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Database: UniProt
Entry: U4UNB3_DENPD
LinkDB: U4UNB3_DENPD
Original site: U4UNB3_DENPD 
ID   U4UNB3_DENPD            Unreviewed;       315 AA.
AC   U4UNB3;
DT   11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2013, sequence version 1.
DT   27-MAR-2024, entry version 23.
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=D910_08830 {ECO:0000313|EMBL:ERL91500.1};
OS   Dendroctonus ponderosae (Mountain pine beetle).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC   Curculionidae; Scolytinae; Dendroctonus.
OX   NCBI_TaxID=77166 {ECO:0000313|EMBL:ERL91500.1, ECO:0000313|Proteomes:UP000030742};
RN   [1] {ECO:0000313|EMBL:ERL91500.1, ECO:0000313|Proteomes:UP000030742}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=23537049; DOI=10.1186/gb-2013-14-3-r27;
RA   Keeling C.I., Yuen M.M., Liao N.Y., Roderick Docking T., Chan S.K.,
RA   Taylor G.A., Palmquist D.L., Jackman S.D., Nguyen A., Li M., Henderson H.,
RA   Janes J.K., Zhao Y., Pandoh P., Moore R., Sperling F.A., W Huber D.P.,
RA   Birol I., Jones S.J., Bohlmann J.;
RT   "Draft genome of the mountain pine beetle, Dendroctonus ponderosae Hopkins,
RT   a major forest pest.";
RL   Genome Biol. 14:R27-R27(2013).
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; KB632288; ERL91500.1; -; Genomic_DNA.
DR   AlphaFoldDB; U4UNB3; -.
DR   STRING; 77166.U4UNB3; -.
DR   OrthoDB; 167848at2759; -.
DR   Proteomes; UP000030742; 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:UP000030742};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT   DOMAIN          46..303
FT                   /note="DTW"
FT                   /evidence="ECO:0000259|SMART:SM01144"
SQ   SEQUENCE   315 AA;  36405 MW;  B4BE639E7B1976AC CRC64;
     MANPKNRKTD QQCIDENPFD GFLIDDNAIL NSIEGRHPCP KCAKSRKLFC YSCFIPIAPL
     EGKLPNVKLP LKIDIIKHKH EIDGKSTAGH AALLASNDVN IYTYPDIPDY TNEAVVMIFP
     GQNAISVSQL VSGENVQSLQ QFQSQPLDQL PPGYNRSTLM QTIPKTREET GFTQRVSKLP
     ISKAVFIDST WHQCKSIYKD EKIRAIPCVV IQNRVSQFWR HQKGSPRWYL ATIEAIHQFL
     LEIHLHSWGL NPNYKGIRNC FTEKGLEQFD GLYSENSQAY NGQYDNLLYF FKHMYEVIHT
     YYQHEDLYAY KRRLK
//
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