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Database: UniProt
Entry: A0A250X6V6_9CHLO
LinkDB: A0A250X6V6_9CHLO
Original site: A0A250X6V6_9CHLO 
ID   A0A250X6V6_9CHLO        Unreviewed;      1089 AA.
AC   A0A250X6V6;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN   ORFNames=CEUSTIGMA_g6261.t1 {ECO:0000313|EMBL:GAX78824.1};
OS   Chlamydomonas eustigma.
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX   NCBI_TaxID=1157962 {ECO:0000313|EMBL:GAX78824.1, ECO:0000313|Proteomes:UP000232323};
RN   [1] {ECO:0000313|EMBL:GAX78824.1, ECO:0000313|Proteomes:UP000232323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-2499 {ECO:0000313|EMBL:GAX78824.1,
RC   ECO:0000313|Proteomes:UP000232323};
RA   Hirooka S., Hirose Y., Kanesaki Y., Higuchi S., Fujiwara T., Onuma R.,
RA   Era A., Ohbayashi R., Uzuka A., Nozaki H., Yoshikawa H., Miyagishima S.Y.;
RT   "Acidophilic green algal genome provides insights into adaptation to an
RT   acidic environment.";
RL   Submitted (AUG-2017) 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   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966,
CC         ECO:0000256|RuleBase:RU000442};
CC   -!- SUBCELLULAR LOCATION: Nucleus {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:GAX78824.1}.
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DR   EMBL; BEGY01000036; GAX78824.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A250X6V6; -.
DR   STRING; 1157962.A0A250X6V6; -.
DR   OrthoDB; 211439at2759; -.
DR   Proteomes; UP000232323; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
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:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   CDD; cd05777; DNA_polB_delta_exo; 1.
DR   CDD; cd05533; POLBc_delta; 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; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   InterPro; IPR025687; Znf-C4pol.
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   Pfam; PF14260; zf-C4pol; 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   4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|RuleBase:RU000442};
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   Exonuclease {ECO:0000256|ARBA:ARBA00022839};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU000442};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU000442};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU000442}; Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000256|RuleBase:RU000442};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU000442};
KW   Reference proteome {ECO:0000313|Proteomes:UP000232323};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000442};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU000442};
KW   Zinc-finger {ECO:0000256|RuleBase:RU000442}.
FT   DOMAIN          151..454
FT                   /note="DNA-directed DNA polymerase family B exonuclease"
FT                   /evidence="ECO:0000259|Pfam:PF03104"
FT   DOMAIN          518..952
FT                   /note="DNA-directed DNA polymerase family B
FT                   multifunctional"
FT                   /evidence="ECO:0000259|Pfam:PF00136"
FT   DOMAIN          990..1065
FT                   /note="C4-type zinc-finger of DNA polymerase delta"
FT                   /evidence="ECO:0000259|Pfam:PF14260"
FT   REGION          1..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        29..52
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1089 AA;  122322 MW;  A4FC87E5A6E864A1 CRC64;
     MADVRRSNGG NAGTSGPLRK RPLMEQDGMI DDVLDDFDND APMHPPEEDD EVDLGEAGRN
     WVRPAVQPFD PKSTSITFQQ VEVDYYIAPR MESMDKEPGQ KQVPVIRMYG VTDYGNSVCA
     FVHGFEPYFY AEKPRNWGTE ALEELQQDLN KQLASKTKGD GNAVLRLEVE RKASVWGYQG
     GAQKDFIRIV MSLPNYVTPA RSLIENGLKV GDFGDIRSTT YESNVLYALR FMIDMNVVGG
     NWVELPAGKY VMPYSPQTYC QIEAHVRYED LLSHTPEGDW ARLAPLRVLS VDIECAGRKG
     HFPEAKLDPV IQIASMITEQ GRDQAAVRNV MTLGSCASIV GAEVMSFDSE AALLLRWRDL
     LLETDPDIII GYNTTNFDLP YLYERAQALG IDKEFHQWGR VRGSRTRIRD TQFSSKAYGT
     HEYKDLPVDG RVQLDLLTAI QREYKLASYS LNAVSAHFLG EQKEDVHHSC ITDLQNGNEE
     TRRRLAVYCL KDAYLPQRLL GKLMFMYNYI EMARVTGVPM SYLLSRGQSI KVFSQVLRKS
     RARGFLIPNI KYSGPQNTDG ATYEGATVLE PKTGYYDKPV ATLDFASLYP SIMMAHNLCY
     TTLVLPERVR EVPAEHIAQS PCGDWFIKSA AQKGILPEIL EELLAARKRA KADLAKESDP
     FKRAVLDGRQ IALKISANSV YGFTGATVGK MPCLQISAST TAYGRTMIMN TRELVMSMYN
     KANGYEADCD VIYGDTDSVM VNFGVSEVGR AMELGREAAA AVSKTFPAPV KLEFEKVYYP
     YLLMNKKRYA GLLWTKPEKH EKIDTKGIET VRRDNCLLVR NVITSCLDRI LINRDVNGAV
     QYVKGVISEL LMNRIDLSLL VISKGLSQDA DVYEGKVAHV ELAKKMRKRD AATAPTTGDR
     VPYVIIKAAK GAKAWEKAED PIYALDHNLP IDVQHYLEHH LSLPLMRLFE PVMKNPKELL
     SGDHTRSILV STPTVASGGI MRFAKVRLSC LGCKAPLDKP VGEGKTPLCK HCLPKEADLY
     QRSLSSVNEL EDLYSELWTQ CQRCQGSLHQ DVLCTSRDCP IFYRRKKVQK DLNEAQAQLI
     RFADDDVTW
//
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