ID A0A395MTG7_9HYPO Unreviewed; 263 AA.
AC A0A395MTG7;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
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=FIE12Z_4562 {ECO:0000313|EMBL:RFN51244.1};
OS Fusarium flagelliforme.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium incarnatum-equiseti species complex.
OX NCBI_TaxID=2675880 {ECO:0000313|EMBL:RFN51244.1, ECO:0000313|Proteomes:UP000265631};
RN [1] {ECO:0000313|EMBL:RFN51244.1, ECO:0000313|Proteomes:UP000265631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 13405 {ECO:0000313|EMBL:RFN51244.1,
RC ECO:0000313|Proteomes:UP000265631};
RX PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA Busman M., Gutierrez S.;
RT "Evolution of structural diversity of trichothecenes, a family of toxins
RT produced by plant pathogenic and entomopathogenic fungi.";
RL PLoS Pathog. 14:e1006946-e1006946(2018).
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004586}. Membrane
CC {ECO:0000256|ARBA:ARBA00004370}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RFN51244.1}.
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DR EMBL; PXXK01000115; RFN51244.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395MTG7; -.
DR STRING; 2594813.A0A395MTG7; -.
DR OrthoDB; 180749at2759; -.
DR Proteomes; UP000265631; 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:UP000265631};
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 242..260
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 5..155
FT /note="UBC core"
FT /evidence="ECO:0000259|PROSITE:PS50127"
FT REGION 146..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 263 AA; 29048 MW; 230AB65A90D3F578 CRC64;
MASKAATKRL TREYKTISEN PPPYIVAHPS ESNILEWHYI ITGPENTPYH GGQYWGTLMF
PPNYPFAPPA IRMHTPSGRF QPSTRLCLSI SDFHPKSFNP AWEVSTILIG LLSFMTSEEM
TTGSVSSTAA ERKYLAARSR WWNSTGNGSH LKSNPQKGNI KAGDGGAKFR GEWPEVDVEN
WEWMTKNKVD PVTGNRLDAD NNGSCRPQLG IAGTSGHQTQ AVVDVVNQQR DAGAGFIFRN
KLFCAGAAIF LYVLVARIIS GDE
//
