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Database: UniProt
Entry: A0A1J9RE62_9EURO
LinkDB: A0A1J9RE62_9EURO
Original site: A0A1J9RE62_9EURO 
ID   A0A1J9RE62_9EURO        Unreviewed;       716 AA.
AC   A0A1J9RE62;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   18-JUN-2025, entry version 35.
DE   RecName: Full=DNA polymerase lambda {ECO:0000256|ARBA:ARBA00016513};
DE            EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN   ORFNames=ACJ73_02317 {ECO:0000313|EMBL:OJD26300.1};
OS   Blastomyces percursus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX   NCBI_TaxID=1658174 {ECO:0000313|EMBL:OJD26300.1, ECO:0000313|Proteomes:UP000242791};
RN   [1] {ECO:0000313|EMBL:OJD26300.1, ECO:0000313|Proteomes:UP000242791}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EI222 {ECO:0000313|EMBL:OJD26300.1,
RC   ECO:0000313|Proteomes:UP000242791};
RA   Cuomo C.A., Schwartz I.S., Kenyon C., De Hoog G.S., Govender N.P.,
RA   Botha A., Moreno L., De Vries M., Munoz J.F., Stielow J.B.;
RT   "Emmonsia species relationships and genome sequence.";
RL   Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=DNA(n) + a 2'-deoxyribonucleoside 5'-triphosphate = DNA(n+1) +
CC         diphosphate; Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-
CC         COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112;
CC         EC=2.7.7.7; Evidence={ECO:0000256|ARBA:ARBA00049244};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-X family.
CC       {ECO:0000256|ARBA:ARBA00008323}.
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:OJD26300.1}.
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DR   EMBL; LGTZ01000243; OJD26300.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1J9RE62; -.
DR   STRING; 1658174.A0A1J9RE62; -.
DR   VEuPathDB; FungiDB:ACJ73_02317; -.
DR   OrthoDB; 205514at2759; -.
DR   Proteomes; UP000242791; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:TreeGrafter.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IEA:TreeGrafter.
DR   CDD; cd00141; NT_POLXc; 1.
DR   FunFam; 1.10.150.20:FF:000010; DNA polymerase lambda; 1.
DR   FunFam; 3.30.210.10:FF:000001; DNA polymerase lambda; 1.
DR   FunFam; 1.10.150.110:FF:000005; DNA polymerase POL4; 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; 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:SF28; 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.
PE   3: Inferred from homology;
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   DNA synthesis {ECO:0000256|ARBA:ARBA00022634};
KW   DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000242791};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          132..228
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
FT   REGION          91..111
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          233..259
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          340..368
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        91..100
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        239..254
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        448
FT                   /note="Nucleophile; Schiff-base intermediate with DNA; for
FT                   5'-dRP lyase activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR622312-50"
SQ   SEQUENCE   716 AA;  80707 MW;  4F284F0B895C480C CRC64;
     MERDKNGYGD SGRLADKETF CEDLYEFSGY SDNSQEINEL AVFLERAKKR NSLDRTLSRT
     PGSEERNTLP DCHTLKRQKV TDAQEIANTM GSNKRMSTRS AHPKRRPIVD GVGGNILASR
     RKREPTVRVR PEHQQIFKDM VFFFIPNDDI APARRMRINK ALEFGASRSF TWDDTVTHVV
     VDKAISFTDV LKYLRIDSWP LSVSLVNASY PTECITFGSL MNASHARFHV SGAPAKNNEA
     SKSDGEPAVR DSPKLKPARN GIYLETPVTS TSPPTNEELQ DPLVPRPFDT HRKDDCADVI
     EQCSQKGHDI LDEIIKQARA EKALPLDQSD EEDVGKASAI VEVDSNSDSE AEKLKEAKKK
     KRSNENPQWQ QTFSCMHKHD GFTDRDNPNA RTIEILQKMS EYYDRISDQW RTLAYRKAIS
     ALRKQKERIV TKEQALAIPG IGERLATKIE EIVWTNRLRR LEEANAEPHD VLLSQFLNIY
     GVGFAQASKW IQQGYQSLDD LKAKACLTKN QQIGIEHYGD FCQRIPRAEV EAHGAIVKKL
     LFTVDPAVRV IIGGSYRRGA ASSGDIDLII TKDGAAQAEI CALMTNIVIP ALFQENFLQA
     GLAVGRRGES SKWHGACALP GSKNPVWRRI DFLYVPGDEI GAALIYFTGN DVFNRSLRLL
     ASKKGMCLNQ RGLFTGVVRR ENRIKLNSGR LLESREEKKI FEILGVPWRP PNHRIC
//
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