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Database: UniProt
Entry: A0A169YG54_9HYPO
LinkDB: A0A169YG54_9HYPO
Original site: A0A169YG54_9HYPO 
ID   A0A169YG54_9HYPO        Unreviewed;       177 AA.
AC   A0A169YG54;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=Diphthamide biosynthesis protein 4 {ECO:0000256|ARBA:ARBA00021797};
GN   ORFNames=BBO_06667 {ECO:0000313|EMBL:OAA39243.1};
OS   Beauveria brongniartii RCEF 3172.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria;
OC   Beauveria brongniartii.
OX   NCBI_TaxID=1081107 {ECO:0000313|EMBL:OAA39243.1, ECO:0000313|Proteomes:UP000076863};
RN   [1] {ECO:0000313|EMBL:OAA39243.1, ECO:0000313|Proteomes:UP000076863}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCEF 3172 {ECO:0000313|EMBL:OAA39243.1,
RC   ECO:0000313|Proteomes:UP000076863};
RX   PubMed=27071652; DOI=10.1093/gbe/evw082;
RA   Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT   "Divergent and convergent evolution of fungal pathogenicity.";
RL   Genome Biol. Evol. 8:1374-1387(2016).
CC   -!- FUNCTION: Required for the first step of diphthamide biosynthesis, the
CC       transfer of 3-amino-3-carboxypropyl from S-adenosyl-L-methionine to a
CC       histidine residue. Diphthamide is a post-translational modification of
CC       histidine which occurs in elongation factor 2.
CC       {ECO:0000256|ARBA:ARBA00003474}.
CC   -!- PATHWAY: Protein modification; peptidyl-diphthamide biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00005156}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the DPH4 family.
CC       {ECO:0000256|ARBA:ARBA00006169}.
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:OAA39243.1}.
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DR   EMBL; AZHA01000023; OAA39243.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A169YG54; -.
DR   OrthoDB; 1054714at2759; -.
DR   UniPathway; UPA00559; -.
DR   Proteomes; UP000076863; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0017183; P:protein histidyl modification to diphthamide; IEA:UniProtKB-UniPathway.
DR   CDD; cd06257; DnaJ; 1.
DR   Gene3D; 1.10.287.110; DnaJ domain; 1.
DR   Gene3D; 3.10.660.10; DPH Zinc finger; 1.
DR   InterPro; IPR001623; DnaJ_domain.
DR   InterPro; IPR044248; DPH3/4-like.
DR   InterPro; IPR007872; DPH_MB_dom.
DR   InterPro; IPR036671; DPH_MB_sf.
DR   InterPro; IPR036869; J_dom_sf.
DR   PANTHER; PTHR21454:SF46; DIPHTHAMIDE BIOSYNTHESIS PROTEIN 4; 1.
DR   PANTHER; PTHR21454; DPH3 HOMOLOG-RELATED; 1.
DR   Pfam; PF00226; DnaJ; 1.
DR   Pfam; PF05207; zf-CSL; 1.
DR   SMART; SM00271; DnaJ; 1.
DR   SUPFAM; SSF46565; Chaperone J-domain; 1.
DR   SUPFAM; SSF144217; CSL zinc finger; 1.
DR   PROSITE; PS50076; DNAJ_2; 1.
DR   PROSITE; PS51074; DPH_MB; 1.
PE   3: Inferred from homology;
FT   DOMAIN          14..92
FT                   /note="J"
FT                   /evidence="ECO:0000259|PROSITE:PS50076"
FT   DOMAIN          111..173
FT                   /note="DPH-type MB"
FT                   /evidence="ECO:0000259|PROSITE:PS51074"
SQ   SEQUENCE   177 AA;  19769 MW;  A9EB6A06E614BF8A CRC64;
     MTSSSAGRPS RTATHYEVLN LQPVLLGAAE PRDASTLVKR AYHRALLRNH PDKAAEAGRE
     QYDVSMFTVD QISDAYAVLS SPQRRKEYDA GLRMSRIAGG GQDEDAKFQT GIENVDLDDL
     DFDEAGQRWY RSCRCGNDRG YSFEEEDLVE SSEDGVLLVG CQDCSLWLKV HFAVVEE
//
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