ID A0A061ENL1_THECC Unreviewed; 974 AA.
AC A0A061ENL1;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE SubName: Full=DNA repair protein xp-C / rad4, putative isoform 1 {ECO:0000313|EMBL:EOY03914.1};
GN ORFNames=TCM_019127 {ECO:0000313|EMBL:EOY03914.1};
OS Theobroma cacao (Cacao) (Cocoa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Byttnerioideae; Theobroma.
OX NCBI_TaxID=3641 {ECO:0000313|EMBL:EOY03914.1, ECO:0000313|Proteomes:UP000026915};
RN [1] {ECO:0000313|EMBL:EOY03914.1, ECO:0000313|Proteomes:UP000026915}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Matina 1-6 {ECO:0000313|Proteomes:UP000026915};
RX PubMed=23731509; DOI=10.1186/gb-2013-14-6-r53;
RA Motamayor J.C., Mockaitis K., Schmutz J., Haiminen N., Iii D.L.,
RA Cornejo O., Findley S.D., Zheng P., Utro F., Royaert S., Saski C.,
RA Jenkins J., Podicheti R., Zhao M., Scheffler B.E., Stack J.C., Feltus F.A.,
RA Mustiga G.M., Amores F., Phillips W., Marelli J.P., May G.D., Shapiro H.,
RA Ma J., Bustamante C.D., Schnell R.J., Main D., Gilbert D., Parida L.,
RA Kuhn D.N.;
RT "The genome sequence of the most widely cultivated cacao type and its use
RT to identify candidate genes regulating pod color.";
RL Genome Biol. 14:R53.1-R53.24(2013).
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; CM001882; EOY03914.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A061ENL1; -.
DR STRING; 3641.A0A061ENL1; -.
DR EnsemblPlants; EOY03914; EOY03914; TCM_019127.
DR Gramene; EOY03914; EOY03914; TCM_019127.
DR eggNOG; KOG2179; Eukaryota.
DR InParanoid; A0A061ENL1; -.
DR OMA; FQAKHLG; -.
DR Proteomes; UP000026915; Chromosome 4.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0000111; C:nucleotide-excision repair factor 2 complex; IBA:GO_Central.
DR GO; GO:0071942; C:XPC complex; IBA:GO_Central.
DR GO; GO:0003684; F:damaged DNA binding; IBA:GO_Central.
DR GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0006298; P:mismatch repair; IBA:GO_Central.
DR GO; GO:0006289; P:nucleotide-excision repair; IBA:GO_Central.
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:UP000026915}.
FT DOMAIN 648..699
FT /note="Rad4 beta-hairpin"
FT /evidence="ECO:0000259|SMART:SM01030"
FT DOMAIN 701..764
FT /note="Rad4 beta-hairpin"
FT /evidence="ECO:0000259|SMART:SM01031"
FT DOMAIN 771..845
FT /note="Rad4 beta-hairpin"
FT /evidence="ECO:0000259|SMART:SM01032"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 106..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 887..927
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..55
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..125
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 887..904
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 905..921
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 974 AA; 107530 MW; D5C073206ABB4E63 CRC64;
MKVTCESDNG NPSGSIHDAG TLAGISQEGV NKLLRRANRR GSSRKEEKNE YLQKNDPKTN
EQVVHTMIVQ NASMAEGCSR NAVGSSQLEV DVGSYVDNLF DDSEDMNDSD WEDGSIPKLD
PVDNSPKERM KGLTIEFDEP SGSAGRKPVR RASAEDKEIA ELVHKVHLLC LLARGRLIDN
ACDDPLIQAS LLSLVPTHLS KISGVSNITS NALSPLVTWF HNNFHVRSLV RAERSFHTAL
AFALETREGT PEEIAALSVA LFRALKFTAR FVSILDVASL KPEADKCEPS SQEANRVGGG
IFSTSTLMVA NPKEVSSSSY PVKSFSCSEK DGHCENSLRS SCKSKGGCPT SNDTQSRYST
AVDEVTDRTS NLFACQAQLD TYGQCAPTKS QGLKRKGDLE FEMQLAMAIS ATTVGTLENS
AGSLDVSNFN GNNSLDASTP SKRWKKIHRV ESATSSQGLS TALGSRKVGS PLFWAEVYCG
GENLTGKWVH VDALNAIIDG EQKVEDAAAA CKTALRYVVA FAGRGAKDVT RRYCMKWYKI
APKRVNSIWW DAVLAPLREL ESGATGGTIN MEKLHNNASN EQEKIKASGM SEYPGTDSPS
NHVILPEKSG QEAFKEYGSK SEVESSTKHS LVATRNSLED MELETRALTE PLPTNQQAYK
NHALYALERW LTKCQILHPR GPILGYCSGH PVYPRTCVQT LKPRERWLRE GLQVKGNEIP
AKVLKRSAKL KKVQVSEEDD YEEIDSKGTI ELYGKWQLEP LCLPHAVDGI VPKNERGQVD
VWSEKCLPPG TVHLRLPRVF SVAKRLEIDY APAMVGFEFR NGRAAPIFDG IVVCSEFKDA
ILEAYAEEEE RRVAEEKKRN EAQAISRWYQ LLSSIITRQK LKSYYGDGSS SQASRNIQDK
NNEINAPDES SKDDRQSTGL WKGDGEDTLC NIPSGTLVED HEHVFLRENE SFDAENSVRT
KRCHCGFSIQ VEEL
//