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Database: UniProt
Entry: G1RXX0_NOMLE
LinkDB: G1RXX0_NOMLE
Original site: G1RXX0_NOMLE 
ID   G1RXX0_NOMLE            Unreviewed;       574 AA.
AC   G1RXX0;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 73.
DE   RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU366014};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU366014};
GN   Name=POLL {ECO:0000313|Ensembl:ENSNLEP00000018097.1};
OS   Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates leucogenys).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC   Nomascus.
OX   NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000018097.1, ECO:0000313|Proteomes:UP000001073};
RN   [1] {ECO:0000313|Ensembl:ENSNLEP00000018097.1, ECO:0000313|Proteomes:UP000001073}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Gibbon Genome Sequencing Consortium;
RL   Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSNLEP00000018097.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: DNA polymerase that functions in several pathways of DNA
CC       repair. Involved in base excision repair (BER) responsible for repair
CC       of lesions that give rise to abasic (AP) sites in DNA. Also contributes
CC       to DNA double-strand break repair by non-homologous end joining and
CC       homologous recombination. Has both template-dependent and template-
CC       independent (terminal transferase) DNA polymerase activities. Has also
CC       a 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity.
CC       {ECO:0000256|RuleBase:RU366014}.
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:RU366014};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU366014}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-X family.
CC       {ECO:0000256|ARBA:ARBA00008323, ECO:0000256|RuleBase:RU366014}.
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DR   EMBL; ADFV01163472; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_003255417.1; XM_003255369.3.
DR   RefSeq; XP_003255418.1; XM_003255370.3.
DR   RefSeq; XP_012361209.1; XM_012505755.1.
DR   AlphaFoldDB; G1RXX0; -.
DR   STRING; 61853.ENSNLEP00000018097; -.
DR   Ensembl; ENSNLET00000018995.2; ENSNLEP00000018097.1; ENSNLEG00000014861.3.
DR   GeneID; 100583874; -.
DR   KEGG; nle:100583874; -.
DR   CTD; 27343; -.
DR   eggNOG; KOG2534; Eukaryota.
DR   GeneTree; ENSGT00940000158515; -.
DR   HOGENOM; CLU_008698_6_1_1; -.
DR   InParanoid; G1RXX0; -.
DR   OMA; KWHGASA; -.
DR   OrthoDB; 49764at2759; -.
DR   TreeFam; TF103011; -.
DR   Proteomes; UP000001073; Chromosome 3.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0035861; C:site of double-strand break; IEA:Ensembl.
DR   GO; GO:0051575; F:5'-deoxyribose-5-phosphate lyase activity; IEA:Ensembl.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006287; P:base-excision repair, gap-filling; IEA:Ensembl.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:Ensembl.
DR   GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IEA:Ensembl.
DR   GO; GO:0006289; P:nucleotide-excision repair; IEA:Ensembl.
DR   CDD; cd17715; BRCT_polymerase_lambda; 1.
DR   CDD; cd00141; NT_POLXc; 1.
DR   Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR   Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR   Gene3D; 3.40.50.10190; BRCT domain; 1.
DR   Gene3D; 1.10.150.110; DNA polymerase beta, N-terminal domain-like; 1.
DR   Gene3D; 3.30.210.10; DNA polymerase, thumb domain; 1.
DR   InterPro; IPR001357; BRCT_dom.
DR   InterPro; IPR036420; BRCT_dom_sf.
DR   InterPro; IPR002054; DNA-dir_DNA_pol_X.
DR   InterPro; IPR019843; DNA_pol-X_BS.
DR   InterPro; IPR010996; DNA_pol_b-like_N.
DR   InterPro; IPR028207; DNA_pol_B_palm_palm.
DR   InterPro; IPR018944; DNA_pol_lambd_fingers_domain.
DR   InterPro; IPR027421; DNA_pol_lamdba_lyase_dom_sf.
DR   InterPro; IPR037160; DNA_Pol_thumb_sf.
DR   InterPro; IPR022312; DNA_pol_X.
DR   InterPro; IPR002008; DNA_pol_X_beta-like.
DR   InterPro; IPR043519; NT_sf.
DR   InterPro; IPR029398; PolB_thumb.
DR   PANTHER; PTHR11276:SF44; DNA POLYMERASE LAMBDA; 1.
DR   PANTHER; PTHR11276; DNA POLYMERASE TYPE-X FAMILY MEMBER; 1.
DR   Pfam; PF14792; DNA_pol_B_palm; 1.
DR   Pfam; PF14791; DNA_pol_B_thumb; 1.
DR   Pfam; PF10391; DNA_pol_lambd_f; 1.
DR   Pfam; PF14716; HHH_8; 1.
DR   PRINTS; PR00869; DNAPOLX.
DR   PRINTS; PR00870; DNAPOLXBETA.
DR   SMART; SM00483; POLXc; 1.
DR   SUPFAM; SSF52113; BRCT domain; 1.
DR   SUPFAM; SSF47802; DNA polymerase beta, N-terminal domain-like; 1.
DR   SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR   SUPFAM; SSF81585; PsbU/PolX domain-like; 1.
DR   PROSITE; PS50172; BRCT; 1.
DR   PROSITE; PS00522; DNA_POLYMERASE_X; 1.
PE   3: Inferred from homology;
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|RuleBase:RU366014};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|RuleBase:RU366014};
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW   DNA synthesis {ECO:0000256|ARBA:ARBA00022634};
KW   DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW   ECO:0000256|RuleBase:RU366014};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000256|RuleBase:RU366014}; Nucleus {ECO:0000256|RuleBase:RU366014};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001073};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU366014}.
FT   DOMAIN          35..131
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
FT   REGION          161..204
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        311
FT                   /note="Nucleophile; Schiff-base intermediate with DNA; for
FT                   5'-dRP lyase activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR622312-50"
SQ   SEQUENCE   574 AA;  63319 MW;  731454AA5236E7B9 CRC64;
     MDPRGILKAF PKRKKIHADA SSKVLAKIPR REEGEAEEWL SSLRAHVVRT GIGRARAELF
     EKQIVQHGGQ LCPAQGPGVT HIVVDEGMDY ERALRLLRLP RLPPGAQLVK SAWLSLCLQE
     RRLVDVAGFS IFIPSRYLDQ PQPSKAEQHA SIPPGTCEAL LQTALSPPPS STRPVSPPQK
     AKEAANTQAQ PISDDEASDG EETQVSAADL EALISGHYPT SLEGDCEPSP ASAVLDKWVC
     AQPSSQKATN HNLHITEKLE VLAKAYSVQG DKWRALGYAK AINALKSFHK PVTSYQEACS
     IPGIGKRMAE KIIEILESGH LRKLDHISDS VPVLELFSNI WGAGTKTAQM WYQQGFRSLE
     DIRSQASLTT QQAIGLKHYS DFLERMPREE ATEIEQTVQK AAQAFNSGLL CVACGSYRRG
     KATCGDVDVL ITHPDGRSHR GIFSRLLDSL RQQGFLTDDL VSQEENGQQQ KYLGVCRLPG
     PGWRHRRLDI IVVPYSEFAC ALLYFTGSAH FNRSMRALAK TKGMSLSEHA LSTAVVRNTH
     GCKVGPGRVL PTPTEKDVFR LLGLPYREPA ERDW
//
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