ID A0A090LIJ6_STRRB Unreviewed; 154 AA.
AC A0A090LIJ6;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=E2 ubiquitin-conjugating enzyme {ECO:0000256|ARBA:ARBA00012486};
DE EC=2.3.2.23 {ECO:0000256|ARBA:ARBA00012486};
GN ORFNames=SRAE_2000197400 {ECO:0000313|EMBL:CEF67310.1,
GN ECO:0000313|WBParaSite:SRAE_2000197400.1,
GN ECO:0000313|WormBase:SRAE_2000197400};
OS Strongyloides ratti (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Strongyloides.
OX NCBI_TaxID=34506 {ECO:0000313|EMBL:CEF67310.1};
RN [1] {ECO:0000313|EMBL:CEF67310.1, ECO:0000313|Proteomes:UP000035682}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ED321 {ECO:0000313|Proteomes:UP000035682,
RC ECO:0000313|WBParaSite:SRAE_2000197400.1}, and ED321 Heterogonic
RC {ECO:0000313|EMBL:CEF67310.1};
RA Martin A.A.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|WBParaSite:SRAE_2000197400.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (DEC-2020) 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 -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000256|RuleBase:RU362109}.
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DR EMBL; LN609529; CEF67310.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A090LIJ6; -.
DR STRING; 34506.A0A090LIJ6; -.
DR EnsemblMetazoa; SRAE_2000197400.1; SRAE_2000197400.1; WBGene00262181.
DR WBParaSite; SRAE_2000197400.1; SRAE_2000197400.1; WBGene00262181.
DR WormBase; SRAE_2000197400; SRP05882; WBGene00262181; -.
DR OMA; RKVTRCV; -.
DR OrthoDB; 149628at2759; -.
DR Proteomes; UP000035682; Chromosome X.
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; PTHR24067; UBIQUITIN-CONJUGATING ENZYME E2; 1.
DR PANTHER; PTHR24067:SF3; UBIQUITIN-CONJUGATING ENZYME E2 G1; 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:UP000035682};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU362109}.
FT DOMAIN 5..153
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"
SQ SEQUENCE 154 AA; 17661 MW; E5BF8A147891D63C CRC64;
MSHTQGKLLL QKQLQELQKN PVDGFSAGLV NDDDVYKWEV LIIGPPDTIY EEYPQRPPKM
RFISEMWHPN IAKNGSVCIS ILHEPGDDHF GYERPEERWL PVHTVETILL SVISILADPN
SESPANVDAA KEFINNYDEF KKKVAQCVRK SQEE
//
