ID   Y1A1_ENCCU              Reviewed;         216 AA.
AC   Q8SSK3;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   25-MAY-2022, entry version 100.
DE   RecName: Full=Probable ubiquitin-conjugating enzyme E2 ECU01_1010;
DE            EC=2.3.2.23;
DE   AltName: Full=E2 ubiquitin-conjugating enzyme ECU01_1010;
GN   OrderedLocusNames=ECU01_1010;
OS   Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC   Encephalitozoon.
OX   NCBI_TaxID=284813;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-M1;
RX   PubMed=11157783; DOI=10.1101/gr.164301;
RA   Peyret P., Katinka M.D., Duprat S., Duffieux F., Barbe V., Barbazanges M.,
RA   Weissenbach J., Saurin W., Vivares C.P.;
RT   "Sequence and analysis of chromosome I of the amitochondriate intracellular
RT   parasite Encephalitozoon cuniculi (Microspora).";
RL   Genome Res. 11:198-207(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-M1;
RX   PubMed=11719806; DOI=10.1038/35106579;
RA   Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA   Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA   Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA   Vivares C.P.;
RT   "Genome sequence and gene compaction of the eukaryote parasite
RT   Encephalitozoon cuniculi.";
RL   Nature 414:450-453(2001).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], AND
RP   DEVELOPMENTAL STAGE.
RX   PubMed=16691553; DOI=10.1002/pmic.200500796;
RA   Brosson D., Kuhn L., Delbac F., Garin J., Vivares C.P., Texier C.;
RT   "Proteomic analysis of the eukaryotic parasite Encephalitozoon cuniculi
RT   (microsporidia): a reference map for proteins expressed in late sporogonial
RT   stages.";
RL   Proteomics 6:3625-3635(2006).
CC   -!- FUNCTION: Catalyzes the covalent attachment of ubiquitin to other
CC       proteins so as to signal them for selective protein degradation.
CC       Involved in the formation of multiubiquitin chains.
CC       {ECO:0000255|PROSITE-ProRule:PRU00388}.
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:0000255|PROSITE-ProRule:PRU00388};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in late sporogonial stages.
CC       {ECO:0000269|PubMed:16691553}.
CC   -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR   EMBL; AL391737; CAD24972.1; -; Genomic_DNA.
DR   RefSeq; XP_965937.1; XM_960844.1.
DR   AlphaFoldDB; Q8SSK3; -.
DR   SMR; Q8SSK3; -.
DR   STRING; 284813.Q8SSK3; -.
DR   GeneID; 860278; -.
DR   KEGG; ecu:ECU01_1010; -.
DR   VEuPathDB; MicrosporidiaDB:ECU01_1010; -.
DR   HOGENOM; CLU_030988_10_1_1; -.
DR   InParanoid; Q8SSK3; -.
DR   OMA; WTPVQNI; -.
DR   OrthoDB; 1317014at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000000819; Chromosome I.
DR   GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IEA:UniProtKB-EC.
DR   CDD; cd00195; UBCc; 1.
DR   Gene3D; 3.10.110.10; -; 1.
DR   InterPro; IPR000608; UBQ-conjugat_E2.
DR   InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR   Pfam; PF00179; UQ_con; 1.
DR   SUPFAM; SSF54495; SSF54495; 1.
DR   PROSITE; PS50127; UBC_2; 1.
PE   1: Evidence at protein level;
KW   Reference proteome; Transferase; Ubl conjugation pathway.
FT   CHAIN           1..216
FT                   /note="Probable ubiquitin-conjugating enzyme E2 ECU01_1010"
FT                   /id="PRO_0000383031"
FT   DOMAIN          29..196
FT                   /note="UBC core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        120
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
SQ   SEQUENCE   216 AA;  25055 MW;  9B45EFCD6C17C0F0 CRC64;
     MFKPSAHRRL PREDDIIQED DEDGPLWPSA LRRLSNEEER LKIADGDERK LFSAYPRGSM
     ENRDYKVWDI YFTLGGDSLY AGRILKAVMK FPSSYPLRPP TLKFVSKMFH PNIYEDGKMC
     ISILEEDKQQ DSSVFGDPKD KWTPVQNIRT IVMSIVVILN SPNISSPANV DASVMYRDNP
     EEYIKEVIRI AREEDEKLRR TDPQAREVAL QMKAEN