ID A0A364L020_9EURO Unreviewed; 1121 AA.
AC A0A364L020;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:RAO69091.1};
GN ORFNames=BHQ10_005103 {ECO:0000313|EMBL:RAO69091.1};
OS Talaromyces amestolkiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=1196081 {ECO:0000313|EMBL:RAO69091.1, ECO:0000313|Proteomes:UP000249363};
RN [1] {ECO:0000313|EMBL:RAO69091.1, ECO:0000313|Proteomes:UP000249363}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIB {ECO:0000313|EMBL:RAO69091.1,
RC ECO:0000313|Proteomes:UP000249363};
RX PubMed=28649280; DOI=10.1186/s13068-017-0844-7;
RA de Eugenio L.I., Mendez-Liter J.A., Nieto-Dominguez M., Alonso L.,
RA Gil-Munoz J., Barriuso J., Prieto A., Martinez M.J.;
RT "Differential ?-glucosidase expression as a function of carbon source
RT availability in Talaromyces amestolkiae: a genomic and proteomic
RT approach.";
RL Biotechnol. Biofuels 10:161-161(2017).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the XPG/RAD2 endonuclease family. XPG subfamily.
CC {ECO:0000256|ARBA:ARBA00005283}.
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:RAO69091.1}.
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DR EMBL; MIKG01000009; RAO69091.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A364L020; -.
DR STRING; 1196081.A0A364L020; -.
DR OrthoDB; 5479162at2759; -.
DR Proteomes; UP000249363; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004519; F:endonuclease activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003697; F:single-stranded DNA binding; IEA:InterPro.
DR GO; GO:0006289; P:nucleotide-excision repair; IEA:InterPro.
DR CDD; cd09904; H3TH_XPG; 1.
DR CDD; cd09868; PIN_XPG_RAD2; 2.
DR Gene3D; 6.10.140.100; -; 1.
DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR Gene3D; 3.40.50.1010; 5'-nuclease; 2.
DR InterPro; IPR036279; 5-3_exonuclease_C_sf.
DR InterPro; IPR008918; HhH2.
DR InterPro; IPR029060; PIN-like_dom_sf.
DR InterPro; IPR003903; UIM_dom.
DR InterPro; IPR006086; XPG-I_dom.
DR InterPro; IPR006084; XPG/Rad2.
DR InterPro; IPR001044; XPG/Rad2_eukaryotes.
DR InterPro; IPR019974; XPG_CS.
DR InterPro; IPR006085; XPG_DNA_repair_N.
DR PANTHER; PTHR16171:SF7; DNA EXCISION REPAIR PROTEIN ERCC-5; 1.
DR PANTHER; PTHR16171; DNA REPAIR PROTEIN COMPLEMENTING XP-G CELLS-RELATED; 1.
DR Pfam; PF00867; XPG_I; 1.
DR Pfam; PF00752; XPG_N; 1.
DR PRINTS; PR00853; XPGRADSUPER.
DR PRINTS; PR00066; XRODRMPGMNTG.
DR SMART; SM00279; HhH2; 1.
DR SMART; SM00726; UIM; 2.
DR SMART; SM00484; XPGI; 1.
DR SMART; SM00485; XPGN; 1.
DR SUPFAM; SSF47807; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR SUPFAM; SSF88723; PIN domain-like; 1.
DR PROSITE; PS50330; UIM; 1.
DR PROSITE; PS00841; XPG_1; 1.
DR PROSITE; PS00842; XPG_2; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000249363}.
FT DOMAIN 1..98
FT /note="XPG N-terminal"
FT /evidence="ECO:0000259|SMART:SM00485"
FT DOMAIN 833..902
FT /note="XPG-I"
FT /evidence="ECO:0000259|SMART:SM00484"
FT REGION 458..583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 646..726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1069..1121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 789..816
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 533..547
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..583
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 668..692
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 695..709
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1069..1112
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1121 AA; 126811 MW; F0C15535B46D2619 CRC64;
MGVTGLWTVV QPCARPVKLE TLNRKRLAVD ASIWIYQFLK AVRDKEGNAL RNAHVVGFFH
RICKLLFFGI KPVFVFDGGA PVLKRQTIAA RKKRREGRRE DAVRTAGKLL AIQIQRRAEE
EQAKRAAGDE DVEEQEPLGA PNYVDEILMT PQERMRNRKF RKQDQYHLPD LETDLSQMGA
PEDPRIMSQE ELEEYARQFH NGEDINLYDF SKIDFDSMFF MSLPATDRYN ILNAARIRSR
LRMGYSKEQL DSMFPDRMAF SKFQIERVKE RNDLTQRLMN LNGMNGADVA FDFNSGRRIA
GERGKEYVLV KNPDVEGGWA LGVVGNKEGS AVDRPIDVDE YGLPDVLPAK DDAFEDVPIE
GLNRLPKLPF LQKGVFDESV RRADMGRRNG LSTARQVQGE DEDEDALFFS APGDTDDLFA
DNEDEELQKA IAMSLEPHQE DHAGKAFPVE SKPTTAFDFE PELTPESDDE DMDFAAALAR
SKQSRPEPKP NSARPEVAPE YKFSGPLPFE SLKINKRAKE ELPQPAPLDD EAGGFEKPTE
SKQSKAKKKA AALPPWFSKE DGIKQDFIAD ETEEEPEKKS YDDVIFSQAA DLKRRSSPDI
IDLEETSNTK QVIDLESDVE AEEGIALDVE PIPEEKPVLM NDIAEDVRAN PPNPPVEITV
PHVPPKEDSV TDASEKAVSD WEPTDDERDA PLQTEMMNSV ASPAKGSTIK PKSPSPELED
EFEDVPLPPT AEEFPNNSVS TEHDAALFED QDHTVVGNDD YSDPEEEDLM LQLAAETEEH
ARFVSEFNNK TQIENARDFE QELKQLRNQQ KKDRRDADEV SQIMVSECQQ LLRLFGLPYI
TAPMEAEAQC AELVTLGLVD GIVTDDSDTF LFGGTRIYKN MFNQSKFVEC FLSSDLEKEY
ALDRVKLIQF AHLLGSDYTE GIPGVGPVTA LEIITEFDNL EEFRDWWMQV QMGMDIPNDP
HQGFRKKFKK MATKIFLPPS FPDRHIDEAY IQPEVDNDPS EFQWGVPDLN GLRSFLMATI
GWSQERTDEV LIPVIRDMNK REQEGTQSNI TRFMAGALGA GAFAPRVRAE GKSRMDKAFG
RLRSEAESRK RGPPRVDEAA QSEEEDSGSS RKKRKRKSQK K
//
