ID A0A199UM92_ANACO Unreviewed; 392 AA.
AC A0A199UM92;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Ubiquitin receptor RAD23 {ECO:0000256|RuleBase:RU367049};
DE AltName: Full=DNA repair protein RAD23 {ECO:0000256|RuleBase:RU367049};
GN Name=LOC109711299 {ECO:0000313|RefSeq:XP_020089855.1};
GN ORFNames=ACMD2_00917 {ECO:0000313|EMBL:OAY65801.1};
OS Ananas comosus (Pineapple) (Ananas ananas).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Bromeliaceae;
OC Bromelioideae; Ananas.
OX NCBI_TaxID=4615 {ECO:0000313|EMBL:OAY65801.1, ECO:0000313|Proteomes:UP000092600};
RN [1] {ECO:0000313|EMBL:OAY65801.1, ECO:0000313|Proteomes:UP000092600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. MD2 {ECO:0000313|Proteomes:UP000092600};
RC TISSUE=Leaf {ECO:0000313|EMBL:OAY65801.1};
RX PubMed=27374615; DOI=10.1093/dnares/dsw026;
RA Redwan R.M., Saidin A., Kumar S.V.;
RT "The draft genome of MD-2 pineapple using hybrid error correction of long
RT reads.";
RL DNA Res. 0:0-0(2016).
RN [2] {ECO:0000313|RefSeq:XP_020089855.1}
RP IDENTIFICATION.
RC TISSUE=Leaf {ECO:0000313|RefSeq:XP_020089855.1};
RG RefSeq;
RL Submitted (NOV-2023) 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}.
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DR EMBL; LSRQ01006666; OAY65801.1; -; Genomic_DNA.
DR RefSeq; XP_020089855.1; XM_020234266.1.
DR STRING; 4615.A0A199UM92; -.
DR EnsemblPlants; Aco002999.1.mrna1; Aco002999.1.mrna1; Aco002999.1.path1.
DR GeneID; 109711299; -.
DR Gramene; Aco002999.1.mrna1; Aco002999.1.mrna1; Aco002999.1.path1.
DR OrthoDB; 158575at2759; -.
DR Proteomes; UP000092600; Unassembled WGS sequence.
DR Proteomes; UP000515123; Linkage group 6.
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; cd14379; UBA1_Rad23_plant; 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 NCBIfam; TIGR00601; rad23; 1.
DR PANTHER; PTHR10621:SF35; UBIQUITIN RECEPTOR RAD23D; 1.
DR PANTHER; PTHR10621; 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 Receptor {ECO:0000313|EMBL:OAY65801.1, ECO:0000313|RefSeq:XP_020089855.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000092600};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 1..79
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS50053"
FT DOMAIN 160..203
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT DOMAIN 345..386
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT REGION 81..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 214..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..123
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..235
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 392 AA; 41378 MW; 97C5AF43C8466561 CRC64;
MKIFVKTLKG TSFEIEAMPE DMVADVKKNI ETAQGQSIYP ADQQMLIHQG KILKDDTTLD
DNKIAENSFI VIMLSKSKGS SSGASSAAKA PTNQAPTSSP VPPAAPTPTP APSPAPAAPT
ASAPTNAPAP TAAPAPALAV SASSEVEAYG QAASNLVAGS GLEQTIQQIL DMGGGTWDRD
TVVRALRAAF NNPERAVEYL YSGIPENVEV PHVARAPSSG QPANPTAQVQ QPAQPAAPPS
SGPNANPLDL FPQGLPSMGS NAGAGSLDML RNSPQFRALL ALVQANPQIL QPMLQELGKQ
NPQVLRLIQE NQAEFLRLVN EPAEGGEGNL LSQLAAAMPQ AITVTPEERE AIERLEAMGF
DRELVLEVFF ACNKNEELAA NYLLDHMHEF EE
//
