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Database: UniProt
Entry: H6CBC7_EXODN
LinkDB: H6CBC7_EXODN
Original site: H6CBC7_EXODN 
ID   H6CBC7_EXODN            Unreviewed;       445 AA.
AC   H6CBC7;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   24-JAN-2024, entry version 52.
DE   RecName: Full=2-(3-amino-3-carboxypropyl)histidine synthase subunit 1 {ECO:0000256|ARBA:ARBA00021915};
DE            EC=2.5.1.108 {ECO:0000256|ARBA:ARBA00012221};
DE   AltName: Full=Diphthamide biosynthesis protein 1 {ECO:0000256|ARBA:ARBA00032574};
DE   AltName: Full=Diphtheria toxin resistance protein 1 {ECO:0000256|ARBA:ARBA00032789};
DE   AltName: Full=S-adenosyl-L-methionine:L-histidine 3-amino-3-carboxypropyltransferase 1 {ECO:0000256|ARBA:ARBA00031690};
GN   ORFNames=HMPREF1120_09013 {ECO:0000313|EMBL:EHY61074.1};
OS   Exophiala dermatitidis (strain ATCC 34100 / CBS 525.76 / NIH/UT8656) (Black
OS   yeast) (Wangiella dermatitidis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=858893 {ECO:0000313|EMBL:EHY61074.1, ECO:0000313|Proteomes:UP000007304};
RN   [1] {ECO:0000313|EMBL:EHY61074.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NIH/UT8656 {ECO:0000313|EMBL:EHY61074.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Cuomo C., Wang Z., Hunicke-Smith S., Szanislo P.J., Earl A., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA   Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA   Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A.,
RA   Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA   Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Exophiala (Wangiella) dermatitidis NIH/UT8656.";
RL   Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-histidyl-[translation elongation factor 2] + S-adenosyl-L-
CC         methionine = 2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation
CC         elongation factor 2] + H(+) + S-methyl-5'-thioadenosine;
CC         Xref=Rhea:RHEA:36783, Rhea:RHEA-COMP:9748, Rhea:RHEA-COMP:9749,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17509, ChEBI:CHEBI:29979,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:73995; EC=2.5.1.108;
CC         Evidence={ECO:0000256|ARBA:ARBA00001323};
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}.
CC   -!- SIMILARITY: Belongs to the DPH1/DPH2 family. DPH1 subfamily.
CC       {ECO:0000256|ARBA:ARBA00010173}.
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DR   EMBL; JH226137; EHY61074.1; -; Genomic_DNA.
DR   RefSeq; XP_009161535.1; XM_009163287.1.
DR   AlphaFoldDB; H6CBC7; -.
DR   STRING; 858893.H6CBC7; -.
DR   GeneID; 20313652; -.
DR   VEuPathDB; FungiDB:HMPREF1120_09013; -.
DR   eggNOG; KOG2648; Eukaryota.
DR   HOGENOM; CLU_037146_1_1_1; -.
DR   InParanoid; H6CBC7; -.
DR   OMA; PGQVLGC; -.
DR   OrthoDB; 5472575at2759; -.
DR   UniPathway; UPA00559; -.
DR   Proteomes; UP000007304; Unassembled WGS sequence.
DR   GO; GO:0090560; F:2-(3-amino-3-carboxypropyl)histidine synthase activity; IEA:InterPro.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
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; 3.40.50.11850; Diphthamide synthesis DPH1/DPH2 domain 2; 1.
DR   Gene3D; 3.40.50.11860; Diphthamide synthesis DPH1/DPH2 domain 3; 1.
DR   InterPro; IPR016435; DPH1/DPH2.
DR   InterPro; IPR042263; DPH1/DPH2_1.
DR   InterPro; IPR042264; DPH1/DPH2_2.
DR   InterPro; IPR042265; DPH1/DPH2_3.
DR   NCBIfam; TIGR00322; diphth2_R; 1.
DR   PANTHER; PTHR10762:SF1; 2-(3-AMINO-3-CARBOXYPROPYL)HISTIDINE SYNTHASE SUBUNIT 1; 1.
DR   PANTHER; PTHR10762; DIPHTHAMIDE BIOSYNTHESIS PROTEIN; 1.
DR   Pfam; PF01866; Diphthamide_syn; 1.
DR   SFLD; SFLDS00032; Radical_SAM_3-amino-3-carboxyp; 1.
PE   3: Inferred from homology;
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007304};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          30..49
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   445 AA;  48919 MW;  399855930E4C5D9D CRC64;
     MDTEQPAMPG AFPASEDTIS TTRTPKRRFV GRRTAEAQAK QKQHVGSSVE ETNAIVAKSQ
     RKTPRALNQI PPEILDDPDI QAAVGLLPHN YSFEIPKTIH RIRTLQAKRV ALQFPEGLLM
     FATTISDILT QFCPGTETLI MGDVTYGACC IDDYTARALG CDLLVHYAHS CLIPVSSSKI
     ATLYIFVDIS IDTKHLVSTL SRNIPPGKTI AMVSTIQFNS ALHTIRPALE AEGLKLVVPQ
     VMPLSKGEVL GCTAPKIGPD AHVDLILYLG DGRFHLEAAM IANPDIPAYR YDPYSRKLTR
     ETYSHDEMLD MRSYAINTAK GAKKWGLILG ALGRQGNPHI LTMIENHLNM QGIPYVNLLL
     SEIFPGKLAM FEDVECWVQI ACPRLSIDWG YAFPRPLLTP YEALVVLGAI QGWEKEGGTY
     PMNYYANNGL GRATEKVAAQ VGVSA
//
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