ID A0A0C9MN52_9FUNG Unreviewed; 208 AA.
AC A0A0C9MN52;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=MAM1_0039d02831 {ECO:0000313|EMBL:GAN03378.1};
OS Mucor ambiguus.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Mucor.
OX NCBI_TaxID=91626 {ECO:0000313|EMBL:GAN03378.1};
RN [1] {ECO:0000313|EMBL:GAN03378.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NBRC 6742 {ECO:0000313|EMBL:GAN03378.1};
RA Takeda I., Yamane N., Morita T., Tamano K., Machida M., Baker S., Koike H.;
RT "Draft genome sequence of an oleaginous Mucoromycotina fungus Mucor
RT ambiguus NBRC6742.";
RL Submitted (SEP-2014) 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; DF836328; GAN03378.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C9MN52; -.
DR OrthoDB; 167848at2759; -.
DR Proteomes; UP000053815; 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:UP000053815};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT DOMAIN 2..171
FT /note="DTW"
FT /evidence="ECO:0000259|SMART:SM01144"
FT REGION 187..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 208 AA; 24580 MW; 1BA81C50A079B0EB CRC64;
MERSTLPSVK LPVHLDVVKH HKELDGKSTA IHAKIIAQDD VDIHTWPEVP DFTDPERTLL
LFPGPNAKQL TDIPRESFNR IVVIDGTWIQ AKQITNNTPI LKKMQRVTIA PRKTHFWRFQ
NVDDQHLATI EAIYYLYREF GETYEAPYDG KYDNLMFYYK FFYNLIQNTY QAQKSAKFSR
RHQQKDYIKY KEDDTEEQGK KEEGKPAL
//
