ID   DTWD2_MACFA             Reviewed;         298 AA.
AC   Q4R7M4;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 39.
DE   RecName: Full=tRNA-uridine aminocarboxypropyltransferase 2 {ECO:0000305};
DE            EC=2.5.1.25 {ECO:0000250|UniProtKB:Q8NBA8};
DE   AltName: Full=DTW domain-containing protein 2;
GN   Name=DTWD2 {ECO:0000250|UniProtKB:Q8NBA8}; ORFNames=QtsA-14809;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the formation of 3-(3-amino-3-carboxypropyl)uridine
CC       (acp3U) at position 20a in the D-loop of several cytoplasmic tRNAs
CC       (acp3U(20a)). Also has a weak activity to form acp3U at position 20 in
CC       the D-loop of tRNAs (acp3U(20)). {ECO:0000250|UniProtKB:Q8NBA8}.
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:0000250|UniProtKB:Q8NBA8};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8NBA8}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q8NBA8}.
CC   -!- DOMAIN: Contains 1 DXTW motif.
CC   -!- SIMILARITY: Belongs to the TDD superfamily. DTWD2 family.
CC       {ECO:0000305}.
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DR   EMBL; AB168791; BAE00898.1; -; mRNA.
DR   RefSeq; NP_001270440.1; NM_001283511.1.
DR   AlphaFoldDB; Q4R7M4; -.
DR   STRING; 9541.XP_005557627.1; -.
DR   GeneID; 101926717; -.
DR   CTD; 285605; -.
DR   eggNOG; KOG4382; Eukaryota.
DR   Proteomes; UP000233100; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016432; F:tRNA-uridine aminocarboxypropyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0006400; P:tRNA modification; ISS:UniProtKB.
DR   InterPro; IPR005636; DTW.
DR   InterPro; IPR039262; DTWD2/YfiP.
DR   PANTHER; PTHR21392; PTHR21392; 1.
DR   Pfam; PF03942; DTW; 1.
DR   SMART; SM01144; DTW; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; Nucleus; Phosphoprotein; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase; tRNA processing.
FT   CHAIN           1..298
FT                   /note="tRNA-uridine aminocarboxypropyltransferase 2"
FT                   /id="PRO_0000271129"
FT   REGION          1..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           178..181
FT                   /note="DXTW"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NBA8"
FT   MOD_RES         132
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NBA8"
SQ   SEQUENCE   298 AA;  33549 MW;  44823036CA2330A4 CRC64;
     MESQKEARIL QEPVARPPGA SRSQTPNAKE RQEGGPVPAA AALGAEADDD SADRLWELPV
     EPAKRRPECS RCSRPQKVCL CPFLPAHPLH ISTHLYIIQH PAEENKVLRT VPLLAACLPQ
     DKCKVKIGRR FSEERDPELS TVCRKSGTLI LYPGAEAANL EEFILDSPVY PSTIIIIDGT
     WSQAKDIFYK NSLFRHPKQV QLKTSISSQY VIRMQPTNRC LSTLECAAVA LSILEKNNYI
     QETLLRPLQA LCSFQLQHGA QIRLSKEHLL KNGLYTKPMP KNKRKLRKME LLMNSVKI