIIGWNVDNFDLPYLQKRAERLGIP 258
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911238500 2425 LcqMISRvpddkieNRFAAERDDYGSDTMseINIVGRITLNLWRIMRN-EVALTNYTFENVSFHVLHqrfplftfrvlsd 2503
Cdd:COG0417    259 L--DLGR-------DGSEPSWREHGGQGF--ASIPGRVVIDLYDALKSaTYKFKSYSLDAVAEELLG------------- 314
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911238500 2504 wfDNKTDLYRWKMVDHYISR----VRGNLQ-------MLEQLDLIGKTSEMARLFGIQFLHVLTRGSQYRVESMMLRIAK 2572
Cdd:COG0417    315 --EGKLIVDGGEIERLWDDDkpalAEYNLRdaeltlrIFEKTLLLPFLIELSRITGLPLDDVGRAGSSAAFENLLLPEAH 392
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911238500 2573 PMNYipVTPNVQQRSQMRAPQCVplIMEPESRFYSNsVLVLDFQSLYPSIVIAYNYCFST 2632
Cdd:COG0417    393 RRGY--LAPNKGEIKGEAYPGGY--VLDPKPGLYEN-VLVLDFKSLYPSIIRTFNISPET 447
DNA_pol_B pfam00136
DNA polymerase family B; This region of DNA polymerase B appears to consist of more than one ...
2554-2639 3.12e-18

DNA polymerase family B; This region of DNA polymerase B appears to consist of more than one structural domain, possibly including elongation, DNA-binding and dNTP binding activities.


Pssm-ID: 395085  Cd Length: 439  Bit Score: 90.36  E-value: 3.12e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911238500 2554 VLTRGSQYRVESMMLRIAKPMNYIpvTPNVQQRSQMRAPQCVPLIMEPESRFYSNSVLVLDFQSLYPSIVIAYNYCFSTC 2633
Cdd:pfam00136    6 VLEGGQQIRVESCLLRLALEEGFI--LPDRPSAKGDEDGYQGATVIEPKKGFYDKPVLVLDFNSLYPSIIQAHNLCYTTL 83

                   ....*.
gi 1911238500 2634 LGHVEN 2639
Cdd:pfam00136   84 VRSVDE 89
PRK05762 PRK05762
DNA polymerase II; Reviewed
2378-2640 1.97e-17

DNA polymerase II; Reviewed


Pssm-ID: 235595 [Multi-domain]  Cd Length: 786  Bit Score: 89.53  E-value: 1.97e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911238500 2378 YAADEKGLFQEIADIIKRYDPDILLGYEIQMHSWGYLLQRAAALSVDLcqMISRVpDDKIENRFAAERDDYGSdtmseIN 2457
Cdd:PRK05762   199 YVADEKALLEKFNAWFAEHDPDVIIGWNVVQFDLRLLQERAERYGIPL--RLGRD-GSELEWREHPFRSGYGF-----AS 270
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911238500 2458 IVGRITLNLWRIMRnevALTN----YTFENVSFHVL---------HQRFPLFTFRvlsdWFDNKTDLYRWKMVDhyisrV 2524
Cdd:PRK05762   271 VPGRLVLDGIDALK---SATWvfdsFSLEYVSQRLLgegkaiddpYDRMDEIDRR----FAEDKPALARYNLKD-----C 338
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911238500 2525 RGNLQMLEQLDLIGKTSEMARLFGIQflhvLTR--GSQYRVESMMLRIAKPMNYipVTPNVQQRsqmrAPQCVP--LIME 2600
Cdd:PRK05762   339 ELVTRIFEKTKLLPFLLERATVTGLP----LDRvgGSVAAFEHLYLPRAHRAGY--VAPNLGER----PGEASPggYVMD 408
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1911238500 2601 PESRFYSNsVLVLDFQSLYPSIVIAYNYCFstcLGHVENL 2640
Cdd:PRK05762   409 SKPGLYDS-VLVLDFKSLYPSIIRTFNIDP---DGLVEGL 444
DNA_polB_delta_exo cd05777
DEDDy 3'-5' exonuclease domain of eukaryotic DNA polymerase delta, a family-B DNA polymerase; ...
2381-2489 7.72e-14

