ID A0A010RFK9_9PEZI Unreviewed; 1053 AA.
AC A0A010RFK9;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Rad4 transglutaminase-like domain-containing protein {ECO:0000313|EMBL:EXF76579.1};
GN ORFNames=CFIO01_12609 {ECO:0000313|EMBL:EXF76579.1};
OS Colletotrichum fioriniae PJ7.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum acutatum species complex.
OX NCBI_TaxID=1445577 {ECO:0000313|EMBL:EXF76579.1, ECO:0000313|Proteomes:UP000020467};
RN [1] {ECO:0000313|EMBL:EXF76579.1, ECO:0000313|Proteomes:UP000020467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PJ7 {ECO:0000313|EMBL:EXF76579.1,
RC ECO:0000313|Proteomes:UP000020467};
RA Baroncelli R., Thon M.R.;
RT "The genome sequence of Colletotrichum fioriniae PJ7.";
RL Submitted (FEB-2014) 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:EXF76579.1}.
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DR EMBL; JARH01000826; EXF76579.1; -; Genomic_DNA.
DR RefSeq; XP_007599774.1; XM_007599712.1.
DR AlphaFoldDB; A0A010RFK9; -.
DR STRING; 1445577.A0A010RFK9; -.
DR KEGG; cfj:CFIO01_12609; -.
DR eggNOG; KOG2179; Eukaryota.
DR HOGENOM; CLU_003639_0_2_1; -.
DR OrthoDB; 181129at2759; -.
DR Proteomes; UP000020467; 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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000020467}.
FT DOMAIN 633..692
FT /note="Rad4 beta-hairpin"
FT /evidence="ECO:0000259|SMART:SM01030"
FT DOMAIN 694..757
FT /note="Rad4 beta-hairpin"
FT /evidence="ECO:0000259|SMART:SM01031"
FT DOMAIN 764..838
FT /note="Rad4 beta-hairpin"
FT /evidence="ECO:0000259|SMART:SM01032"
FT REGION 1..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 207..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 371..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 605..638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 928..1053
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 831..860
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 894..921
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..20
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..76
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..443
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 606..638
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 963..979
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1008..1025
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1033..1053
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1053 AA; 118022 MW; C6D312A3F250A1B6 CRC64;
MPPHVPRKRL REESPVKQTP KRQRVTKGQG KTPASSGRRK PTLYDDLDAT TTSESSKVGR
AALDTISDSD ETSSLSDLSD GDFEDVPLAN GRKAEEASDE DDNDDIEFED VPAPRTTLAV
APTTSKDLQL TLDAGLGTAM TDPYGDKKGP TKREKKIRNV THCIHVQYLL WHNAIRNSWI
SDQEVQAIMM SHVPPRLWEE VERWRRTSGL DTKPKQPPTK AAKSAKKTRG KGKGKKTEDE
DSRDWGAAAE RLEAGAVDMS HGDPLFRLMR ALVAWWRQRF RVTAPGIRKW GYMSPERLGR
LRKAWEREGK DEEKFGEQIN GLEGFRKCAQ ECTGSRDVGS QLFTALMRAL GLQARMVANL
QPVGFGWTKL EEADPEMEKN ATSAPKSSDE ASEAADGTRG KAKRGTKKTT TKNAPVKKTS
KQAPKAASGR KTGTRQASNK SAVIEIDDSD DELGLEHPDS DDASVVELAV TPRKSTAALK
KFDKDLEFPH YWTEVLSPVT KKYLPADPIV KNIVGTNREL VESLEPRGGK AEKAKQVMAY
VVGFSPDGTA KDVTVRYLRK QLWPGRTKGA RMPLEKVPIY NRHGKVKRYG QFDWFKLAMK
GYAKGSRKHP LTEEDDVEDS TDLKPAQPEK KEVKEGSETM AYYKQSKEFC LERHMKREEA
LLPTAEPVKT FHHKGKGGEI SPEPVYSRKD VVNVKSAETW HKQGRAPKPG EMPLKRVPYR
AATTNRRREI AEAEAASGEK VLQGLYSFEQ TEWIIPPPIK DGIIPKNNYG NIDLFAEHMC
PEGAAHVPFR GAVKVCKRLA IDYAEAVVDF EFGNRMAVPV IQGVVIAEEY HDQVMEEIRK
DEAERARKED EKRRKAALSM WSKFLKGLRI VERIRQDYGH VDDSVPVFQK HGAAKATKNA
HADEEEDKNQ LDAEAMQMRE EEMAGGFFPE GHDEEEVEQP KRFTSGFFPV VDENDEDEDM
DDALQVDHGH VEKSHAVNGS DGAEDAGNAE DQMEASPEPG PLPAPVKAKP KPKKKAVARR
SSRRRRRPIS ESEDEDEEED DDDDFVASDD DYE
//
