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Database: UniProt
Entry: A0A0A2LBC1_PENIT
LinkDB: A0A0A2LBC1_PENIT
Original site: A0A0A2LBC1_PENIT 
ID   A0A0A2LBC1_PENIT        Unreviewed;      1113 AA.
AC   A0A0A2LBC1;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   28-MAR-2018, entry version 21.
DE   SubName: Full=XPG/RAD2 endonuclease {ECO:0000313|EMBL:KGO76503.1};
GN   ORFNames=PITC_087820 {ECO:0000313|EMBL:KGO76503.1};
OS   Penicillium italicum (Blue mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=40296 {ECO:0000313|EMBL:KGO76503.1, ECO:0000313|Proteomes:UP000030104};
RN   [1] {ECO:0000313|EMBL:KGO76503.1, ECO:0000313|Proteomes:UP000030104}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PHI-1 {ECO:0000313|EMBL:KGO76503.1,
RC   ECO:0000313|Proteomes:UP000030104};
RX   PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA   Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA   Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L.,
RA   Gabaldon T.;
RT   "Genome, transcriptome, and functional analyses of Penicillium
RT   expansum provide new insights into secondary metabolism and
RT   pathogenicity.";
RL   Mol. Plant Microbe Interact. 28:232-248(2015).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|SAAS:SAAS00636245}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KGO76503.1}.
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DR   EMBL; JQGA01000243; KGO76503.1; -; Genomic_DNA.
DR   EnsemblFungi; KGO76503; KGO76503; PITC_087820.
DR   PhylomeDB; A0A0A2LBC1; -.
DR   Proteomes; UP000030104; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0003697; F:single-stranded DNA binding; IEA:InterPro.
DR   GO; GO:1901255; P:nucleotide-excision repair involved in interstrand cross-link repair; IEA:EnsemblFungi.
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   Pfam; PF02809; UIM; 2.
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; SSF47807; 2.
DR   SUPFAM; SSF88723; SSF88723; 2.
DR   PROSITE; PS00841; XPG_1; 1.
DR   PROSITE; PS00842; XPG_2; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000030104};
KW   Endonuclease {ECO:0000313|EMBL:KGO76503.1};
KW   Hydrolase {ECO:0000313|EMBL:KGO76503.1};
KW   Nuclease {ECO:0000313|EMBL:KGO76503.1};
KW   Nucleus {ECO:0000256|SAAS:SAAS00636222};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030104}.
FT   DOMAIN        1     98       XPGN. {ECO:0000259|SMART:SM00485}.
FT   DOMAIN      805    874       XPGI. {ECO:0000259|SMART:SM00484}.
FT   COILED      608    631       {ECO:0000256|SAM:Coils}.
FT   COILED      768    788       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   1113 AA;  126258 MW;  E54FC21D2F80B200 CRC64;
     MGVTGLWTVV QPCARPIKLE TLNKKRLAVD ASIWIYQFLK AVRDQEGNAL RNSHIVGFFR
     RICKLLYFGI RPVFVFDGGA PVMKRQTIAG RKKKREGHRE DAARTAGKLL AVQMQRSAEE
     EDARRRNKSQ RQEEEEVPDA PVYAEEAFMT ETEKQKSRKF KKKDAYHLPN LDVSLQDMGA
     PNDPRIMSQE ELEEYARHFH QGQDINLYDF SKIDFDSMFF LSLPPTDRYN ILNAARLRSR
     LRMGYSKEQL DTMFPDRMAF SKFQIDRVAE RNDLTQRLMN INGMNGEDAF YKSGQRIAGE
     RGREYVLVKD REHEGGWVLG VVGNREGHEE KPIDLDRPEI LSDEDEVSDE DEFEDVPIEG
     LNRLPKLPFL QEGLFDRSLQ LQTNENLDMR RAIQESRQTA QRQSANKHRV QEVEDDSLFV
     EAEGNIAQQQ NDDTDEFFDG DDDDLERAIA LSLQPDKIDD EDMPDIPIHR PVVSAPSYQM
     VPDVESESDD GMDFAAAIAR TKVSKKAPFA PNPFGGPLPF ESIKLTKVTK DNDKAGEIDK
     NAGGFVKEPT NKPKQADPLP PWFVGEPSDV GFIVDPIQDP EKDDEGSAAP DHLFLSNRRS
     PNIIDVDEVS ATKEVVDLEE EKEEKEEKEE EERPKHDLQV QEIEKIYNEI STNQDEKPVS
     ETALAPIDET LDGPSVRTEH SLSPEFEDVV SQLPTQGPEI TVVSDQKAQP QHRPQLFEEV
     NQLENFVQDQ ADYSDPEDEE LFKQLAAEGE EHVRFANTLN SAAPSQEAFD YEQELKQLRS
     QQRNERRDAD EVTTIMINEC QQLLALFGLP YITAPMEAEA QCAKLVSLGL VDGIVTDDSD
     VFLFGGTRVY KNMFNQSKFV ECYLTSDLEK EYALHRQKLI SFAHLLGSDY TEGIPGIGPV
     TALEILTEFS NLKEFRDWWT ELQMGTNNTE DSHLAFRKKF RKKASKIFLP PSFPDAKVDE
     AYLEPTVDDD PSQFQWGVPD LNGLRTFLMT TIGWSQERTD EVLVPVIRDM NRREQEGTQS
     NITQFMQGPQ GAGAFAPRVR TGGPSRMEMA FSRLRQEAQA GGTSLDGEQS TKNGESEEAS
     VSQKKGKRGG STTKAKTGAN KKRKTRRANS PES
//
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