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   27-MAR-2024, entry version 129.
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   PaxDb; 187420-MTH_1208; -.
DR   EnsemblBacteria; AAB85697; AAB85697; MTH_1208.
DR   GeneID; 77401736; -.
DR   KEGG; mth:MTH_1208; -.
DR   PATRIC; fig|187420.15.peg.1186; -.
DR   HOGENOM; CLU_000203_6_0_2; -.
DR   InParanoid; O27276; -.
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   CDD; cd05780; DNA_polB_Kod1_like_exo; 1.
DR   Gene3D; 3.30.342.10; DNA Polymerase, chain B, domain 1; 1.
DR   Gene3D; 1.10.287.690; Helix hairpin bin; 1.
DR   Gene3D; 3.90.1600.10; Palm domain of DNA polymerase; 1.
DR   Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 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   PANTHER; PTHR10322; DNA POLYMERASE CATALYTIC SUBUNIT; 1.
DR   PANTHER; PTHR10322:SF23; DNA POLYMERASE DELTA CATALYTIC SUBUNIT; 1.
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; SSF56672; DNA/RNA polymerases; 1.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 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
//