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Database: UniProt
Entry: A0A180GZ73_PUCT1
LinkDB: A0A180GZ73_PUCT1
Original site: A0A180GZ73_PUCT1 
ID   A0A180GZ73_PUCT1        Unreviewed;       167 AA.
AC   A0A180GZ73;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
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};
GN   ORFNames=PTTG_01169 {ECO:0000313|EMBL:OAV98125.1};
OS   Puccinia triticina (isolate 1-1 / race 1 (BBBD)) (Brown leaf rust fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX   NCBI_TaxID=630390 {ECO:0000313|EMBL:OAV98125.1};
RN   [1] {ECO:0000313|EMBL:OAV98125.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1-1 BBBD Race 1 {ECO:0000313|EMBL:OAV98125.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M.,
RA   Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S.B.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., Larson L.,
RA   Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.,
RA   Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., Walk T., White J.,
RA   Yandava C., Izard J., Baranova O.V., Blanton J.M., Tanner A.C.,
RA   Dewhirst F.E., Haas B., Nusbaum C., Birren B.;
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:OAV98125.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1-1 BBBD Race 1 {ECO:0000313|EMBL:OAV98125.1};
RA   Cuomo C.A., Bakkeren G., Szabo L., Khalil H., Joly D., Goldberg J.,
RA   Young S., Zeng Q., Fellers J.;
RT   "Comparative analysis highlights variable genome content of wheat rusts and
RT   divergence of the mating loci.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC       {ECO:0000256|RuleBase:RU362109}.
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:OAV98125.1}.
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DR   EMBL; ADAS02000009; OAV98124.1; -; Genomic_DNA.
DR   EMBL; ADAS02000009; OAV98125.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A180GZ73; -.
DR   STRING; 630390.A0A180GZ73; -.
DR   VEuPathDB; FungiDB:PTTG_01169; -.
DR   OrthoDB; 5478564at2759; -.
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|RuleBase:RU362109};
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   167 AA;  18348 MW;  985C45FC62A31FDA CRC64;
     MSTASRRRLI RDFKRLSSDP PGGISGAPCP DNIMVWNAVI FGPADTPFED GTFRLILTFD
     ESYPNKPPTV KFLSKMFHPN VYANGELCLD ILQNRWSPTY DVAAILTSVQ SLLHDPNPNS
     PANAEAANLY RDNMKDYVKK VRATVEASWI DEGTIPGTGD SSTATPA
//
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