ID B0Y6N9_ASPFC Unreviewed; 106 AA.
AC B0Y6N9;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Diphthamide biosynthesis protein 3 {ECO:0000256|ARBA:ARBA00041070};
GN ORFNames=AFUB_067620 {ECO:0000313|EMBL:EDP50424.1};
OS Aspergillus fumigatus (strain CBS 144.89 / FGSC A1163 / CEA10) (Neosartorya
OS fumigata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=451804 {ECO:0000313|EMBL:EDP50424.1, ECO:0000313|Proteomes:UP000001699};
RN [1] {ECO:0000313|EMBL:EDP50424.1, ECO:0000313|Proteomes:UP000001699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CEA10 / CBS 144.89 / FGSC A1163
RC {ECO:0000313|Proteomes:UP000001699};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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}.
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DR EMBL; DS499598; EDP50424.1; -; Genomic_DNA.
DR AlphaFoldDB; B0Y6N9; -.
DR EnsemblFungi; EDP50424; EDP50424; AFUB_067620.
DR VEuPathDB; FungiDB:AFUB_067620; -.
DR HOGENOM; CLU_155991_4_0_1; -.
DR PhylomeDB; B0Y6N9; -.
DR UniPathway; UPA00559; -.
DR Proteomes; UP000001699; 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;
FT DOMAIN 8..64
FT /note="DPH-type MB"
FT /evidence="ECO:0000259|PROSITE:PS51074"
SQ SEQUENCE 106 AA; 11767 MW; 83C777FDEC92D845 CRC64;
MADEALSIYD EIEIEDMTFD PNLQIYHYPC PCGDRFEIAI DDLRDGEDIA VCPSCSLMIR
VIFEVVCSLP ASTRSRIWDA DNVPYLQSDL PKDGNQPAPG AVSVQA
//
