ID A0A099Z6K8_TINGU Unreviewed; 140 AA.
AC A0A099Z6K8;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=E2 ubiquitin-conjugating enzyme {ECO:0000256|ARBA:ARBA00012486};
DE EC=2.3.2.23 {ECO:0000256|ARBA:ARBA00012486};
DE Flags: Fragment;
GN ORFNames=N309_03810 {ECO:0000313|EMBL:KGL77352.1};
OS Tinamus guttatus (White-throated tinamou).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Palaeognathae; Tinamiformes; Tinamidae; Tinamus.
OX NCBI_TaxID=94827 {ECO:0000313|EMBL:KGL77352.1, ECO:0000313|Proteomes:UP000053641};
RN [1] {ECO:0000313|EMBL:KGL77352.1, ECO:0000313|Proteomes:UP000053641}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N309 {ECO:0000313|EMBL:KGL77352.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (JUN-2014) 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}.
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DR EMBL; KL890043; KGL77352.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A099Z6K8; -.
DR STRING; 94827.A0A099Z6K8; -.
DR Proteomes; UP000053641; 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:SF36; UBIQUITIN-CONJUGATING ENZYME E2 D1; 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:UP000053641};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU362109}.
FT DOMAIN 1..140
FT /note="UBC core"
FT /evidence="ECO:0000259|PROSITE:PS50127"
FT ACT_SITE 78
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10133"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KGL77352.1"
FT NON_TER 140
FT /evidence="ECO:0000313|EMBL:KGL77352.1"
SQ SEQUENCE 140 AA; 15761 MW; 5023CDED2FC2CC0A CRC64;
QELSDLQRDP PAHCSAGPVG DDLFHWQATI MGPPDSAYQG GVFFLTVHFP TDYPFKPPKI
AFTTKIYHPN INSNGSICLD ILRSQWSPAL TVSKVLLSIC SLLCDPNPDD PLVPDIAQIY
KSDKEKYNRH AREWTQKYAM
//
