ID A0A1V4JU29_PATFA Unreviewed; 147 AA.
AC A0A1V4JU29;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=Ubiquitin-conjugating enzyme E2 D3 isoform A {ECO:0000313|EMBL:OPJ75673.1};
GN Name=UBE2D3 {ECO:0000313|EMBL:OPJ75673.1};
GN ORFNames=AV530_011867 {ECO:0000313|EMBL:OPJ75673.1};
OS Patagioenas fasciata monilis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Patagioenas.
OX NCBI_TaxID=372326 {ECO:0000313|EMBL:OPJ75673.1, ECO:0000313|Proteomes:UP000190648};
RN [1] {ECO:0000313|EMBL:OPJ75673.1, ECO:0000313|Proteomes:UP000190648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BTP2013 {ECO:0000313|EMBL:OPJ75673.1};
RC TISSUE=Blood {ECO:0000313|EMBL:OPJ75673.1};
RA Soares A.E., Novak B.J., Rice E.S., O'Connell B., Chang D., Weber S.,
RA Shapiro B.;
RT "Band-tailed pigeon sequencing and assembly.";
RL Submitted (FEB-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]-L-lysine = [E1 ubiquitin-activating enzyme]-L-
CC cysteine + N(6)-monoubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.24; Evidence={ECO:0000256|ARBA:ARBA00035845};
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:OPJ75673.1}.
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DR EMBL; LSYS01006159; OPJ75673.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V4JU29; -.
DR SMR; A0A1V4JU29; -.
DR Proteomes; UP000190648; 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; PTHR24068; UBIQUITIN-CONJUGATING ENZYME E2; 1.
DR PANTHER; PTHR24068:SF415; UBIQUITIN-CONJUGATING ENZYME E2 D3; 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|RuleBase:RU362109};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362109};
KW Reference proteome {ECO:0000313|Proteomes:UP000190648};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU362109}.
FT DOMAIN 1..147
FT /note="UBC core"
FT /evidence="ECO:0000259|PROSITE:PS50127"
FT ACT_SITE 85
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10133"
SQ SEQUENCE 147 AA; 16687 MW; ADD74A8A708EFEE3 CRC64;
MALKRINKEL SDLARDPPAQ CSAGPVGDDM FHWQATIMGP NDSPYQGGVF FLTIHFPTDY
PFKPPKVAFT TRIYHPNINS NGSICLDILR SQWSPALTIS KVLLSICSLL CDPNPDDPLV
PEIARIYKTD RDKYNRISRE WTQKYAM
//
