ID V2YBJ4_MONRO Unreviewed; 225 AA.
AC V2YBJ4;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=E2 ubiquitin-conjugating enzyme {ECO:0000256|ARBA:ARBA00012486};
DE EC=2.3.2.23 {ECO:0000256|ARBA:ARBA00012486};
GN ORFNames=Moror_5339 {ECO:0000313|EMBL:ESK89064.1};
OS Moniliophthora roreri (strain MCA 2997) (Cocoa frosty pod rot fungus)
OS (Crinipellis roreri).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX NCBI_TaxID=1381753 {ECO:0000313|EMBL:ESK89064.1, ECO:0000313|Proteomes:UP000017559};
RN [1] {ECO:0000313|EMBL:ESK89064.1, ECO:0000313|Proteomes:UP000017559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK89064.1,
RC ECO:0000313|Proteomes:UP000017559};
RX PubMed=24571091; DOI=10.1186/1471-2164-15-164;
RA Meinhardt L.W., Costa G.G.L., Thomazella D.P.T., Teixeira P.J.P.L.,
RA Carazzolle M.F., Schuster S.C., Carlson J.E., Guiltinan M.J.,
RA Mieczkowski P., Farmer A., Ramaraj T., Crozier J., Davis R.E., Shao J.,
RA Melnick R.L., Pereira G.A.G., Bailey B.A.;
RT "Genome and secretome analysis of the hemibiotrophic fungal pathogen,
RT Moniliophthora roreri, which causes frosty pod rot disease of cacao:
RT mechanisms of the biotrophic and necrotrophic phases.";
RL BMC Genomics 15:164-164(2014).
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:ESK89064.1}.
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DR EMBL; AWSO01000593; ESK89064.1; -; Genomic_DNA.
DR RefSeq; XP_007851632.1; XM_007853441.1.
DR AlphaFoldDB; V2YBJ4; -.
DR STRING; 1381753.V2YBJ4; -.
DR KEGG; mrr:Moror_5339; -.
DR HOGENOM; CLU_030988_13_1_1; -.
DR OrthoDB; 102270at2759; -.
DR Proteomes; UP000017559; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IEA:UniProtKB-EC.
DR CDD; cd14311; UBA_II_E2_UBC1; 1.
DR CDD; cd00195; UBCc; 1.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 1.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR015368; UBA_C_fun.
DR InterPro; IPR000608; UBQ-conjugat_E2.
DR InterPro; IPR023313; UBQ-conjugating_AS.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR PANTHER; PTHR24067:SF347; E2 UBIQUITIN-CONJUGATING ENZYME; 1.
DR PANTHER; PTHR24067; UBIQUITIN-CONJUGATING ENZYME E2; 1.
DR Pfam; PF09288; UBA_3; 1.
DR Pfam; PF00179; UQ_con; 1.
DR SMART; SM00212; UBCc; 1.
DR SUPFAM; SSF46934; UBA-like; 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 Reference proteome {ECO:0000313|Proteomes:UP000017559};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU362109}.
FT DOMAIN 3..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 225 AA; 24764 MW; 1685867773A00114 CRC64;
MDARLRRVNK EIADCKNDKT SNIALDLIDN SPFHLKGSFP GPEGTPYEGG HFEVDIVIPD
AYPFQPVKMK FLTKVYHPNV SSASGAICLD ILKDAWSPVL TLKSTLISLQ SLLCSPEPND
PQDAEVAKHY TTSKSSFDET ARYWTQIYAG GPGNKTGVSN GGKASSKVDT RDEVAIAGLE
KAHVDQFESL GFPRSKVIDV LRRLNYRGPN VAQISEDRIV EELLK
//
