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Database: UniProt
Entry: G4YQX2_PHYSP
LinkDB: G4YQX2_PHYSP
Original site: G4YQX2_PHYSP 
ID   G4YQX2_PHYSP            Unreviewed;       679 AA.
AC   G4YQX2;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   24-JAN-2024, entry version 57.
DE   RecName: Full=N-acetyltransferase domain-containing protein {ECO:0000259|PROSITE:PS51186};
GN   ORFNames=PHYSODRAFT_264096 {ECO:0000313|EMBL:EGZ30600.1};
OS   Phytophthora sojae (strain P6497) (Soybean stem and root rot agent)
OS   (Phytophthora megasperma f. sp. glycines).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=1094619 {ECO:0000313|EMBL:EGZ30600.1, ECO:0000313|Proteomes:UP000002640};
RN   [1] {ECO:0000313|EMBL:EGZ30600.1, ECO:0000313|Proteomes:UP000002640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P6497 {ECO:0000313|EMBL:EGZ30600.1,
RC   ECO:0000313|Proteomes:UP000002640};
RX   PubMed=16946064; DOI=10.1126/science.1128796;
RA   Tyler B.M., Tripathy S., Zhang X., Dehal P., Jiang R.H., Aerts A.,
RA   Arredondo F.D., Baxter L., Bensasson D., Beynon J.L., Chapman J.,
RA   Damasceno C.M., Dorrance A.E., Dou D., Dickerman A.W., Dubchak I.L.,
RA   Garbelotto M., Gijzen M., Gordon S.G., Govers F., Grunwald N.J., Huang W.,
RA   Ivors K.L., Jones R.W., Kamoun S., Krampis K., Lamour K.H., Lee M.K.,
RA   McDonald W.H., Medina M., Meijer H.J., Nordberg E.K., Maclean D.J.,
RA   Ospina-Giraldo M.D., Morris P.F., Phuntumart V., Putnam N.H., Rash S.,
RA   Rose J.K., Sakihama Y., Salamov A.A., Savidor A., Scheuring C.F.,
RA   Smith B.M., Sobral B.W., Terry A., Torto-Alalibo T.A., Win J., Xu Z.,
RA   Zhang H., Grigoriev I.V., Rokhsar D.S., Boore J.L.;
RT   "Phytophthora genome sequences uncover evolutionary origins and mechanisms
RT   of pathogenesis.";
RL   Science 313:1261-1266(2006).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + H2O + S-adenosyl-L-methionine + uridine(34) in
CC         tRNA = 5'-deoxyadenosine + 5-(carboxymethyl)uridine(34) in tRNA + CoA
CC         + 2 H(+) + L-methionine; Xref=Rhea:RHEA:61020, Rhea:RHEA-COMP:10407,
CC         Rhea:RHEA-COMP:11727, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17319, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:57844, ChEBI:CHEBI:59789, ChEBI:CHEBI:65315,
CC         ChEBI:CHEBI:74882; Evidence={ECO:0000256|ARBA:ARBA00034985};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61021;
CC         Evidence={ECO:0000256|ARBA:ARBA00034985};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
CC   -!- PATHWAY: tRNA modification. {ECO:0000256|ARBA:ARBA00005217}.
CC   -!- SIMILARITY: Belongs to the ELP3 family.
CC       {ECO:0000256|ARBA:ARBA00005494}.
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DR   EMBL; JH159151; EGZ30600.1; -; Genomic_DNA.
DR   RefSeq; XP_009517875.1; XM_009519580.1.
DR   AlphaFoldDB; G4YQX2; -.
DR   STRING; 1094619.G4YQX2; -.
DR   EnsemblProtists; EGZ30600; EGZ30600; PHYSODRAFT_264096.
DR   GeneID; 20639577; -.
DR   KEGG; psoj:PHYSODRAFT_264096; -.
DR   InParanoid; G4YQX2; -.
DR   OMA; IRNWETP; -.
DR   UniPathway; UPA00988; -.
DR   Proteomes; UP000002640; Unassembled WGS sequence.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR   CDD; cd04301; NAT_SF; 1.
DR   CDD; cd01335; Radical_SAM; 1.
DR   Gene3D; 3.40.630.30; -; 1.
DR   Gene3D; 3.80.30.20; tm_1862 like domain; 1.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR039661; ELP3.
DR   InterPro; IPR034687; ELP3-like.
DR   InterPro; IPR006638; Elp3/MiaA/NifB-like_rSAM.
DR   InterPro; IPR000182; GNAT_dom.
DR   InterPro; IPR032432; Radical_SAM_C.
DR   InterPro; IPR007197; rSAM.
DR   InterPro; IPR023404; rSAM_horseshoe.
DR   NCBIfam; TIGR01211; ELP3; 1.
DR   PANTHER; PTHR11135:SF2; ELONGATOR COMPLEX PROTEIN 3; 1.
DR   PANTHER; PTHR11135; HISTONE ACETYLTRANSFERASE-RELATED; 1.
DR   Pfam; PF00583; Acetyltransf_1; 1.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   Pfam; PF16199; Radical_SAM_C; 1.
DR   SFLD; SFLDF00344; ELP3-like; 1.
DR   SFLD; SFLDS00029; Radical_SAM; 1.
DR   SMART; SM00729; Elp3; 1.
DR   SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR   SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR   PROSITE; PS51186; GNAT; 1.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002640};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694};
KW   tRNA-binding {ECO:0000256|ARBA:ARBA00022555}.
FT   DOMAIN          509..654
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS51186"
FT   REGION          1..75
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        12..53
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   679 AA;  75885 MW;  2DAC63B3E2646E24 CRC64;
     MADVQPPASA PDATPSDATA STSIANASAT SPAIATSSSA LGASQTSDIE SIQVPKSAPR
     GDVNDPATYK RSQDPDWKNT GLDDIYATWD KLVPVEELPK FEEMGLFLVE HDPQTARELE
     KAFVLLRRKF KCLPKKSQMK FVLGLLVQKG EAPKGLALEK LLVKKAQKSQ SGVLVVTVLT
     SPYPEVGGKK QRFSCQWNCY YCPNEPDQPR SYLHDEPSVL RANRNDFDPV LQFCDRCVTL
     AMNGHPVDKI ELLVLGGTWA SYPVEYQENF IRDLFYAANT FFDREKRERR SLDEEKLENE
     TAAVKIIGIT LETRPDCITP EELRRFRRYG CTRVQLGIQH TDDAILKKIN RGCTSADAVR
     ALKLLRDCCY KTDIHLMPNL PGSDPEKDRA MFDYVLHSPD LQADQWKIYP CEITPWTVIK
     KWYDEGSYVP YSDDKLIDLL MDVKAQVHPW IRLNRVIRDI PSQYILGGMD EPNLRQVICN
     KMIARGTPCK CIRCREVKTD DAAIASAECV IREYEANEGA EYFISFETPD RSKICGFTRL
     RLSQSAGGGV FPELEGAALI RELHVYGQLV AAIAKSKKAA VDAAASDAEG SHAQHTGFGT
     QLMMKAEEIA RAHGYKKMAV IAGVGVRNFY RRLGFEVEGE GELMIKHLKE LPAPSVWSKV
     NAFVSDNIGK ELTPGQLVH
//
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