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DPH2_ASPFU
ID   DPH2_ASPFU              Reviewed;         565 AA.
AC   Q4WN99;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=2-(3-amino-3-carboxypropyl)histidine synthase subunit 2 {ECO:0000305};
DE   AltName: Full=Diphthamide biosynthesis protein 2;
DE   AltName: Full=Diphtheria toxin resistance protein 2 {ECO:0000305};
DE   AltName: Full=S-adenosyl-L-methionine:L-histidine 3-amino-3-carboxypropyltransferase 2 {ECO:0000305};
GN   Name=dph2; ORFNames=AFUA_6G07100;
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(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 dph3 and a NADH-dependent
CC       reductase, predominantly cbr1 (By similarity). Facilitates the
CC       reduction of the catalytic iron-sulfur cluster found in the dph1
CC       subunit (By similarity). {ECO:0000250|UniProtKB:P32461}.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000250|UniProtKB:P32461};
CC       Note=Binds 1 [4Fe-4S] cluster per subunit. The cluster facilitates the
CC       reduction of the catalytic iron-sulfur cluster in the dph1 subunit.
CC       {ECO:0000250|UniProtKB:P32461};
CC   -!- PATHWAY: Protein modification; peptidyl-diphthamide biosynthesis.
CC       {ECO:0000250|UniProtKB:P32461}.
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:P32461}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P32461}.
CC   -!- SIMILARITY: Belongs to the DPH1/DPH2 family. DPH2 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AAHF01000006; EAL88565.1; -; Genomic_DNA.
DR   RefSeq; XP_750603.1; XM_745510.1.
DR   AlphaFoldDB; Q4WN99; -.
DR   SMR; Q4WN99; -.
DR   STRING; 746128.CADAFUBP00007111; -.
DR   EnsemblFungi; EAL88565; EAL88565; AFUA_6G07100.
DR   GeneID; 3508816; -.
DR   KEGG; afm:AFUA_6G07100; -.
DR   VEuPathDB; FungiDB:Afu6g07100; -.
DR   eggNOG; KOG2648; Eukaryota.
DR   HOGENOM; CLU_015210_1_1_1; -.
DR   InParanoid; Q4WN99; -.
DR   OMA; PFNNMYD; -.
DR   OrthoDB; 750182at2759; -.
DR   UniPathway; UPA00559; -.
DR   Proteomes; UP000002530; Chromosome 6.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
DR   GO; GO:0090560; F:2-(3-amino-3-carboxypropyl)histidine synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; ISS:UniProtKB.
DR   GO; GO:0017183; P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine; ISS:UniProtKB.
DR   Gene3D; 3.40.50.11840; -; 1.
DR   Gene3D; 3.40.50.11860; -; 1.
DR   InterPro; IPR010014; DHP2.
DR   InterPro; IPR016435; DPH1/DPH2.
DR   InterPro; IPR042263; DPH1/DPH2_1.
DR   InterPro; IPR042265; DPH1/DPH2_3.
DR   PANTHER; PTHR10762; PTHR10762; 1.
DR   PANTHER; PTHR10762:SF2; PTHR10762:SF2; 1.
DR   Pfam; PF01866; Diphthamide_syn; 1.
DR   SFLD; SFLDS00032; Radical_SAM_3-amino-3-carboxyp; 1.
DR   TIGRFAMs; TIGR00322; diphth2_R; 1.
DR   TIGRFAMs; TIGR00272; DPH2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Iron; Iron-sulfur; Metal-binding; Reference proteome.
FT   CHAIN           1..565
FT                   /note="2-(3-amino-3-carboxypropyl)histidine synthase
FT                   subunit 2"
FT                   /id="PRO_0000083383"
FT   REGION          424..458
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          464..483
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        434..449
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         139
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:P32461"
FT   BINDING         160
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:P32461"
FT   BINDING         377
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:P32461"
SQ   SEQUENCE   565 AA;  62076 MW;  9F651FFA78526F02 CRC64;
     MATEMQAAPV LSTPDSLILE ATEPVARQNA TRTLSDEELS ITYDIERTLQ EIRQARYKRI
     ALQFPDDMLP DAPRVFQLLS RGLACRDVDK ITVEKNGNGT GGVESEKLAQ DVSQLSVDDK
     PEPEPKLYIL ADTSYGTCCV DEVAAEHVNA DVVVHYGRSC LSPTARLPVI YVFTHKELPI
     EPVIQAFKAT YPDQATKIIL AADVTYCDHI PAVYARLMEE GYTNLYATEL IHCPSSAIPN
     RTVPDSVREN PDTLSEWQLF HISDPPTALL LTLASRVAAI HIYPTTDAPS DNVKPLPVST
     SAALGRRYAI LTRLSTVPIF GILINTLSVK NYLHIVEHVK QKIADAGKKS YMFVVGKLNA
     AKVANFSEIG GWVVIGCWES SLVDSKDFWK PVITPFELEL ALKGDHERVW TGAWQSDFQS
     ILDQPAEEAQ TADHEESPND DDDMSEPESA PPEFDLRTGR YVSHTRPMRN PAPRVSAQSD
     DAVSAASGPA AARALARRAK GELAMIGGTV SPGAEYLRSQ RTWKGLGSDF DIQYDDEDPS
     DSTLVVEGRK GIARGYTVGD SIEKH
 
 
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