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Database: UniProt
Entry: A0A183MPN3_9TREM
LinkDB: A0A183MPN3_9TREM
Original site: A0A183MPN3_9TREM 
ID   A0A183MPN3_9TREM        Unreviewed;       149 AA.
AC   A0A183MPN3;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=E2 ubiquitin-conjugating enzyme {ECO:0000256|ARBA:ARBA00012486};
DE            EC=2.3.2.23 {ECO:0000256|ARBA:ARBA00012486};
GN   ORFNames=SMRZ_LOCUS18008 {ECO:0000313|EMBL:VDP26126.1};
OS   Schistosoma margrebowiei.
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC   Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX   NCBI_TaxID=48269 {ECO:0000313|WBParaSite:SMRZ_0001800901-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:SMRZ_0001800901-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (JUN-2016) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDP26126.1, ECO:0000313|Proteomes:UP000277204}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Zambia {ECO:0000313|EMBL:VDP26126.1,
RC   ECO:0000313|Proteomes:UP000277204};
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) 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; UZAI01017524; VDP26126.1; -; Genomic_DNA.
DR   STRING; 48269.A0A183MPN3; -.
DR   WBParaSite; SMRG1_81530.1; SMRG1_81530.1; SMRG1_81530.
DR   WBParaSite; SMRZ_0001800901-mRNA-1; SMRZ_0001800901-mRNA-1; SMRZ_0001800901.
DR   Proteomes; UP000050790; Unassembled WGS sequence.
DR   Proteomes; UP000277204; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:UniProt.
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:SF565; BCDNA.GH02435; 1.
DR   PANTHER; PTHR24068; UBIQUITIN-CONJUGATING ENZYME E2; 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:UP000277204};
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   149 AA;  16959 MW;  96B82A69B483234D CRC64;
     MALRRISKEL KDLRLDPPTQ CSAGPIKDDL FAWQATIMGP ADSPYEGGIF FLEIQFPTDY
     PFKPPKISFM TKIYHPNINL SGHICLDILR GQWSPALTIS KVLLSICSLL TDPNPDDPLC
     PDVARQYKTD RKKYDELARE WTQKYAMGP
//
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