ID   S5Z575_9CREN            Unreviewed;       653 AA.
AC   S5Z575;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 48.
DE   RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN   ORFNames=N186_00060 {ECO:0000313|EMBL:AGT34410.1};
OS   Thermofilum adornatum.
OC   Archaea; Thermoproteota; Thermoprotei; Thermofilales; Thermofilaceae;
OC   Thermofilum.
OX   NCBI_TaxID=1365176 {ECO:0000313|EMBL:AGT34410.1, ECO:0000313|Proteomes:UP000015543};
RN   [1] {ECO:0000313|EMBL:AGT34410.1, ECO:0000313|Proteomes:UP000015543}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1910b {ECO:0000313|Proteomes:UP000015543};
RX   PubMed=24029764;
RA   Dominova I.N., Kublanov I.V., Podosokorskaya O.A., Derbikova K.S.,
RA   Patrushev M.V., Toshchakov S.V.;
RT   "Complete Genomic Sequence of 'Thermofilum adornatus' Strain 1910bT, a
RT   Hyperthermophilic Anaerobic Organotrophic Crenarchaeon.";
RL   Genome Announc. 1:e00726-13(2013).
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:0000256|ARBA:ARBA00024632,
CC         ECO:0000256|RuleBase:RU000442};
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-B family.
CC       {ECO:0000256|ARBA:ARBA00005755, ECO:0000256|RuleBase:RU000442}.
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; CP006646; AGT34410.1; -; Genomic_DNA.
DR   AlphaFoldDB; S5Z575; -.
DR   KEGG; thb:N186_00060; -.
DR   PATRIC; fig|1365176.7.peg.12; -.
DR   eggNOG; arCOG00329; Archaea.
DR   HOGENOM; CLU_000203_6_2_2; -.
DR   Proteomes; UP000015543; 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:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.132.60; DNA polymerase family B, C-terminal domain; 1.
DR   Gene3D; 1.10.287.690; Helix hairpin bin; 1.
DR   Gene3D; 3.90.1600.10; Palm domain of DNA polymerase; 1.
DR   InterPro; IPR006172; DNA-dir_DNA_pol_B.
DR   InterPro; IPR017964; DNA-dir_DNA_pol_B_CS.
DR   InterPro; IPR006134; DNA-dir_DNA_pol_B_multi_dom.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR042087; DNA_pol_B_thumb.
DR   InterPro; IPR023211; DNA_pol_palm_dom_sf.
DR   InterPro; IPR012337; RNaseH-like_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; 2.
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   3: Inferred from homology;
KW   DNA replication {ECO:0000256|RuleBase:RU000442};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU000442};
KW   DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW   ECO:0000256|RuleBase:RU000442};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000256|RuleBase:RU000442};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015543};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000442}.
FT   DOMAIN          294..336
FT                   /note="DNA-directed DNA polymerase family B
FT                   multifunctional"
FT                   /evidence="ECO:0000259|Pfam:PF00136"
FT   DOMAIN          342..585
FT                   /note="DNA-directed DNA polymerase family B
FT                   multifunctional"
FT                   /evidence="ECO:0000259|Pfam:PF00136"
SQ   SEQUENCE   653 AA;  72912 MW;  CCFC5B8CA8AE931F CRC64;
     MVDASVSRGE ARLWLRGLDG GVEALRRGFE DYFLVESSAL GFLASLWDQG FSVEEVERRL
     VGGKTGAFLR VSHGSRRLLQ KALKVVEGAG FTSYDSDVNV VQKLFAEVGI VALRSYRRSG
     WLFVEGEDRV EPLPLVTVSL DLHVRGGFLS KAVIRSNGGE KVFEGSESRI LEGLDAVLKE
     LDPDVVAVNM PVKELRKLAI GVRRRHGWFR LGRGDGVLEG RIFVERGLLD GIGLAGLEER
     CRATGLSPTL AGMTSYGRLI DARQVYLLLR RGYAVPRARH RNVHVRTMLE LHRGDRGGLI
     YQPVTGIYGN VAELDFESMF PNLIVRYNIS YETVSLGGVA REPRGILVDV VEPLLERRLR
     FKHMARELSG DAKRFADQRQ KELKMILVSS YGYSGNNYNR LGNPLTFEWI NRLARRVMLG
     VYGLLREKGY TVIYGDTDSV FVYRDGASRS DYEELAGEIA EKYGMPIKVD KLFRFIAFPE
     AKTTRASPVK RYFGVTAEGE YVFKGVEAAR SDYPPFVRSF QARLVETVFS TLEKSGVDGA
     LSAAEELLKR EVERLRSGLV PVEELLIEKT LRREKYKVKA MHVVAAQQAG VSGKGSKVCF
     VLAKHPKSSP HLRVRVPGTG TILPDYDAYE KLLVRAYETV ISSLVNVNIP ASH
//