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Database: UniProt
Entry: A0A068Y6X6_ECHMU
LinkDB: A0A068Y6X6_ECHMU
Original site: A0A068Y6X6_ECHMU 
ID   A0A068Y6X6_ECHMU        Unreviewed;       834 AA.
AC   A0A068Y6X6;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=Nucleotide excision repair protein {ECO:0000313|EMBL:CUT99350.1};
OS   Echinococcus multilocularis (Fox tapeworm).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC   Eucestoda; Cyclophyllidea; Taeniidae; Echinococcus.
OX   NCBI_TaxID=6211 {ECO:0000313|EMBL:CUT99350.1};
RN   [1] {ECO:0000313|EMBL:CUT99350.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23485966; DOI=10.1038/nature12031;
RA   Tsai I.J., Zarowiecki M., Holroyd N., Garciarrubio A., Sanchez-Flores A.,
RA   Brooks K.L., Tracey A., Bobes R.J., Fragoso G., Sciutto E., Aslett M.,
RA   Beasley H., Bennett H.M., Cai J., Camicia F., Clark R., Cucher M.,
RA   De Silva N., Day T.A., Deplazes P., Estrada K., Fernandez C., Holland P.W.,
RA   Hou J., Hu S., Huckvale T., Hung S.S., Kamenetzky L., Keane J.A., Kiss F.,
RA   Koziol U., Lambert O., Liu K., Luo X., Luo Y., Macchiaroli N., Nichol S.,
RA   Paps J., Parkinson J., Pouchkina-Stantcheva N., Riddiford N., Rosenzvit M.,
RA   Salinas G., Wasmuth J.D., Zamanian M., Zheng Y., Cai X., Soberon X.,
RA   Olson P.D., Laclette J.P., Brehm K., Berriman M., Garciarrubio A.,
RA   Bobes R.J., Fragoso G., Sanchez-Flores A., Estrada K., Cevallos M.A.,
RA   Morett E., Gonzalez V., Portillo T., Ochoa-Leyva A., Jose M.V., Sciutto E.,
RA   Landa A., Jimenez L., Valdes V., Carrero J.C., Larralde C.,
RA   Morales-Montor J., Limon-Lason J., Soberon X., Laclette J.P.;
RT   "The genomes of four tapeworm species reveal adaptations to parasitism.";
RL   Nature 496:57-63(2013).
RN   [2] {ECO:0000313|EMBL:CUT99350.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Zhang Y., Guo Z.;
RL   Submitted (NOV-2015) 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; LN902845; CUT99350.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A068Y6X6; -.
DR   STRING; 6211.A0A068Y6X6; -.
DR   eggNOG; KOG2179; Eukaryota.
DR   OMA; GRFANKA; -.
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; 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   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}.
FT   DOMAIN          488..548
FT                   /note="Rad4 beta-hairpin"
FT                   /evidence="ECO:0000259|SMART:SM01030"
FT   DOMAIN          550..608
FT                   /note="Rad4 beta-hairpin"
FT                   /evidence="ECO:0000259|SMART:SM01031"
FT   DOMAIN          615..690
FT                   /note="Rad4 beta-hairpin"
FT                   /evidence="ECO:0000259|SMART:SM01032"
FT   REGION          18..94
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          118..149
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          789..834
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        75..94
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        795..811
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        818..834
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   834 AA;  93214 MW;  E61AEC3D8B264318 CRC64;
     MPSLRTRRRV YKSQYFEKLS DSDAAVSSGD EFTPPPKLKS TPRSKTASRR NKSQSKAEPS
     NAASPIILDM KGRPLSRSNG KKKDNTEEDL TVTKLFRKFS RRSKKVKVEE APKEVVKVEE
     FSTDSEPSDA DGWEDVSNPP SDAEAKQAAS SHKEFEFLSQ LIQKPENGAT KVEDEGPLEI
     SVSALPRGRS SCKDPKALAA LALARQIRER ARTLHIFYVL EFLTFGRFAN KACDDAMIRA
     LALSLIVIPK SWDLAALQSL VHTFASLNHN GPKIKNPDIR EAIQTRLQVG STSAVDCALL
     MVAALRACGL DTRLVLAFAP PSLKPGTNTT ARGLKKLKPL GLSSRNSKII SSESEDEKQR
     LSSKYFFFGE VYLPSDEVWY SVDLSSPTGR VMADVSFPFT NFPYVVGFHS THCSYLGRTP
     IDLAPRYDPT WMSMSRDHRI PDPLWKKLLA TLRGHCDGDV VDLRAKDVGG MEEMRDAAGM
     ERIFDYLRSL PLPVKVQNFK GHPLYALRRH LLKFEVIYPP DAPVVGFLKV GGKASGVTEP
     VYPRECVHIC HTRESWLKEA KTIRLGEKPA KEVKAMMTMK RKLLQETNGP TPMVELFGPW
     QVEDYVPPVA ENGVVPRNEH GNVELFKPCM LPIGCVHIRL PGIQHTAKRL EIDAAPAMVG
     WTFHKAGWAH PEYDGFVVCR EVVPILVDAW REERMSAAVA AAVDRTERAL SNWKRLTRNL
     LLWQRIEAGF QLAKATVHAA PLPMSTGEVK KSSSSKPTLS DLPWQSLATA KPVFPRLLDV
     SDLVKAVPNA KPKLISKRSA RKPPRRKRRR QRQPSTSEDD EEEDEESFTS LDSD
//
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