DEDDy 3'-5' exonuclease domain of eukaryotic DNA polymerase delta, a family-B DNA polymerase; The 3'-5' exonuclease domain of eukaryotic DNA polymerase delta. DNA polymerase delta is a family-B DNA polymerase with a catalytic subunit that contains a DEDDy-type DnaQ-like 3'-5' exonuclease domain. It is one of the three DNA-dependent type B DNA polymerases (alpha and epsilon are the other two) that have been identified as essential for nuclear DNA replication in eukaryotes. DNA polymerase delta is the enzyme responsible for both elongation and maturation of Okazaki fragments on the lagging strand. It is also implicated in mismatch repair (MMR) and base excision repair (BER). The catalytic subunit displays both polymerase and 3'-5' exonuclease activities. The exonuclease domain contains three sequence motifs termed ExoI, ExoII and ExoIII, with a specific YX(3)D pattern at ExoIII. These motifs are clustered around the active site and contain four conserved acidic residues necessary for metal binding and catalysis. The exonuclease domain of family B polymerase also contains a beta hairpin structure that plays an important role in active site switching in the event of nucleotide misincorporation.


Pssm-ID: 99820 [Multi-domain]  Cd Length: 230  Bit Score: 73.38  E-value: 7.72e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911238500 2381 DEKGLFQEIADIIKRYDPDILLGYEIQMHSWGYLLQRAAALSVDLCQMISRVPDDKI---ENRFAAERddYGSDTMSEIN 2457
Cdd:cd05777     70 TEEELLLAWRDFVQEVDPDIITGYNICNFDLPYLLERAKALKLNTFPFLGRIKNIKStikDTTFSSKQ--MGTRETKEIN 147
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1911238500 2458 IVGRITLNLWRIMRNEVALTNYTFENVSFHVL 2489
Cdd:cd05777    148 IEGRIQFDLLQVIQRDYKLRSYSLNSVSAHFL 179
POLBc cd00145
DNA polymerase type-B family catalytic domain. DNA-directed DNA polymerases elongate DNA by ...
2591-2646 7.13e-13

DNA polymerase type-B family catalytic domain. DNA-directed DNA polymerases elongate DNA by adding nucleotide triphosphate (dNTP) residues to the 5'-end of the growing chain of DNA. DNA-directed DNA polymerases are multifunctional with both synthetic (polymerase) and degradative modes (exonucleases) and play roles in the processes of DNA replication, repair, and recombination. DNA-dependent DNA polymerases can be classified in six main groups based upon their phylogenetic relationships with E. coli polymerase I (class A), E. coli polymerase II (class B), E. coli polymerase III (class C), euryarchaeota polymerase II (class D), human polymerase beta (class x), E. coli UmuC/DinB, and eukaryotic RAP 30/Xeroderma pigmentosum variant (class Y). Family B DNA polymerases include E. coli DNA polymerase II, some eubacterial phage DNA polymerases, nuclear replicative DNA polymerases (alpha, delta, epsilon, and zeta), and eukaryotic viral and plasmid-borne enzymes. DNA polymerase is made up of distinct domains and sub-domains. The polymerase domain of DNA polymerase type B (Pol domain) is responsible for the template-directed polymerization of dNTPs onto the growing primer strand of duplex DNA that is usually magnesium dependent. In general, the architecture of the Pol domain has been likened to a right hand with fingers, thumb, and palm sub-domains with a deep groove to accommodate the nucleic acid substrate. There are a few conserved motifs in the Pol domain of family B DNA polymerases. The conserved aspartic acid residues in the DTDS motifs of the palm sub-domain is crucial for binding to divalent metal ion and is suggested to be important for polymerase catalysis.


