ID A0A078A256_STYLE Unreviewed; 1122 AA.
AC A0A078A256;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN Name=Contig13618.g14525 {ECO:0000313|EMBL:CDW75907.1};
GN ORFNames=STYLEM_4903 {ECO:0000313|EMBL:CDW75907.1};
OS Stylonychia lemnae (Ciliate).
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC Stichotrichia; Sporadotrichida; Oxytrichidae; Stylonychinae; Stylonychia.
OX NCBI_TaxID=5949 {ECO:0000313|EMBL:CDW75907.1, ECO:0000313|Proteomes:UP000039865};
RN [1] {ECO:0000313|EMBL:CDW75907.1, ECO:0000313|Proteomes:UP000039865}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=130c {ECO:0000313|EMBL:CDW75907.1,
RC ECO:0000313|Proteomes:UP000039865};
RA Swart Estienne;
RL Submitted (JUN-2014) 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}.
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; CCKQ01004746; CDW75907.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A078A256; -.
DR EnsemblProtists; CDW75907; CDW75907; STYLEM_4903.
DR InParanoid; A0A078A256; -.
DR OMA; FITGVEM; -.
DR OrthoDB; 211439at2759; -.
DR Proteomes; UP000039865; Unassembled WGS sequence.
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; 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; 2.
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 Reference proteome {ECO:0000313|Proteomes:UP000039865};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000442}.
FT DOMAIN 299..564
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 619..1049
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
FT REGION 1..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..55
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..78
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1122 AA; 129135 MW; A0FD303BFBC6A416 CRC64;
MGKLKKVVQS SSPSTNTAPD LTANNSSQTM ADPQEEIDSN DIDLENVHMS TDDKNLSDKS
NSPPTTDTNT QKDRKPASCK QQGQFKLIGD GSSSKCTQPT PKKKSPITDA SNEFPVRMEN
PSETIIANFC STQTRKVQYD YEDDGDQDNQ LRPEDIEDPE TIKKRLMLLV SKGQLEAEQE
QKTVMNTLHK AKDDEAMYEK TFLREASTTI NTQLDRPPRG NINPESEDFL FMCLDVDFYI
EKPPKHMKEL DQEQDTTIIR MYGVNNKGNS ILVHVFNFRP YFFIQLTYNH HIDQSHLPEL
KRYLNSKLPN QQGVVDLELV ERQSIQNYNE KNQRFIKVYT MLPKFVNQLR SFVEKGLQFN
GVAFWTTTYE SNLPHALRFM IDNQIVGMSW IKINKGAYSV RDKSKQKSVC QIELDVLSSQ
EMKCYKQCEG EYAQIAPLRI LSFDIECSAE KGKFPQPDRD PIIQIAMICQ INGETEPFIR
NVFTLKNCAP IIGTKVYSFM DERDLLKAWR DFVIVIDPDI ITGYNIVNFD IPYIIGRAES
LKIQDYPKFG RIKELFTKFL GEQKEDVQHT IISELQNQNE FTRRRLAIYC IKDAYLPLRL
MWKLDCLYHM CEISRVCGVP LSYLFTRGQQ IKVASQLYRK SQELGYLIPT DKSNNQDGKY
EGAVVIEPIR GFYQDPVAIL DFASLYPSIM MAHNLCYSTL IPNYKLKDVD VSMYERTPNG
DYFVKKSVKK GVLPIILEEL IQARKRVKLD LSRTTDPFEM RLLDSRQNAL KTAANSVYGF
TGAQVGQLPC LAISCSVTAY GRTMLDRTKN LVKEKFCVKN GYPYDSEVIY GDTDSVMIKF
GAKSIEETMI LGREAAEYVT SFFENPIKLE FEKIYCPYLL MNKKRYAGLL WTNPVKYDKI
DAKGIETVRR DNCPLVKDVV NTVLKKILVE RSYEDAINYY KSKFNLIFKC LQGLGKKAKK
ISNNDEKEAY VAKQAHVELA EKMRKRDEAS APSVGDRVAF VMIKGTKDAK GYEKSEDPLY
VLDNNLPIDY NHYLQHQLKQ PLIRIFEPIL QNPEQVLFVG EHTRTIYVPK SRLRLKRTIM
ICGCNARDAK GHCTWIFYAK VETALYSIGE SRQLKIQRSL EK
//
