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Database: UniProt
Entry: R1E712_EMIHU
LinkDB: R1E712_EMIHU
Original site: R1E712_EMIHU 
ID   R1E712_EMIHU            Unreviewed;       441 AA.
AC   R1E712;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=tRNA-uridine aminocarboxypropyltransferase 1 {ECO:0000256|ARBA:ARBA00039242};
DE            EC=2.5.1.25 {ECO:0000256|ARBA:ARBA00012386};
DE   AltName: Full=DTW domain-containing protein 1 {ECO:0000256|ARBA:ARBA00042508};
GN   ORFNames=EMIHUDRAFT_240292 {ECO:0000313|EMBL:EOD22510.1};
OS   Emiliania huxleyi (Coccolithophore) (Pontosphaera huxleyi).
OC   Eukaryota; Haptista; Haptophyta; Prymnesiophyceae; Isochrysidales;
OC   Noelaerhabdaceae; Emiliania.
OX   NCBI_TaxID=2903 {ECO:0000313|EMBL:EOD22510.1};
RN   [1] {ECO:0000313|EMBL:EOD22510.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CCMP1516 {ECO:0000313|EMBL:EOD22510.1};
RG   DOE Joint Genome Institute;
RA   Read B., Kegel J., Klute M., Kuo A., Lefebvre S.C., Maumus F., Mayer C.,
RA   Miller J., Allen A., Bidle K., Borodovsky M., Bowler C., Brownlee C.,
RA   Claverie J.-M., Cock M., De Vargas C., Elias M., Frickenhaus S.,
RA   Gladyshev V.N., Gonzalez K., Guda C., Hadaegh A., Herman E.,
RA   Iglesias-Rodriguez D., Jones B., Lawson T., Leese F., Lin Y.-C.,
RA   Lindquist E., Lobanov A., Lucas S., Malik S.-H.B., Marsh M.E., Mock T.,
RA   Monier A., Moreau H., Mueller-Roeber B., Napier J., Ogata H., Parker M.,
RA   Probert I., Quesneville H., Raines C., Rensing S., Riano-Pachon D.M.,
RA   Richier S., Rokitta S., Salamov A., Sarno A.F., Schmutz J., Schroeder D.,
RA   Shiraiwa Y., Soanes D.M., Valentin K., Van Der Giezen M., Van Der Peer Y.,
RA   Vardi A., Verret F., Von Dassow P., Wheeler G., Williams B., Wilson W.,
RA   Wolfe G., Wurch L.L., Young J., Dacks J.B., Delwiche C.F., Dyhrman S.,
RA   Glockner G., John U., Richards T., Worden A.Z., Zhang X., Grigoriev I.V.;
RT   "Genome variability drives Emilianias global distribution.";
RL   Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000013827}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CCMP1516 {ECO:0000313|Proteomes:UP000013827};
RX   PubMed=23760476; DOI=10.1038/nature12221;
RA   Read B.A., Kegel J., Klute M.J., Kuo A., Lefebvre S.C., Maumus F.,
RA   Mayer C., Miller J., Monier A., Salamov A., Young J., Aguilar M.,
RA   Claverie J.M., Frickenhaus S., Gonzalez K., Herman E.K., Lin Y.C.,
RA   Napier J., Ogata H., Sarno A.F., Shmutz J., Schroeder D., de Vargas C.,
RA   Verret F., von Dassow P., Valentin K., Van de Peer Y., Wheeler G.,
RA   Dacks J.B., Delwiche C.F., Dyhrman S.T., Glockner G., John U., Richards T.,
RA   Worden A.Z., Zhang X., Grigoriev I.V., Allen A.E., Bidle K., Borodovsky M.,
RA   Bowler C., Brownlee C., Cock J.M., Elias M., Gladyshev V.N., Groth M.,
RA   Guda C., Hadaegh A., Iglesias-Rodriguez M.D., Jenkins J., Jones B.M.,
RA   Lawson T., Leese F., Lindquist E., Lobanov A., Lomsadze A., Malik S.B.,
RA   Marsh M.E., Mackinder L., Mock T., Mueller-Roeber B., Pagarete A.,
RA   Parker M., Probert I., Quesneville H., Raines C., Rensing S.A.,
RA   Riano-Pachon D.M., Richier S., Rokitta S., Shiraiwa Y., Soanes D.M.,
RA   van der Giezen M., Wahlund T.M., Williams B., Wilson W., Wolfe G.,
RA   Wurch L.L.;
RT   "Pan genome of the phytoplankton Emiliania underpins its global
RT   distribution.";
RL   Nature 499:209-213(2013).
