DPOL1_SULAC
ID DPOL1_SULAC Reviewed; 876 AA.
AC P95690; Q4J8M7;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 2.
DT 25-MAY-2022, entry version 122.
DE RecName: Full=DNA polymerase 1;
DE EC=2.7.7.7;
DE AltName: Full=DNA polymerase I;
GN Name=dpo1; Synonyms=polS; OrderedLocusNames=Saci_1537;
OS Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS 15157 / NCIMB 11770).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=330779;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=8921881; DOI=10.1016/0378-1119(96)00298-3;
RA Datukishvili N., Pokholok D., Lottspeich F., Prangishvili D., Rechinsky V.;
RT "The DNA polymerase-encoding gene from a thermoacidophilic archaeon
RT Sulfolobus acidocaldarius.";
RL Gene 177:271-273(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT "The genome of Sulfolobus acidocaldarius, a model organism of the
RT Crenarchaeota.";
RL J. Bacteriol. 187:4992-4999(2005).
RN [3]
RP CHARACTERIZATION.
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=3927262; DOI=10.1093/nar/13.14.5269;
RA Klimczak L.J., Grummt F., Burger K.J.;
RT "Purification and characterization of DNA polymerase from the
RT archaebacterium Sulfolobus acidocaldarius.";
RL Nucleic Acids Res. 13:5269-5282(1985).
CC -!- FUNCTION: This polymerase possesses two enzymatic activities: DNA
CC synthesis (polymerase) and an exonucleolytic activity that degrades
CC single-stranded DNA in the 3'- to 5'-direction.
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 -!- SIMILARITY: Belongs to the DNA polymerase type-B family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U33846; AAC44598.1; -; Genomic_DNA.
DR EMBL; CP000077; AAY80851.1; -; Genomic_DNA.
DR PIR; JC5186; JC5186.
DR RefSeq; WP_011278353.1; NC_007181.1.
DR AlphaFoldDB; P95690; -.
DR SMR; P95690; -.
DR STRING; 330779.Saci_1537; -.
DR PRIDE; P95690; -.
DR EnsemblBacteria; AAY80851; AAY80851; Saci_1537.
DR GeneID; 3474573; -.
DR KEGG; sai:Saci_1537; -.
DR PATRIC; fig|330779.12.peg.1478; -.
DR eggNOG; arCOG15272; Archaea.
DR HOGENOM; CLU_000203_6_0_2; -.
DR OMA; WIRNMLY; -.
DR BRENDA; 2.7.7.7; 6160.
DR Proteomes; UP000001018; 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..876
FT /note="DNA polymerase 1"
FT /id="PRO_0000046482"
FT CONFLICT 198..203
FT /note="AFADAD -> LSDAY (in Ref. 1; AAC44598)"
FT /evidence="ECO:0000305"
FT CONFLICT 364
FT /note="R -> S (in Ref. 1; AAC44598)"
FT /evidence="ECO:0000305"
FT CONFLICT 378
FT /note="D -> Y (in Ref. 1; AAC44598)"
FT /evidence="ECO:0000305"
FT CONFLICT 399
FT /note="L -> M (in Ref. 1; AAC44598)"
FT /evidence="ECO:0000305"
FT CONFLICT 532
FT /note="D -> E (in Ref. 1; AAC44598)"
FT /evidence="ECO:0000305"
FT CONFLICT 564..565
FT /note="IT -> YQ (in Ref. 1; AAC44598)"
FT /evidence="ECO:0000305"
FT CONFLICT 686..687
FT /note="KS -> NT (in Ref. 1; AAC44598)"
FT /evidence="ECO:0000305"
FT CONFLICT 693
FT /note="F -> Y (in Ref. 1; AAC44598)"
FT /evidence="ECO:0000305"
FT CONFLICT 761
FT /note="N -> Y (in Ref. 1; AAC44598)"
FT /evidence="ECO:0000305"
FT CONFLICT 826..827
FT /note="PI -> AY (in Ref. 1; AAC44598)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 876 AA; 100778 MW; 323A950A14A01FEF CRC64;
MSKQATLFDF SIKKNESKEQ TNQESVEVPK QTANRTKIEW IKEAEDGKVY FLLQVDYDGK
KSRAVCKLYD KEGKKIYIMQ DESGHKPYFL TDIDPDKVNK ITKVVRDPSF DHLELINKVD
PYTGKKIRLT KIVVKDPLAV RRMRSSLPKA YEAHIKYYNN YVYDNGLIPG LIYKVNKGKL
TQLNPELKGE EINEIKKAFA DADEMTKETV NDWIPILETE VPDIKRVSLD IEVYTPNRGR
IPDPERAEFP IISVALAGND GSKIVLALKR EDVNSDFSKK DGVQVEIFDS EKKLLARLFE
IIREYPMLLT FNGDDFDIPY IYFRALRLNF SPEEVPLDVV SGEGKFLAGI HIDLYKFFFN
RAVRIYAFEG KYSEYSLDAV ATALLGISKV KLDTFISFLD IDKLIEYNLR DAEITLKLTT
FNNNLVLKLM VLLARISKLG LEELTRTEVS TWIKNLYYWE HRKRNWLIPL KEEILVRSNQ
VKTAAVIKGK KYKGAVVIDP PAGVYFNVVV LDFASLYPSI IKNWNISYET IDIDECTKKV
WVEDETGEKL HYVCMDKPGI TAVITGLIRD FRVKVYKKKA KYSNISEEQR SLYDVVQRAM
KVFINATYGV FGAENFPLYA PAVAESVTAI GRYIITTTYK QAEKLNLKVI YGDTDSLFLY
NPTKDKLEEL IKFVKQNFNL DLEVDKSYKY VAFSGLKKNY FGVYPDGKTE IKGMLAKKRN
TPEFIKKEFA EIKNMLASLN SPNDIPEVKN KLEIKIKDIY NKLRNKGYNL DDLAFRIMLS
KPLDSYTKNT PQHVKAGLQL RAFGVNVLPR DVIMFVKVKS KDGVKPIQLA KISEIDIEKY
VETLRTTFEQ ILKAFGISWD EIVSTISIDS FFGSKK
