GenomeNet

Database: UniProt
Entry: A0A0W7VY60_9HYPO
LinkDB: A0A0W7VY60_9HYPO
Original site: A0A0W7VY60_9HYPO 
ID   A0A0W7VY60_9HYPO        Unreviewed;       367 AA.
AC   A0A0W7VY60;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=UV excision repair protein RAD23 {ECO:0000256|RuleBase:RU367049};
GN   ORFNames=TGAM01_v203126 {ECO:0000313|EMBL:PON27990.1}, TGAMA5MH_01411
GN   {ECO:0000313|EMBL:PNP47589.1};
OS   Trichoderma gamsii.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=398673 {ECO:0000313|EMBL:PON27990.1, ECO:0000313|Proteomes:UP000054821};
RN   [1] {ECO:0000313|EMBL:PON27990.1, ECO:0000313|Proteomes:UP000054821}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T6085 {ECO:0000313|EMBL:PON27990.1,
RC   ECO:0000313|Proteomes:UP000054821};
RX   PubMed=26893428;
RA   Baroncelli R., Zapparata A., Piaggeschi G., Sarrocco S., Vannacci G.;
RT   "Draft Whole-Genome Sequence of Trichoderma gamsii T6085, a Promising
RT   Biocontrol Agent of Fusarium Head Blight on Wheat.";
RL   Genome Announc. 4:e01747-15(2016).
RN   [2] {ECO:0000313|EMBL:PNP47589.1, ECO:0000313|Proteomes:UP000236546}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A5MH {ECO:0000313|EMBL:PNP47589.1,
RC   ECO:0000313|Proteomes:UP000236546};
RA   Gardiner D., Kazan K., Vos C., Harvey P.;
RT   "Genomes of Trichoderma spp. with biocontrol activity.";
RL   Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:PON27990.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=T6085 {ECO:0000313|EMBL:PON27990.1};
RA   Baroncelli R.;
RT   "Trichoderma gamsii strain T6085, whole genome shotgun sequencing
RT   project.";
RL   Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PON27990.1}.
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; MTYH01000013; PNP47589.1; -; Genomic_DNA.
DR   EMBL; JPDN02000008; PON27990.1; -; Genomic_DNA.
DR   RefSeq; XP_018664404.1; XM_018802486.1.
DR   AlphaFoldDB; A0A0W7VY60; -.
DR   STRING; 398673.A0A0W7VY60; -.
DR   GeneID; 29982569; -.
DR   OrthoDB; 158575at2759; -.
DR   Proteomes; UP000054821; Unassembled WGS sequence.
DR   Proteomes; UP000236546; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; 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; 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; 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; 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:UP000054821};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          1..76
FT                   /note="Ubiquitin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50053"
FT   DOMAIN          139..179
FT                   /note="UBA"
FT                   /evidence="ECO:0000259|PROSITE:PS50030"
FT   DOMAIN          317..358
FT                   /note="UBA"
FT                   /evidence="ECO:0000259|PROSITE:PS50030"
FT   REGION          83..134
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          186..214
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        93..122
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   367 AA;  39283 MW;  2A4AC7C28E685947 CRC64;
     MKVTFRDLKQ QKFVLDVEPT DRISAVKEKI AAEKGWEPKT QKLIYSGKIL KDDDTVESYN
     IEEKGFVVCM VNKPRPAAAA APAAAAAPPA TPAQRVPSTP AVPPAPSQTS SQAPPPATPT
     PNRSVESPSG GVSGLAMGAE RAEAIANMEA MGFERTQIEA AMRAAFNNPD RAVEYLLTGI
     PENIQQEQQQ RASQQQAAAA APAAAPTGND DDNINLFDLA AQRRGGGASD APAAAAAGQG
     DLGNLDFLRH NAQFQQLRQV VQQQPQMLEP ILQQLGAGNP QLAQLIASNP DQFLQLLGED
     AEDDVPLPPG AQAISVTEEE RDAIERLCRL GFDRDQAIQA YFACDKNEEL AANFLFDQPE
     DDEPPTN
//
DBGET integrated database retrieval system