ID A0A195CBA3_9HYME Unreviewed; 600 AA.
AC A0A195CBA3;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
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=ALC62_11428 {ECO:0000313|EMBL:KYM98082.1};
OS Cyphomyrmex costatus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Cyphomyrmex.
OX NCBI_TaxID=456900 {ECO:0000313|EMBL:KYM98082.1, ECO:0000313|Proteomes:UP000078542};
RN [1] {ECO:0000313|EMBL:KYM98082.1, ECO:0000313|Proteomes:UP000078542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS0001 {ECO:0000313|EMBL:KYM98082.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KYM98082.1};
RA Nygaard S., Hu H., Boomsma J., Zhang G.;
RT "Cyphomyrmex costatus WGS genome.";
RL Submitted (MAR-2016) 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; KQ978023; KYM98082.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A195CBA3; -.
DR STRING; 456900.A0A195CBA3; -.
DR UniPathway; UPA00559; -.
DR Proteomes; UP000078542; 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:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0017183; P:protein histidyl modification to diphthamide; IEA:UniProtKB-UniPathway.
DR CDD; cd19712; bHLH_TS_dimmed_like; 1.
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 Gene3D; 4.10.280.10; Helix-loop-helix DNA-binding domain; 1.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR016435; DPH1/DPH2.
DR InterPro; IPR042263; DPH1/DPH2_1.
DR InterPro; IPR042264; DPH1/DPH2_2.
DR InterPro; IPR042265; DPH1/DPH2_3.
DR InterPro; IPR022428; Dph2_arc.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR NCBIfam; TIGR03682; arCOG04112; 1.
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 Pfam; PF00010; HLH; 1.
DR SFLD; SFLDG01121; Diphthamide_biosynthesis; 1.
DR SFLD; SFLDS00032; Radical_SAM_3-amino-3-carboxyp; 1.
DR SMART; SM00353; HLH; 1.
DR SUPFAM; SSF47459; HLH, helix-loop-helix DNA-binding domain; 1.
DR PROSITE; PS50888; BHLH; 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:UP000078542};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 474..526
FT /note="BHLH"
FT /evidence="ECO:0000259|PROSITE:PS50888"
FT REGION 429..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 536..556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 573..600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..455
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 580..594
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 600 AA; 68238 MW; 6EEAC9A45A34E27F CRC64;
MAEQNDSVVV IKAKPVRKVF KAPTRVSKIP EELLNDPLLN SAIAALPENY NFEIHKTIWR
IREAKAKRVV LQMPEGLLIY ATTIADIIED FTEAETVIMA DVTYGACCID DYTTRALDAD
FLVHYGHSCL IPVDQTAGIK VLYVFVTIKI DISHCVDCLK VTLSVTTKIA LVSTIQFATT
VQAVAAELRR EGYEISVPQS KPLSPGEILG CTAPQVRCAD AVMYIGDGRF HLEAVMIANP
KLRAFKYDPY AKKLTEEFYD HERMLKTRHE AIQRATETDK YALVLSTLGR QGSPRVLKTL
QDKIEALGKE NVVILLSEIF PDKIKLFKDV DAFIQVACPR LSIDWGVAFE KPFLTPYEGA
VALRMAEFDK DRPYPMDFYA TISLGPWTAN HRESEMEKTD ACCGHFLTSL INDLTIDIDK
KRKEYTMRSK VTNENTWATE SKQRSNKRLR QTRKTESSGL SKSSKGNTAW ERTLRRLESN
ERERMRMHCM NDAFQSLREV IPHVSKEKRL SKMETLTLAK NYIVALTDVI CAMRSEERSD
NERTNNSERQ DSPIIEQQLK STTVCVNVPA ASESYDSETK NFYQNKHSRW EKDQDNITGL
//
