ID A0A0J6Y589_COCIT Unreviewed; 226 AA.
AC A0A0J6Y589;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Ubiquitin carrier protein UBC2 {ECO:0000256|ARBA:ARBA00042190};
DE AltName: Full=Ubiquitin-protein ligase UBC2 {ECO:0000256|ARBA:ARBA00041569};
GN ORFNames=CIRG_03518 {ECO:0000313|EMBL:KMP03826.1};
OS Coccidioides immitis RMSCC 2394.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=404692 {ECO:0000313|EMBL:KMP03826.1, ECO:0000313|Proteomes:UP000054565};
RN [1] {ECO:0000313|Proteomes:UP000054565}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RMSCC 2394 {ECO:0000313|Proteomes:UP000054565};
RX PubMed=20516208; DOI=10.1101/gr.103911.109;
RA Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA Taylor J.W., Rounsley S.D.;
RT "Population genomic sequencing of Coccidioides fungi reveals recent
RT hybridization and transposon control.";
RL Genome Res. 20:938-946(2010).
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000256|RuleBase:RU362109}.
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DR EMBL; DS028094; KMP03826.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J6Y589; -.
DR STRING; 404692.A0A0J6Y589; -.
DR Proteomes; UP000054565; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016740; F:transferase activity; 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:SF364; UBIQUITIN-CONJUGATING ENZYME E2-34 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 Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU362109}.
FT DOMAIN 1..159
FT /note="UBC core"
FT /evidence="ECO:0000259|PROSITE:PS50127"
FT REGION 164..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..204
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 84
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10133"
SQ SEQUENCE 226 AA; 25723 MW; 327534A031E22537 CRC64;
MAQRILLNEY KALSKEKWVD VELKNEDIFN WNIALIVLNP DSLYYGGYFK GRMTFPNNYP
YSPPSFKFIR PLFHPNIYDN GELCISILHS PGEDEMSGES AAERWSPAQR VESVLISILS
LLDDAEINSA ANVNASVMLR DNPEKYKQKV RDDVEKSKRD IPKGFVMPTH ETSISKPEKA
EVVDEDFWID SDNGEEDDDI FGGSDSDAVD YSHEDNDSST DVEEQL
//