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Database: UniProt
Entry: A0A5N6G1F8_PETAA
LinkDB: A0A5N6G1F8_PETAA
Original site: A0A5N6G1F8_PETAA 
ID   A0A5N6G1F8_PETAA        Unreviewed;       906 AA.
AC   A0A5N6G1F8;
DT   22-APR-2020, integrated into UniProtKB/TrEMBL.
DT   22-APR-2020, sequence version 1.
DT   27-MAR-2024, entry version 10.
DE   SubName: Full=Rad4 transglutaminase-like domain-containing protein {ECO:0000313|EMBL:KAB8235355.1};
GN   ORFNames=BDW43DRAFT_31019 {ECO:0000313|EMBL:KAB8235355.1};
OS   Petromyces alliaceus (Aspergillus alliaceus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=209559 {ECO:0000313|EMBL:KAB8235355.1, ECO:0000313|Proteomes:UP000326931};
RN   [1] {ECO:0000313|EMBL:KAB8235355.1, ECO:0000313|Proteomes:UP000326931}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 536.65 {ECO:0000313|EMBL:KAB8235355.1,
RC   ECO:0000313|Proteomes:UP000326931};
RG   DOE Joint Genome Institute;
RA   Kjaerbolling I., Vesth T., Frisvad J.C., Nybo J.L., Theobald S.,
RA   Kildgaard S., Isbrandt T., Kuo A., Sato A., Lyhne E.K., Kogle M.E.,
RA   Wiebenga A., Kun R.S., Lubbers R.J., Makela M.R., Barry K., Chovatia M.,
RA   Clum A., Daum C., Haridas S., He G., LaButti K., Lipzen A., Mondo S.,
RA   Riley R., Salamov A., Simmons B.A., Magnuson J.K., Henrissat B.,
RA   Mortensen U.H., Larsen T.O., Devries R.P., Grigoriev I.V., Machida M.,
RA   Baker S.E., Andersen M.R.;
RT   "Friends and foes A comparative genomics study of 23 Aspergillus species
RT   from section Flavi.";
RL   Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
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; ML733071; KAB8235355.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5N6G1F8; -.
DR   OMA; TWPGKTK; -.
DR   OrthoDB; 181129at2759; -.
DR   Proteomes; UP000326931; Unassembled WGS sequence.
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:UP000326931}.
FT   DOMAIN          526..583
FT                   /note="Rad4 beta-hairpin"
FT                   /evidence="ECO:0000259|SMART:SM01030"
FT   DOMAIN          585..648
FT                   /note="Rad4 beta-hairpin"
FT                   /evidence="ECO:0000259|SMART:SM01031"
FT   DOMAIN          655..729
FT                   /note="Rad4 beta-hairpin"
FT                   /evidence="ECO:0000259|SMART:SM01032"
FT   REGION          1..90
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          178..224
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          338..376
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          768..906
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        61..75
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        349..365
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        768..784
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        864..883
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   906 AA;  102311 MW;  2A49D9C62BF360F0 CRC64;
     MPPFVPRKRL SSAEPPSAKR HNATAIPSVD IAALDDESDS PLSDVPSEST PQAQETKDEA
     GDESGSDDDE VDWEDAMESK ATSATAITPS MTPAHVQDLE LTLDQNEVHL SDIIDGKKAP
     SKIERQIRIH SHCLHVQFLL YHNALRNAWA NDSQVHETLR RKLPDALHKE VKKWKVSSGL
     ELPEKAPEDT TKEKKKKGKQ RRKPERDWGE GSSRMEPGQP DMSRGDPIIT LLKVLAAFWK
     KQFKITAPGL RKHGYRPMSH LEAQISAFNK EEHDPERFGE RVCGVDEFRQ AAERMEGSRD
     LGAQLFTALL RALAIEARLV ASLQPLGFGW TKAETSTQKA KVEAEVQTET GEAEDAMDVD
     SEDSDSDQDT LKRPNNLKKY DKDLPFPIYW TEVVSPITHQ IIPVDPLVLP NAVATTPELQ
     VAFEPRGAKA ERAKQVICYV VAFSSDKTAK DVTTRYLRRR TWPGKTKGYR MPVEKIPVPG
     RRGKFYEYNW FRVILRIYER PAKDRTAVDD YEENDLVPNQ PEKKAVKERD TLQSLRASTE
     FVLERFLRRE EALKPGSQHV RTFVTGKGNK AKEEKVYRRS DVLKCLSAES WHKEGRQIKK
     GEAPLKRVPI RAVTLLRKRE VDELERETGE KPKQGLYAKY QTEYIIPPPI HNGVIPKNDY
     GNIDCFVPSM VPRGAAHIPY PGTVRICKKL GIDYAEAVTG FEFGSKMAVP VIEGVVVAAE
     NEDLVKDAWR ADAAEKREKE RRKAEARILQ TWRKFLFGLR IAERVREEYG QSSLDHERDV
     HNPFTSRRSG QQQACPPVPE PYVHEPSEDE DPVDRGGGFL LPGEHDGDDG GLIVESHQPS
     RSVPRPVNEP DEQEIVGEEI PDMSSVQELS SPPQVSASDE QVSDSEPEYA PPTTRRRTRN
     VTRKGQ
//
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