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Database: UniProt
Entry: F4WAE0_ACREC
LinkDB: F4WAE0_ACREC
Original site: F4WAE0_ACREC 
ID   F4WAE0_ACREC            Unreviewed;       310 AA.
AC   F4WAE0;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 29.
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=G5I_02476 {ECO:0000313|EMBL:EGI68823.1};
OS   Acromyrmex echinatior (Panamanian leafcutter ant) (Acromyrmex octospinosus
OS   echinatior).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Myrmicinae; Acromyrmex.
OX   NCBI_TaxID=103372 {ECO:0000313|Proteomes:UP000007755};
RN   [1] {ECO:0000313|EMBL:EGI68823.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Nygaard S., Zhang G.;
RT   "The genome of the leaf-cutting ant Acromyrmex echinatior suggests key
RT   adaptations to social evolution and fungus farming.";
RL   Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
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; GL888048; EGI68823.1; -; Genomic_DNA.
DR   RefSeq; XP_011049091.1; XM_011050789.1.
DR   AlphaFoldDB; F4WAE0; -.
DR   STRING; 103372.F4WAE0; -.
DR   EnsemblMetazoa; XM_011050789.1; XP_011049091.1; LOC105142903.
DR   GeneID; 105142903; -.
DR   KEGG; aec:105142903; -.
DR   eggNOG; KOG3795; Eukaryota.
DR   InParanoid; F4WAE0; -.
DR   OrthoDB; 167848at2759; -.
DR   Proteomes; UP000007755; 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:UP000007755};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT   DOMAIN          55..298
FT                   /note="DTW"
FT                   /evidence="ECO:0000259|SMART:SM01144"
SQ   SEQUENCE   310 AA;  36894 MW;  A8E5761D37329DEF CRC64;
     MAESIVKHST DNLSELEEKQ RIIDGNPFCY LKINDTKELK LVESRRKCDL CQKSRKFFCY
     TCYHPVLSCK YYPRVKLPIK IDIIKHPREI PGKSTAIHAA IIAPMDVKIY TYPDFPEISN
     KEETVLVFPG KDSTKNISVK DLFIRKEGKD DASGERSETD LLWPIKRAIF IDSTWHQTKS
     IYKDQRLREL RCVVLKSRVS QFWRHQKDSP RWYLATIESI HQFLVELHTC AIGMDEDYEE
     TIKRYLDVND IKNTRYTDYI HQYSGINSEE LMQKYSGQYD NLLYFFKYMF EHIHSIYNRN
     QLKAYKRPLT
//
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