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Database: UniProt
Entry: G3TZH0_LOXAF
LinkDB: G3TZH0_LOXAF
Original site: G3TZH0_LOXAF 
ID   G3TZH0_LOXAF            Unreviewed;       203 AA.
AC   G3TZH0;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   RecName: Full=E2 ubiquitin-conjugating enzyme {ECO:0000256|ARBA:ARBA00012486};
DE            EC=2.3.2.23 {ECO:0000256|ARBA:ARBA00012486};
GN   Name=UBE2K {ECO:0000313|Ensembl:ENSLAFP00000020978.1};
OS   Loxodonta africana (African elephant).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX   NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000020978.1, ECO:0000313|Proteomes:UP000007646};
RN   [1] {ECO:0000313|Ensembl:ENSLAFP00000020978.1, ECO:0000313|Proteomes:UP000007646}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000020978.1,
RC   ECO:0000313|Proteomes:UP000007646};
RA   Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT   "The Genome Sequence of Loxodonta africana (African elephant).";
RL   Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLAFP00000020978.1}
RP   IDENTIFICATION.
RC   STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000020978.1};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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   -!- PATHWAY: Protein modification. {ECO:0000256|ARBA:ARBA00043952}.
CC   -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC       {ECO:0000256|RuleBase:RU362109}.
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DR   AlphaFoldDB; G3TZH0; -.
DR   STRING; 9785.ENSLAFP00000020978; -.
DR   Ensembl; ENSLAFT00000030864.1; ENSLAFP00000020978.1; ENSLAFG00000007163.4.
DR   eggNOG; KOG0418; Eukaryota.
DR   GeneTree; ENSGT00670000098059; -.
DR   InParanoid; G3TZH0; -.
DR   TreeFam; TF101127; -.
DR   Proteomes; UP000007646; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR   GO; GO:0032433; C:filopodium tip; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IEA:UniProtKB-EC.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR   GO; GO:0034450; F:ubiquitin-ubiquitin ligase activity; IEA:Ensembl.
DR   GO; GO:0035458; P:cellular response to interferon-beta; IEA:Ensembl.
DR   GO; GO:0010994; P:free ubiquitin chain polymerization; IEA:Ensembl.
DR   GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; IEA:Ensembl.
DR   GO; GO:1903265; P:positive regulation of tumor necrosis factor-mediated signaling pathway; IEA:Ensembl.
DR   GO; GO:0060340; P:positive regulation of type I interferon-mediated signaling pathway; IEA:Ensembl.
DR   GO; GO:0070936; P:protein K48-linked ubiquitination; IEA:Ensembl.
DR   GO; GO:0032434; P:regulation of proteasomal ubiquitin-dependent protein catabolic process; IEA:Ensembl.
DR   CDD; cd14390; UBA_II_E2_UBE2K; 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; IPR015940; UBA.
DR   InterPro; IPR009060; UBA-like_sf.
DR   InterPro; IPR042599; UBE2K_UBA.
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:SF147; UBIQUITIN-CONJUGATING ENZYME E2 K; 1.
DR   Pfam; PF00627; UBA; 1.
DR   Pfam; PF00179; UQ_con; 1.
DR   SMART; SM00165; UBA; 1.
DR   SMART; SM00212; UBCc; 1.
DR   SUPFAM; SSF46934; UBA-like; 1.
DR   SUPFAM; SSF54495; UBC-like; 1.
DR   PROSITE; PS50030; UBA; 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:UP000007646};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|RuleBase:RU362109}.
FT   DOMAIN          7..157
FT                   /note="UBC core"
FT                   /evidence="ECO:0000259|PROSITE:PS50127"
FT   DOMAIN          163..203
FT                   /note="UBA"
FT                   /evidence="ECO:0000259|PROSITE:PS50030"
FT   ACT_SITE        95
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10133"
SQ   SEQUENCE   203 AA;  22641 MW;  54FBDC09BD818E83 CRC64;
     LVNVYVNPIR ELSELFKATD DSETTSKNQI KVDLVDENFT ELRGEIAGPP DTPYEGGRYQ
     LEIKIPETYP FNPPKVRFIT KIWHPNISSV TGAICLDILK DQWAAAMTLR TVLLSLQALL
     AAAEPDDPQD AVVANQYKQN PEMFKQTARL WAHVYAGAPV SSPEYTKKIE NLCAMGFDRN
     AVIVALSSKS WDVETATELL LSN
//
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