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Database: UniProt
Entry: A0A016UJ13_9BILA
LinkDB: A0A016UJ13_9BILA
Original site: A0A016UJ13_9BILA 
ID   A0A016UJ13_9BILA        Unreviewed;       202 AA.
AC   A0A016UJ13;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 22.
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=Acey_s0037.g3480 {ECO:0000313|EMBL:EYC15369.1};
GN   Synonyms=Acey-Y53C12A.10 {ECO:0000313|EMBL:EYC15369.1};
GN   ORFNames=Y032_0037g3480 {ECO:0000313|EMBL:EYC15369.1};
OS   Ancylostoma ceylanicum.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Strongylida;
OC   Ancylostomatoidea; Ancylostomatidae; Ancylostomatinae; Ancylostoma.
OX   NCBI_TaxID=53326 {ECO:0000313|EMBL:EYC15369.1, ECO:0000313|Proteomes:UP000024635};
RN   [1] {ECO:0000313|Proteomes:UP000024635}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX   PubMed=25730766; DOI=10.1038/ng.3237;
RA   Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA   Aroian R.V.;
RT   "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT   ceylanicum identify infection-specific gene families.";
RL   Nat. Genet. 47:416-422(2015).
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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EYC15369.1}.
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DR   EMBL; JARK01001373; EYC15369.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A016UJ13; -.
DR   Proteomes; UP000024635; 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:UP000024635};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT   DOMAIN          3..176
FT                   /note="DTW"
FT                   /evidence="ECO:0000259|SMART:SM01144"
SQ   SEQUENCE   202 AA;  23225 MW;  5BE2E8F5B51F88E1 CRC64;
     MQKNPFQLPC DVDIVKHPSE KNSKSSAIHC KIVAPEQTRV FDVPDVFDYS SEVSADGEGS
     SVLVFPSPSA VSIEEFVRTR GPIKRLVVLD CTWFQVHMMQ RIPQIQGLPC VSLTKYRTAF
     WRPQHNVDES GLATIEAIYY ALKEYQEFGL RRPYQGEFDD LLYWFFLTRN HVDMKQEEYR
     KRMLDCAQPA GIPEAKINKS SG
//
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