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O27276 (DPOL1_METTH) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Protein attributes

Sequence length586 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

In addition to polymerase activity, this DNA polymerase exhibits 3'-5' exonuclease activity. Ref.2

Catalytic activity

Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1). Ref.2

Enzyme regulation

DNA polymerase is inhibited by replication protein A (RPA), while 3'-5' exonuclease activity is not. Polymerase inhibition can be overcome by replication factor C (RFC) and PCNA. Ref.2

Subunit structure

Formed of a complex between PolB1 and PolB2; the exonuclease activity is associated with subunit 1. Probably binds replication protein A (RPA). Ref.2

Miscellaneous

In some Methanobacteriaceae the PolB protein is split over 2 genes.

Sequence similarities

Belongs to the DNA polymerase type-B family.

Biophysicochemical properties

Temperature dependence:

Optimum temperature for DNA polymerase is 60 degrees Celsius, functional between 60 and 80 degrees Celsius. Exonuclease activity is higher at 70 than 50 degrees Celsius. Ref.2

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 586586DNA polymerase PolB subunit 1
PRO_0000046477

Sequences

Sequence LengthMass (Da)Tools
O27276 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: D406B5BC399B951A

FASTA58667,966
        10         20         30         40         50         60 
MEDYRMVLLD IDYVTVDEVP VIRLFGKDKS GGNEPIIAHD RSFRPYIYAI PTDLDECLRE 

        70         80         90        100        110        120 
LEELELEKLE VKEMRDLGRP TEVIRIEFRH PQDVPKIRDR IRDLESVRDI REHDIPFYRR 

       130        140        150        160        170        180 
YLIDKSIVPM EELEFQGVEV DSAPSVTTDV RTVEVTGRVQ STGSGAHGLD ILSFDIEVRN 

       190        200        210        220        230        240 
PHGMPDPEKD EIVMIGVAGN MGYESVISTA GDHLDFVEVV EDERELLERF AEIVIDKKPD 

       250        260        270        280        290        300 
ILVGYNSDNF DFPYITRRAA ILGAELDLGW DGSKIRTMRR GFANATAIKG TVHVDLYPVM 

       310        320        330        340        350        360 
RRYMNLDRYT LERVYQELFG EEKIDLPGDR LWEYWDRDEL RDELFRYSLD DVVATHRIAE 

       370        380        390        400        410        420 
KILPLNLELT RLVGQPLFDI SRMATGQQAE WFLVRKAYQY GELVPNKPSQ SDFSSRRGRR 

       430        440        450        460        470        480 
AVGGYVKEPE KGLHENIVQF DFRSLYPSII ISKNISPDTL TDDEESECYV APEYGYRFRK 

       490        500        510        520        530        540 
SPRGFVPSVI GEILSERVRI KEEMKGSDDP MERKILNVQQ EALKRLANTM YGVYGYSRFR 

       550        560        570        580 
WYSMECAEAI TAWGRDYIKK TIKTAEEFGF HTVYADTDGF YATYRG 

« Hide

References

« Hide 'large scale' references
[1]"Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics."
Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J., Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D., Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R. expand/collapse author list , Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D., Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A., Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J., Reeve J.N.
J. Bacteriol. 179:7135-7155(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H.
[2]"Isolation and characterization of a split B-type DNA polymerase from the archaeon Methanobacterium thermoautotrophicum deltaH."
Kelman Z., Pietrokovski S., Hurwitz J.
J. Biol. Chem. 274:28751-28761(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS A DNA POLYMERASE, FUNCTION AS AN EXONUCLEASE, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, INTERACTION WITH POLB2 AND RPA, SUBUNIT.
Strain: ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000666 Genomic DNA. Translation: AAB85697.1.
PIRC69028.
RefSeqNP_276336.1. NC_000916.1.

3D structure databases

ProteinModelPortalO27276.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING187420.MTH1208.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAB85697; AAB85697; MTH_1208.
GeneID1471616.
KEGGmth:MTH1208.

Phylogenomic databases

eggNOGCOG0417.
KOK02319.
OMAHFEADIP.

Enzyme and pathway databases

BioCycMTHE187420:GJNM-1210-MONOMER.

Family and domain databases

Gene3D3.30.420.10. 1 hit.
3.90.1600.10. 2 hits.
InterProIPR006172. DNA-dir_DNA_pol_B.
IPR017964. DNA-dir_DNA_pol_B_CS.
IPR006133. DNA-dir_DNA_pol_B_exonuc.
IPR006134. DNA-dir_DNA_pol_B_multi_dom.
IPR023211. DNA_pol_palm_dom.
IPR012337. RNaseH-like_dom.
[Graphical view]
PfamPF00136. DNA_pol_B. 1 hit.
PF03104. DNA_pol_B_exo1. 1 hit.
[Graphical view]
PRINTSPR00106. DNAPOLB.
SMARTSM00486. POLBc. 1 hit.
[Graphical view]
SUPFAMSSF53098. SSF53098. 2 hits.
PROSITEPS00116. DNA_POLYMERASE_B. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDPOL1_METTH
AccessionPrimary (citable) accession number: O27276
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: January 1, 1998
Last modified: July 9, 2014
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families