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Database: UniProt
Entry: G8BIH7_CANPC
LinkDB: G8BIH7_CANPC
Original site: G8BIH7_CANPC 
ID   G8BIH7_CANPC            Unreviewed;       541 AA.
AC   G8BIH7;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 51.
DE   RecName: Full=2-(3-amino-3-carboxypropyl)histidine synthase subunit 2 {ECO:0000256|RuleBase:RU364133};
GN   OrderedLocusNames=CPAR2_402430 {ECO:0000313|CGD:CAL0000153979,
GN   ECO:0000313|EMBL:CCE44442.1};
OS   Candida parapsilosis (strain CDC 317 / ATCC MYA-4646) (Yeast) (Monilia
OS   parapsilosis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=578454 {ECO:0000313|EMBL:CCE44442.1, ECO:0000313|Proteomes:UP000005221};
RN   [1] {ECO:0000313|Proteomes:UP000005221}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 317 / ATCC MYA-4646 {ECO:0000313|Proteomes:UP000005221};
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA   Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA   Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA   Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA   Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA   Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA   Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
RN   [2] {ECO:0000313|Proteomes:UP000005221}
RP   GENOME REANNOTATION.
RC   STRAIN=CDC 317 / ATCC MYA-4646 {ECO:0000313|Proteomes:UP000005221};
RX   PubMed=22192698; DOI=10.1186/1471-2164-12-628;
RA   Guida A., Lindstaedt C., Maguire S.L., Ding C., Higgins D.G., Corton N.J.,
RA   Berriman M., Butler G.;
RT   "Using RNA-seq to determine the transcriptional landscape and the hypoxic
RT   response of the pathogenic yeast Candida parapsilosis.";
RL   BMC Genomics 12:628-628(2011).
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. Facilitates the reduction of the catalytic iron-sulfur
CC       cluster found in the DPH1 subunit. {ECO:0000256|RuleBase:RU364133}.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
CC   -!- PATHWAY: Protein modification; peptidyl-diphthamide biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00005156, ECO:0000256|RuleBase:RU364133}.
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:0000256|ARBA:ARBA00034128}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU364133}.
CC   -!- SIMILARITY: Belongs to the DPH1/DPH2 family. DPH2 subfamily.
CC       {ECO:0000256|ARBA:ARBA00006179, ECO:0000256|RuleBase:RU364133}.
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DR   EMBL; HE605208; CCE44442.1; -; Genomic_DNA.
DR   AlphaFoldDB; G8BIH7; -.
DR   STRING; 578454.G8BIH7; -.
DR   EnsemblFungi; CPAR2_402430-T; CPAR2_402430-T-p1; CPAR2_402430.
DR   CGD; CAL0000153979; CPAR2_402430.
DR   VEuPathDB; FungiDB:CPAR2_402430; -.
DR   eggNOG; KOG2648; Eukaryota.
DR   UniPathway; UPA00559; -.
DR   Proteomes; UP000005221; Chromosome 4.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0032991; C:protein-containing complex; IEA:EnsemblFungi.
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; IEA:EnsemblFungi.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0017183; P:protein histidyl modification to diphthamide; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.11840; Diphthamide synthesis DPH1/DPH2 domain 1; 1.
DR   Gene3D; 3.40.50.11860; Diphthamide synthesis DPH1/DPH2 domain 3; 1.
DR   InterPro; IPR010014; DHP2.
DR   InterPro; IPR016435; DPH1/DPH2.
DR   InterPro; IPR042263; DPH1/DPH2_1.
DR   InterPro; IPR042265; DPH1/DPH2_3.
DR   NCBIfam; TIGR00322; diphth2_R; 1.
DR   NCBIfam; TIGR00272; DPH2; 1.
DR   PANTHER; PTHR10762:SF2; 2-(3-AMINO-3-CARBOXYPROPYL)HISTIDINE SYNTHASE SUBUNIT 2; 1.
DR   PANTHER; PTHR10762; DIPHTHAMIDE BIOSYNTHESIS PROTEIN; 1.
DR   Pfam; PF01866; Diphthamide_syn; 1.
DR   SFLD; SFLDG01121; Diphthamide_biosynthesis; 1.
DR   SFLD; SFLDF00408; Diphthamide_biosynthesis_famil; 1.
DR   SFLD; SFLDS00032; Radical_SAM_3-amino-3-carboxyp; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|RuleBase:RU364133};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU364133};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU364133};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU364133};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005221}.
FT   REGION          409..441
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        415..432
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   541 AA;  61432 MW;  07ABF4EA33973902 CRC64;
     MHSEEPVAPA LSTYQDESTF SYDKVQSTHK ERRHLHLKSP QDQNEVLNKI RDYYSLDILA
     EKLSEIDGDE PRYKRITLQF PDELICDSAT IVHYLQEKLE IDASNPKQKL WILADTSYSA
     CCVDEIAAEH VHSDLVIHFG DACLNEVAKL NSKYVLGKPE VDVDEMARQF KNRYSTGDKV
     VLMANAPFTY ILYQLKDKLS GYKDVIVADL IVPSWKSEII GYLPTYDNKV SKFNRTFPVE
     NISECELFHV TVPEAPRLLQ LTTNFASVTT YEPDTSTISQ GPYPNLMRRY KFVHVARSAG
     TIGILVNTLS LSNTKQLINT IKDKIKKAGK KHYIFVVGKP NVAKLANFES IDLWCVLGCD
     HQGIIIDQVN EFFKPIVTPY ELLLGLSDEL TWTGKWITDY KSVIEDYKHD EEDAPREDDG
     DDKDEASSDE EPEFDPVTGT YVSMSRPLRQ INHLSIKNEG EQETKANNEK RLVERFSNSV
     AIRNTVSTSA MHLQNRQWTG LGSDYANDDG SDVEEEGALV TEGRLGIARG YDFDTQKQQS
     K
//
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