ID A0A2K8PF61_STRLA Unreviewed; 467 AA.
AC A0A2K8PF61;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Cysteine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00041};
DE EC=6.1.1.16 {ECO:0000256|HAMAP-Rule:MF_00041};
DE AltName: Full=Cysteinyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00041};
DE Short=CysRS {ECO:0000256|HAMAP-Rule:MF_00041};
GN Name=cysS {ECO:0000256|HAMAP-Rule:MF_00041,
GN ECO:0000313|EMBL:ATZ25382.1};
GN ORFNames=SLAV_17665 {ECO:0000313|EMBL:ATZ25382.1}, SLLC_15745
GN {ECO:0000313|EMBL:QUQ55210.1};
OS Streptomyces lavendulae subsp. lavendulae.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=58340 {ECO:0000313|EMBL:ATZ25382.1, ECO:0000313|Proteomes:UP000231791};
RN [1] {ECO:0000313|EMBL:ATZ25382.1, ECO:0000313|Proteomes:UP000231791}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCM 3239 {ECO:0000313|EMBL:ATZ25382.1,
RC ECO:0000313|Proteomes:UP000231791};
RA Busche T., Novakova R., Al'Dilaimi A., Homerova D., Feckova L.,
RA Rezuchova B., Mingyar E., Csolleiova D., Bekeova C., Winkler A.,
RA Sevcikova B., Kalinowski J., Kormanec J., Ruckert C.;
RT "Complete genome sequence of Streptomyces lavendulae subsp. lavendulae CCM
RT 3239 (formerly 'Streptomyces aureofaciens CCM 3239'), the producer of the
RT angucycline-type antibiotic auricin.";
RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:QUQ55210.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Del-LP {ECO:0000313|EMBL:QUQ55210.1};
RA Novakova R., Ruckert C., Knirschova R., Feckova L., Busche T.,
RA Csolleiova D., Homerova D., Rezuchova B., Javorova R., Sevcikova B.,
RA Kalinowski J., Kormanec J.;
RT "The linear plasmid pSA3239 is essential for the replication of the
RT Streptomyces lavendulae subsp. lavendulae CCM 3239 chromosome.";
RL Submitted (APR-2021) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-cysteine + tRNA(Cys) = AMP + diphosphate + L-
CC cysteinyl-tRNA(Cys); Xref=Rhea:RHEA:17773, Rhea:RHEA-COMP:9661,
CC Rhea:RHEA-COMP:9679, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:35235, ChEBI:CHEBI:78442, ChEBI:CHEBI:78517,
CC ChEBI:CHEBI:456215; EC=6.1.1.16; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_00041};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00041};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00041};
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245, ECO:0000256|HAMAP-
CC Rule:MF_00041}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00041}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|HAMAP-Rule:MF_00041}.
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DR EMBL; CP024985; ATZ25382.1; -; Genomic_DNA.
DR EMBL; CP073778; QUQ55210.1; -; Genomic_DNA.
DR RefSeq; WP_030232390.1; NZ_JOEW01000019.1.
DR AlphaFoldDB; A0A2K8PF61; -.
DR GeneID; 82165507; -.
DR KEGG; slx:SLAV_17665; -.
DR OrthoDB; 9815130at2; -.
DR Proteomes; UP000231791; Chromosome.
DR Proteomes; UP000676025; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004817; F:cysteine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006423; P:cysteinyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd00672; CysRS_core; 1.
DR Gene3D; 1.20.120.1910; Cysteine-tRNA ligase, C-terminal anti-codon recognition domain; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR HAMAP; MF_00041; Cys_tRNA_synth; 1.
DR InterPro; IPR015803; Cys-tRNA-ligase.
DR InterPro; IPR015273; Cys-tRNA-synt_Ia_DALR.
DR InterPro; IPR024909; Cys-tRNA/MSH_ligase.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR032678; tRNA-synt_1_cat_dom.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR NCBIfam; TIGR00435; cysS; 1.
DR PANTHER; PTHR10890:SF3; CYSTEINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR PANTHER; PTHR10890; CYSTEINYL-TRNA SYNTHETASE; 1.
DR Pfam; PF09190; DALR_2; 1.
DR Pfam; PF01406; tRNA-synt_1e; 1.
DR PRINTS; PR00983; TRNASYNTHCYS.
DR SMART; SM00840; DALR_2; 1.
DR SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|HAMAP-Rule:MF_00041};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00041}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00041};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00041};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00041};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00041};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00041}; Reference proteome {ECO:0000313|Proteomes:UP000231791};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00041}.
FT DOMAIN 341..403
FT /note="Cysteinyl-tRNA synthetase class Ia DALR"
FT /evidence="ECO:0000259|SMART:SM00840"
FT REGION 162..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 447..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 31..41
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00041"
FT MOTIF 264..268
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00041"
FT COMPBIAS 168..183
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 29
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00041"
FT BINDING 208
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00041"
FT BINDING 233
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00041"
FT BINDING 237
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00041"
FT BINDING 267
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00041"
SQ SEQUENCE 467 AA; 52363 MW; B32F4377CB66C11B CRC64;
MTIRLYDTSA RQIRDFTPLV PGCVSIYLCG ATVQAAPHIG HIRSYLNFDV MRRWFAYRGY
DVTFIRNVTD IDDKIIAKSA EQGRPWWSIG YDNELAFNNG YDALGCLRPT YEPRATGHVP
EMIEMMRGLI ERGHAYESEG NVYFDVKSFP GYLSLSRQEL DNIRQPESTG ETGKRDPRDF
AMWKSAKPGE PSWETPWGRG RPGWHLECSA MAHKYLGEAF DIHGGGLDLI FPHHENEIAQ
AQAFGDEFAK YWVHNAWVTM SGEKMSKSLG NSVLVSEMVK QWRPIVLRYY LGTPHYRSMI
EYSEEALREA ESAFARIEGF YQRVIEKAGG PVEAAAEVPP AFAEAMDDDL GVPQALAIVH
TTVRQGNSAL AADDKDAAIA RLSEVRAMLG VLGLDPLDPH WAGESADRGE DLHGAVDTLV
RLVLEQRESA RSRKDWATAD AIRDQLQQSG LVIEDSPTGP RWTLGPR
//
