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Database: UniProt
Entry: A0A0J8RHL2_COCIT
LinkDB: A0A0J8RHL2_COCIT
Original site: A0A0J8RHL2_COCIT 
ID   A0A0J8RHL2_COCIT        Unreviewed;       844 AA.
AC   A0A0J8RHL2;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=DNA repair protein rhp42 {ECO:0000313|EMBL:KMU84106.1};
GN   ORFNames=CIHG_01892 {ECO:0000313|EMBL:KMU84106.1};
OS   Coccidioides immitis H538.4.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX   NCBI_TaxID=396776 {ECO:0000313|EMBL:KMU84106.1, ECO:0000313|Proteomes:UP000054563};
RN   [1] {ECO:0000313|Proteomes:UP000054563}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H538.4 {ECO:0000313|Proteomes:UP000054563};
RX   PubMed=20516208; DOI=10.1101/gr.103911.109;
RA   Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA   Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA   Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA   FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA   Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA   Taylor J.W., Rounsley S.D.;
RT   "Population genomic sequencing of Coccidioides fungi reveals recent
RT   hybridization and transposon control.";
RL   Genome Res. 20:938-946(2010).
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; DS016984; KMU84106.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0J8RHL2; -.
DR   STRING; 396776.A0A0J8RHL2; -.
DR   VEuPathDB; FungiDB:CIHG_01892; -.
DR   eggNOG; KOG2179; Eukaryota.
DR   Proteomes; UP000054563; 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; 3.30.70.2460; 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:UP000054563}.
FT   DOMAIN          516..573
FT                   /note="Rad4 beta-hairpin"
FT                   /evidence="ECO:0000259|SMART:SM01030"
FT   DOMAIN          575..638
FT                   /note="Rad4 beta-hairpin"
FT                   /evidence="ECO:0000259|SMART:SM01031"
FT   DOMAIN          645..719
FT                   /note="Rad4 beta-hairpin"
FT                   /evidence="ECO:0000259|SMART:SM01032"
FT   REGION          1..75
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          179..214
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          333..375
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          787..844
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        43..64
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        187..207
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        787..814
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   844 AA;  95874 MW;  18FB19B9AD6AD48B CRC64;
     MPPFVPRKDH STQDTPSKRG LLEALDTPPK SATLEKLKAQ KISLESDSSS LSSLSSSDLE
     NSANSAGVDD DDDDEEVNWE DVLGAPSGSN AAPTPELRDL DITIQKNHVS LTEPLGGKKG
     PSKIERFIRI QTHCMHVQFL LFHNAIRNWW INDPEIHEIL REKLPEGIKK EIQRWRIAAG
     LETPKPTPKE SSKKRKRDRD WTEDSSYVEP NRPDLSRGDP TIHLLKVLAA YWKKHFKITS
     PGLHKRGYRP ASVLEEELRA FNRGEEDENR FGEKIQDLNE FREHARRLYG SRDVGSQLFT
     ALLRALGLET RLVASLQPIG FGWAKIEKYA SADETAPNSP VESEESSLDE ELPPRPKGKS
     KISNKRQQLA DGDSPFPTYW SEVESPVTQE IIPVESLILP NSVAMTPELL AAFEPRGAKA
     EKAKQVIAYV VAYSPDATAK DVTIRYLRRQ TWPGKTKGFR IPVEKPVEIE LSTGPYVYDW
     FKATMRGYIR PRDKRTTVDE KEDLSLVAKQ PEKKAPKEGD TLQSLKASKD FVLERFLRRE
     EALRPGASHV RMFISGKGAK QKEEKVYRRS DVQKCLSAES WHKEGRRIKL GELPLKLVPI
     RAVTRNRKLE VDRMERETGE KPKQGLYALH QTEYIIPDPI QDGIIPKNEY GNIDCFTPWM
     VPKGAVHIPW PATVRVCKKL RVDYAEAVIG FEFSSKMAVP IIQGVVVAAE NEDLVKDAWR
     AEDAQRRERE RLKQEKLILT TWRKFIMGLR ISERIQEEYG DTIEMESQNP FVNQRNIIPS
     DVQPVDRDEA DYHDGGGFLV PGEDEPEHDQ LGIQAQPRKV EGSREVPIAL DNDTSEELSD
     IESV
//
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