RN   [3] {ECO:0000313|EnsemblProtists:EOD22510}
RP   IDENTIFICATION.
RG   EnsemblProtists;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Catalyzes the formation of 3-(3-amino-3-carboxypropyl)uridine
CC       (acp3U) at position 20 in the D-loop of several cytoplasmic tRNAs
CC       (acp3U(20)). {ECO:0000256|ARBA:ARBA00037050}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a uridine in tRNA + S-adenosyl-L-methionine = a 3-[(3S)-3-
CC         amino-3-carboxypropyl]uridine in tRNA + H(+) + S-methyl-5'-
CC         thioadenosine; Xref=Rhea:RHEA:62432, Rhea:RHEA-COMP:13339, Rhea:RHEA-
CC         COMP:16092, ChEBI:CHEBI:15378, ChEBI:CHEBI:17509, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:65315, ChEBI:CHEBI:82930; EC=2.5.1.25;
CC         Evidence={ECO:0000256|ARBA:ARBA00024168};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the TDD superfamily. DTWD1 family.
CC       {ECO:0000256|ARBA:ARBA00038290}.
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DR   EMBL; KB865709; EOD22510.1; -; Genomic_DNA.
DR   RefSeq; XP_005774939.1; XM_005774882.1.
DR   STRING; 2903.R1E712; -.
DR   PaxDb; 2903-EOD22510; -.
DR   EnsemblProtists; EOD22510; EOD22510; EMIHUDRAFT_240292.
DR   GeneID; 17268056; -.
DR   KEGG; ehx:EMIHUDRAFT_240292; -.
DR   eggNOG; KOG3795; Eukaryota.
DR   HOGENOM; CLU_050612_0_0_1; -.
DR   Proteomes; UP000013827; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016432; F:tRNA-uridine aminocarboxypropyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR   InterPro; IPR005636; DTW.
DR   PANTHER; PTHR15627; NATURAL KILLER CELL-SPECIFIC ANTIGEN KLIP1; 1.
DR   PANTHER; PTHR15627:SF8; TRNA-URIDINE AMINOCARBOXYPROPYLTRANSFERASE 1; 1.
DR   Pfam; PF03942; DTW; 1.
DR   SMART; SM01144; DTW; 1.
PE   3: Inferred from homology;
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000013827};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT   DOMAIN          187..397
FT                   /note="DTW"
FT                   /evidence="ECO:0000259|SMART:SM01144"
FT   REGION          282..301
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   441 AA;  47837 MW;  A9D32266173132F1 CRC64;
     MSSFEARGDF FPSPYEPGGT SFRGFAKILA AAPPPCLIVR PRRWHVGMAG GPRLRGIAVP
     TEVPRIDLSL QRRSEHTHGV VGAIRRGAAP LNIHLVGPAH AKMRATDEHM AELLAPEPSA
     EAAGGQLFRV GDISSAAAIA KARRSDFREV FDERDREGDA RLAKLKLAPL GQESPGRERC
     SGCGVMRSAF CSECLAMLPG QARPEIAKLP FRFVIITHPK EPRSRSTGVH AAVLAAGCVT
     LRTFDKGDEA CLPPELFPAG RTFLLFPSDD ALTVPQLAAK REPAGTKAPA KARVQEGDGA
     DEDGNAGRLV VVVIDSTWSQ ARQIMGHPCL QALPRVAVAS HRTAFWRRQH LGENYLATVE
     AVYYVCTESH GDAYDGRYDN LLFFFVKFRS LVRQRIGTIP CPTEAKGKVC TKLQCQHSHS
     LSLGADDHGR KQPVLLPAGE L
//
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