ID W6KVX8_9TRYP Unreviewed; 394 AA.
AC W6KVX8;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=UV excision repair protein RAD23 {ECO:0000256|RuleBase:RU367049};
GN ORFNames=GSEM1_T00006352001 {ECO:0000313|EMBL:CCW61521.1};
OS Phytomonas sp. EM1.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Phytomonas.
OX NCBI_TaxID=479712 {ECO:0000313|EMBL:CCW61521.1, ECO:0000313|Proteomes:UP000027080};
RN [1] {ECO:0000313|EMBL:CCW61521.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=EM1 {ECO:0000313|EMBL:CCW61521.1};
RA Genoscope - CEA;
RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CCW61521.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EM1 {ECO:0000313|EMBL:CCW61521.1};
RX PubMed=24516393; DOI=10.1371/journal.pgen.1004007;
RA Porcel B.M., Denoeud F., Opperdoes F., Noel B., Madoui M.A.,
RA Hammarton T.C., Field M.C., Da Silva C., Couloux A., Poulain J.,
RA Katinka M., Jabbari K., Aury J.M., Campbell D.A., Cintron R., Dickens N.J.,
RA Docampo R., Sturm N.R., Koumandou V.L., Fabre S., Flegontov P., Lukes J.,
RA Michaeli S., Mottram J.C., Szoor B., Zilberstein D., Bringaud F.,
RA Wincker P., Dollet M.;
RT "The Streamlined Genome of Phytomonas spp. Relative to Human Pathogenic
RT Kinetoplastids Reveals a Parasite Tailored for Plants.";
RL PLoS Genet. 10:e1004007-e1004007(2014).
CC -!- FUNCTION: Multiubiquitin chain receptor involved in modulation of
CC proteasomal degradation. Involved in nucleotide excision repair.
CC {ECO:0000256|RuleBase:RU367049}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU367049}.
CC Cytoplasm {ECO:0000256|RuleBase:RU367049}.
CC -!- SIMILARITY: Belongs to the RAD23 family.
CC {ECO:0000256|RuleBase:RU367049}.
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DR EMBL; HF955065; CCW61521.1; -; Genomic_DNA.
DR AlphaFoldDB; W6KVX8; -.
DR EnsemblProtists; CCW61521; CCW61521; GSEM1_T00006352001.
DR OrthoDB; 158575at2759; -.
DR Proteomes; UP000027080; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003684; F:damaged DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; IEA:UniProtKB-UniRule.
DR GO; GO:0043130; F:ubiquitin binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006289; P:nucleotide-excision repair; IEA:UniProtKB-UniRule.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd14280; UBA1_Rad23_like; 1.
DR CDD; cd14281; UBA2_Rad23_like; 1.
DR CDD; cd01805; Ubl_Rad23; 1.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 2.
DR Gene3D; 1.10.10.540; XPC-binding domain; 1.
DR InterPro; IPR004806; Rad23.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR015360; XPC-bd.
DR InterPro; IPR036353; XPC-bd_sf.
DR PANTHER; PTHR10621; UV EXCISION REPAIR PROTEIN RAD23; 1.
DR PANTHER; PTHR10621:SF0; UV EXCISION REPAIR PROTEIN RAD23; 1.
DR Pfam; PF00627; UBA; 1.
DR Pfam; PF00240; ubiquitin; 1.
DR Pfam; PF09280; XPC-binding; 1.
DR PRINTS; PR01839; RAD23PROTEIN.
DR SMART; SM00165; UBA; 2.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF46934; UBA-like; 2.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR SUPFAM; SSF101238; XPC-binding domain; 1.
DR PROSITE; PS50030; UBA; 2.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|RuleBase:RU367049};
KW DNA damage {ECO:0000256|RuleBase:RU367049};
KW DNA repair {ECO:0000256|RuleBase:RU367049};
KW Nucleus {ECO:0000256|RuleBase:RU367049};
KW Reference proteome {ECO:0000313|Proteomes:UP000027080}.
FT DOMAIN 1..71
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS50053"
FT DOMAIN 134..181
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT DOMAIN 317..360
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT REGION 71..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 192..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..211
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 394 AA; 42131 MW; B6FF635116C40CD4 CRC64;
MKIFLKTITG KMQDLDVSAT TTILDIKKTL ESEYDISTLR LCYKGAILAD TVTVEDAKMA
ENATLIITGK KCSIPKPPQP SSPTTSGTIP SASADPTTHP GVSPEVQPSP QPIPEPRAAT
AAVAPTPLPP ARVNPDSTSD VSSGLIDGIV AMGFEDRAQV SLALRAAFMN PDRAVEYLCT
GIPPNLLREL SHPTQPVADP ATTPTPTSVA ATRSSNVLRA VSSVQPAPGA SELRTALWTI
PQFENIRAVF QSNQASFPVV IEQIRDRYPN IFQLIEANQE EFLQVMNETA GQPGNPMTTG
ASGNITDTVP VELQLTASDQ AAVQQLVELG AGMWDEQSAL MVYLATQRNQ EIAANVLFEN
GGIPPNLLEQ FAADLRHLGD EDNDEPGDME EEPK
//
