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Database: UniProt
Entry: W2Q327_PHYPN
LinkDB: W2Q327_PHYPN
Original site: W2Q327_PHYPN 
ID   W2Q327_PHYPN            Unreviewed;      1095 AA.
AC   W2Q327;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   RecName: Full=RNA cytidine acetyltransferase {ECO:0000256|HAMAP-Rule:MF_03211};
DE            EC=2.3.1.- {ECO:0000256|HAMAP-Rule:MF_03211};
DE   AltName: Full=18S rRNA cytosine acetyltransferase {ECO:0000256|HAMAP-Rule:MF_03211};
GN   ORFNames=PPTG_13430 {ECO:0000313|EMBL:ETN07598.1};
OS   Phytophthora parasitica (strain INRA-310).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=761204 {ECO:0000313|EMBL:ETN07598.1, ECO:0000313|Proteomes:UP000018817};
RN   [1] {ECO:0000313|Proteomes:UP000018817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=INRA-310 {ECO:0000313|Proteomes:UP000018817};
RG   The Broad Institute Genome Sequencing Platform;
RA   Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA   Machado M., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Chapman S.B.,
RA   Gearin G., Goldberg J., Griggs A., Gujja S., Hansen M., Heiman D.,
RA   Howarth C., Larimer J., Lui A., MacDonald P.J.P., McCowen C.,
RA   Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA   Saif S., Shea T., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ETN07598.1, ECO:0000313|Proteomes:UP000018817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=INRA-310 {ECO:0000313|EMBL:ETN07598.1,
RC   ECO:0000313|Proteomes:UP000018817};
RG   The Broad Institute Genomics Platform;
RA   Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA   Machado M., Johnson C.S., Arredondo F., Hong C., Coffey M., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA   Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA   Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Phytophthora parasitica INRA-310.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: RNA cytidine acetyltransferase with specificity toward both
CC       18S rRNA and tRNAs. Catalyzes the formation of N(4)-acetylcytidine
CC       (ac4C) in 18S rRNA. Required for early nucleolar cleavages of precursor
CC       rRNA at sites A0, A1 and A2 during 18S rRNA synthesis. Catalyzes the
CC       formation of ac4C in serine and leucine tRNAs. Requires a tRNA-binding
CC       adapter protein for full tRNA acetyltransferase activity but not for
CC       18S rRNA acetylation. {ECO:0000256|HAMAP-Rule:MF_03211}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a cytidine in 18S rRNA + acetyl-CoA + ATP + H2O = ADP + an
CC         N(4)-acetylcytidine in 18S rRNA + CoA + H(+) + phosphate;
CC         Xref=Rhea:RHEA:51424, Rhea:RHEA-COMP:13575, Rhea:RHEA-COMP:13576,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:74900, ChEBI:CHEBI:82748, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_03211};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a cytidine in tRNA + acetyl-CoA + ATP + H2O = ADP + an N(4)-
CC         acetylcytidine in tRNA + CoA + H(+) + phosphate;
CC         Xref=Rhea:RHEA:53876, Rhea:RHEA-COMP:13670, Rhea:RHEA-COMP:13671,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:74900, ChEBI:CHEBI:82748, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_03211};
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC       {ECO:0000256|ARBA:ARBA00004604, ECO:0000256|HAMAP-Rule:MF_03211}.
CC   -!- SIMILARITY: Belongs to the RNA cytidine acetyltransferase family. NAT10
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_03211}.
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DR   EMBL; KI669592; ETN07598.1; -; Genomic_DNA.
DR   RefSeq; XP_008907355.1; XM_008909107.1.
DR   AlphaFoldDB; W2Q327; -.
DR   STRING; 761204.W2Q327; -.
DR   EnsemblProtists; ETN07598; ETN07598; PPTG_13430.
DR   GeneID; 20182792; -.
DR   VEuPathDB; FungiDB:PPTG_13430; -.
DR   OMA; CGDSNNC; -.
DR   OrthoDB; 1119820at2759; -.
DR   Proteomes; UP000018817; Unassembled WGS sequence.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008080; F:N-acetyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0042274; P:ribosomal small subunit biogenesis; IEA:UniProtKB-UniRule.
DR   GO; GO:0000154; P:rRNA modification; IEA:UniProtKB-UniRule.
DR   GO; GO:0051391; P:tRNA acetylation; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.11040; -; 1.
DR   Gene3D; 3.40.630.30; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   HAMAP; MF_03211; RNA_acetyltr_Nat10; 1.
DR   InterPro; IPR000182; GNAT_dom.
DR   InterPro; IPR007807; Helicase_dom.
