ID   DPH4_EMENI              Reviewed;         188 AA.
AC   P0C0V5; C8VNH6; Q5BCV0;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Diphthamide biosynthesis protein 4;
GN   Name=dph4; ORFNames=AN10224;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
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 (By similarity).
CC       {ECO:0000250}.
CC   -!- PATHWAY: Protein modification; peptidyl-diphthamide biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- DOMAIN: The DPH-type metal-binding (MB) domain can bind either zinc or
CC       iron ions. {ECO:0000255|PROSITE-ProRule:PRU00456}.
CC   -!- SIMILARITY: Belongs to the DPH4 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAA64750.1; Type=Erroneous gene model prediction; Note=The predicted gene AN1630 has been split into 2 genes: AN10220 and AN10224.; Evidence={ECO:0000305};
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DR   EMBL; AACD01000026; EAA64750.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BN001307; CBF85256.1; -; Genomic_DNA.
DR   RefSeq; XP_659234.1; XM_654142.1.
DR   AlphaFoldDB; P0C0V5; -.
DR   STRING; 162425.CADANIAP00008268; -.
DR   EnsemblFungi; CBF85256; CBF85256; ANIA_10224.
DR   EnsemblFungi; EAA64750; EAA64750; AN1630.2.
DR   GeneID; 2875528; -.
DR   KEGG; ani:AN1630.2; -.
DR   VEuPathDB; FungiDB:AN10224; -.
DR   eggNOG; KOG0714; Eukaryota.
DR   HOGENOM; CLU_036959_1_2_1; -.
DR   InParanoid; P0C0V5; -.
DR   OMA; CWYRGCR; -.
DR   OrthoDB; 1580122at2759; -.
DR   UniPathway; UPA00559; -.
DR   Proteomes; UP000000560; Chromosome VII.
DR   Proteomes; UP000005890; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0017183; P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine; IBA:GO_Central.
DR   GO; GO:0002098; P:tRNA wobble uridine modification; IBA:GO_Central.
DR   CDD; cd06257; DnaJ; 1.
DR   Gene3D; 1.10.287.110; -; 1.
DR   Gene3D; 3.10.660.10; -; 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; PTHR21454; 1.
DR   Pfam; PF00226; DnaJ; 1.
DR   Pfam; PF05207; zf-CSL; 1.
DR   SMART; SM00271; DnaJ; 1.
DR   SUPFAM; SSF144217; SSF144217; 1.
DR   SUPFAM; SSF46565; SSF46565; 1.
DR   PROSITE; PS50076; DNAJ_2; 1.
DR   PROSITE; PS51074; DPH_MB; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Iron; Metal-binding; Nucleus; Reference proteome; Zinc.
FT   CHAIN           1..188
FT                   /note="Diphthamide biosynthesis protein 4"
FT                   /id="PRO_0000071148"
FT   DOMAIN          13..97
FT                   /note="J"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT   DOMAIN          120..184
FT                   /note="DPH-type MB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00456"
FT   BINDING         144
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00456"
FT   BINDING         146
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00456"
FT   BINDING         172
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00456"
FT   BINDING         175
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00456"
SQ   SEQUENCE   188 AA;  20548 MW;  E3612B893C1BFBC7 CRC64;
     MTQTSAAPTT TPSFYEILNL PFPSTGLSKQ QLKIAYHKAL LKHHPDKAVA VAKENLPSSN
     HGPAQPPSNQ KITIDAITTA YKTLSDPVQR AEYDRVLRLD RNRVNGAGDK NGNGTVFHTG
     LEVVDLEDLD CDEGGDEAMW YMACRCGDER GFSLSESDLE READSGEIVV GCRGCSLYTK
     VLFAVQDD