ID A0A078A0U2_STYLE Unreviewed; 327 AA.
AC A0A078A0U2;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
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 Name=Contig1879.g2031 {ECO:0000313|EMBL:CDW75755.1};
GN ORFNames=STYLEM_4750 {ECO:0000313|EMBL:CDW75755.1};
OS Stylonychia lemnae (Ciliate).
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC Stichotrichia; Sporadotrichida; Oxytrichidae; Stylonychinae; Stylonychia.
OX NCBI_TaxID=5949 {ECO:0000313|EMBL:CDW75755.1, ECO:0000313|Proteomes:UP000039865};
RN [1] {ECO:0000313|EMBL:CDW75755.1, ECO:0000313|Proteomes:UP000039865}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=130c {ECO:0000313|EMBL:CDW75755.1,
RC ECO:0000313|Proteomes:UP000039865};
RA Swart Estienne;
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
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}.
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; CCKQ01004593; CDW75755.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A078A0U2; -.
DR EnsemblProtists; CDW75755; CDW75755; STYLEM_4750.
DR InParanoid; A0A078A0U2; -.
DR OMA; KSRKTCF; -.
DR OrthoDB; 179313at2759; -.
DR Proteomes; UP000039865; 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:UP000039865};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT DOMAIN 81..286
FT /note="DTW"
FT /evidence="ECO:0000259|SMART:SM01144"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 305..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 327 AA; 38992 MW; F4E1B62CEE5B43F3 CRC64;
MKRQSNTMEK KGQEEEEVKE QGVQKRQKLD QNNQEKKIDF SVLNERQDQQ QSYIDKLKLN
SFNALIEMKG RKDCPKCKCS RKYFCYDCYI PLNDDLATVP RVDLPIEVTV YIYLLELYFN
RLRHPKEKIS KSSIVASKIV APEKVQIVHE MDISSLRDDD EDYDSVVLLF PTDDAQEVIK
MSEEELAKIK KVVIIDCTWN QTHHFLKQAN VKKIKKIKIQ TEKTVFWRYQ RISEANLATI
EALYYFFRDY DVNKNCSGDY AKYDGKYDNL LYYYAFNYKL IQYEYVEGSK KDKKFIRMDN
YIKGRDEPEQ DTKHHKPAYL AQNDKKE
//