DR   InterPro; IPR033688; NAT10.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR032672; TmcA/NAT10/Kre33.
DR   InterPro; IPR013562; TmcA_N.
DR   InterPro; IPR027992; tRNA_bind_dom.
DR   PANTHER; PTHR10925; N-ACETYLTRANSFERASE 10; 1.
DR   PANTHER; PTHR10925:SF5; RNA CYTIDINE ACETYLTRANSFERASE; 1.
DR   Pfam; PF13718; GNAT_acetyltr_2; 1.
DR   Pfam; PF05127; Helicase_RecD; 1.
DR   Pfam; PF08351; TmcA_N; 1.
DR   Pfam; PF13725; tRNA_bind_2; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315, ECO:0000256|HAMAP-
KW   Rule:MF_03211};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_03211};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_03211};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|HAMAP-Rule:MF_03211};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018817};
KW   rRNA processing {ECO:0000256|ARBA:ARBA00022552, ECO:0000256|HAMAP-
KW   Rule:MF_03211};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_03211};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW   Rule:MF_03211}.
FT   DOMAIN          9..201
FT                   /note="tRNA(Met) cytidine acetyltransferase TmcA N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08351"
FT   DOMAIN          282..517
FT                   /note="Helicase"
FT                   /evidence="ECO:0000259|Pfam:PF05127"
FT   DOMAIN          558..793
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF13718"
FT   DOMAIN          806..1035
FT                   /note="Possible tRNA binding"
FT                   /evidence="ECO:0000259|Pfam:PF13725"
FT   REGION          439..462
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          692..724
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          984..1010
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1041..1095
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1052..1082
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         287..296
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03211"
FT   BINDING         499
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03211"
FT   BINDING         662..664
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03211"
FT   BINDING         669..675
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03211"
FT   BINDING         766
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03211"
SQ   SEQUENCE   1095 AA;  122726 MW;  F01B098BA7D907A9 CRC64;
     MVKKKVDARV RTLLENCIQE NFRSFVVLVG DHGKDQVMNL HYILSKAAVK ARPRVLWCYK
     KELGFSTHRQ KRMRQIKKQQ QRGLYDPSKD DPFELFIAST DIRWCYYKET HKVLGSTYGM
     CVLQDFEAVT PNIMARTIET VEGGGVVVLL LRTMDSLKQL YTMSMDVHAR FRTESHQDVV
     ARFNERFILS LASCERCVVL DDELNVLPIS KHTRKIEPLP PRDSTTELTK DELELQELKT
     SLRETQPVGA LVEQARTLDQ AKAILTFVEA VSEKTLRSTV ALTAGRGRGK SAALGMALAG
     AVAYGYSNIF VTAPSPENLK TVFDFVFKGF DALKYKEHLD YEIVQSTNPE FNHAVVRVNI
     FREHRQTIQY IQPTHHEKLA QAELVAIDEA AAIPLPVVKN LLGPYLVFMS STINGYEGTG
     RSLSLKLLQK LREQQGSAGE AAARAAASIH GDQKRRKGEQ KLHEERWQAA SNAAHAAAAG
     SASSSARVLR EVALETPIRY APNDPVERWL NALLCLDATN ASHRLVAGTP HPRDCELYYV
     NRDSLFSYHK LSESFLQRIM ALYVSSHYKN QPNDLQLLSD APAHHVFALL GPGAEAQGNA
     GQLPDVLCVV QVALEGEISK ASVKAQLTRG QRASGDLIPW TVAQQFQDSE FAALSGARVV
     RIATHPDVTG MGYGSRAIEL LTKYYQGEIT SDVADGESEE KEKEDKLEDD DDDEEEKKSK
     LRKEKIKPRK TLPPLLLPLD ERPCERLHWF GTSFGLTLPL HNFWSRAKFR SVYIRQTAND
     LTGEHTAIML RSLRCDDLPA APADGWLDEF VADSRRRFTS LLSYDFSKFP CALALGLLSD
     ESAGSNEDEK QLTLHRSATG EISPAELAMV LTPYDAKRLK SYAKNMVDYH MIVDLIPSLA
     RLYFLQRLPQ MSLSYLQRAI LVSLGLQHQS VDVIQQELNV PSNQLLALFN KAVRKFLGQI
     EQLMEKQLEE ETANSKKLAE VAAQSQAMAP TETTLDEEMR EGAQAEKAKQ QQKLLDSLNL
     MKYAVRGDDA DWDAALAQAE NGGAVVQVKS KKQNKTKKES KEPKKEYKHN KRSADADGDR
     KKGKKSKKSK YANLS
//
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