ID A0A395SDZ1_FUSSP Unreviewed; 816 AA.
AC A0A395SDZ1;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=DNA polymerase lambda {ECO:0000256|ARBA:ARBA00016513};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN ORFNames=FSPOR_3935 {ECO:0000313|EMBL:RGP70634.1};
OS Fusarium sporotrichioides.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=5514 {ECO:0000313|EMBL:RGP70634.1, ECO:0000313|Proteomes:UP000266152};
RN [1] {ECO:0000313|EMBL:RGP70634.1, ECO:0000313|Proteomes:UP000266152}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 3299 {ECO:0000313|EMBL:RGP70634.1,
RC ECO:0000313|Proteomes:UP000266152};
RX PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA Busman M., Gutierrez S.;
RT "Evolution of structural diversity of trichothecenes, a family of toxins
RT produced by plant pathogenic and entomopathogenic fungi.";
RL PLoS Pathog. 14:e1006946-e1006946(2018).
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}.
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:RGP70634.1}.
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DR EMBL; PXOF01000050; RGP70634.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395SDZ1; -.
DR STRING; 5514.A0A395SDZ1; -.
DR Proteomes; UP000266152; 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:UP000266152};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 181..276
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 34..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 139..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 289..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 428..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..323
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 540
FT /note="Nucleophile; Schiff-base intermediate with DNA; for
FT 5'-dRP lyase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR622312-50"
SQ SEQUENCE 816 AA; 91950 MW; A0A9687950900D0D CRC64;
MASLEEKEAF FKQLQPLDSD DEFDAEEKHE RLRCRRFFAP KSKPKPQPQP TSKPQAKEPL
VLDLANQESQ LSRMTPRRVA SAPTPAPTRG VTIIKGTPMT AMDQKSKLGT LLNQRSDGAI
LVDDTPIPDT ARQTQRILPR SGSSPLLDPG RSLGPVVGES PSPSLTMKKR KRESLLKLRP
ESEQIFRGIA FLYVPDDDIA PARRLRITKA REFGATWVRA PRIATHIVVE KHIKFEELEG
ILKKTNRNLP PIVVNEEYFI DCVQFKTLLQ SNQKKYHLIG QLMTTENESS VIPRSPSEPV
HSLAPKPLEK NSKRWDHVPP QGTPERSEES PHPTQIPETP ALIDSQPVIL NLQDMASSRP
ASNGGSATHS RNTSLSALQD AGGAKQLHKE DSHKDELSEY IKIMAEYKDL PLDADDEDAQ
TAADIGDMEP EEQQLSASED EFARTRKSRR KTRSSSKYTT FEDRFSCNSA GAKDAKAGNP
NARTIEVLQK MADYYNRIND HWRTTAYRKV ISTLKRQETK ITSAEEAQRL PSVGSRLAQK
IEEIVTTDRL QRLEYAEKEP MDEALQLFLG VYGVGNSQAQ QWLAQGFRTL EDLKANAKLS
PNQSLGIEHY EDLNTRIPRR EVEALGTVVK KAAQYIDPEV ELIIGGSYRR GAETSGDIDF
IITKPNTESS ADLRPFLDSL VQRLEAEGFL VARLASSRSA GDGSKWHGCC VLPKISGFND
DNYMPVWRRI DFLLVPESER GAALLYFTGN DIFNRSMRLL ASKKGMRLNQ RGLYKDVMRG
PQRIKVTEGE LVEGRDERRI FDSLGVKWRE PHERWC
//