DPOL1_METTH
ID DPOL1_METTH Reviewed; 586 AA.
AC O27276;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 124.
DE RecName: Full=DNA polymerase PolB subunit 1;
DE EC=2.7.7.7;
GN Name=polB1; OrderedLocusNames=MTH_1208;
OS Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=187420;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA Reeve J.N.;
RT "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT functional analysis and comparative genomics.";
RL J. Bacteriol. 179:7135-7155(1997).
RN [2]
RP FUNCTION AS A DNA POLYMERASE, FUNCTION AS AN EXONUCLEASE, CATALYTIC
RP ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, INTERACTION
RP WITH POLB2 AND RPA, AND SUBUNIT.
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=10497247; DOI=10.1074/jbc.274.40.28751;
RA Kelman Z., Pietrokovski S., Hurwitz J.;
RT "Isolation and characterization of a split B-type DNA polymerase from the
RT archaeon Methanobacterium thermoautotrophicum deltaH.";
RL J. Biol. Chem. 274:28751-28761(1999).
CC -!- FUNCTION: In addition to polymerase activity, this DNA polymerase
CC exhibits 3'-5' exonuclease activity. {ECO:0000269|PubMed:10497247}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC ChEBI:CHEBI:173112; EC=2.7.7.7;
CC Evidence={ECO:0000269|PubMed:10497247};
CC -!- ACTIVITY REGULATION: DNA polymerase is inhibited by replication protein
CC A (RPA), while 3'-5' exonuclease activity is not. Polymerase inhibition
CC can be overcome by replication factor C (RFC) and PCNA.
CC {ECO:0000269|PubMed:10497247}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Optimum temperature for DNA polymerase is 60 degrees Celsius,
CC functional between 60 and 80 degrees Celsius. Exonuclease activity is
CC higher at 70 than 50 degrees Celsius. {ECO:0000269|PubMed:10497247};
CC -!- SUBUNIT: Formed of a complex between PolB1 and PolB2; the exonuclease
CC activity is associated with subunit 1. Probably binds replication
CC protein A (RPA). {ECO:0000269|PubMed:10497247}.
CC -!- MISCELLANEOUS: In some Methanobacteriaceae the PolB protein is split
CC over 2 genes.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-B family. {ECO:0000305}.
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DR EMBL; AE000666; AAB85697.1; -; Genomic_DNA.
DR PIR; C69028; C69028.
DR RefSeq; WP_010876832.1; NC_000916.1.
DR AlphaFoldDB; O27276; -.
DR SMR; O27276; -.
DR STRING; 187420.MTH_1208; -.
DR EnsemblBacteria; AAB85697; AAB85697; MTH_1208.
DR GeneID; 1471616; -.
DR KEGG; mth:MTH_1208; -.
DR PATRIC; fig|187420.15.peg.1186; -.
DR HOGENOM; CLU_000203_6_0_2; -.
DR OMA; FVLTRHW; -.
DR Proteomes; UP000005223; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR Gene3D; 3.30.420.10; -; 1.
DR Gene3D; 3.90.1600.10; -; 1.
DR InterPro; IPR006172; DNA-dir_DNA_pol_B.
DR InterPro; IPR017964; DNA-dir_DNA_pol_B_CS.
DR InterPro; IPR006133; DNA-dir_DNA_pol_B_exonuc.
DR InterPro; IPR006134; DNA-dir_DNA_pol_B_multi_dom.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR023211; DNA_pol_palm_dom_sf.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR Pfam; PF00136; DNA_pol_B; 1.
DR Pfam; PF03104; DNA_pol_B_exo1; 1.
DR PRINTS; PR00106; DNAPOLB.
DR SMART; SM00486; POLBc; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS00116; DNA_POLYMERASE_B; 1.
PE 1: Evidence at protein level;
KW DNA replication; DNA-binding; DNA-directed DNA polymerase; Exonuclease;
KW Hydrolase; Nuclease; Nucleotidyltransferase; Reference proteome;
KW Transferase.
FT CHAIN 1..586
FT /note="DNA polymerase PolB subunit 1"
FT /id="PRO_0000046477"
SQ SEQUENCE 586 AA; 67966 MW; D406B5BC399B951A CRC64;
MEDYRMVLLD IDYVTVDEVP VIRLFGKDKS GGNEPIIAHD RSFRPYIYAI PTDLDECLRE
LEELELEKLE VKEMRDLGRP TEVIRIEFRH PQDVPKIRDR IRDLESVRDI REHDIPFYRR
YLIDKSIVPM EELEFQGVEV DSAPSVTTDV RTVEVTGRVQ STGSGAHGLD ILSFDIEVRN
PHGMPDPEKD EIVMIGVAGN MGYESVISTA GDHLDFVEVV EDERELLERF AEIVIDKKPD
ILVGYNSDNF DFPYITRRAA ILGAELDLGW DGSKIRTMRR GFANATAIKG TVHVDLYPVM
RRYMNLDRYT LERVYQELFG EEKIDLPGDR LWEYWDRDEL RDELFRYSLD DVVATHRIAE
KILPLNLELT RLVGQPLFDI SRMATGQQAE WFLVRKAYQY GELVPNKPSQ SDFSSRRGRR
AVGGYVKEPE KGLHENIVQF DFRSLYPSII ISKNISPDTL TDDEESECYV APEYGYRFRK
SPRGFVPSVI GEILSERVRI KEEMKGSDDP MERKILNVQQ EALKRLANTM YGVYGYSRFR
WYSMECAEAI TAWGRDYIKK TIKTAEEFGF HTVYADTDGF YATYRG
