GenomeNet

Database: UniProt
Entry: A0A172YSH7_9GAMM
LinkDB: A0A172YSH7_9GAMM
Original site: A0A172YSH7_9GAMM 
ID   A0A172YSH7_9GAMM        Unreviewed;       408 AA.
AC   A0A172YSH7;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   RecName: Full=tRNA(Ile)-lysidine synthase {ECO:0000256|HAMAP-Rule:MF_01161};
DE            EC=6.3.4.19 {ECO:0000256|HAMAP-Rule:MF_01161};
DE   AltName: Full=tRNA(Ile)-2-lysyl-cytidine synthase {ECO:0000256|HAMAP-Rule:MF_01161};
DE   AltName: Full=tRNA(Ile)-lysidine synthetase {ECO:0000256|HAMAP-Rule:MF_01161};
GN   Name=tilS {ECO:0000256|HAMAP-Rule:MF_01161};
GN   ORFNames=A3K93_09805 {ECO:0000313|EMBL:ANF83161.1};
OS   Acinetobacter sp. NCu2D-2.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=1608473 {ECO:0000313|EMBL:ANF83161.1, ECO:0000313|Proteomes:UP000186584};
RN   [1] {ECO:0000313|Proteomes:UP000186584}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCu2D-2 {ECO:0000313|Proteomes:UP000186584};
RA   Wilharm G.;
RT   "Acinetobacter strain NCu2D-2 is the representative of a novel species.";
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Ligates lysine onto the cytidine present at position 34 of
CC       the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an
CC       ATP-dependent manner. Cytidine is converted to lysidine, thus changing
CC       the amino acid specificity of the tRNA from methionine to isoleucine.
CC       {ECO:0000256|HAMAP-Rule:MF_01161}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + cytidine(34) in tRNA(Ile2) + L-lysine = AMP +
CC         diphosphate + H(+) + lysidine(34) in tRNA(Ile2);
CC         Xref=Rhea:RHEA:43744, Rhea:RHEA-COMP:10625, Rhea:RHEA-COMP:10670,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:32551,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:82748, ChEBI:CHEBI:83665,
CC         ChEBI:CHEBI:456215; EC=6.3.4.19;
CC         Evidence={ECO:0000256|ARBA:ARBA00000047, ECO:0000256|HAMAP-
CC         Rule:MF_01161};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|HAMAP-Rule:MF_01161}.
CC   -!- SIMILARITY: Belongs to the tRNA(Ile)-lysidine synthase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01161}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01161}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP015594; ANF83161.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A172YSH7; -.
DR   STRING; 1608473.A3K93_09805; -.
DR   KEGG; aciu:A3K93_09805; -.
DR   Proteomes; UP000186584; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016879; F:ligase activity, forming carbon-nitrogen bonds; IEA:UniProtKB-UniRule.
DR   GO; GO:0006400; P:tRNA modification; IEA:UniProtKB-UniRule.
DR   CDD; cd01992; PP-ATPase; 1.
DR   Gene3D; 1.20.59.20; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   HAMAP; MF_01161; tRNA_Ile_lys_synt; 1.
DR   InterPro; IPR012796; Lysidine-tRNA-synth_C.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR011063; TilS/TtcA_N.
DR   InterPro; IPR012094; tRNA_Ile_lys_synt.
DR   InterPro; IPR012795; tRNA_Ile_lys_synt_N.
DR   InterPro; IPR015262; tRNA_Ile_lys_synt_subst-bd.
DR   NCBIfam; TIGR02433; lysidine_TilS_C; 1.
DR   NCBIfam; TIGR02432; lysidine_TilS_N; 1.
DR   PANTHER; PTHR43033; TRNA(ILE)-LYSIDINE SYNTHASE-RELATED; 1.
DR   PANTHER; PTHR43033:SF1; TRNA(ILE)-LYSIDINE SYNTHASE-RELATED; 1.
DR   Pfam; PF01171; ATP_bind_3; 1.
DR   Pfam; PF09179; TilS; 1.
DR   Pfam; PF11734; TilS_C; 1.
DR   SMART; SM00977; TilS_C; 1.
DR   SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR   SUPFAM; SSF82829; MesJ substrate recognition domain-like; 1.
DR   SUPFAM; SSF56037; PheT/TilS domain; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01161};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_01161};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_01161}.
FT   DOMAIN          332..405
FT                   /note="Lysidine-tRNA(Ile) synthetase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00977"
SQ   SEQUENCE   408 AA;  47047 MW;  EFD740F7CF4A8ABC CRC64;
     MDSMLLLHLM FFLCPEKITA IYVDHQLQAV SASWGEFVAA ECKKLNIPCI VQTVTVASGN
     LEQQARHSRY AAYAQHLKDH EILVLAHHQQ DQAETLMLRL LSGAGVDGLA AMKAIDIRED
     FTIWRPLLDV SREQICQWAD DLNISHIEDP TNLDTHYDRA WARQQLWPLL TERFPKMQMA
     LSRTAELMRD AQHILADVLS EDLKQCGDDK QLNLDKLSEL SLARQRQLLS AWMKGQDQYR
     PSLDMVERLQ REVIQAKPDA KTELHYKDFY YVRYQRQLFR LHRSEYVFDP NQYVGTTPIE
     IHPDLPLTLP SGEFCIAQAE YGLSPDLFHQ TLHIQFRAGG EKVHLHGRVG TWPLKKAIQE
     AQIFPWQRHT IQILSKDNVI LGVFTPNGFW LAQSAYCVAD GWLPLRSS
//
DBGET integrated database retrieval system