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Database: UniProt
Entry: A0A395STP8_9HYPO
LinkDB: A0A395STP8_9HYPO
Original site: A0A395STP8_9HYPO 
ID   A0A395STP8_9HYPO        Unreviewed;       403 AA.
AC   A0A395STP8;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=UBC core domain-containing protein {ECO:0000259|PROSITE:PS50127};
GN   ORFNames=FLONG3_5685 {ECO:0000313|EMBL:RGP75432.1};
OS   Fusarium longipes.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX   NCBI_TaxID=694270 {ECO:0000313|EMBL:RGP75432.1, ECO:0000313|Proteomes:UP000266234};
RN   [1] {ECO:0000313|EMBL:RGP75432.1, ECO:0000313|Proteomes:UP000266234}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 20695 {ECO:0000313|EMBL:RGP75432.1,
RC   ECO:0000313|Proteomes:UP000266234};
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   -!- 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:RGP75432.1}.
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DR   EMBL; PXOG01000122; RGP75432.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A395STP8; -.
DR   STRING; 694270.A0A395STP8; -.
DR   Proteomes; UP000266234; Unassembled WGS sequence.
DR   Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 2.
DR   InterPro; IPR000608; UBQ-conjugat_E2.
DR   InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR   PANTHER; PTHR24067:SF292; CONJUGATING ENZYME, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G15040)-RELATED; 1.
DR   PANTHER; PTHR24067; UBIQUITIN-CONJUGATING ENZYME E2; 1.
DR   Pfam; PF00179; UQ_con; 2.
DR   SMART; SM00212; UBCc; 2.
DR   SUPFAM; SSF54495; UBC-like; 2.
DR   PROSITE; PS50127; UBC_2; 2.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000266234};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT   DOMAIN          1..124
FT                   /note="UBC core"
FT                   /evidence="ECO:0000259|PROSITE:PS50127"
FT   DOMAIN          249..403
FT                   /note="UBC core"
FT                   /evidence="ECO:0000259|PROSITE:PS50127"
FT   REGION          382..403
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   403 AA;  46364 MW;  92B9872202A21AA7 CRC64;
     MGPHETPYEF GFFEFAIRFH KDYPSKSPTV VCVTTNGGRC RFNPNVYSNG KVCLSILGTW
     RGERGEEWSS AQGLESILLS IQSLLSSNPY ENEPGFEDAN EESDKKAQKD YVQKIRHETL
     RISVIQRLEG YLGLSSNGAQ QHSTSGPDME DEDVDEATVP FEPFKDLCKR RFLWYFESYL
     AAVEKGKTET KPNQMFARMP FESPGNNSMD GKFNYPELER RLHAIKAAVD AEPLKWAEEG
     LEAKKWETTV AVNLQHQFEQ VVEAFKRGDM PHDVFLENEN PFVWVVTYFG RPMTNLDGGL
     FRIKMNFSVR FPEEQPRVKF ETKIFHHHIA ADGTACYTPN PAKREDVRSH IEAIFAILED
     DEPAYDPRKI VNPEATKMYW GGGADDKKKY NRRLRRSVQQ SME
//
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