ID W3XNW5_PESFW Unreviewed; 287 AA.
AC W3XNW5;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Diphthamide biosynthesis protein 4 {ECO:0000256|ARBA:ARBA00021797};
GN ORFNames=PFICI_01556 {ECO:0000313|EMBL:ETS87728.1};
OS Pestalotiopsis fici (strain W106-1 / CGMCC3.15140).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Sporocadaceae; Pestalotiopsis.
OX NCBI_TaxID=1229662 {ECO:0000313|EMBL:ETS87728.1, ECO:0000313|Proteomes:UP000030651};
RN [1] {ECO:0000313|Proteomes:UP000030651}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W106-1 / CGMCC3.15140 {ECO:0000313|Proteomes:UP000030651};
RX PubMed=25623211; DOI=10.1186/s12864-014-1190-9;
RA Wang X., Zhang X., Liu L., Xiang M., Wang W., Sun X., Che Y., Guo L.,
RA Liu G., Guo L., Wang C., Yin W.B., Stadler M., Zhang X., Liu X.;
RT "Genomic and transcriptomic analysis of the endophytic fungus
RT Pestalotiopsis fici reveals its lifestyle and high potential for synthesis
RT of natural products.";
RL BMC Genomics 16:28-28(2015).
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}.
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DR EMBL; KI912109; ETS87728.1; -; Genomic_DNA.
DR RefSeq; XP_007828328.1; XM_007830137.1.
DR AlphaFoldDB; W3XNW5; -.
DR STRING; 1229662.W3XNW5; -.
DR GeneID; 19266569; -.
DR KEGG; pfy:PFICI_01556; -.
DR eggNOG; KOG0714; Eukaryota.
DR HOGENOM; CLU_017633_7_0_1; -.
DR InParanoid; W3XNW5; -.
DR OMA; WYHACRC; -.
DR OrthoDB; 1054714at2759; -.
DR UniPathway; UPA00559; -.
DR Proteomes; UP000030651; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; 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 PRINTS; PR00625; JDOMAIN.
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;
KW Reference proteome {ECO:0000313|Proteomes:UP000030651}.
FT DOMAIN 11..100
FT /note="J"
FT /evidence="ECO:0000259|PROSITE:PS50076"
FT DOMAIN 155..218
FT /note="DPH-type MB"
FT /evidence="ECO:0000259|PROSITE:PS51074"
FT REGION 1..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 96..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 136..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 221..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..75
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..154
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..246
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..263
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 287 AA; 31517 MW; B6979527E0FE45FE CRC64;
MAPSSSSQEP SHFEVLSLTP NSLDGQDSST QAKTVKQAYR RALLKHHPDK NQQAKAQDSP
ADPAETKKKN GDEQFTVDQI TEAFTVLSDT RQRREYVRSL QTESRTSTTG GGGGANFSSS
SRQKQDYTYQ QTFNFKHSQQ QPAQQQQARP HSSSGVETVD LDDVKWDGKR QVYHHTCGRC
GTDRGYCFRE LDLDEVGEDG ELMVQCTGCS LWLRVLFDEA EDDEDDEERQ QGGAGKDVKS
RSGSQGEELR HTTSGSSSGK SGGWSWKFNF GISIGGGASA SASAGRK
//
