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
//