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Database: UniProt
Entry: A0A182MLC0_9DIPT
LinkDB: A0A182MLC0_9DIPT
Original site: A0A182MLC0_9DIPT 
ID   A0A182MLC0_9DIPT        Unreviewed;       199 AA.
AC   A0A182MLC0;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=E2 ubiquitin-conjugating enzyme {ECO:0000256|ARBA:ARBA00012486};
DE            EC=2.3.2.23 {ECO:0000256|ARBA:ARBA00012486};
OS   Anopheles culicifacies.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles; culicifacies species complex.
OX   NCBI_TaxID=139723 {ECO:0000313|EnsemblMetazoa:ACUA021038-PA, ECO:0000313|Proteomes:UP000075883};
RN   [1] {ECO:0000313|Proteomes:UP000075883}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A-37 {ECO:0000313|Proteomes:UP000075883};
RG   The Broad Institute Genomics Platform;
RA   Neafsey D.E., Besansky N., Howell P., Walton C., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Anopheles culicifacies species A.";
RL   Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:ACUA021038-PA}
RP   IDENTIFICATION.
RC   STRAIN=A-37 {ECO:0000313|EnsemblMetazoa:ACUA021038-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   EMBL; AXCM01001770; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; A0A182MLC0; -.
DR   STRING; 139723.A0A182MLC0; -.
DR   EnsemblMetazoa; ACUA021038-RA; ACUA021038-PA; ACUA021038.
DR   VEuPathDB; VectorBase:ACUA021038; -.
DR   OrthoDB; 102270at2759; -.
DR   Proteomes; UP000075883; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IEA:UniProtKB-EC.
DR   CDD; cd14391; UBA_II_E2_UBCD4; 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; IPR042614; UBCD4_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   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|RuleBase:RU362109}.
FT   DOMAIN          4..154
FT                   /note="UBC core"
FT                   /evidence="ECO:0000259|PROSITE:PS50127"
FT   DOMAIN          161..199
FT                   /note="UBA"
FT                   /evidence="ECO:0000259|PROSITE:PS50030"
FT   ACT_SITE        92
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10133"
SQ   SEQUENCE   199 AA;  22513 MW;  D46A27CBD03EE87E CRC64;
     MANMAVSRIK REFKEVLKSE EITQCSIKLE MVNDNFTELR GEIAGPPDTP YEGGKFVLEI
     TVPETYPFNP PKVKFMTKIW HPNISSVTGA ICLDILKDNW AAAMTLRTVL LSLQALLAAA
     EPDDPQDAVV ATQYKDNHEM FILTAKHWTN VYAGGPFANT DFDQKVQRLR DMGIPEYDAR
     AALSRHNWHL ERASEQLFS
//
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