Pssm-ID: 99912 [Multi-domain]  Cd Length: 323  Bit Score: 72.40  E-value: 7.13e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1911238500 2591 APQCVPLIMEPEsRFYSNSVLVLDFQSLYPSIVIAYNYCFSTCLGHVENLGKSSYD 2646
Cdd:cd00145      1 EPYEGGYVFDPI-PGLYENVIVLDFKSLYPSIIITYNLSPTTLVGNGEIAAPEDYI 55
PTZ00166 PTZ00166
DNA polymerase delta catalytic subunit; Provisional
41-182 1.04e-11

DNA polymerase delta catalytic subunit; Provisional


Pssm-ID: 240301 [Multi-domain]  Cd Length: 1054  Bit Score: 70.83  E-value: 1.04e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911238500   41 FGATPAGQKTCLHLHGIFPYLYVPydgygqQPESYLSQMAFSIDRALNVALGTPSS---TTQHVFKVSLVSGMPFYGYHE 117
Cdd:PTZ00166    80 YGVTKEGHSVLVNVHNFFPYFYIE------APPNFLPEDSQKLKRELNAQLSEQSQfkkYQNTVLDIEIVKKESLMYYKG 153
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1911238500  118 K-ERHFMKIYLYNPAMVKRICELLQSGAIMN-------KFYQPHEAHIPYLLQLFIDYNLYGMNLINLAAVKF 182
Cdd:PTZ00166   154 NgEKDFLKITVQLPKMVPRLRSLIESGVVVCgggwdgiRLFQTYESNVPFVLRFLIDNNITGGSWLTLPKGKY 226
DNA_pol_B_exo1 pfam03104
DNA polymerase family B, exonuclease domain; This domain has 3' to 5' exonuclease activity and ...
2314-2484 2.42e-11

DNA polymerase family B, exonuclease domain; This domain has 3' to 5' exonuclease activity and adopts a ribonuclease H type fold.


Pssm-ID: 397292  Cd Length: 333  Bit Score: 67.83  E-value: 2.42e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911238500 2314 PDPEF--DP---ICALFYCISSDTPLPNTdkteltgVIVIdkdKTVSSQDIrYQTPLLIRSGITRLEVTYAADEKGLFQE 2388
Cdd:pfam03104  172 PDAENvkDPiiqISCMLDGQGEPEPEPRF-------LFTL---RECDSEDI-EDFEYTPKPIYPGVKVFEFPSEKELLRR 240
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911238500 2389 IADIIKRYDPDILLGYEIQMHSWGYLLQRAAALSVDLCQMISRVPDDkieNRFAAERDDYGSDTMSEINIVGRITLNLWR 2468
Cdd:pfam03104  241 FFEFIRQYDPDIITGYNGDNFDWPYILNRAKELYIVKLSSIGRLNRG---GRSKVREIGFGTRSYEKVKISGRLHLDLYR 317
                          170
                   ....*....|....*.
gi 1911238500 2469 IMRNEVALTNYTFENV 2484
Cdd:pfam03104  318 VIKRDYKLPSYKLNAV 333
POLBc_alpha cd05532
DNA polymerase type-B alpha subfamily catalytic domain. Three DNA-dependent DNA polymerases ...
2597-2639 2.51e-10

DNA polymerase type-B alpha subfamily catalytic domain. Three DNA-dependent DNA polymerases type B (alpha, delta, and epsilon) have been identified as essential for nuclear DNA replication in eukaryotes. DNA polymerase (Pol) alpha is almost exclusively required for the initiation of DNA replication and the priming of Okazaki fragments during elongation. In most organisms no specific repair role, other than check point control, has been assigned to this enzyme. Pol alpha contains both polymerase and exonuclease domains, but lacks exonuclease activity suggesting that the exonuclease domain may be for structural purposes only.


Pssm-ID: 99915  Cd Length: 400  Bit Score: 65.29  E-value: 2.51e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1911238500 2597 LIMEPESRFYSNSVLVLDFQSLYPSIVIAYNYCFSTCLGHVEN 2639
Cdd:cd05532     12 LVLEPKKGLYDKFILLLDFNSLYPSIIQEYNICFTTVDRADPD 54
pol2 TIGR00592
DNA polymerase (pol2); All proteins in this superfamily for which functions are known are DNA ...
2379-2632 2.84e-09

