ID A0A3F3PXZ0_9EURO Unreviewed; 932 AA.
AC A0A3F3PXZ0;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=Rad4 transglutaminase-like domain-domain-containing protein {ECO:0000313|EMBL:RDH31783.1};
GN ORFNames=BDQ94DRAFT_56800 {ECO:0000313|EMBL:RDH31783.1};
OS Aspergillus welwitschiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1341132 {ECO:0000313|EMBL:RDH31783.1, ECO:0000313|Proteomes:UP000253729};
RN [1] {ECO:0000313|EMBL:RDH31783.1, ECO:0000313|Proteomes:UP000253729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 139.54b {ECO:0000313|EMBL:RDH31783.1,
RC ECO:0000313|Proteomes:UP000253729};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (JUL-2018) 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; KZ852053; RDH31783.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3F3PXZ0; -.
DR STRING; 1341132.A0A3F3PXZ0; -.
DR OrthoDB; 181129at2759; -.
DR Proteomes; UP000253729; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:InterPro.
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; 3.30.70.2460; 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:SF2; DNA REPAIR PROTEIN RAD34; 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:UP000253729}.
FT DOMAIN 519..576
FT /note="Rad4 beta-hairpin"
FT /evidence="ECO:0000259|SMART:SM01030"
FT DOMAIN 578..641
FT /note="Rad4 beta-hairpin"
FT /evidence="ECO:0000259|SMART:SM01031"
FT DOMAIN 648..722
FT /note="Rad4 beta-hairpin"
FT /evidence="ECO:0000259|SMART:SM01032"
FT REGION 1..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 172..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 327..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 498..527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 763..932
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..67
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..355
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..523
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 763..790
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 800..826
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 836..856
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 899..913
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 932 AA; 104898 MW; C987E0E314C3308F CRC64;
MPPYVPRKRL SSEDPPAAKR RHATPPIAAV IEDTDTESSL SDVPEETETP QALDGSDEES
SDSDEVDWED AIESNANATP ATPSILNPDQ HQDLELTLDK NEIHLTDLLE GKKGPSKIER
QIRIQTHCLH VQFLLHHNAI RNVWANDSQL HEILRRKLPQ PIHKEVKKWR IASGLEAPEP
PPEKKSKKGK GKQRRQSERD WAEGSSRLEP GQPDMSSGDP IIILLKVLAA YWKSKFKITA
PGLRKQGYRP MAQLEAQIKS FQKDDHDPEK HGERIASIEE FRQAAENMQG SRDVGAQLFT
ALLRALDIEA RLVASLQPLG FGWTKSETYT TKPSADTEPS TENAETEDAI DVESDSSEDD
TKPARSKYFS KYDEDLPFPI YWTEVASPIT HQIIPVDPLI LRNPVATTPE LQAAFEPRGG
KAEKAKQVIC YVVAYSSDKT AKDVTTRYLR RRTWPGKTKG YRIPVEKIPI PGRKGKYYEV
DWFRVILRVY QRAQPQRTAV DDLEDTKDLL PNQPERKPGK EGDTLQSLRT STEFVLERFL
RREEALKPGA RHVRTFKTGK GAKAKEEKVF RRKDVLKCLS AESWHKEGRR PKAGEMPLKR
VPIRAVTLLR KREVDEFERQ NGEKPKQGLY AIHQTEYIIP DPICDGVIPK NEYGNIDCFV
PSMVPRGAVH IPWPGTVRVC KKLGVDYAEA VTGFEFGSKM AVPVIQGVVV AAENEDLVKD
AWLVDDAEKR KREQRKAEAR ILQTWRKFLF GLRIKQRVQE EYGGNADDGV DHERDAHNPF
TNRRDRLPDQ DASASASAPA HPEHDEEVHG GGFLLPGEDE DGADVDRGGG FLLPGQEGDD
HDDGGLIVDH HEQQQQHVST EPATPEVVDA EIADSDDDDD GKVENPISLS SDSELSSPVE
IPDSEESDAE SESDYEPEPR PTRRSTRRGG RR
//