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DPH3_CRYNJ
ID   DPH3_CRYNJ              Reviewed;         153 AA.
AC   P0CN22; Q55ZX7; Q5KP86;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 41.
DE   RecName: Full=Diphthamide biosynthesis protein 3;
GN   Name=DPH3; OrderedLocusNames=CNA03820;
OS   Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS   MYA-565) (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=214684;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JEC21 / ATCC MYA-565;
RX   PubMed=15653466; DOI=10.1126/science.1103773;
RA   Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA   Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA   Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA   Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA   Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA   Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA   Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA   Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA   Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA   Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT   "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT   neoformans.";
RL   Science 307:1321-1324(2005).
CC   -!- FUNCTION: Required for the first step of diphthamide biosynthesis, a
CC       post-translational modification of histidine which occurs in elongation
CC       factor 2. DPH1 and DPH2 transfer a 3-amino-3-carboxypropyl (ACP) group
CC       from S-adenosyl-L-methionine (SAM) to a histidine residue, the reaction
CC       is assisted by a reduction system comprising KTI11/DPH3 and a NADH-
CC       dependent reductase, predominantly CBR1. Acts as an electron donor to
CC       reduce the Fe-S cluster in DPH1-DPH2 keeping the [4Fe-4S] clusters in
CC       the active and reduced state. Restores iron to DPH1-DPH2 iron-sulfur
CC       clusters which have degraded from [4Fe-4S] to [3Fe-4S] by donating an
CC       iron atom to reform [4Fe-4S] clusters, in a manner dependent on the
CC       presence of elongation factor 2 and SAM. Associates with the elongator
CC       complex and is required for tRNA Wobble base modifications mediated by
CC       the elongator complex. The elongator complex is required for multiple
CC       tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine),
CC       mcm5s 2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-
CC       carbamoylmethyl uridine). {ECO:0000250|UniProtKB:Q3E840}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[3Fe-4S](1+)-[protein] + Fe(2+)-[Dph3] = [3Fe-4S](0)-[protein]
CC         + Fe(3+)-[Dph3]; Xref=Rhea:RHEA:71235, Rhea:RHEA-COMP:17996,
CC         Rhea:RHEA-COMP:17997, Rhea:RHEA-COMP:18002, Rhea:RHEA-COMP:18003,
CC         ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:33751,
CC         ChEBI:CHEBI:47402, ChEBI:CHEBI:83228;
CC         Evidence={ECO:0000250|UniProtKB:Q3E840};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 [3Fe-4S](0)-[protein] + 2 Fe(2+)-[Dph3] + NADH = 2 [4Fe-
CC         4S](1+)-[protein] + 2 [Dph3] + H(+) + NAD(+); Xref=Rhea:RHEA:71239,
CC         Rhea:RHEA-COMP:17997, Rhea:RHEA-COMP:17998, Rhea:RHEA-COMP:18001,
CC         Rhea:RHEA-COMP:18002, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033,
CC         ChEBI:CHEBI:33723, ChEBI:CHEBI:47402, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:83228;
CC         Evidence={ECO:0000250|UniProtKB:Q3E840};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000250|UniProtKB:Q3E840};
CC   -!- PATHWAY: Protein modification; peptidyl-diphthamide biosynthesis.
CC       {ECO:0000250|UniProtKB:Q3E840}.
CC   -!- SUBUNIT: Component of the 2-(3-amino-3-carboxypropyl)histidine synthase
CC       complex composed of DPH1, DPH2, DPH3 and a NADH-dependent reductase,
CC       predominantly CBR1. {ECO:0000250|UniProtKB:Q3E840}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- DOMAIN: The DPH-type metal-binding (MB) domain can also bind zinc.
CC       However, iron is the physiological binding partner as zinc binding
CC       impairs the protein electron donor function.
CC       {ECO:0000250|UniProtKB:Q3E840}.
CC   -!- SIMILARITY: Belongs to the DPH3 family. {ECO:0000305}.
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DR   EMBL; AE017341; AAW40902.1; -; Genomic_DNA.
DR   RefSeq; XP_566721.1; XM_566721.1.
DR   AlphaFoldDB; P0CN22; -.
DR   SMR; P0CN22; -.
DR   STRING; 5207.AAW40902; -.
DR   PaxDb; P0CN22; -.
DR   EnsemblFungi; AAW40902; AAW40902; CNA03820.
DR   VEuPathDB; FungiDB:CNA03820; -.
DR   eggNOG; KOG2923; Eukaryota.
DR   HOGENOM; CLU_1713169_0_0_1; -.
DR   InParanoid; P0CN22; -.
DR   OMA; SQKEECT; -.
DR   UniPathway; UPA00559; -.
DR   Proteomes; UP000002149; Chromosome 1.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0008198; F:ferrous iron binding; ISS:UniProtKB.
DR   GO; GO:0034986; F:iron chaperone activity; ISS:UniProtKB.
DR   GO; GO:0016491; F:oxidoreductase activity; ISS:UniProtKB.
DR   GO; GO:0017183; P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine; ISS:UniProtKB.
DR   GO; GO:0002926; P:tRNA wobble base 5-methoxycarbonylmethyl-2-thiouridinylation; ISS:UniProtKB.
DR   GO; GO:0002098; P:tRNA wobble uridine modification; IBA:GO_Central.
DR   Gene3D; 3.10.660.10; -; 1.
DR   InterPro; IPR044248; DPH3/4-like.
DR   InterPro; IPR007872; DPH_MB_dom.
DR   InterPro; IPR036671; DPH_MB_sf.
DR   PANTHER; PTHR21454; PTHR21454; 1.
DR   Pfam; PF05207; zf-CSL; 1.
DR   SUPFAM; SSF144217; SSF144217; 1.
DR   PROSITE; PS51074; DPH_MB; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Iron; Metal-binding; Nucleus; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..153
FT                   /note="Diphthamide biosynthesis protein 3"
FT                   /id="PRO_0000082629"
FT   DOMAIN          4..60
FT                   /note="DPH-type MB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00456"
FT   REGION          69..153
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        100..121
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        130..153
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         26
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:Q3E840"
FT   BINDING         28
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:Q3E840"
FT   BINDING         48
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:Q3E840"
FT   BINDING         51
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:Q3E840"
SQ   SEQUENCE   153 AA;  16987 MW;  F9034CF4B479709E CRC64;
     MPNYYDELEI EDFAWDPVAR VFHYPCPCGD RFEISKGQLR DGEEIAICPS CSLIVRVIYD
     YLDWEDYVTT DDEDDGGSVD TPLSNTSPDP AYPVVVGSAE VESQSKTASS AVSSQKEECT
     SLSDRLAGLQ VESGKEDDPV QEHKREDSSD VLH
 
 
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