DNA polymerase (pol2); All proteins in this superfamily for which functions are known are DNA polymerases.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273159 [Multi-domain]  Cd Length: 1172  Bit Score: 63.15  E-value: 2.84e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911238500 2379 AADEKGLFQEIADIIKRYDPDILLGYEIQMHSWGYLLQRAAALSVDLCQMISRVPDDKIENRFAAERddygsdtmseinI 2458
Cdd:TIGR00592  581 LATERALIKKFMAKVKKIDPDEIVGHDYQQRALKVLANRINDLKIPTWSKIGRLRRSPKFGRRFGER------------T 648
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911238500 2459 VGRITLNLWRIMRNEVALTNYTFENVSFHVLH-QRFPLFTFRVLSDWFDNKTDLYrwkMVDHYISRVRGNLQMLEQLDLI 2537
Cdd:TIGR00592  649 CGRMICDVEISAKELIRCKSYDLSELVQQILKtERKVIPIDNINNMYSESSSLTY---LLEHTWKDAMFILQIMCELNVL 725
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911238500 2538 GKTSEMARLFGIQFLHVLTRGSQYRVESMMLRIAKPMNYI-PVTPNVQQRSQMR--------------APQCVPLIMEPE 2602
Cdd:TIGR00592  726 PLALQITNIAGNIMSRTLMGGRSERNEFLLLHAFYENNYIvPDKQIFRKQQKLGdedeeidgykkgkkAAYAGGLVLEPK 805
                          250       260       270
                   ....*....|....*....|....*....|
gi 1911238500 2603 SRFYSNSVLVLDFQSLYPSIVIAYNYCFST 2632
Cdd:TIGR00592  806 VGLYDKYVLLMDFNSLYPSIIQEFNICFTT 835
REV3L_RBD cd22287
REV7 binding domain found in protein reversionless 3-like (REV3L) and similar proteins; REV3L, ...
1874-1896 6.56e-09

REV7 binding domain found in protein reversionless 3-like (REV3L) and similar proteins; REV3L, also called REV3-like, or REV3, or DNA polymerase zeta catalytic subunit (POLZ), is the catalytic subunit of the DNA polymerase zeta complex, an error-prone polymerase specialized in translesion DNA synthesis (TLS). REV3L lacks an intrinsic 3'-5' exonuclease activity and thus has no proofreading function. The model corresponds to a conserved region that is responsible for the binding of REV7.


Pssm-ID: 412083  Cd Length: 23  Bit Score: 53.33  E-value: 6.56e-09
                           10        20
                   ....*....|....*....|...
gi 1911238500 1874 RTAHILKPLMSPPSREEIMATLL 1896
Cdd:cd22287      1 RTAHILKPLMSPPSREEIMATLL 23
DNA_polB_Kod1_like_exo cd05780
DEDDy 3'-5' exonuclease domain of Pyrococcus kodakaraensis Kod1 and similar archaeal family-B ...
2375-2489 5.43e-08

DEDDy 3'-5' exonuclease domain of Pyrococcus kodakaraensis Kod1 and similar archaeal family-B DNA polymerases; The 3'-5' exonuclease domain of archaeal family-B DNA polymerases with similarity to Pyrococcus kodakaraensis Kod1, including polymerases from Desulfurococcus (D. Tok Pol) and Thermococcus gorgonarius (Tgo Pol). Kod1, D. Tok Pol, and Tgo Pol are thermostable enzymes that exhibit both polymerase and 3'-5' exonuclease activities. They are family-B DNA polymerases. Their amino termini harbor a DEDDy-type DnaQ-like 3'-5' exonuclease domain that contains three sequence motifs termed ExoI, ExoII and ExoIII, with a specific YX(3)D pattern at ExoIII. These motifs are clustered around the active site and are involved in metal binding and catalysis. The exonuclease domain of family B polymerases contains a beta hairpin structure that plays an important role in active site switching in the event of nucleotide misincorporation. Members of this subfamily show similarity to eukaryotic DNA polymerases involved in DNA replication. Some archaea possess multiple family-B DNA polymerases. Phylogenetic analyses of eubacterial, archaeal, and eukaryotic family-B DNA polymerases support independent gene duplications during the evolution of archaeal and eukaryotic family-B DNA polymerases.


