ID A0A0B2UPD6_TOXCA Unreviewed; 1770 AA.
AC A0A0B2UPD6;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN Name=REV3L {ECO:0000313|EMBL:KHN72846.1};
GN ORFNames=Tcan_03902 {ECO:0000313|EMBL:KHN72846.1};
OS Toxocara canis (Canine roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Ascaridomorpha; Ascaridoidea; Toxocaridae; Toxocara.
OX NCBI_TaxID=6265 {ECO:0000313|EMBL:KHN72846.1, ECO:0000313|Proteomes:UP000031036};
RN [1] {ECO:0000313|EMBL:KHN72846.1, ECO:0000313|Proteomes:UP000031036}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PN_DK_2014 {ECO:0000313|EMBL:KHN72846.1};
RA Zhu X.-Q., Korhonen P.K., Cai H., Young N.D., Nejsum P.,
RA von Samson-Himmelstjerna G., Boag P.R., Tan P., Li Q., Min J., Yang Y.,
RA Wang X., Fang X., Hall R.S., Hofmann A., Sternberg P.W., Jex A.R.,
RA Gasser R.B.;
RT "Genetic blueprint of the zoonotic pathogen Toxocara canis.";
RL Submitted (NOV-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|RuleBase:RU000442};
CC -!- SIMILARITY: Belongs to the DNA polymerase type-B family.
CC {ECO:0000256|ARBA:ARBA00005755, ECO:0000256|RuleBase:RU000442}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KHN72846.1}.
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DR EMBL; JPKZ01003189; KHN72846.1; -; Genomic_DNA.
DR STRING; 6265.A0A0B2UPD6; -.
DR OMA; CHVECDA; -.
DR Proteomes; UP000031036; Unassembled WGS sequence.
DR GO; GO:0016035; C:zeta DNA polymerase complex; IEA:InterPro.
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 GO; GO:0019985; P:translesion synthesis; IEA:InterPro.
DR CDD; cd05778; DNA_polB_zeta_exo; 1.
DR CDD; cd05534; POLBc_zeta; 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; IPR030559; PolZ_Rev3.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR PANTHER; PTHR45812; DNA POLYMERASE ZETA CATALYTIC SUBUNIT; 1.
DR PANTHER; PTHR45812:SF1; DNA POLYMERASE ZETA CATALYTIC SUBUNIT; 1.
DR Pfam; PF00136; DNA_pol_B; 1.
DR Pfam; PF03104; DNA_pol_B_exo1; 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 damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW DNA replication {ECO:0000256|RuleBase:RU000442};
KW DNA-binding {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:UP000031036};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000442}.
FT DOMAIN 100..175
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 952..1098
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 1208..1661
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
FT REGION 547..574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 621..702
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 718..821
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..567
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 652..702
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 721..737
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 745..817
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1770 AA; 200318 MW; 5C2C2E9B8DA83B1A CRC64;
MASLCMRNVL CEFYLDKPNG FNRVLARSSK ILPVIRLFGI LESGQKCCVH IHGVFPYIVL
RLGTPLTPEV SDVLRSTLAS LVSHRKPNIR SEIIEASIYD IVSFDAKSLY GYYNDDDHFA
KIFFTNPQYL RVVSNVLYEE AISNPILQVY EAHTPYLMQF FIDYSIFGMD LVHFNDVKFR
ISPIKDIGEN YFAGMTVGKI LSDASLLSPL LPSTNVAIEC DVFASNISNA QHYTSSEGLS
SNPGLDYIWK DEMRRCRQRG KKLMIESSQE ERPPPITANE RDWLDRLCNV VKKLKSLLND
GVMANIELTA RSTFDSTIIE MNRTLMASNS TENAEAVIHE EEKEEDLILE LSEHDTLLFQ
DDEAEYVDSR KEHEVVRRLF CFDTYIGGLS SNPGLDYIWK DEMRRCRQRG KKLMIESSQE
ERPPPITANE RDWLDRLCNV VKKLKSLLND GVMANIELTA RSTFDSTIIE MNRTLMASNS
TENAEAVIHE EEKEEDLILE LSEHDTLLFQ DDEAEYVDSR KEHEVEMEDM SQPLFSLYLP
SQKAGRSWVQ DKPNANNDVS RSTSEVLDDA SRNSDVDSFL EELSRLTSYD GGSSKDERLD
CESAMRKPSR NLPIDFSLLD EAGSTKRPDS VSNLVSTEAM RCDDKDDQKG SEQGSSQSNG
SGDIFEVEHS SGHGSTGTVR SNCDNNLASS SQPEWNRQSS SLSARTLVRL HSETRIEKNS
VKKCQQTQQN SQHCISEGSE DLFEKSSLDS ASTSKRHSSQ RSDLNGSQTP RCSPTAIASQ
STSHESISRT NHTSLNKFRP SKRAKTSTPT SENVTSAEKQ MSEEEDIIWN MVESYENDIG
SLWSARRPVK RRIDFDRFHY KIISGMQIKG TQDSDDSGVW LSPTFQLPLR CRSDPITSSD
NEPNQTVMGE TMLEFSQRSV DEQSDRVNYE TMLESWYERR SFNNYEGVEE KLEATVRIPS
GPGSNPDTDH TDLRHLCVMS MEVLAPTRPG CPVPDPQFDR VIGIFCSVSL DVCMQESDYD
EECILLDSSV IQTESSSEQI ICVENESALF DAFAEIVKRI DPDMVIGYDT RRYSWGYLME
RSIALGRNLL SELSRYTIDV SEYYRPDIPK FVLDPSPRGR LLLNIWRILR HELALRSYTR
SAIVQTVLGR RFPHFSHSAI SEWICSGEKH LISVVTKHLR LCARLNLQIM SQLDLFTRTA
EMARVYGIQF AEVLSRGSQF RVESMLLRLA RRHSLAAPSV SPAQRTAMCA PEVLPLNMEP
ESGYYRDPVI VLDFQSLYPS IMIAYNYCFS TCLGKVSNMD NVSQTGLVDS MELGGLVYSL
PANELTSMVE NGNVHISPTG TAFCKKSIRR GIMPIMLEEI LNTRIMVKKA AKDYKDSRRL
ARILDARQMA LKFVANVTYG YSAANFSGRM PCVEVADSIV SKGRETLERA IAHVNEGNYG
QARVIYGDTD SMFVLCPGST RKEAFEIGEK IANDVTMANP NPVKLKLEKV MHPLVLESKK
RYVGMSYEKL DDTEGVFDAK GIETVRRDSC PLVSRILEKS LRLLFADKVA AVVRYLDMQL
SNLDRVPLSD FVFSRQYRST YADTAVVAAK RISEKRRAKC ARDEPESGER VPYVIVDGEL
NATLISCVRE PNEYVKNPRL TLNYDYYVQR HVLPSLQRAF NYVPLHFEWC RPTNGDCYKC
GALGARPWCE KCSHNPKALL LALCDDSKQR QLHSQLDRAC RKCLGLRLCD IEYSSCVNMA
CAVVQKRITL RKSNTSQAVA LHSLSKTSAL
//
