ID A1RT55_PYRIL Unreviewed; 785 AA.
AC A1RT55;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 99.
DE RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN OrderedLocusNames=Pisl_0961 {ECO:0000313|EMBL:ABL88137.1};
OS Pyrobaculum islandicum (strain DSM 4184 / JCM 9189 / GEO3).
OC Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=384616 {ECO:0000313|EMBL:ABL88137.1, ECO:0000313|Proteomes:UP000002595};
RN [1] {ECO:0000313|Proteomes:UP000002595}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 4184 / JCM 9189 / GEO3 {ECO:0000313|Proteomes:UP000002595};
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Meincke L., Brettin T.,
RA Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Lowe T., Richardson P.;
RT "Complete sequence of Pyrobaculum islandicum DSM 4184.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP000504; ABL88137.1; -; Genomic_DNA.
DR RefSeq; WP_011762712.1; NC_008701.1.
DR AlphaFoldDB; A1RT55; -.
DR STRING; 384616.Pisl_0961; -.
DR GeneID; 4616358; -.
DR KEGG; pis:Pisl_0961; -.
DR eggNOG; arCOG00328; Archaea.
DR HOGENOM; CLU_000203_6_0_2; -.
DR OrthoDB; 323192at2157; -.
DR Proteomes; UP000002595; 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 CDD; cd05781; DNA_polB_B3_exo; 1.
DR CDD; cd05536; POLBc_B3; 1.
DR Gene3D; 1.10.132.60; DNA polymerase family B, C-terminal domain; 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; IPR042087; DNA_pol_B_thumb.
DR InterPro; IPR023211; DNA_pol_palm_dom_sf.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR NCBIfam; TIGR00592; pol2; 1.
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 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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000442}.
FT DOMAIN 72..291
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 367..763
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
SQ SEQUENCE 785 AA; 89749 MW; 10FB8B66A8F3730D CRC64;
MELKVWPLDI TYAVVGSVPE IRIFGILSSG ERVVLIDRSF KPYFYVDCAV CEPAALKTAL
SRVAPIDDVQ IVERRFLGRS KKFLKVIAKI PEDVRKLREA AMSIPRVSGV YEADIRFYMR
YMIDMGVVPC SWNVAEVEEG GRLGGIPTYV VSQWYGIDEG FPPSLKVMAF DIEVYNERGS
PDPIRDPVVM LAIKTNDGHE EVFEASGKDD RGVVRAFVDF IRSYDPDVIV GYNSNGFDWP
YLVERAKAVG VPLKVDRLSN PPQQSVYGHW SIVGRANVDL YNIVEEFPEI KLKTLDRVAE
YFGVMKREER VLIPGHKIYE YWKDPNKRPL LKRYVLDDVR STLGLADKLL PFLIQLSSVS
GLPLDQVAAA SVGNRVEWML LRYAYRLGEV APNREEREYE PYKGAIVLEP KPGMYEDVLV
LDFSSMYPNI MMKYNLSPDT YLEPGEPDPP EGVNVAPEVG HRFRRSPPGF VPQVLKSLVE
LRKAVREEAK KYPPDSPEFK ILDERQRALK VMANAIYGYL GWVGARWYKR EVAESVTAFA
RAILKDVIEQ ARRLGIVVVY GDTDSLFVKK HGDVDKLIKY VEEKYGIDIK VDKDYAKVLF
TEAKKRYAGL LRDGRIDIVG FEVVRGDWSE LAKDVQLRVI EIILKSRDIV EARHGVIKYI
REIIERLKNY KFNIDDLIIW KTLDKELDEY KAYPPHVHAA QILKRHGYRV GKGTTIGYVI
VKGGEKVSER ALPYILLDDI KKIDIDYYIE RQIIPAALRI AEVIGVKESD LKTGRMERSL
LDFLS
//
