ID A0A084QGS1_STAC4 Unreviewed; 810 AA.
AC A0A084QGS1;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=DNA polymerase lambda {ECO:0000256|ARBA:ARBA00016513};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN ORFNames=S40285_03286 {ECO:0000313|EMBL:KFA63156.1};
OS Stachybotrys chlorohalonata (strain IBT 40285).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Stachybotryaceae; Stachybotrys.
OX NCBI_TaxID=1283841 {ECO:0000313|EMBL:KFA63156.1, ECO:0000313|Proteomes:UP000028524};
RN [1] {ECO:0000313|EMBL:KFA63156.1, ECO:0000313|Proteomes:UP000028524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 40285 {ECO:0000313|EMBL:KFA63156.1,
RC ECO:0000313|Proteomes:UP000028524};
RX PubMed=25015739; DOI=10.1186/1471-2164-15-590;
RA Semeiks J., Borek D., Otwinowski Z., Grishin N.V.;
RT "Comparative genome sequencing reveals chemotype-specific gene clusters in
RT the toxigenic black mold Stachybotrys.";
RL BMC Genomics 15:590-590(2014).
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 -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SIMILARITY: Belongs to the DNA polymerase type-X family.
CC {ECO:0000256|ARBA:ARBA00008323}.
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DR EMBL; KL660754; KFA63156.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A084QGS1; -.
DR STRING; 1283841.A0A084QGS1; -.
DR HOGENOM; CLU_008698_3_0_1; -.
DR InParanoid; A0A084QGS1; -.
DR OMA; KWHGASA; -.
DR OrthoDB; 49764at2759; -.
DR Proteomes; UP000028524; Unassembled WGS sequence.
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:0006281; P:DNA repair; IEA:UniProtKB-KW.
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:SF43; DNA POLYMERASE IV; 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};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Reference proteome {ECO:0000313|Proteomes:UP000028524};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 178..272
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 24..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 125..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 291..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 352..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 419..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..387
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 426..450
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 533
FT /note="Nucleophile; Schiff-base intermediate with DNA; for
FT 5'-dRP lyase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR622312-50"
SQ SEQUENCE 810 AA; 90781 MW; 2085F145CFEC7C2C CRC64;
MDVPQPVLDD KVARFNLLEY LENDEDDEFD SQEQRNRQRC RMFFQPPPAP TKTPTRRAER
AEDNGVLAQG TSRSAASRAR RVSSVPIVQP KVIKGTPVGA TAAMGHLHDL LDDGASVIKE
TPLTEVSRPG SKGIRRGDST PLNPAARSLM RNASDHSPLT NVGTRKRKRE AAPKMKPPQQ
QIFQGLSFHY IPNNDIAPAR RIRIAKAREY GATWTLNIAV ATHVIVDKAI TYKDIERLLP
HDAAHALTVV NEDYPIDCIQ FRTILDPEQR KYLLRGQPHV IHDDPITVPA SSSEESIASL
QLKPPHKNQS RWDYLPPNSI ESTPRSSEAQ VNVEIDSQPA VQGLDEILDS QEKSNNANGG
ISHDKHQHKP EQPRIVLGTP EDRPHMPADE LSECINTMLE FKDLPLDVDD LDEVYASTAC
LDDSDEDPQP SQKRPELKKP RKRESATGRK DMAFEDLFAC NQAGETKAKP ANPNIRTIEI
LQSMADYYDR VNDHWRTTAY RKAISTLKRQ DVKIGTEEEA YRLPSVGRRL AQKIEEIVTT
DKLQRLEHAK AEPMDAPLQL FLGIYGVGLA QAQQWIGQGF RTLDDLKQGA RLTENQRVGV
DHYDDLNARI PRREVAALGA VVKDAARKVD PRMELIIGGS YRRGAESSGD IDIIVTKPGT
RSTSELRGFL DELVRRLEAE GFLVARLASS RPGGDGSKWH GCCVLPRGLG VKDDTAYCPV
WRRIDILLVP GTQKGAALIY FTGNDIFNRS MRLLASKKGM RLNQRGLYKD ALRGPGRAKV
TEGELVEGRD ERRIFEILGV KWREPQERWC
//
