ID G5AQF1_HETGA Unreviewed; 489 AA.
AC G5AQF1;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 24-JAN-2024, entry version 59.
DE RecName: Full=2-(3-amino-3-carboxypropyl)histidine synthase subunit 2 {ECO:0000256|ARBA:ARBA00021914, ECO:0000256|RuleBase:RU364133};
GN Name=DPH2 {ECO:0000313|EMBL:JAO00971.1};
GN ORFNames=GW7_04339 {ECO:0000313|EMBL:EHA99261.1};
OS Heterocephalus glaber (Naked mole rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Heterocephalus.
OX NCBI_TaxID=10181 {ECO:0000313|EMBL:EHA99261.1, ECO:0000313|Proteomes:UP000006813};
RN [1] {ECO:0000313|EMBL:EHA99261.1, ECO:0000313|Proteomes:UP000006813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993625; DOI=10.1038/nature10533;
RA Kim E.B., Fang X., Fushan A.A., Huang Z., Lobanov A.V., Han L.,
RA Marino S.M., Sun X., Turanov A.A., Yang P., Yim S.H., Zhao X.,
RA Kasaikina M.V., Stoletzki N., Peng C., Polak P., Xiong Z., Kiezun A.,
RA Zhu Y., Chen Y., Kryukov G.V., Zhang Q., Peshkin L., Yang L., Bronson R.T.,
RA Buffenstein R., Wang B., Han C., Li Q., Chen L., Zhao W., Sunyaev S.R.,
RA Park T.J., Zhang G., Wang J., Gladyshev V.N.;
RT "Genome sequencing reveals insights into physiology and longevity of the
RT naked mole rat.";
RL Nature 479:223-227(2011).
RN [2] {ECO:0000313|EMBL:JAO00971.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Kidney {ECO:0000313|EMBL:JAO00971.1};
RA Bens M., Sahm A., Jahn N., Morhart M., Holtze S., Hildebrandt T.B.,
RA Platzer M., Szafranski K.;
RT "FRAMA: From RNA-seq data to annotated mRNA assemblies.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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; JH166497; EHA99261.1; -; Genomic_DNA.
DR EMBL; GEBF01002662; JAO00971.1; -; Transcribed_RNA.
DR RefSeq; XP_004871953.1; XM_004871896.1.
DR AlphaFoldDB; G5AQF1; -.
DR STRING; 10181.G5AQF1; -.
DR Ensembl; ENSHGLT00100024516; ENSHGLP00100024269; ENSHGLG00100017819.
DR GeneID; 101717886; -.
DR KEGG; hgl:101717886; -.
DR CTD; 1802; -.
DR eggNOG; KOG2648; Eukaryota.
DR InParanoid; G5AQF1; -.
DR OMA; IEGWVVV; -.
DR OrthoDB; 5491765at2759; -.
DR UniPathway; UPA00559; -.
DR Proteomes; UP000006813; Unassembled WGS sequence.
DR Bgee; ENSHGLG00000002061; Expressed in adrenal gland and 10 other cell types or tissues.
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; 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 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:UP000006813}.
SQ SEQUENCE 489 AA; 52229 MW; 496E7067DA3F0513 CRC64;
MESPFSSPVE AVLQREAGLP GLLTPLADLD RVYELERIVG FVRDLGCQRV ALQFPDQLLG
DAGAVAARLE ETTGSKMFIL GDTAYGSCCV DVLGAEQAGA QALVHFGTAC LSPPARPLPV
TFILGQRSVA LELCAKAFEV QNPDPTVPMV LLSEPACAHA LEALAMLLHP KYQDLIVSSP
ALPLPSESPS PEPKPLECFG RHFPLAPGRC LEEYGAFYVG GSKASPNSDL DPDLSRLLLG
WAPGQPFFSC CPDTGQTQDE GVRAGRLRAR RRYLVERARD ARVVGLLAGT LGVARHCEAL
AHFRNLTRAA GKRSYVLALG RPTPAKLANF PEMDVFVLLA CPLGALAPQP SGSFFRPVLT
PCELEAACNP AWPPPGLAPY LTHYADLLPG SPFHVPLPPP ESELWDAPDV SLISGELRPP
LACRPLNDPG CSALTPRPQL ELAESSPAAS FLSFRSWQGL ELRLGQTPVT EAVSGRRGIA
IAYEDEGSS
//
