ID A0A1C7MEI8_GRIFR Unreviewed; 326 AA.
AC A0A1C7MEI8;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=E2 ubiquitin-conjugating enzyme {ECO:0000256|ARBA:ARBA00012486};
DE EC=2.3.2.23 {ECO:0000256|ARBA:ARBA00012486};
GN ORFNames=A0H81_05207 {ECO:0000313|EMBL:OBZ74806.1};
OS Grifola frondosa (Maitake) (Polyporus frondosus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Grifolaceae; Grifola.
OX NCBI_TaxID=5627 {ECO:0000313|EMBL:OBZ74806.1, ECO:0000313|Proteomes:UP000092993};
RN [1] {ECO:0000313|EMBL:OBZ74806.1, ECO:0000313|Proteomes:UP000092993}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=9006-11 {ECO:0000313|EMBL:OBZ74806.1,
RC ECO:0000313|Proteomes:UP000092993};
RA Min B., Park H., Kim J.-G., Cho H., Oh Y.-L., Kong W.-S., Choi I.-G.;
RT "Whole genome sequencing of Grifola frondosa 9006-11.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine +
CC [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-
CC activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-
CC conjugating enzyme]-L-cysteine.; EC=2.3.2.23;
CC Evidence={ECO:0000256|ARBA:ARBA00000485};
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:OBZ74806.1}.
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DR EMBL; LUGG01000005; OBZ74806.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C7MEI8; -.
DR STRING; 5627.A0A1C7MEI8; -.
DR OMA; WKSTYGI; -.
DR OrthoDB; 179223at2759; -.
DR Proteomes; UP000092993; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:UniProt.
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:SF154; UBIQUITIN-CONJUGATING ENZYME E2 G2; 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 Reference proteome {ECO:0000313|Proteomes:UP000092993};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU362109}.
FT DOMAIN 6..152
FT /note="UBC core"
FT /evidence="ECO:0000259|PROSITE:PS50127"
FT REGION 156..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 265..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..173
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..213
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..238
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 90
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10133"
SQ SEQUENCE 326 AA; 34791 MW; 52BD28C46E827F13 CRC64;
MSVPPAVLRR LMRELHELRT NPPEGIRVVT NEDNMLDVTG IIEGPEGTPY AGGYFKVKFS
FTEEFPAAPP KCWFATKIFH PNVSSAGEIC VNTLKKDWKA SYGIAHILVT VKCLLIYPNP
ESALDEEAGK LLLENYDSYC ERAKLITSVH ATPKVRPAEF NTPSATESAS KPSTSQPAPP
PPTPAPTTPH VPPSTPTTHK TAPPTPTPPS QPLQSSTPNT FATSTSTSSL SSEKSAGKER
LPSPSPLGTA DANVGVGVSP GTKAVKRSAV TGGWERRETE EGVEASLTPS VCGAGGCELM
DIGMHARRVL MLWGLWNSFL APIIVV
//
