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Database: UniProt
Entry: A0A024GER1_9STRA
LinkDB: A0A024GER1_9STRA
Original site: A0A024GER1_9STRA 
ID   A0A024GER1_9STRA        Unreviewed;      1747 AA.
AC   A0A024GER1;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN   ORFNames=BN9_062270 {ECO:0000313|EMBL:CCI45354.1};
OS   Albugo candida.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Albuginales; Albuginaceae; Albugo.
OX   NCBI_TaxID=65357 {ECO:0000313|EMBL:CCI45354.1, ECO:0000313|Proteomes:UP000053237};
RN   [1] {ECO:0000313|EMBL:CCI45354.1, ECO:0000313|Proteomes:UP000053237}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ac Nc2 {ECO:0000313|EMBL:CCI45354.1,
RC   ECO:0000313|Proteomes:UP000053237};
RA   Gardiner A., Kemen E., Schultz-Larsen T., MacLean D., Van Oosterhout C.,
RA   Jones J.D.G.;
RT   "Recombination and specialization in a pathogen metapopulation.";
RL   Submitted (MAY-2012) 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:CCI45354.1}.
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DR   EMBL; CAIX01000095; CCI45354.1; -; Genomic_DNA.
DR   STRING; 65357.A0A024GER1; -.
DR   InParanoid; A0A024GER1; -.
DR   OrthoDB; 211439at2759; -.
DR   Proteomes; UP000053237; 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; 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:UP000053237};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000442}.
FT   DOMAIN          747..981
FT                   /note="DNA-directed DNA polymerase family B exonuclease"
FT                   /evidence="ECO:0000259|Pfam:PF03104"
FT   DOMAIN          1109..1580
FT                   /note="DNA-directed DNA polymerase family B
FT                   multifunctional"
FT                   /evidence="ECO:0000259|Pfam:PF00136"
FT   REGION          460..521
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          786..809
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        469..489
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        494..521
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1747 AA;  198745 MW;  82299998E94EA7C4 CRC64;
     MSSVVERTND EEFIRVDVVH VDYYMNTPLP DNELFNLPKS PYYRKAHRVP VIRIFGSTSA
     GQKTLVHLHG VLPYFYLRCE NDPIFEKLSE LQKLLPALAT DIEKSFQKKL DHSSTISSNA
     KFSNVIAKLM IVKGIPFYGY HDQPCLFIQL FYYNPRHSNH LVHMLESGQI VKRVFQTFES
     HVPYMLQMFA DYHIEGMNPL YLSNVKFRAP LPVSQHHLMD DMSAIVDTRE MCRRIYLQGN
     VPEHMISSSS KQISVGIRGR HVPVTDFPQS NGCRQSSCSL ELDVAIASVL NSRRFREHQI
     SLETRGIVNN VPSLAVLWEE EKERRRMAHL DESPELPDSY PRETDTQQKR FFGSRSKTDV
     RLSQTLLSQS HFYDQMKTSL NKIMTKIINV KSEGIEEKRG HSEVEGDDLV PMSSQIHSPD
     TENQFSFSQN CCGMSDTKRA EEDLDILNFL LKMKNPLEDS STGVELENEV ADYRSDRSDE
     SDKRNDAAEA TAILESQRVS TSESPNHKSN ATANRPSKWW EVSTDKSQHA ADIGSSRINR
     ASDRTKKLQK QDFFSLNAKS CSRKAQLTTD SQASETITYS REVWAADTNR IKTDCTQSQC
     IKSSQEMIHQ SNTNNRLKAT PDTSPILCLS KQRKRRKASI KRDSVQENKV WLYRARPPTF
     EELIESSQSL GILPHHNTGA FYSDPGDLPK KPLKFGGYKF QFTDQNDVTK LDRFDTSLQR
     HELSSNTIGR VFRGLDELIS VEQGEHKRSG YRDANHNRLY TTAMLPPSQS MVRNWLSKEA
     SSRQNEVKRE ALSTSNQINS STSLSATEQV HSTSTPNITT LSVEVCAFCR GSLSPDPAID
     AIGAIAYAIS AKEGFHRNKT KHTGVIINTA EDKAIPDSQN TLVKESQDTL RFDANFAQLI
     TAKRKLIGKR FCLGRHDAAV FAVSSEEEIF TCFNKVVETW DPDFLTGFEV QKSSIGYLVD
     RAMHLNINLI QTMSRLPQTP IDARNPVSHV NVDDKDPGKI KTSIGTIWGM AKASGLWIHG
     RHVINLWRVA RSELKLARYS IEDIVQSVLQ QTWPTYSWQE MSTSFREEGL RRWKMLDHLL
     DKAVVNLKLL SRMQFITRTS EMARLFGIDF YSVLSRGSQF RVEAVMLRVT KRNNFVLLSP
     SRNQVAAQAP MECIPLVMEP QSRYYSDPVV VLDFQSLYPS LVIAYNLCYS TYLGRLENGM
     KPELETFMGV TSFSPDEKGF TNCDQEIHIA PNGTLFCPKS RRRGIVPAIL EEILATRIMI
     KHAMKKHQSP TLSKNLYKKL DARQLALKLI ANVTYGYTAA GFSGRMPCAQ LADAIVQTGR
     CTLEATVRVV ESHSEWNARV VYGDTDSLFV LLEGRSKNEA FCIGQEIAKK ITALNPRSEN
     LFDIRMWQCS SLVCRPVELK MEKVYFGCIL VSKKRYVGYK YESLDQVQGE LDAKGVEIVR
     RDSCVLVQKL MRTSLQLLFE TRDLSRIKRV MIHLRRQMLS NQIPLRDYVF AKEVRLGSYA
     DNSHAPPAAL VSLKAMASDP RAEPRYAERV PYVVINGFPG ARLIDLVISP YRFVANPSGN
     TINYQYYIEK QIIPSLERLF LLVGVNIRDW FASVSKVNSK ANGYASIDIE DLLQEKPQHP
     RRYTPSNRKS IEFFYKSVRC YLCGSVIPSS SMISLDWIRT NALCPCCQEN AQRSLLQLKH
     GEVLLDMQLG KLRQLCSLCT EGNQFIWYQT CQSLPCPIWN QSQILGDRVG RIISKSPEEE
     KESLVGL
//
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