Pssm-ID: 99823 [Multi-domain]  Cd Length: 195  Bit Score: 55.44  E-value: 5.43e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911238500 2375 EVTYAADEKGLFQEIADIIKRYDPDILLGYEIQMHSWGYLLQRAAALSVDLcqmisRVPDDKIENRFAAERDDYGSDtms 2454
Cdd:cd05780     49 FVEVVKTEKEMIKRFIEIVKEKDPDVIYTYNGDNFDFPYLKKRAEKLGIEL-----DLGRDGSEIKIQRGGFNNASE--- 120
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1911238500 2455 einIVGRITLNLWRIMRNEVALTNYTFENVSFHVL 2489
Cdd:cd05780    121 ---IKGRIHVDLYPVARRTLNLTRYTLERVYEELF 152
POLBc_delta cd05533
DNA polymerase type-B delta subfamily catalytic domain. Three DNA-dependent DNA polymerases ...
2598-2645 1.89e-07

DNA polymerase type-B delta subfamily catalytic domain. Three DNA-dependent DNA polymerases type B (alpha, delta, and epsilon) have been identified as essential for nuclear DNA replication in eukaryotes. Presently, no direct data is available regarding the strand specificity of DNA polymerase during DNA replication in vivo. However, mutation analysis supports the hypothesis that DNA polymerase delta is the enzyme responsible for both elongation and maturation of Okazaki fragments on the lagging strand.


Pssm-ID: 99916  Cd Length: 393  Bit Score: 56.12  E-value: 1.89e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1911238500 2598 IMEPESRFYSNSVLVLDFQSLYPSIVIAYNYCFSTCL--GHVENLGKSSY 2645
Cdd:cd05533      8 VIEPIKGYYDVPIATLDFASLYPSIMMAHNLCYTTLLnkNTAKKLPPEDY 57
DNA_pol_B_exo1 pfam03104
DNA polymerase family B, exonuclease domain; This domain has 3' to 5' exonuclease activity and ...
51-189 3.72e-07

DNA polymerase family B, exonuclease domain; This domain has 3' to 5' exonuclease activity and adopts a ribonuclease H type fold.


Pssm-ID: 397292  Cd Length: 333  Bit Score: 54.73  E-value: 3.72e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911238500   51 CLHLHGIFPYLYVPYDGYGQQPE--SYLSQMAFSIDRALNVALGTPSSttqhvfkvslvsgmpFYGYHEKERHFMKIYLY 128
Cdd:pfam03104    9 CVNVFGFKPYFYCLAPDGKELEEviEEIKELYEGLDKIEKIELKLKKS---------------LYGYEEDPVPYLKVSFA 73
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1911238500  129 NPAMVKRICELLQSGAIMNKFyqphEAHIPYLLQLFIDYNLYGMNLINLAAVKFRKARRKS 189
Cdd:pfam03104   74 NPRPLLKIRKYLSPENISDVY----EYDVDYLERFLIDNDIVGFGWYKVKVYPFRAEGRIS 130
DNA_polB_B3_exo cd05781
DEDDy 3'-5' exonuclease domain of Sulfurisphaera ohwakuensis DNA polymerase B3 and similar ...
2381-2485 7.73e-07

DEDDy 3'-5' exonuclease domain of Sulfurisphaera ohwakuensis DNA polymerase B3 and similar archaeal family-B DNA polymerases; The 3'-5' exonuclease domain of archaeal proteins with similarity to Sulfurisphaera ohwakuensis DNA polymerase B3. B3 is a family-B DNA polymerase. Family-B DNA polymerases contain an N-terminal DEDDy DnaQ-like exonuclease domain in the same polypeptide chain as the polymerase domain, similar to family-A DNA polymerases. B3 exhibits both polymerase and 3'-5' exonuclease activities. This exonuclease domain contains three sequence motifs termed ExoI, ExoII and ExoIII, with a specific YX(3)D pattern at ExoIII. These motifs are clustered around the active site and are involved in metal binding and catalysis. The exonuclease domain of family B polymerases also contains a beta hairpin structure that plays an important role in active site switching in the event of nucleotide misincorporation. Archaeal proteins that are involved in DNA replication are similar to those from eukaryotes. Some archaea possess multiple family-B DNA polymerases. B3 is mainly found in crenarchaea. Phylogenetic analyses of eubacterial, archaeal, and eukaryotic family B-DNA polymerases support independent gene duplications during the evolution of archaeal and eukaryotic family-B DNA polymerases.


