ID A0A1A9WWD7_9MUSC Unreviewed; 351 AA.
AC A0A1A9WWD7;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, 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};
OS Glossina brevipalpis.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Hippoboscoidea;
OC Glossinidae; Glossina.
OX NCBI_TaxID=37001 {ECO:0000313|EnsemblMetazoa:GBRI034898-PA, ECO:0000313|Proteomes:UP000091820};
RN [1] {ECO:0000313|Proteomes:UP000091820}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IAEA {ECO:0000313|Proteomes:UP000091820};
RA Aksoy S., Warren W., Wilson R.K.;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:GBRI034898-PA}
RP IDENTIFICATION.
RC STRAIN=IAEA {ECO:0000313|EnsemblMetazoa:GBRI034898-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-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 AlphaFoldDB; A0A1A9WWD7; -.
DR STRING; 37001.A0A1A9WWD7; -.
DR EnsemblMetazoa; GBRI034898-RA; GBRI034898-PA; GBRI034898.
DR VEuPathDB; VectorBase:GBRI034898; -.
DR OrthoDB; 619890at2759; -.
DR Proteomes; UP000091820; 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; 2.
DR Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 2.
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:SF128; UBIQUITIN-CONJUGATING ENZYME E2 H; 1.
DR Pfam; PF00179; UQ_con; 2.
DR SMART; SM00212; UBCc; 2.
DR SUPFAM; SSF54495; UBC-like; 2.
DR PROSITE; PS00183; UBC_1; 2.
DR PROSITE; PS50127; UBC_2; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU362109};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362109};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU362109}.
FT DOMAIN 1..150
FT /note="UBC core"
FT /evidence="ECO:0000259|PROSITE:PS50127"
FT DOMAIN 160..318
FT /note="UBC core"
FT /evidence="ECO:0000259|PROSITE:PS50127"
FT REGION 156..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 324..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 87
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10133"
FT ACT_SITE 255
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10133"
SQ SEQUENCE 351 AA; 40482 MW; 1690F65656E86122 CRC64;
MTSPTTNKRR IDKDIMKLLK SKHEVIITGG LNEFQVKFFG PLETPYQKGV WKVNVYLPDD
YPFKSPSIQF VNKIYHPNIG ESSGTVCVDV INQAWTALYD LSNIFECFLP QLLTYPNPTD
PLNREAARLF INEPEEYNRK VVQYVQRYAI EVTLNERENS DSESSMSDYS EQDADKHRKD
SDIIKLIESK HEVIILGGLN EFQVKFFGPG ETPYQKGVWK VRVYLPDNYP FKSPSIGFVN
KIYHPNIDES SGTVCLDVIN QAWTPLYNLS NIFECFLPQL LTYPNPTDPL NREAATLYMH
AREAYDRKVV LYVQRYATEE ALRAAQVERE SSDSESSMSD YSVEDARDME V
//
