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Database: UniProt
Entry: G1KXJ4_ANOCA
LinkDB: G1KXJ4_ANOCA
Original site: G1KXJ4_ANOCA 
ID   G1KXJ4_ANOCA            Unreviewed;      1113 AA.
AC   G1KXJ4;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 2.
DT   27-MAR-2024, entry version 74.
DE   RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN   Name=POLD1 {ECO:0000313|Ensembl:ENSACAP00000020141.2};
OS   Anolis carolinensis (Green anole) (American chameleon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Iguania; Dactyloidae; Anolis.
OX   NCBI_TaxID=28377 {ECO:0000313|Ensembl:ENSACAP00000020141.2, ECO:0000313|Proteomes:UP000001646};
RN   [1] {ECO:0000313|Ensembl:ENSACAP00000020141.2, ECO:0000313|Proteomes:UP000001646}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JBL SC #1 {ECO:0000313|Ensembl:ENSACAP00000020141.2,
RC   ECO:0000313|Proteomes:UP000001646};
RG   The Genome Sequencing Platform;
RA   Di Palma F., Alfoldi J., Heiman D., Young S., Grabherr M., Johnson J.,
RA   Lander E.S., Lindblad-Toh K.;
RT   "The Genome Sequence of Anolis carolinensis (Green Anole Lizard).";
RL   Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSACAP00000020141.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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}.
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DR   RefSeq; XP_003222764.2; XM_003222716.3.
DR   AlphaFoldDB; G1KXJ4; -.
DR   STRING; 28377.ENSACAP00000020141; -.
DR   Ensembl; ENSACAT00000022846.3; ENSACAP00000020141.2; ENSACAG00000023481.3.
DR   GeneID; 100564729; -.
DR   KEGG; acs:100564729; -.
DR   CTD; 5424; -.
DR   eggNOG; KOG0969; Eukaryota.
DR   GeneTree; ENSGT00560000077365; -.
DR   HOGENOM; CLU_000203_2_0_1; -.
DR   InParanoid; G1KXJ4; -.
DR   OrthoDB; 211439at2759; -.
DR   TreeFam; TF352785; -.
DR   Proteomes; UP000001646; Chromosome 6.
DR   Bgee; ENSACAG00000023481; Expressed in hindlimb bud and 12 other cell types or tissues.
DR   GO; GO:0016235; C:aggresome; IEA:Ensembl.
DR   GO; GO:0000781; C:chromosome, telomeric region; IEA:Ensembl.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0043625; C:delta DNA polymerase complex; IBA:GO_Central.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0000109; C:nucleotide-excision repair complex; IEA:Ensembl.
DR   GO; GO:0008296; F:3'-5'-DNA exonuclease activity; IBA:GO_Central.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR   GO; GO:0003684; F:damaged DNA binding; IEA:Ensembl.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IBA:GO_Central.
DR   GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0006287; P:base-excision repair, gap-filling; IBA:GO_Central.
DR   GO; GO:0034644; P:cellular response to UV; IEA:Ensembl.
DR   GO; GO:0045004; P:DNA replication proofreading; IBA:GO_Central.
DR   GO; GO:0006261; P:DNA-templated DNA replication; IBA:GO_Central.
DR   GO; GO:0070987; P:error-free translesion synthesis; IEA:Ensembl.
DR   GO; GO:0055089; P:fatty acid homeostasis; IEA:Ensembl.
DR   GO; GO:0006297; P:nucleotide-excision repair, DNA gap filling; IBA:GO_Central.
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 excision {ECO:0000256|ARBA:ARBA00022769};
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:UP000001646};
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          174..486
FT                   /note="DNA-directed DNA polymerase family B exonuclease"
FT                   /evidence="ECO:0000259|Pfam:PF03104"
FT   DOMAIN          550..982
FT                   /note="DNA-directed DNA polymerase family B
FT                   multifunctional"
FT                   /evidence="ECO:0000259|Pfam:PF00136"
FT   DOMAIN          1021..1091
FT                   /note="C4-type zinc-finger of DNA polymerase delta"
FT                   /evidence="ECO:0000259|Pfam:PF14260"
FT   REGION          1..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1113 AA;  125539 MW;  B6B2F65E60B7EBF3 CRC64;
     MENKRKASKG GSSMGEPTLS QRKKSRGDWE EDAPSQFEEE LAFLDEVESE MALEAKETQL
     VPDDIPLGNL FSSVRNPKWQ RPPPPEINPK EDALCFQQVE LDYYVGTHIP GFPGSTQGPV
     PVLRMFGVTE AGNSLCCHIH GFAPYFYVPA QTGFKADHLA EFQRELNAAV LRDMRSNKDN
     LSQVVLAVEI CNKQNMYGYH GENFIPFLKI TMAMPRLIAP AKRLLEQGLR CGTLGVHNYQ
     AFEANIDFEI RFMVDRDVVG CNWIELPAGK YRLRQEQSAG ESSKENPPKV SLCQLEADVA
     WMDFISYPPE GEWQRIAPLR VLSFDIECAG RKGIFPEPEK DPVIQIANMV QRQGEKDPFV
     RNVFTLQSCA PIVGSQVLCF QKEGELLKAW AEFIRTVDPD IITGYNIQNF DLPYLINRAQ
     TLKVSTFPFL GRIPARKSVI RDSSFQSKQM GRRENKVINT EGRAQFDLLQ VLLRDYKLRS
     YTLNAVSYHF LQEQKEDVQH SIITDLQNGT EQSRRRLAVY CLKDAYLPLR LLEKLMCVIN
     YMEMARVTGV PLSYLLARGQ QIKVVSQLLR QAVKQNLVMP VVKSEGGEDY AGATVIEPLK
     GYYDVPIATL DFSSLYPSIM MAHNLCYTTL LQQGAVERHG LSADKFIRTP TGDHFVKASV
     RKGLLPEILE NLLAARKRAK TELKQETDPF KRQVLDGRQL ALKVSANSVY GFTGAQVGKL
     PCLEISQSVT GFGRQMIEKT KQLVESKYTI ANGYSADAKV VYGDTDSVMC RLGVPSVAEA
     MEIGREAAAW VSSHFIPPIK LEFEKVYFPY LLINKKRYAG LYFSSNPDTH DKMDCKGIET
     VRRDNCPLVA NLINTCLQKL LIDRDPAGAV AHAKEVISDL LCNRVDISQL VITKELTRTA
     DEYAGRQAHV ELAERMRRRD PGSAPNLGDR VPYVIIGAAK GVAAYMKSED PIYVLENNLP
     IDTQYYLEQQ LAKPLLRIFE PILGEGKAQN ILLKGEHTRC KTVLTAKVGG LMAFATKRST
     CIGCRAVLNH HGAVCKFCLS RQSELYQKEV TYLSSLEEKF SRLWTQCQRC QGSLHEDVLC
     TSRDCPIFYM RKKVQKDLDD QEVLISRFGP PTW
//
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