ID A0A0D2BUB1_9EURO Unreviewed; 123 AA.
AC A0A0D2BUB1;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Diphthamide biosynthesis protein 3 {ECO:0000256|ARBA:ARBA00041070};
GN ORFNames=PV07_10943 {ECO:0000313|EMBL:KIW22668.1};
OS Cladophialophora immunda.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Cladophialophora.
OX NCBI_TaxID=569365 {ECO:0000313|EMBL:KIW22668.1, ECO:0000313|Proteomes:UP000054466};
RN [1] {ECO:0000313|EMBL:KIW22668.1, ECO:0000313|Proteomes:UP000054466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 83496 {ECO:0000313|EMBL:KIW22668.1,
RC ECO:0000313|Proteomes:UP000054466};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Cladophialophora immunda CBS83496.";
RL Submitted (JAN-2015) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KN847046; KIW22668.1; -; Genomic_DNA.
DR RefSeq; XP_016242884.1; XM_016398322.1.
DR AlphaFoldDB; A0A0D2BUB1; -.
DR STRING; 569365.A0A0D2BUB1; -.
DR GeneID; 27350137; -.
DR VEuPathDB; FungiDB:PV07_10943; -.
DR HOGENOM; CLU_155991_0_0_1; -.
DR OrthoDB; 1054714at2759; -.
DR UniPathway; UPA00559; -.
DR Proteomes; UP000054466; 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:UP000054466}.
FT DOMAIN 32..88
FT /note="DPH-type MB"
FT /evidence="ECO:0000259|PROSITE:PS51074"
FT REGION 90..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..115
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 123 AA; 13421 MW; 96759C9E7EADEE47 CRC64;
MPSTTTTAAA ASTTLNLTGS GSAATTAEDL DIYDEIEIED MTYDPALQIY HYPCPCGDRF
EISLGSLREG EDVAVCPSCS LMVRVIFDLE DLAGGEGDED DEEEEREEKD EEKKEAEEEE
AAK
//
