ID A0A507QZC6_MONPU Unreviewed; 208 AA.
AC A0A507QZC6;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Diphthamide biosynthesis protein 4 {ECO:0000256|ARBA:ARBA00021797};
GN Name=DPH4 {ECO:0000313|EMBL:TQB73347.1};
GN ORFNames=MPDQ_005932 {ECO:0000313|EMBL:TQB73347.1};
OS Monascus purpureus (Red mold) (Monascus anka).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Monascus.
OX NCBI_TaxID=5098 {ECO:0000313|EMBL:TQB73347.1, ECO:0000313|Proteomes:UP000319663};
RN [1] {ECO:0000313|EMBL:TQB73347.1, ECO:0000313|Proteomes:UP000319663}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HQ1 {ECO:0000313|EMBL:TQB73347.1};
RA Geng C., Zhang Y.;
RT "Wine fermentation using esterase from Monascus purpureus.";
RL Submitted (JUN-2019) to the EMBL/GenBank/DDBJ databases.
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:TQB73347.1}.
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DR EMBL; VIFY01000046; TQB73347.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A507QZC6; -.
DR STRING; 5098.A0A507QZC6; -.
DR UniPathway; UPA00559; -.
DR Proteomes; UP000319663; 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 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:UP000319663}.
FT DOMAIN 9..95
FT /note="J"
FT /evidence="ECO:0000259|PROSITE:PS50076"
FT DOMAIN 116..185
FT /note="DPH-type MB"
FT /evidence="ECO:0000259|PROSITE:PS51074"
SQ SEQUENCE 208 AA; 23170 MW; 86B0D5239F0B9077 CRC64;
MAKTPIKHDF YQILSLSSPL QRPSTALSKE QIKSAYHKAL LRHHPDKANL GQTPSVSVSV
SVTTSNNTTY TIDEITTAYK TISDPKLRAD YDRSLRLERL SVAERERNGD VSFHTGLEVV
DLEDLLYEEG LDEDAGAGGF WYRGCRCGDE RGFLVTEQDL EREVEHGEVV VGCRGCSLWM
KVLFAVENEG EDQDQTADEA AGLEKGKT
//
