ID I2GUX6_TETBL Unreviewed; 219 AA.
AC I2GUX6;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=E2 ubiquitin-conjugating enzyme {ECO:0000256|ARBA:ARBA00012486};
DE EC=2.3.2.23 {ECO:0000256|ARBA:ARBA00012486};
GN Name=TBLA0A01290 {ECO:0000313|EMBL:CCH57928.1};
GN ORFNames=TBLA_0A01290 {ECO:0000313|EMBL:CCH57928.1};
OS Tetrapisispora blattae (strain ATCC 34711 / CBS 6284 / DSM 70876 / NBRC
OS 10599 / NRRL Y-10934 / UCD 77-7) (Yeast) (Kluyveromyces blattae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Tetrapisispora.
OX NCBI_TaxID=1071380 {ECO:0000313|EMBL:CCH57928.1, ECO:0000313|Proteomes:UP000002866};
RN [1] {ECO:0000313|EMBL:CCH57928.1, ECO:0000313|Proteomes:UP000002866}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 34711 / CBS 6284 / DSM 70876 / NBRC 10599 / NRRL Y-10934 /
RC UCD 77-7 {ECO:0000313|Proteomes:UP000002866};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000256|RuleBase:RU362109}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; HE806316; CCH57928.1; -; Genomic_DNA.
DR RefSeq; XP_004177447.1; XM_004177399.1.
DR AlphaFoldDB; I2GUX6; -.
DR STRING; 1071380.I2GUX6; -.
DR GeneID; 14492987; -.
DR KEGG; tbl:TBLA_0A01290; -.
DR eggNOG; KOG0416; Eukaryota.
DR HOGENOM; CLU_030988_7_1_1; -.
DR InParanoid; I2GUX6; -.
DR OMA; SPSIGFC; -.
DR OrthoDB; 619890at2759; -.
DR Proteomes; UP000002866; Chromosome 1.
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; PTHR24068; UBIQUITIN-CONJUGATING ENZYME E2; 1.
DR PANTHER; PTHR24068:SF128; UBIQUITIN-CONJUGATING ENZYME E2 H; 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|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU362109};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362109};
KW Reference proteome {ECO:0000313|Proteomes:UP000002866};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU362109}.
FT DOMAIN 3..148
FT /note="UBC core"
FT /evidence="ECO:0000259|PROSITE:PS50127"
FT REGION 153..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..181
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..198
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..219
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 85
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10133"
SQ SEQUENCE 219 AA; 25368 MW; B66B3F2D58D198B0 CRC64;
MSNSKRRIET DVMKLLMSNH DVELVNDNMQ EFFIKFFGPD ETPYEKGVWR LHVELPDNYP
YKSPSIGFVN KIFHPNIDIA SGSICLDVIN STWSPLYDLI NIVEWMIPGL LKEPNGTDPL
NNEAAGLQLR DKKLYEEKIK EYIDKYATPE KYEKLFGRKE EEEDEEEDDD DDDDDDDDDD
EEGRKNKDKI RGDLSDSELE EGGISEELSD IDVSDDDDD
//
