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Database: UniProt
Entry: A0A166JG82_9AGAM
LinkDB: A0A166JG82_9AGAM
Original site: A0A166JG82_9AGAM 
ID   A0A166JG82_9AGAM        Unreviewed;       301 AA.
AC   A0A166JG82;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
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=FIBSPDRAFT_826544 {ECO:0000313|EMBL:KZP20826.1};
OS   Fibularhizoctonia sp. CBS 109695.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Atheliales; Atheliaceae; Fibularhizoctonia.
OX   NCBI_TaxID=436010 {ECO:0000313|EMBL:KZP20826.1, ECO:0000313|Proteomes:UP000076532};
RN   [1] {ECO:0000313|EMBL:KZP20826.1, ECO:0000313|Proteomes:UP000076532}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 109695 {ECO:0000313|EMBL:KZP20826.1,
RC   ECO:0000313|Proteomes:UP000076532};
RX   PubMed=26659563; DOI=10.1093/molbev/msv337;
RA   Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA   Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA   Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA   Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT   "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT   Insights into the Origins of Lignocellulose Decay Capabilities.";
RL   Mol. Biol. Evol. 33:959-970(2016).
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004586}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004370}.
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DR   EMBL; KV417552; KZP20826.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A166JG82; -.
DR   STRING; 436010.A0A166JG82; -.
DR   OrthoDB; 180749at2759; -.
DR   Proteomes; UP000076532; 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   Reference proteome {ECO:0000313|Proteomes:UP000076532};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT   DOMAIN          9..162
FT                   /note="UBC core"
FT                   /evidence="ECO:0000259|PROSITE:PS50127"
FT   REGION          207..268
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        236..255
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   301 AA;  32524 MW;  248E373AE7E4EE5F CRC64;
     MAALNKNNSA VKRIMQEARE LANDPCTDYS GAPLEDDIFE WHCTLRGPAD TEFEGGLYHF
     RILLPAEYPF RPPSIMILTP NGRFELNTKI CISFTNYHED LWQPAWGVRT AIIGLQGFFP
     LKGQAAVGVG SIEYPVSERK RLAALSREWI CPHCQQTNLD ALPDPAAAGD PSSSCVVAAA
     PASVNTATAD SLSIPQLDST EDDATSLIDT GAVDTPRSGP PTPEMEEDRE AEDPPTAAGT
     TQSQNARSES ASEISNLPHP VPHDHSRILL NPTTTRSVRT VDSAIGVLLV LAVALVCRRL
     V
//
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