ID A0A0C9SRM7_PLICR Unreviewed; 497 AA.
AC A0A0C9SRM7;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=2-(3-amino-3-carboxypropyl)histidine synthase subunit 2 {ECO:0000256|RuleBase:RU364133};
GN ORFNames=PLICRDRAFT_57334 {ECO:0000313|EMBL:KII84822.1};
OS Plicaturopsis crispa FD-325 SS-3.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Amylocorticiales; Amylocorticiaceae; Plicaturopsis.
OX NCBI_TaxID=944288 {ECO:0000313|EMBL:KII84822.1, ECO:0000313|Proteomes:UP000053263};
RN [1] {ECO:0000313|EMBL:KII84822.1, ECO:0000313|Proteomes:UP000053263}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FD-325 SS-3 {ECO:0000313|EMBL:KII84822.1,
RC ECO:0000313|Proteomes:UP000053263};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL Submitted (JUN-2014) 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 -!- SUBUNIT: Component of the 2-(3-amino-3-carboxypropyl)histidine synthase
CC complex composed of DPH1, DPH2, DPH3 and a NADH-dependent reductase,
CC predominantly CBR1. {ECO:0000256|ARBA:ARBA00034128}.
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}.
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DR EMBL; KN832569; KII84822.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C9SRM7; -.
DR HOGENOM; CLU_015210_1_0_1; -.
DR OrthoDB; 5491765at2759; -.
DR UniPathway; UPA00559; -.
DR Proteomes; UP000053263; 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:UP000053263}.
FT REGION 195..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 386..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 472..497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 497 AA; 54696 MW; D95B44E7EF1217D2 CRC64;
MSADPTTISA SGEDAITRTI DVNVDETPNP LSSPDEFEDY YEINRTAEEI ARRGYKRIAL
QFPDELLHDS VPIYRLLKSK IEKGQELYVL ADTSYGSCCV DEVAAQHVDA DALVHYGHAC
MSQTSRLPHL NVDACVSSLI DSTLASKVSA EGTAAATSVL LRHDVAYTRQ ADEIVRKLRH
ALRIPVLYAP IPTSTTPPTA AGTERTVNHP DSNAEDVVTE DPVILYVGGE SLGLTNLLMA
HNASIVYSFD PCTNTGRLES GRTNRLLMRR YAVVQKSRDA DVFGILVGTL GVASYLPLIT
HIRRLLAQAR KKSYTITVGK LNPAKLANFM EIECFVLVAC PENSIIDTKD FLRPIITPYE
LEIALKAEQS WTGRYVLDFE RLLNAEPSEE TPESREADEE DPDQPVFSMV TGKYRHAKRY
GGEEAPSRAA DENTSALVRR NQDGVIAKIQ DNAAGQFLRA RTYQGLEQRL GEDAPGVLEQ
GRSGIAKGYK DDHASAL
//
