ID A0A0K0JSB7_BRUMA Unreviewed; 332 AA.
AC A0A0K0JSB7;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=UV excision repair protein RAD23 {ECO:0000256|RuleBase:RU367049};
GN Name=bma-rad-23 {ECO:0000313|WormBase:Bm7416};
GN Synonyms=Bma-rad-23 {ECO:0000313|EMBL:CRZ23070.1,
GN ECO:0000313|WBParaSite:Bm7416.1};
GN ORFNames=Bm7416 {ECO:0000313|WormBase:Bm7416}, BM_Bm7416
GN {ECO:0000313|EMBL:CRZ23070.1};
OS Brugia malayi (Filarial nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Brugia.
OX NCBI_TaxID=6279 {ECO:0000313|EMBL:CRZ23070.1};
RN [1] {ECO:0000313|EMBL:CRZ23070.1, ECO:0000313|Proteomes:UP000006672}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FR3 {ECO:0000313|EMBL:CRZ23070.1,
RC ECO:0000313|Proteomes:UP000006672};
RX PubMed=17885136; DOI=10.1126/science.1145406;
RA Ghedin E., Wang S., Spiro D., Caler E., Zhao Q., Crabtree J., Allen J.E.,
RA Delcher A.L., Guiliano D.B., Miranda-Saavedra D., Angiuoli S.V., Creasy T.,
RA Amedeo P., Haas B., El-Sayed N.M., Wortman J.R., Feldblyum T., Tallon L.,
RA Schatz M., Shumway M., Koo H., Salzberg S.L., Schobel S., Pertea M.,
RA Pop M., White O., Barton G.J., Carlow C.K., Crawford M.J., Daub J.,
RA Dimmic M.W., Estes C.F., Foster J.M., Ganatra M., Gregory W.F.,
RA Johnson N.M., Jin J., Komuniecki R., Korf I., Kumar S., Laney S., Li B.W.,
RA Li W., Lindblom T.H., Lustigman S., Ma D., Maina C.V., Martin D.M.,
RA McCarter J.P., McReynolds L., Mitreva M., Nutman T.B., Parkinson J.,
RA Peregrin-Alvarez J.M., Poole C., Ren Q., Saunders L., Sluder A.E.,
RA Smith K., Stanke M., Unnasch T.R., Ware J., Wei A.D., Weil G.,
RA Williams D.J., Zhang Y., Williams S.A., Fraser-Liggett C., Slatko B.,
RA Blaxter M.L., Scott A.L.;
RT "Draft genome of the filarial nematode parasite Brugia malayi.";
RL Science 317:1756-1760(2007).
RN [2] {ECO:0000313|EMBL:CRZ23070.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FR3 {ECO:0000313|EMBL:CRZ23070.1};
RA Gao Y.W., Fan S.T., Sun H.T., Wang Z., Gao X.L., Li Y.G., Wang T.C.,
RA Zhang K., Xu W.W., Yu Z.J., Xia X.Z.;
RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|WBParaSite:Bm7416.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (DEC-2019) to UniProtKB.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LN856790; CRZ23070.1; -; Genomic_DNA.
DR STRING; 6279.A0A0K0JSB7; -.
DR EnsemblMetazoa; Bm7416.1; Bm7416.1; WBGene00227677.
DR WBParaSite; Bm7416.1; Bm7416.1; WBGene00227677.
DR WormBase; Bm7416; BM23943; WBGene00227677; Bma-rad-23.
DR OMA; PHMLEPI; -.
DR OrthoDB; 158575at2759; -.
DR Proteomes; UP000006672; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; cd14380; UBA2_Rad23; 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; IPR006636; STI1_HS-bd.
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; 2.
DR Pfam; PF00240; ubiquitin; 1.
DR Pfam; PF09280; XPC-binding; 1.
DR PRINTS; PR01839; RAD23PROTEIN.
DR SMART; SM00727; STI1; 1.
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|ARBA:ARBA00022763, ECO:0000256|RuleBase:RU367049};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|RuleBase:RU367049};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU367049};
KW Reference proteome {ECO:0000313|Proteomes:UP000006672};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 1..79
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS50053"
FT DOMAIN 124..164
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT DOMAIN 271..311
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT REGION 103..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 332 AA; 36125 MW; 1AB81172A4A5CB84 CRC64;
MLVTFKTIAQ VSFEIELDPH LTIGEVKAKI AEEKGEVEYP TECQKLIYNG KVLDDAQTVE
EVMIDPSKFV VVMIARKKPI GAPVESTPQP SNLQIPAGAQ VTTAPVSVAD SGPSTPQNPD
DLTPEQEETA QAIVAMGYPR DKVIRALRAS FFNGDRAVEY LCSGIPEEED LGGHQESAEH
EEGERAQGLG LDFLRQLPQF EQLRELVQSN PAILPQIIQQ IAQSNPALME AIQNNQEEFV
NLLNNGSVSS GGGGVAPSAG EQRQVAIHVT EAERDAINRL KSMGFPEQLV IEAYFACDKN
EDLAANYILA RMDEAAAELD ALEHQSEESH GP
//
