ID A0A061H8Q7_9BASI Unreviewed; 805 AA.
AC A0A061H8Q7;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Diphthamide biosynthesis protein 4 {ECO:0000256|ARBA:ARBA00021797};
GN ORFNames=PFL1_04227 {ECO:0000313|EMBL:EPQ28400.1};
OS Pseudozyma flocculosa PF-1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Pseudozyma.
OX NCBI_TaxID=1277687 {ECO:0000313|EMBL:EPQ28400.1, ECO:0000313|Proteomes:UP000053664};
RN [1] {ECO:0000313|EMBL:EPQ28400.1, ECO:0000313|Proteomes:UP000053664}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PF-1 {ECO:0000313|EMBL:EPQ28400.1,
RC ECO:0000313|Proteomes:UP000053664};
RX PubMed=23800965; DOI=10.1105/tpc.113.113969;
RA Lefebvre F., Joly D.L., Labbe C., Teichmann B., Linning R., Belzile F.,
RA Bakkeren G., Belanger R.R.;
RT "The transition from a phytopathogenic smut ancestor to an anamorphic
RT biocontrol agent deciphered by comparative whole-genome analysis.";
RL Plant Cell 25:1946-1959(2013).
CC -!- FUNCTION: Required for the first step of diphthamide biosynthesis, the
CC transfer of 3-amino-3-carboxypropyl from S-adenosyl-L-methionine to a
CC histidine residue. Diphthamide is a post-translational modification of
CC histidine which occurs in elongation factor 2.
CC {ECO:0000256|ARBA:ARBA00003474}.
CC -!- SIMILARITY: Belongs to the DPH4 family.
CC {ECO:0000256|ARBA:ARBA00006169}.
CC -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC {ECO:0000256|ARBA:ARBA00005964}.
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DR EMBL; KE361635; EPQ28400.1; -; Genomic_DNA.
DR RefSeq; XP_007879941.1; XM_007881750.1.
DR AlphaFoldDB; A0A061H8Q7; -.
DR GeneID; 19318333; -.
DR KEGG; pfp:PFL1_04227; -.
DR eggNOG; KOG0715; Eukaryota.
DR eggNOG; KOG1516; Eukaryota.
DR HOGENOM; CLU_006586_17_1_1; -.
DR OrthoDB; 1552062at2759; -.
DR Proteomes; UP000053664; Unassembled WGS sequence.
DR CDD; cd06257; DnaJ; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 1.10.287.110; DnaJ domain; 1.
DR Gene3D; 3.10.660.10; DPH Zinc finger; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002018; CarbesteraseB.
DR InterPro; IPR019826; Carboxylesterase_B_AS.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR007872; DPH_MB_dom.
DR InterPro; IPR036671; DPH_MB_sf.
DR InterPro; IPR036869; J_dom_sf.
DR PANTHER; PTHR43142; CARBOXYLIC ESTER HYDROLASE; 1.
DR PANTHER; PTHR43142:SF1; CARBOXYLIC ESTER HYDROLASE; 1.
DR Pfam; PF00135; COesterase; 1.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF05207; zf-CSL; 1.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF46565; Chaperone J-domain; 1.
DR SUPFAM; SSF144217; CSL zinc finger; 1.
DR PROSITE; PS00122; CARBOXYLESTERASE_B_1; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
DR PROSITE; PS51074; DPH_MB; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000053664}.
FT DOMAIN 449..522
FT /note="J"
FT /evidence="ECO:0000259|PROSITE:PS50076"
FT DOMAIN 549..606
FT /note="DPH-type MB"
FT /evidence="ECO:0000259|PROSITE:PS51074"
FT REGION 418..441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 529..564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 805 AA; 88563 MW; CDA707444243D660 CRC64;
MGQSTSKAIP SDAAAVEIPS RGSIRGVLLT DAATAKPKTQ RFSGIPYAQP PVGPLRWRRP
QPLSPDFSFD DGGRRYHEPG NVCPQPLTYF ANTGFEIPPQ PLAYNKSEDC LQLTIWVPVD
EHGQRKPPSA GKQGLPVLFF IHGGWLQIGN PNLDVNKDPS DLIASAGLDC IVVSPGYRLN
AFGFLAHNAL RDEDESGLTG NYGFWDQRLA LEWVRDNIAH FGGDPGNIAI GGISAGAHSS
HSQLLHEFDL CRADPSYRPI IKRVFLQSNA VAWPPKRVEE TAEQFEELCA ALDIPISLAD
GDKIERLRKV GDVELAEVVT KLDMHTFRAV RDDRPGAFVR SSWTSSMADG SFGRWCEEQS
ITVLAGEVDK EEKVYEVVNS PHDLDSFVLQ LTNYYPEALV QAILPLYGLP QTKKMPPLGA
SALPTSAGQH EAVSDSDRAA STEGGELEDL YTIFGVSRTA SKAEIRAAYL GLVRQHHPDK
AQQSDSSLLA PDTSSSALIR QLNTAYSILS DDLTRQAYDR ALEAQISQAE AAKQQRDGKG
QAMRLGGEGS DDSDSDSEDD ERGEEVTFVH PCRCGHDYRI SGTQISQGVE LVACNGCSEV
VRVTWFDHDD PATAAAAAAV ASASDKQKQA VPTTAREWAQ LFGQVSADSQ VYLTSRTLIE
DLVKGGMAPH AILRYRCDFR APIFDTFAPA SMGVSHSFDD LVWWYALCTG GWTEQQLKRL
RKWLDPYIRF LHGPPAGTDV REWREDMAVA WYGPEYDVDT TTEASWIRTL KADATIQVEK
TDQRGDDKRS LIRAMREIRE KVAAT
//