Pssm-ID: 99824 [Multi-domain]  Cd Length: 188  Bit Score: 51.94  E-value: 7.73e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911238500 2381 DEKGLFQEIADIIKRYDPDILLGYEIQMHSWGYLLQRAAALSV--DLCQMISRVPddkienrfaaERDDYGsdtmsEINI 2458
Cdd:cd05781     47 DDRKIIREFVKYVKEYDPDIIVGYNSNAFDWPYLVERARVLGVklDVGRRGGSEP----------STGVYG-----HYSI 111
                           90       100
                   ....*....|....*....|....*..
gi 1911238500 2459 VGRITLNLWRIMRNEVALTNYTFENVS 2485
Cdd:cd05781    112 TGRLNVDLYDFAEEIPEVKVKTLENVA 138
POLBc_B3 cd05536
DNA polymerase type-B B3 subfamily catalytic domain. Archaeal proteins that are involved in ...
2597-2627 5.57e-04

DNA polymerase type-B B3 subfamily catalytic domain. Archaeal proteins that are involved in DNA replication are similar to those from eukaryotes. Some members of the archaea also possess multiple family B DNA polymerases (B1, B2 and B3). So far there is no specific function(s) has been assigned for different members of the archaea type B DNA polymerases. Phylogenetic analyses of eubacterial, archaeal, and eukaryotic family B DNA polymerases are support independent gene duplications during the evolution of archaeal and eukaryotic family B DNA polymerases. Structural comparison of the thermostable DNA polymerase type B to its mesostable homolog suggests several adaptations to high temperature such as shorter loops, disulfide bridges, and increasing electrostatic interaction at subdomain interfaces.


Pssm-ID: 99919  Cd Length: 371  Bit Score: 45.01  E-value: 5.57e-04
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1911238500 2597 LIMEPESRFYSNsVLVLDFQSLYPSIVIAYN 2627
Cdd:cd05536      8 IVLEPEKGLHEN-IVVLDFSSLYPSIMIKYN 37
DNA_polB_alpha_exo cd05776
inactive DEDDy 3'-5' exonuclease domain of eukaryotic DNA polymerase alpha, a family-B DNA ...
2322-2489 2.73e-03

inactive DEDDy 3'-5' exonuclease domain of eukaryotic DNA polymerase alpha, a family-B DNA polymerase; The 3'-5' exonuclease domain of eukaryotic DNA polymerase alpha. DNA polymerase alpha is a family-B DNA polymerase with a catalytic subunit that contains a DnaQ-like 3'-5' exonuclease domain. It is one of the three DNA-dependent type B DNA polymerases (delta and epsilon are the other two) that have been identified as essential for nuclear DNA replication in eukaryotes. DNA polymerase alpha is almost exclusively required for the initiation of DNA replication and the priming of Okazaki fragments during elongation. It associates with DNA primase and is the only enzyme able to start DNA synthesis de novo. The catalytic subunit contains both polymerase and 3'-5' exonuclease domains, but only exhibits polymerase activity. The 3'-5' exonuclease domain contains three sequence motifs termed ExoI, ExoII and ExoIII, without the four conserved acidic residues that are crucial for metal binding and catalysis. This explains why in most organisms, that no specific repair role, other than check point control, has been assigned to this enzyme. The exonuclease domain may have a structural role.


Pssm-ID: 99819 [Multi-domain]  Cd Length: 234  Bit Score: 41.83  E-value: 2.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911238500 2322 CALFYCISSDTPLPNTDKTELTGVIVIDKDKTVSSQDIRYQtpllirSGITRLEVTYAADEKGLFQEIADIIKRYDPDIL 2401
Cdd:cd05776     28 MLVHRNVSLDKPTPPPPFQSHTCTLTRPLGRSPPPDLFEKN------AKKKKTKVRIFENERALLNFFLAKLQKIDPDVL 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911238500 2402 LGYEIQMHSWGYLLQRAAALSVDLCQMISR----VPDDKIENRFAAERDdygsdtmseiNIVGRITLNLWRIMRNEVALT 2477
Cdd:cd05776    102 VGHDLEGFDLDVLLSRIQELKVPHWSRIGRlkrsVWPKKKGGGKFGERE----------LTAGRLLCDTYLSAKELIRCK 171
                          170
                   ....*....|..
gi 1911238500 2478 NYTFENVSFHVL 2489
Cdd:cd05776    172 SYDLTELSQQVL 183
DNA_polB_like2_exo cd05785
Uncharacterized bacterial subgroup of the DEDDy 3'-5' exonuclease domain of family-B DNA ...
2380-2487 3.01e-03

