GenomeNet

Database: UniProt
Entry: A0A0N0NLX1_9EURO
LinkDB: A0A0N0NLX1_9EURO
Original site: A0A0N0NLX1_9EURO 
ID   A0A0N0NLX1_9EURO        Unreviewed;      1366 AA.
AC   A0A0N0NLX1;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   SubName: Full=DNA repair protein rad13 {ECO:0000313|EMBL:KPI39791.1};
GN   ORFNames=AB675_3484 {ECO:0000313|EMBL:KPI39791.1};
OS   Phialophora attinorum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Phialophora.
OX   NCBI_TaxID=1664694 {ECO:0000313|EMBL:KPI39791.1, ECO:0000313|Proteomes:UP000038010};
RN   [1] {ECO:0000313|EMBL:KPI39791.1, ECO:0000313|Proteomes:UP000038010}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 131958 {ECO:0000313|EMBL:KPI39791.1,
RC   ECO:0000313|Proteomes:UP000038010};
RA   Moreno L.F., Stielow B.J., de Hoog S., Vicente V.A., Weiss V.A.,
RA   de Vries M., Cruz L.M., Souza E.M.;
RT   "Draft genome of the ant-associated black yeast Phialophora attae CBS
RT   131958.";
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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:KPI39791.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LFJN01000014; KPI39791.1; -; Genomic_DNA.
DR   RefSeq; XP_017999754.1; XM_018143537.1.
DR   STRING; 1664694.A0A0N0NLX1; -.
DR   GeneID; 28735417; -.
DR   OrthoDB; 5479162at2759; -.
DR   Proteomes; UP000038010; 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; 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   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000038010}.
FT   DOMAIN          1..98
FT                   /note="XPG N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00485"
FT   DOMAIN          958..1027
FT                   /note="XPG-I"
FT                   /evidence="ECO:0000259|SMART:SM00484"
FT   REGION          121..144
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          429..874
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1243..1366
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          914..941
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        121..138
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        434..449
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        450..467
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        475..494
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        605..632
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        649..664
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        669..711
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        818..834
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1262..1278
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1295..1329
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1366 AA;  152392 MW;  D00FF9D75C634419 CRC64;
     MGVTNLWTVV SPTARPTSLA SLNRKRLAVD ASIWIYQFLK AVRDKEGNAL RNSHVVGFFR
     RICKLLYFGI KPVFVFDGGA PVLKRETVRK RRSRREGRRE DAVRTAGKLL AVQMERVVEE
     EREKERRRRE RGRDVEDEDR EEDVGDEGQL VYVDEIGMGE AERRKGRAEG FKRRDQYHLP
     DLDVRIEDMG APNDPRIMSQ VELEEYARQF HSGEDINLYD FSKIDFESPF FLSLPAGDRY
     NILNAARLRS RLRMGYTKDQ LNGMFPDRMA FSKFQIERVK ERNELTQRLM HINGMADDWD
     SGGRIAGEKG KEYVLVRNEG VEGGWALGVV SNKLGTSKGM AIDVDEEYGD QVKSEEESDE
     FEDVEIEGLN RLPKSWKRKR ARSVDYDYSY EDAAEQIAKK RKAVYDGRKA AAQNPPPRTA
     PVVAVNGEDD PLFVPQEQPD EDDDLFEDVD IGHANDADAE DDLQKAIAMS LEDATGEGDD
     TRNGHTKLVS DDEDDMFGAA LAASRKSKPK AQKNGKELSK TALTGAAPNF SGPLPFESMN
     LGQSLLGKKK AKKVEENLSG GFDRNLGEDA FRKERPPQPA PSWFDAAPKT KDMKRMEDAD
     DGEDGEDHVT HNDQDRSRRE VLHRHPTREV IDLEAEGSTQ PKPSQIELSS DDDDDDDAEL
     PQEPQAEPDD WQLPEHEEVK DDIRRQRERD AEEEAREARY AMAREIAGES DMPDEVLPPA
     VPQVEPAKDV ILQPEGQEVP AMDEVADRVR ENPPSPTSQP NYIPSPKPAE DLPQQADADE
     DMVEWSASEP NSPLFVPAQA EDDDDEFEDV PMNGVQPPTL LYQESTNEAS TMPLDANQYL
     MPDEDEQPSA NDANANDPRD ISAGPTEPQI DDDFSDSDEE LMRQLANEVE EHARFTSALT
     NPHKQTSAST SNGATATDAA LRDYEQELKQ LRSQQKSNLR DADEVTQTMI TECQSLLSLF
     GLPYITAPME AEAQCAELVR LGLVDGIVTD DSDIFLFGGT RIYKNMFNAQ KFVECYLASD
     LEKEYTLTRE KLIQFAHLLG SDYTEGVPGV GPVTALEILT DFPSLTEFAE WVTAVQRAVV
     SPHPATALDG LLGTPFRRKF KSQATKKLFL PNGFPDLRVD KAYLEPEVDS DPSQFQWGVP
     DLEKLRSFLM ATIGWTQERT DEVLVPVIRD MNKREKEGTQ ANITRWFEGG VGVGGDTRGR
     VRAGGANAAA AAAAEDTAAG LGQRNRTGAE SGRMKNAFKR LRGEAERKRR GLDDDYDEEV
     DGDARVDRAE KADDIEATAE QNGSDIADEV ESLTADDSAA PKKKKEAGRS RATTSRKAKK
     AASSDDASHD DEEGTADDES YQPSSGRKKQ LPGRARGGGR RKAKAV
//
DBGET integrated database retrieval system