ID A8WSY5_CAEBR Unreviewed; 479 AA.
AC A8WSY5;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 94.
DE RecName: Full=2-(3-amino-3-carboxypropyl)histidine synthase subunit 2 {ECO:0000256|ARBA:ARBA00021914, ECO:0000256|RuleBase:RU364133};
GN Name=dph-2 {ECO:0000313|WormBase:CBG03025};
GN Synonyms=Cbr-dph-2 {ECO:0000313|EMBL:CAP23595.1};
GN ORFNames=CBG03025 {ECO:0000313|WormBase:CBG03025}, CBG_03025
GN {ECO:0000313|EMBL:CAP23595.1};
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238 {ECO:0000313|EMBL:CAP23595.1, ECO:0000313|Proteomes:UP000008549};
RN [1] {ECO:0000313|EMBL:CAP23595.1, ECO:0000313|Proteomes:UP000008549}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16 {ECO:0000313|EMBL:CAP23595.1,
RC ECO:0000313|Proteomes:UP000008549};
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
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 -!- SIMILARITY: Belongs to the DPH1/DPH2 family. DPH2 subfamily.
CC {ECO:0000256|ARBA:ARBA00006179, ECO:0000256|RuleBase:RU364133}.
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DR EMBL; HE601438; CAP23595.1; -; Genomic_DNA.
DR RefSeq; XP_002631227.1; XM_002631181.1.
DR AlphaFoldDB; A8WSY5; -.
DR STRING; 6238.A8WSY5; -.
DR EnsemblMetazoa; CBG03025.1; CBG03025.1; WBGene00025970.
DR GeneID; 8572741; -.
DR KEGG; cbr:CBG_03025; -.
DR CTD; 8572741; -.
DR WormBase; CBG03025; CBP00644; WBGene00025970; Cbr-dph-2.
DR eggNOG; KOG2648; Eukaryota.
DR HOGENOM; CLU_015210_1_0_1; -.
DR InParanoid; A8WSY5; -.
DR OMA; TCRPLEH; -.
DR OrthoDB; 5491765at2759; -.
DR UniPathway; UPA00559; -.
DR Proteomes; UP000008549; Unassembled WGS sequence.
DR GO; GO:0090560; F:2-(3-amino-3-carboxypropyl)histidine synthase activity; IEA:UniProtKB-EC.
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; IBA:GO_Central.
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; SFLDS00032; Radical_SAM_3-amino-3-carboxyp; 1.
PE 3: Inferred from homology;
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:UP000008549}.
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 460..479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 479 AA; 53364 MW; 3ED3CEAEBAF89664 CRC64;
MTESVPGPFF TTATPTDHIQ DEQSPYTGYF ESLSENDIHL FFEIEATSEW IRNSNHQRIA
LQFPDSLLPY SKRVTKLIES KIGDDENPEI VKKTFVLADT TYRSCCVDEV AAAHANCTAL
VHFGEACHSA PTDKIDVKFV LGNLPTFIDE FRVKLKEIVN ELSTDHIVLL MDSCFAHEQE
KVVAVIEEIV PPTKKVSCAS LPSEENLKEH RKNVYLGREI SAALRDNLPA DLIFCGFPNS
PLLPIWLLSY PSCMTVTHYN PMDKSIQHEN TRSSRLLRKR LFLVEKLKDA DTVGLVVGSV
GVDKHREAVK RMRELCKAAG KKIYVISVGK INVPKLSNFS TDIDVFVLLS CPFGVVLDSS
DYFRPVVSFF EAEIALNPSK TWAADFGWSA EFAAFLEDKI ETEVPEVDVG DFSLISGKVR
VVTKEDEKEG DGPRSIAIYN PGYCNDRTWK GLDDGITASE DSTTVTEGRS GIAQGYSGK
//
