ID A0A1V9YH72_9STRA Unreviewed; 1451 AA.
AC A0A1V9YH72;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN ORFNames=ACHHYP_12413 {ECO:0000313|EMBL:OQR85051.1};
OS Achlya hypogyna.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Achlya.
OX NCBI_TaxID=1202772 {ECO:0000313|EMBL:OQR85051.1, ECO:0000313|Proteomes:UP000243579};
RN [1] {ECO:0000313|EMBL:OQR85051.1, ECO:0000313|Proteomes:UP000243579}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 48635 {ECO:0000313|EMBL:OQR85051.1,
RC ECO:0000313|Proteomes:UP000243579};
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:OQR85051.1}.
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DR EMBL; JNBR01001827; OQR85051.1; -; Genomic_DNA.
DR STRING; 1202772.A0A1V9YH72; -.
DR OrthoDB; 211439at2759; -.
DR Proteomes; UP000243579; 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; 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|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:UP000243579};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000442}.
FT DOMAIN 607..789
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 855..1300
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
FT REGION 246..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 310..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 365..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1451 AA; 161179 MW; 93A7D175033D5776 CRC64;
MEDDTVVRVE VVDVSYYLAK PLPVQAVKAL PEGPCYERAR QVPVVRVFGA TPEGPKCCLH
VHGVFPYFYM RCENDPAFDD VATLMELLPT IGRDLEAALR SMATAPETDA QKAKTKPSKP
IPPSIAKLVI VKGIPFYGYH ATEVFFVKVF FYDPAKTSRI VQAVESGHVA ARMFADYHIE
GMNYLRVRDA TFRTQTGTST DWPVRQSNCA IEADVSCKNI LNPQFVNLDS DACYVPSLAP
LWEEEKQRRR DQGLAATPEA APSIPRDALR RRHSEPDGSP SQSPLSQSHF NTRMWASLNE
IIRQAASKHG NSEMLSNDGS ESPFPAGLDD SNFAYSQLDH APKDDEADAS DELLRLLSRL
QEDRLREAVA PPSSPDAASD DEADDDHTDE AAAEERNAQA ILDSQRDFEL QSSQDVLPLE
ECEKPTTAPA WWERDQSICE SQCSVDELGA PRILSPDRAA SQAAASFAAA DISPLSQSHG
GRRYTWRYTV PAPKLDDLLP LPPSATPSVF YSNAADVPDK PVVYAGQRYA FPKPGVEHLP
EFPSTHRALA ALKPPAPSTR IRRRRTPLRL PPTWQELQAT TGPASMPSPP TPTPAPVARP
AHLHISNLTL LSVEVHASSR GELLPDPSFD AVEAIAMVVD TTFQQLQTRR YSLLVLDAAL
ALTPLRLHGH DYAVEYVPTE RALLERFVER VAEWDPDFLV GFEIQVATYG YLIDRGAQLD
PPINLIETLS RLPHTRMDSR NQALAEGNVG AAHGMKKAAG IWIYGRHILN VWRCARSELK
LARYTFEAVV AHVLKRRFPK HAPATLSAWF IAGGSQRLRT LEHVGERADV TLQLVDRLQL
VTRTSEMARL FGIDFFSVLS RGSQYRVEAV NIRVTKRLNY IMVSASRAQV AAQPPMEIIP
LVMEPLSSFY AEPVVVLDFQ SLYPSMVIAY NLCYSTFIGR LVNGLDPALE TVLGVVADHR
PNVDALRAAG GDTIVTPNGA LFCPKAHRLG VLPRVLDEIL STRIMIKQAM KQTTDKRLVK
VLDARQLALK MIANVTYGYT AASFSGRMPC AQLADAIVHS GRVTLEAAVR LVESHPTWHA
RVVYGDTDSL FVQLRGRSLR DAWAIGQEIA TAVTAANPKP VCLKLEKVYM GSFLVSKKRY
VGLKFEGPDE VKGVLDAKGI ETVRRDSCGV VQKPMRRWLE LMFTKRDVSK GKAYLQQYWQ
NMHHQRIPLR DFIFAKEVRL GTYAGQGPPA VLVATKAMAK DPRAEPRYAE RVAYVVVRGP
PGARLMDLVV PPEELACHDK YTLNVDYYVT KQMLPSLERL ALLMGVNVRQ WYLELPRVVE
KALPSLGASS VMRIDAYYAS QHCVLCGALN SRPRRLADGG WLCPACKHEP QKSFLLLQNY
KSGLERQLLA ARSTCAQCMG STSHDADWTE RRHMVCVNDD CDVWNRWLRG AALLEACGDP
MQLTANSHED G
//