ID Q2UEU2_ASPOR Unreviewed; 919 AA.
AC Q2UEU2;
DT 24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:BAE59923.1};
GN ORFNames=AO090026000480 {ECO:0000313|EMBL:BAE59923.1};
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516 {ECO:0000313|EMBL:BAE59923.1, ECO:0000313|Proteomes:UP000006564};
RN [1] {ECO:0000313|EMBL:BAE59923.1, ECO:0000313|Proteomes:UP000006564}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40 {ECO:0000313|Proteomes:UP000006564};
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the XPC family. {ECO:0000256|ARBA:ARBA00009525}.
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DR EMBL; AP007159; BAE59923.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2UEU2; -.
DR STRING; 510516.Q2UEU2; -.
DR EnsemblFungi; BAE59923; BAE59923; AO090026000480.
DR VEuPathDB; FungiDB:AO090026000480; -.
DR HOGENOM; CLU_003639_0_1_1; -.
DR OMA; TWPGKTK; -.
DR OrthoDB; 181129at2759; -.
DR Proteomes; UP000006564; Chromosome 3.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR GO; GO:0006289; P:nucleotide-excision repair; IEA:InterPro.
DR Gene3D; 2.20.20.110; Rad4, beta-hairpin domain BHD1; 1.
DR Gene3D; 3.30.60.290; Rad4, beta-hairpin domain BHD2; 1.
DR Gene3D; 3.30.70.2460; Rad4, beta-hairpin domain BHD3; 1.
DR Gene3D; 3.90.260.10; Transglutaminase-like; 1.
DR InterPro; IPR018327; BHD_2.
DR InterPro; IPR004583; DNA_repair_Rad4.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR018325; Rad4/PNGase_transGLS-fold.
DR InterPro; IPR018326; Rad4_beta-hairpin_dom1.
DR InterPro; IPR018328; Rad4_beta-hairpin_dom3.
DR InterPro; IPR042488; Rad4_BHD3_sf.
DR InterPro; IPR036985; Transglutaminase-like_sf.
DR PANTHER; PTHR12135:SF0; DNA REPAIR PROTEIN COMPLEMENTING XP-C CELLS; 1.
DR PANTHER; PTHR12135; DNA REPAIR PROTEIN XP-C / RAD4; 1.
DR Pfam; PF10403; BHD_1; 1.
DR Pfam; PF10404; BHD_2; 1.
DR Pfam; PF10405; BHD_3; 1.
DR Pfam; PF03835; Rad4; 1.
DR SMART; SM01030; BHD_1; 1.
DR SMART; SM01031; BHD_2; 1.
DR SMART; SM01032; BHD_3; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000006564}.
FT DOMAIN 522..579
FT /note="Rad4 beta-hairpin"
FT /evidence="ECO:0000259|SMART:SM01030"
FT DOMAIN 581..644
FT /note="Rad4 beta-hairpin"
FT /evidence="ECO:0000259|SMART:SM01031"
FT DOMAIN 651..725
FT /note="Rad4 beta-hairpin"
FT /evidence="ECO:0000259|SMART:SM01032"
FT REGION 1..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 181..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 346..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 509..528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 764..910
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..73
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..526
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 764..779
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 823..844
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 871..890
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 919 AA; 102956 MW; 1AA06E014E604B6A CRC64;
MPPFVPRKRL SSADPPSAKR HNATAAPSVD IAALDDESDS PLSDVPSEAA LQDQDLEDEA
SDESESDDDE VDWEDAMDSK ATTATATTPS MTPAHVQDLE LTLDKNEVHL SDIIDGKKAP
SKIERQIRVL THCLHVQFLL HHNAIRNAWA NDSQVHDILR RKLPEALYKE VKKWKVSSGL
ELPEKPPEET TKKKKWKQRR KSERDWGEGS SRMEPGQPDM SRGDPIITLL KVLAAYWKKQ
FKITAPGLRK RGYRPMSHLE ADISAFNKEE HDPERFGEKV CGIEEFRQAA ERMEGSRDLG
AQLFTALLRA LSIEARLVAS LQPLGFGWTK AETYTPKVKV EAEAQTEIGD TEDADSDDSD
VVQKPVGSIT NPKGYDKDLP VPIYWTEVAS PVTHQIIPVD PLVLPNAVAT TPELQAAFEP
RGAKAEKAKQ VICYVIAYSS DKTAKDVTTR YLRRRTWPGK TKGYRMPVEK IPVPGRRGKF
HEYNWFRVIL RIYERSTKSR TAVDDLEDAN DLVPNQPEKK SAKEGDTLQS LKASTEFVLE
RFLRREEALK PGSQHVRTFV SGKGIKAKEE KIYRRADVLK CLSAESWHKE GRQIKKGEAP
LKRVPIRAVT LLRKREVDEL ERETGEKPKQ GLYAKYQTEY IIPPPIRNGV IPKNDYGNID
CFVPSMVPRG ATHIPWPGTV RICKKLGIDY AEAVTGFEFG SKMAVPVIEG VVIASENEDL
VKDAWRADAA EKREKERRKA EARILQTWRK FLFGLRIAER VREEYGESSR DHERDAYNPF
TSRKSGQQAP APEPHVREPS EEGDPVDYGG GFLLPGEDDG DDGDLIVERH QPSQPERENE
VAAAAESDDA AVMEMEISDT SSVQELSSSP EIADSEDELP DSEPESEESC SEGELDRPIE
SSASDVTLPE GVLLVVASC
//
