ID A0A177BU18_9PLEO Unreviewed; 152 AA.
AC A0A177BU18;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=E2 ubiquitin-conjugating enzyme {ECO:0000256|ARBA:ARBA00012486};
DE EC=2.3.2.23 {ECO:0000256|ARBA:ARBA00012486};
GN ORFNames=CC84DRAFT_1131598 {ECO:0000313|EMBL:OAF98913.1};
OS Paraphaeosphaeria sporulosa.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Didymosphaeriaceae;
OC Paraphaeosphaeria.
OX NCBI_TaxID=1460663 {ECO:0000313|EMBL:OAF98913.1, ECO:0000313|Proteomes:UP000077069};
RN [1] {ECO:0000313|EMBL:OAF98913.1, ECO:0000313|Proteomes:UP000077069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP3s5-JAC2a {ECO:0000313|EMBL:OAF98913.1,
RC ECO:0000313|Proteomes:UP000077069};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-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 -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine +
CC [acceptor protein]-N-terminal-amino acid = [E1 ubiquitin-activating
CC enzyme]-L-cysteine + N-terminal-ubiquitinyl-[acceptor protein].;
CC EC=2.3.2.25; Evidence={ECO:0000256|ARBA:ARBA00035805};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KV441563; OAF98913.1; -; Genomic_DNA.
DR RefSeq; XP_018029279.1; XM_018175908.1.
DR AlphaFoldDB; A0A177BU18; -.
DR STRING; 1460663.A0A177BU18; -.
DR GeneID; 28759394; -.
DR InParanoid; A0A177BU18; -.
DR OrthoDB; 452at2759; -.
DR Proteomes; UP000077069; Unassembled WGS sequence.
DR CDD; cd00195; UBCc; 1.
DR Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 1.
DR InterPro; IPR000608; UBQ-conjugat_E2.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR PANTHER; PTHR24067; UBIQUITIN-CONJUGATING ENZYME E2; 1.
DR PANTHER; PTHR24067:SF373; UBIQUITIN-CONJUGATING ENZYME E2 W; 1.
DR Pfam; PF00179; UQ_con; 1.
DR SMART; SM00212; UBCc; 1.
DR SUPFAM; SSF54495; UBC-like; 1.
DR PROSITE; PS50127; UBC_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000077069};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 2..152
FT /note="UBC core"
FT /evidence="ECO:0000259|PROSITE:PS50127"
SQ SEQUENCE 152 AA; 17531 MW; 63AEDAAE79670AD6 CRC64;
MFASKRLGKE LTKLQDKLPP GITLVKADDF RDWLMDIQVM DENPIYKGET YRLKFTFSQS
YPIEAPEVVF VRDETHPIPI HPHIYSNGII CLDLLDRQGW SPVHNVESVC VSLQSMLTSN
TKNERPPGDE AFVRSNTQRP RDINFVFHDN SV
//
