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Database: UniProt
Entry: A0A067R4K4_ZOONE
LinkDB: A0A067R4K4_ZOONE
Original site: A0A067R4K4_ZOONE 
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}.
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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
//
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