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Database: UniProt
Entry: A0A2T3YSI2_9HYPO
LinkDB: A0A2T3YSI2_9HYPO
Original site: A0A2T3YSI2_9HYPO 
ID   A0A2T3YSI2_9HYPO        Unreviewed;       305 AA.
AC   A0A2T3YSI2;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=Ubiquitin-conjugating enzyme E2 6 {ECO:0000256|ARBA:ARBA00039885};
DE            EC=2.3.2.23 {ECO:0000256|ARBA:ARBA00012486};
DE   AltName: Full=E2 ubiquitin-conjugating enzyme 6 {ECO:0000256|ARBA:ARBA00042181};
GN   ORFNames=M441DRAFT_62809 {ECO:0000313|EMBL:PTB35528.1};
OS   Trichoderma asperellum CBS 433.97.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=1042311 {ECO:0000313|EMBL:PTB35528.1, ECO:0000313|Proteomes:UP000240493};
RN   [1] {ECO:0000313|EMBL:PTB35528.1, ECO:0000313|Proteomes:UP000240493}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 433.97 {ECO:0000313|EMBL:PTB35528.1,
RC   ECO:0000313|Proteomes:UP000240493};
RG   DOE Joint Genome Institute;
RA   Aerts A., Atanasova L., Chenthamara K., Zhang J., Grujic M., Henrissat B.,
RA   Kuo A., Salamov A., Lipzen A., Labutti K., Barry K., Miao Y., Rahimi M.J.,
RA   Shen Q., Grigoriev I.V., Kubicek C.P., Druzhinina I.S.;
RT   "Multiple horizontal gene transfer events from other fungi enriched the
RT   ability of initially mycotrophic Trichoderma (Ascomycota) to feed on dead
RT   plant biomass.";
RL   Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004586}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004370}.
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DR   EMBL; KZ679275; PTB35528.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T3YSI2; -.
DR   STRING; 1042311.A0A2T3YSI2; -.
DR   OrthoDB; 180749at2759; -.
DR   Proteomes; UP000240493; Unassembled WGS sequence.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   CDD; cd00195; UBCc; 1.
DR   Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 1.
DR   InterPro; IPR000608; UBQ-conjugat_E2.
DR   InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR   PANTHER; PTHR24067:SF257; UBC CORE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR24067; UBIQUITIN-CONJUGATING ENZYME E2; 1.
DR   Pfam; PF00179; UQ_con; 1.
DR   SMART; SM00212; UBCc; 1.
DR   SUPFAM; SSF54495; UBC-like; 1.
DR   PROSITE; PS50127; UBC_2; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000240493};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT   TRANSMEM        282..303
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          16..167
FT                   /note="UBC core"
FT                   /evidence="ECO:0000259|PROSITE:PS50127"
FT   REGION          200..225
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        200..218
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   305 AA;  33463 MW;  1C98C3743EA7C669 CRC64;
     MATSTGAASY TNTKSPTIRR ILREAAELSN TPSPDYTAEP LESDLFEWHF TLRGPPNSAY
     SQGVYHGRII LPPAYPLRPP SFRFSTPNGR FEANREICLS ISGHHEETWQ PAWGIRTALV
     ALRSFMETDV LGQLGGMETT EAVRRRLAQE SVSFKCAVCA KSNADIIAEC EDRCKETAAL
     CQEIAVPAEL NMNWRDELEA TKNDHSSSTR RSENPSEPVR DGELPVAEPS EAELAEGFVQ
     TTPNITDDLS THPPTPMLAI RNRQAPFPTS PTGTGAEGVP LWIDRVIVAL VILLVAIVLK
     VLLGI
//
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