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Database: UniProt
Entry: A0A178Z5H7_9EURO
LinkDB: A0A178Z5H7_9EURO
Original site: A0A178Z5H7_9EURO 
ID   A0A178Z5H7_9EURO        Unreviewed;      1089 AA.
AC   A0A178Z5H7;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Rad4 beta-hairpin domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=AYL99_11164 {ECO:0000313|EMBL:OAP54716.1};
OS   Fonsecaea erecta.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX   NCBI_TaxID=1367422 {ECO:0000313|EMBL:OAP54716.1, ECO:0000313|Proteomes:UP000078343};
RN   [1] {ECO:0000313|EMBL:OAP54716.1, ECO:0000313|Proteomes:UP000078343}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 125763 {ECO:0000313|EMBL:OAP54716.1,
RC   ECO:0000313|Proteomes:UP000078343};
RA   Weiss V.A., Vicente V.A., Raittz R.T., Moreno L.F., De Souza E.M.,
RA   Pedrosa F.O., Steffens M.B., Faoro H., Tadra-Sfeir M.Z., Najafzadeh M.J.,
RA   Felipe M.S., Teixeira M., Sun J., Xi L., Gomes R., De Azevedo C.M.,
RA   Salgado C.G., Da Silva M.B., Nascimento M.F., Queiroz-Telles F.,
RA   Attili D.S., Gorbushina A.;
RT   "Draft genome of Fonsecaea erecta CBS 125763.";
RL   Submitted (APR-2016) 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}.
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:OAP54716.1}.
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DR   EMBL; LVYI01000013; OAP54716.1; -; Genomic_DNA.
DR   RefSeq; XP_018688083.1; XM_018842670.1.
DR   AlphaFoldDB; A0A178Z5H7; -.
DR   STRING; 1367422.A0A178Z5H7; -.
DR   GeneID; 30015332; -.
DR   OrthoDB; 181129at2759; -.
DR   Proteomes; UP000078343; 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:SF3; DNA REPAIR PROTEIN RAD4; 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:UP000078343}.
FT   DOMAIN          480..538
FT                   /note="Rad4 beta-hairpin"
FT                   /evidence="ECO:0000259|SMART:SM01030"
FT   DOMAIN          540..603
FT                   /note="Rad4 beta-hairpin"
FT                   /evidence="ECO:0000259|SMART:SM01031"
FT   DOMAIN          610..684
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          723..759
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          823..899
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          920..1089
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        51..67
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        998..1033
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1034..1048
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1089 AA;  120487 MW;  C980A4532D60D774 CRC64;
     MPRRKGQPTA RATRTTRRSA RQRKEPQDDI PEIYGDMLAE AIAEEQASAS NSRASKRRKM
     SEEPSTKIEL DFDLFGSAAN VHDGEETASA DDAPPKLQPV VFDDFEISDE SDAEFEDVDL
     EPATNDVAEG RPLEQKTLEL DLSKTSTPRR AIQRRMPVSL AERKLRLDVH KAHLVLLLAH
     LKCRNRWCNS EFVHSILKPL VSRKLISLLH VDESKPQFQR SHSFTKGIEE VCALWRQQWK
     ITARGMKRAH WREDVDAVKE SEDAEDLIDF DDFKAAAISR SGSRDLGAQL FCALLRSVAV
     DARLVCSLQV LPFSGIAKGQ TPEKPKPQYI YAPAQDYGSA SHDGRVNMRP AGAPDPKRKR
     IVESPFPIFW VEVFSPSVQT WIPLDPLVRN TINKPKTGFE PPASDQLNSM IYVVAFEDDE
     SARDVTRRYT QWYNAKTRKQ RVESTKGGEK WWEVTMSVFE KPFSETRDEI EDATLLKRAE
     SEPMPKNIQD FRGHPVYVLE RHLRLNEVIH PRHEVGKVST GPLKSAKLES VFRRRDVHVC
     RTADAWYRRG RDVNQGEQPL KRVVPKRQRN QDVAMAEDLE NEDEASEGMA LYAEYQTSVY
     EPPPVVDEKI PRNAYGNLDV YVPSMIPAGA VHIRHPLASA AARVLGIDYA EAVTGFQFKG
     RQGTAVIDGV VVSMNMTNAM INVIEGLESQ ASEEIQEART KIILAMWKKW LTALRVHEHV
     HRHYGNQKHG TGDKGNDDDD DDDAEEDTMH RDEEGGGGFM LDQAELDQSE ENANSVPLTT
     PNLKPLGQLL PAEVVHQDVI VIRSPNKLKQ LPLSDLLRSH DRVTEETPHE TSDAGGGFIS
     EDGMVDQSPP HREGHEHAPS VRQNLANDEG GGFIPDEAED DQGGGFLPED EDGDGEPHAR
     FITAHDGWIT NTEDTMGMLS SETEHASTKE RLDSTSASAG AGAGSGAENA TAAGAGDSSA
     KPRSISTAGG RGLSRSGKED PATSTTRSRH IPDTDMVAPS DQSPSRPMNN TATLEPDHPF
     SGSGQTTTTD QGDGGDETGD RFEAAHGPEL QRSESGTTPA SVAGSLLSHD PEDDDAEPEW
     LLSSLGEID
//
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