Uncharacterized bacterial subgroup of the DEDDy 3'-5' exonuclease domain of family-B DNA polymerases; A subfamily of the 3'-5' exonuclease domain of family-B DNA polymerases. This subfamily is composed of uncharacterized bacterial family-B DNA polymerases. Family-B DNA polymerases contain an N-terminal DEDDy DnaQ-like exonuclease domain in the same polypeptide chain as the polymerase domain, similar to family-A DNA polymerases. This exonuclease domain contains three sequence motifs termed ExoI, ExoII and ExoIII, with a specific YX(3)D pattern at ExoIII. These motifs are involved in metal binding and catalysis. The exonuclease domain of family-B DNA polymerases has a fundamental role in proofreading activity. It contains a beta hairpin structure that plays an important role in active site switching in the event of a nucleotide misincorporation. Family-B DNA polymerases are predominantly involved in DNA replication and DNA repair.


Pssm-ID: 99828 [Multi-domain]  Cd Length: 207  Bit Score: 41.63  E-value: 3.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911238500 2380 ADEKGLFQEIADIIKRYDPDILLGYEIQMHSWGYLLQRAAALSVDLC----QMISRVPDDKIenRFAAERDDYgsdtmSE 2455
Cdd:cd05785     56 AAEKELLEELVAIIRERDPDVIEGHNIFRFDLPYLRRRCRRHGVPLAigrdGSIPRQRPSRF--RFAERLIDY-----PR 128
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1911238500 2456 INIVGRITLNLW-RIMRNEVA---LTNYTFENVSFH 2487
Cdd:cd05785    129 YDIPGRHVIDTYfLVQLFDVSsrdLPSYGLKAVAKH 164
POLBc_Pol_II cd05537
DNA polymerase type-II subfamily catalytic domain. Bacteria contain five DNA polymerases (I, ...
2597-2623 8.47e-03

DNA polymerase type-II subfamily catalytic domain. Bacteria contain five DNA polymerases (I, II, III, IV and V). DNA polymerase II (Pol II) is a prototype for the B-family of polymerases. The role of Pol II in a variety of cellular activities, such as repair of DNA damaged by UV irradiation or oxidation has been proven by genetic studies. DNA polymerase III is the main enzyme responsible for replication of the bacterial chromosome; however, In vivo studies have also shown that Pol II is able to participate in chromosomal DNA replication with larger role in lagging-strand replication.


Pssm-ID: 99920  Cd Length: 371  Bit Score: 41.10  E-value: 8.47e-03
                           10        20
                   ....*....|....*....|....*..
gi 1911238500 2597 LIMEPESRFYSNsVLVLDFQSLYPSIV 2623
Cdd:cd05537      7 YVMDSKPGLYKN-VLVLDFKSLYPSII 32
POLBc_B1 cd05530
DNA polymerase type-B B1 subfamily catalytic domain. Archaeal proteins that are involved in ...
2597-2632 9.28e-03

DNA polymerase type-B B1 subfamily catalytic domain. Archaeal proteins that are involved in DNA replication are similar to those from eukaryotes. Some archaeal members also possess multiple family B DNA polymerases (B1, B2 and B3). So far there is no specific function(s) has been assigned for different members of the archaea type B DNA polymerases. Phylogenetic analyses of eubacterial, archaeal, and eukaryotic family B DNA polymerases are support independent gene duplications during the evolution of archaeal and eukaryotic family B DNA polymerases.


Pssm-ID: 99913  Cd Length: 372  Bit Score: 41.18  E-value: 9.28e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1911238500 2597 LIMEPESRFYSNsVLVLDFQSLYPSIVIAYNYCFST 2632
Cdd:cd05530     17 IVLEPPPGIFFN-VVVLDFASLYPSIIKVWNLSYET 51
 
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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