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Database: UniProt
Entry: A0A1Z5SMX1_HORWE
LinkDB: A0A1Z5SMX1_HORWE
Original site: A0A1Z5SMX1_HORWE 
ID   A0A1Z5SMX1_HORWE        Unreviewed;        95 AA.
AC   A0A1Z5SMX1;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Diphthamide biosynthesis protein 3 {ECO:0000256|ARBA:ARBA00041070};
GN   ORFNames=BTJ68_14612 {ECO:0000313|EMBL:OTA22111.1};
OS   Hortaea werneckii EXF-2000.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Hortaea.
OX   NCBI_TaxID=1157616 {ECO:0000313|EMBL:OTA22111.1, ECO:0000313|Proteomes:UP000194280};
RN   [1] {ECO:0000313|EMBL:OTA22111.1, ECO:0000313|Proteomes:UP000194280}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EXF-2000 {ECO:0000313|EMBL:OTA22111.1,
RC   ECO:0000313|Proteomes:UP000194280};
RA   Sinha S., Flibotte S., Neira M., Lenassi M., Gostincar C., Stajich J.E.,
RA   Nislow C.E.;
RT   "The recent genome duplication of the halophilic yeast Hortaea werneckii:
RT   insights from long-read sequencing.";
RL   Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 [3Fe-4S](0)-[protein] + 2 Fe(2+)-[Dph3] + NADH = 2 [4Fe-
CC         4S](1+)-[protein] + 2 [Dph3] + H(+) + NAD(+); Xref=Rhea:RHEA:71239,
CC         Rhea:RHEA-COMP:17997, Rhea:RHEA-COMP:17998, Rhea:RHEA-COMP:18001,
CC         Rhea:RHEA-COMP:18002, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033,
CC         ChEBI:CHEBI:33723, ChEBI:CHEBI:47402, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:83228;
CC         Evidence={ECO:0000256|ARBA:ARBA00036715};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[3Fe-4S](1+)-[protein] + Fe(2+)-[Dph3] = [3Fe-4S](0)-[protein]
CC         + Fe(3+)-[Dph3]; Xref=Rhea:RHEA:71235, Rhea:RHEA-COMP:17996,
CC         Rhea:RHEA-COMP:17997, Rhea:RHEA-COMP:18002, Rhea:RHEA-COMP:18003,
CC         ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:33751,
CC         ChEBI:CHEBI:47402, ChEBI:CHEBI:83228;
CC         Evidence={ECO:0000256|ARBA:ARBA00036267};
CC   -!- PATHWAY: Protein modification; peptidyl-diphthamide biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00005156}.
CC   -!- SIMILARITY: Belongs to the DPH3 family.
CC       {ECO:0000256|ARBA:ARBA00024032}.
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:OTA22111.1}.
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DR   EMBL; MUNK01000402; OTA22111.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Z5SMX1; -.
DR   STRING; 1157616.A0A1Z5SMX1; -.
DR   VEuPathDB; FungiDB:BTJ68_14612; -.
DR   InParanoid; A0A1Z5SMX1; -.
DR   OrthoDB; 1054714at2759; -.
DR   UniPathway; UPA00559; -.
DR   Proteomes; UP000194280; Unassembled WGS sequence.
DR   GO; GO:0017183; P:protein histidyl modification to diphthamide; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.10.660.10; DPH Zinc finger; 1.
DR   InterPro; IPR007872; DPH_MB_dom.
DR   InterPro; IPR036671; DPH_MB_sf.
DR   PANTHER; PTHR21454:SF31; DPH3 HOMOLOG; 1.
DR   PANTHER; PTHR21454; DPH3 HOMOLOG-RELATED; 1.
DR   Pfam; PF05207; zf-CSL; 1.
DR   SUPFAM; SSF144217; CSL zinc finger; 1.
DR   PROSITE; PS51074; DPH_MB; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000194280}.
FT   DOMAIN          6..63
FT                   /note="DPH-type MB"
FT                   /evidence="ECO:0000259|PROSITE:PS51074"
FT   REGION          66..95
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        66..82
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   95 AA;  10823 MW;  92AD3B554D148995 CRC64;
     MADENIYDEI EIEDMTWDPT MQIYHYPCPC GDRFEISIDD LRDEETDIAV CPSCSLQIRV
     IYEADDLPKP EGEQKQEEVK KGVETQAQQP VAAAA
//
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