ID A0A1W0A9K2_9STRA Unreviewed; 1447 AA.
AC A0A1W0A9K2;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, 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 ORFNames=THRCLA_01100 {ECO:0000313|EMBL:OQS06869.1};
OS Thraustotheca clavata.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Thraustotheca.
OX NCBI_TaxID=74557 {ECO:0000313|EMBL:OQS06869.1, ECO:0000313|Proteomes:UP000243217};
RN [1] {ECO:0000313|EMBL:OQS06869.1, ECO:0000313|Proteomes:UP000243217}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 34112 {ECO:0000313|EMBL:OQS06869.1,
RC ECO:0000313|Proteomes:UP000243217};
RX PubMed=25527045; DOI=10.1093/gbe/evu276;
RA Misner I., Blouin N., Leonard G., Richards T.A., Lane C.E.;
RT "The secreted proteins of Achlya hypogyna and Thraustotheca clavata
RT identify the ancestral oomycete secretome and reveal gene acquisitions by
RT horizontal gene transfer.";
RL Genome Biol. Evol. 7:120-135(2014).
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:OQS06869.1}.
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DR EMBL; JNBS01000298; OQS06869.1; -; Genomic_DNA.
DR STRING; 74557.A0A1W0A9K2; -.
DR OrthoDB; 211439at2759; -.
DR Proteomes; UP000243217; 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; IPR010095; Cas12f1-like_TNB.
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 Pfam; PF07282; OrfB_Zn_ribbon; 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 damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
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:UP000243217};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000442}.
FT DOMAIN 121..227
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 606..790
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 856..1301
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
FT DOMAIN 1320..1376
FT /note="Cas12f1-like TNB"
FT /evidence="ECO:0000259|Pfam:PF07282"
FT REGION 252..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 364..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 408..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 564..597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..286
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 568..595
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1447 AA; 164850 MW; F68CD53A11A303DD CRC64;
MTDVKQRMYV EVVDVSYYMA KPLPSHAIPC LPEGPCYEKA KLVPVLRVYG ATPEGLKCCL
HVHGVFPYFY MRCEGDPTFD DANQLVQLLS TIAKDIENAL RSAQENKRAN LPPSIAKLVI
VKGIPFYGYH AQEMFFIKVF YYDPSKCSRL VQIVESGLVA NRIFQPFEAH IPYLLQMFVD
YHIEGMNYIN IRDFKFRSQF DPSQTDWPYR QSNCAIESDV SCKSILNCIN TAKDGCYVPA
LNSLWEEEKQ RRKNQGLTAT PEVDPSIPRN TLSSHESDSQ GPLSQSNFNK RMWASLQTIL
HSTSTDLNTS IQSVRDDENE FSGDLDNNDF AYSQLNQDAA KDLSEELLQL LSRLQDNRQR
EFTKLQVQDH EDSSSDDDSD DYSDDGNEAT ENHHAQTIME SQADFELYSS EQEQDSTNTN
SKPSKWWERD QTISEVQCSI ETLGAPRVSF SLSQSEPEED EIKPHPKVST TFKVRKRWVY
TRVPPSVLDL FPLPPQTTPQ VFYSNIKDVP EKPVAYAGQS YTFPKPGIKY LTDYPNHQYS
SLLNEEVYST RIYRRRTPLR KPPTWGDLQV YDSQQHPHTP RTPRTPMSSA NTPAPAPRPT
HLHISNLTLL SLEIHVNTRQ SLLPDPNQDE VQAIAIVVET TYQEIHSKKY YLIVVDSANL
KQTKVLNGNV YNIEYVHTER ALLERLVERT IEWDPDFFVG YEVQQSSFGY LIDRGGQLDP
PINLIELLSR LPYIKMDSRN QEVLRDDGNI GAKHGMKKAS GIWIHGRHVL NLWRCARSEL
KLSRYNFEEV VAHVLKRPFP KYTHATLTKW FSNGGVLRLR TLEHIALQTE LNLKVMDRMQ
LITRTSEMAR LFGIDFFSVL SRGSQYRVEA VNIRVTKRLN YIMVSPNRQQ VAAQPPMECI
PLVMEPLSAF YGDPVVVLDF QSLYPSMVIA YNICYSTCFG RLQNGLDPSL ETVLGVVTPY
QADLDGLKTS GQDTIVTPNG ALFCPKHVRS GVLPLVLQEI LSTRIMIKKA MKDTSDPRLT
KVLDARQMAL KMIANVTYGY TAASFSGRMP CAQLADAIVH CGRITLESAI KLVESHPTWH
AQVVYGDTDS LFVQLRGRSL QEAWAIGQQI ASQVTANNPK PVCLKLEKVY MGCFLVSKKR
YVGYKFESPT QTVGILDAKG IETIRRDSCG VVQKSMRHWL KLLFKTRDVS QCKKYLQNYW
KKMHEFKIPL QDFIFAKEVR LGTYAGQGPP AVLVATKAMA KDPRAEPRYA ERVCYVVVRG
PPGARLMDLV VQPEELVYNK QYILNIEYYI TKQIIPSYER LALLTGINIR QWYQELPRFT
EKASMYASSV MRIDAYYTSQ HCILCGAQNS RPRYGEANWL CGACKKDTLG SYNLLQSHAI
TLDNQAIAIR QVCMQCMGST THGANWLQAN AMVCMNNGCD VWNLWLRTAQ LYETSEGQSD
AVFKTTV
//
