ID W9YT57_9EURO Unreviewed; 571 AA.
AC W9YT57;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE RecName: Full=2-(3-amino-3-carboxypropyl)histidine synthase subunit 2 {ECO:0000256|RuleBase:RU364133};
GN ORFNames=A1O1_01218 {ECO:0000313|EMBL:EXJ96092.1};
OS Capronia coronata CBS 617.96.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Capronia.
OX NCBI_TaxID=1182541 {ECO:0000313|EMBL:EXJ96092.1, ECO:0000313|Proteomes:UP000019484};
RN [1] {ECO:0000313|EMBL:EXJ96092.1, ECO:0000313|Proteomes:UP000019484}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 617.96 {ECO:0000313|EMBL:EXJ96092.1,
RC ECO:0000313|Proteomes:UP000019484};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Capronia coronata CBS 617.96.";
RL Submitted (MAR-2013) 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 -!- 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EXJ96092.1}.
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DR EMBL; AMWN01000001; EXJ96092.1; -; Genomic_DNA.
DR RefSeq; XP_007720321.1; XM_007722131.1.
DR AlphaFoldDB; W9YT57; -.
DR STRING; 1182541.W9YT57; -.
DR GeneID; 19156120; -.
DR eggNOG; KOG2648; Eukaryota.
DR HOGENOM; CLU_015210_1_1_1; -.
DR OrthoDB; 5491765at2759; -.
DR UniPathway; UPA00559; -.
DR Proteomes; UP000019484; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 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:UP000019484}.
FT REGION 423..507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..471
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 481..504
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 571 AA; 62707 MW; 7AF8EDD0AB97BD3D CRC64;
MVEELTAPPV LSTPDTHVLD EELSAAAHHP VEALSDDQIK TRYEINRTIA EIKQRRWRRV
ALQFPDQMLP HSARVYQLLA RGLRETTASQ DDAREGSATL AAGVASLAVE DDKPVRLTIL
GDTSYGSCCV DEIAAEHVEA DAVVHYGRAC LSPTARLPVL HIFTTMELDH EAVVKSFRES
FPDLDAKVVL TADVPYSAHV ESVIKILQQL GYTNVFAASI VHDPSSSIPN RTVPESVTDD
PSSLSQWSLF HISEPPTSLL LTLTSRMASV RVYPTDAINT ATAASASSAL ETSTRFLLRR
RYATVTSLTT VPVWGILINT LSVKNYMDIL SHIQRQVAAA GKKSYLFVVG KLNPAKVANF
SEIGGWIVIG CWESSLVDSK EFYKPIITPF ELELALQSDD SRLWTGQWRA DFQNVLEDAA
KRAEQTATDL ESRPAGDGLR GMSGAEDHET ETHTDSESES EPPEFDLRTG RYVSRSRPMQ
RNRAVYGTNQ QSVPSGSAPQ SGTLTRRGKG DMIAVNGVVS PGAEYLAQKR TWRGLGTDFE
VRYEEEEQGD VVEEGRTGVA RGYTVGDSVR S
//
