ID A0A067R4K4_ZOONE Unreviewed; 343 AA.
AC A0A067R4K4;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 30.
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=L798_08400 {ECO:0000313|EMBL:KDR17142.1};
OS Zootermopsis nevadensis (Dampwood termite).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Polyneoptera; Dictyoptera; Blattodea; Blattoidea; Termitoidae;
OC Termopsidae; Zootermopsis.
OX NCBI_TaxID=136037 {ECO:0000313|EMBL:KDR17142.1, ECO:0000313|Proteomes:UP000027135};
RN [1] {ECO:0000313|EMBL:KDR17142.1, ECO:0000313|Proteomes:UP000027135}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Whole organism {ECO:0000313|EMBL:KDR17142.1};
RX PubMed=24845553; DOI=10.1038/ncomms4636;
RA Terrapon N., Li C., Robertson H.M., Ji L., Meng X., Booth W., Chen Z.,
RA Childers C.P., Glastad K.M., Gokhale K., Gowin J., Gronenberg W.,
RA Hermansen R.A., Hu H., Hunt B.G., Huylmans A.K., Khalil S.M.,
RA Mitchell R.D., Munoz-Torres M.C., Mustard J.A., Pan H., Reese J.T.,
RA Scharf M.E., Sun F., Vogel H., Xiao J., Yang W., Yang Z., Yang Z., Zhou J.,
RA Zhu J., Brent C.S., Elsik C.G., Goodisman M.A., Liberles D.A., Roe R.M.,
RA Vargo E.L., Vilcinskas A., Wang J., Bornberg-Bauer E., Korb J., Zhang G.,
RA Liebig J.;
RT "Molecular traces of alternative social organization in a termite genome.";
RL Nat. Commun. 5:3636-3636(2014).
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; KK852751; KDR17142.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A067R4K4; -.
DR STRING; 136037.A0A067R4K4; -.
DR EnsemblMetazoa; KDR17142; KDR17142; L798_08400.
DR eggNOG; KOG3795; Eukaryota.
DR InParanoid; A0A067R4K4; -.
DR OMA; CAESSEM; -.
DR OrthoDB; 167848at2759; -.
DR Proteomes; UP000027135; Unassembled WGS sequence.
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:UP000027135};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT DOMAIN 41..331
FT /note="DTW"
FT /evidence="ECO:0000259|SMART:SM01144"
FT REGION 237..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..254
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..288
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 343 AA; 39323 MW; 9BE1A307E9F72843 CRC64;
MEPLKRMCDD SEPFKDLKIE NWMILDEVSQ RQPCVLCKKS RKYFCYNCFI PVQDLQGLVP
KVKLPIKIDI IKHSREIDGK STAVHAAVLA PDDVNIYTYP CIPDYGSNEK VVLVFPGKDA
VSVENIFDSL SEMDADNAEP RPKKLNVGAR LPITKAVFID STWNQSRGIY KDQRVRDLPC
IVLQSRISQF WRHQNGSPRW YLATIEAIHQ FLVELHTVAW NMNSVNLCAE SSEMKATGNG
QKTQERSTCV ETSKNIDTTD RDANAADRIS HLSGTSNGNV TGEQSSNPDW LRNEHKKISD
ASECFGPYRG EYDNLLFFFC YMYNKIHKLY DHEDLRAYKR PLK
//