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Database: UniProt
Entry: F0UW88_AJEC8
LinkDB: F0UW88_AJEC8
Original site: F0UW88_AJEC8 
ID   F0UW88_AJEC8            Unreviewed;       151 AA.
AC   F0UW88;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   RecName: Full=Ubiquitin-conjugating enzyme E2 2 {ECO:0000256|ARBA:ARBA00039884};
DE            EC=2.3.2.23 {ECO:0000256|ARBA:ARBA00012486};
DE   AltName: Full=E2 ubiquitin-conjugating enzyme 2 {ECO:0000256|ARBA:ARBA00042179};
DE   AltName: Full=Ubiquitin carrier protein UBC2 {ECO:0000256|ARBA:ARBA00042190};
DE   AltName: Full=Ubiquitin-protein ligase UBC2 {ECO:0000256|ARBA:ARBA00041569};
GN   ORFNames=HCEG_09380 {ECO:0000313|EMBL:EGC42598.1}, I7I53_08711
GN   {ECO:0000313|EMBL:QSS48651.1};
OS   Ajellomyces capsulatus (strain H88) (Darling's disease fungus) (Histoplasma
OS   capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX   NCBI_TaxID=544711 {ECO:0000313|Proteomes:UP000008142};
RN   [1] {ECO:0000313|Proteomes:UP000008142}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H88 {ECO:0000313|Proteomes:UP000008142};
RA   Champion M., Cuomo C., Ma L.-J., Henn M.R., Sil A., Goldman B., Young S.K.,
RA   Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A., Borenstein D.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heiman D., Hepburn T., Howarth C., Jen D., Larson L., Lewis B.,
RA   Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C., Klein B.,
RA   McEwen J.G., Puccia R., Goldman G.H., Felipe M.S., Nino-Vega G.,
RA   San-Blas G., Taylor J., Mendoza L., Galagan J., Nusbaum C., Birren B.;
RT   "Annotation of Ajellomyces capsulatus strain H88.";
RL   Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EGC42598.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H88 {ECO:0000313|EMBL:EGC42598.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Champion M., Cuomo C., Ma L.-J., Henn M.R., Sil A., Goldman B., Young S.K.,
RA   Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A., Borenstein D.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heiman D., Hepburn T., Howarth C., Jen D., Larson L., Lewis B.,
RA   Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C., Klein B.,
RA   McEwen J.G., Puccia R., Goldman G.H., Felipe M.S., Nino-Vega G.,
RA   San-Blas G., Taylor J., Mendoza L., Galagan J., Nusbaum C., Birren B.;
RT   "Annotation of Ajellomyces capsulatus strain H88.";
RL   Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:QSS48651.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=H88 {ECO:0000313|EMBL:QSS48651.1};
RA   Voorhies M., Cohen S., Shea T.P., Petrus S., Munoz J.F., Poplawski S.,
RA   Goldman W.E., Michael T., Cuomo C.A., Sil A., Beyhan S.;
RT   "Chromosome-level genome assembly of a human fungal pathogen reveals
RT   clustering of transcriptionally co-regulated genes.";
RL   Submitted (JAN-2021) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC       {ECO:0000256|RuleBase:RU362109}.
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DR   EMBL; DS990646; EGC42598.1; -; Genomic_DNA.
DR   EMBL; CP069102; QSS48651.1; -; Genomic_DNA.
DR   AlphaFoldDB; F0UW88; -.
DR   STRING; 544711.F0UW88; -.
DR   VEuPathDB; FungiDB:I7I53_08711; -.
DR   HOGENOM; CLU_030988_10_2_1; -.
DR   OMA; DHKSQYI; -.
DR   Proteomes; UP000008142; Unassembled WGS sequence.
DR   Proteomes; UP000663419; Chromosome 1.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:UniProt.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR   CDD; cd00195; UBCc; 1.
DR   Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 1.
DR   InterPro; IPR000608; UBQ-conjugat_E2.
DR   InterPro; IPR023313; UBQ-conjugating_AS.
DR   InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR   PANTHER; PTHR24067; UBIQUITIN-CONJUGATING ENZYME E2; 1.
DR   PANTHER; PTHR24067:SF254; UBIQUITIN-CONJUGATING ENZYME E2-17 KDA; 1.
DR   Pfam; PF00179; UQ_con; 1.
DR   SMART; SM00212; UBCc; 1.
DR   SUPFAM; SSF54495; UBC-like; 1.
DR   PROSITE; PS00183; UBC_1; 1.
DR   PROSITE; PS50127; UBC_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU362109};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU362109};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008142};
KW   Sporulation {ECO:0000256|ARBA:ARBA00022969};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|RuleBase:RU362109}.
FT   DOMAIN          4..150
FT                   /note="UBC core"
FT                   /evidence="ECO:0000259|PROSITE:PS50127"
FT   ACT_SITE        88
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10133"
SQ   SEQUENCE   151 AA;  17169 MW;  65C6FD784D87950D CRC64;
     MSTAARRRLM RDFKRMQTDP PAGVSASPIA DNVMTWNAVI IGPADTPFED GTFRLVMHFE
     EQYPNKPPGV KFVSQMFHPN VYGTGELCLD ILQNRWSPTY DVAAILTSIQ SLLNDPNTSS
     PANVEASNLY KDNRREYTKR VRETVEKSWE D
//
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