ID A0A0B5HT63_ARCG3 Unreviewed; 291 AA.
AC A0A0B5HT63;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=tRNA(Ile)-lysidine/2-thiocytidine synthase N-terminal domain-containing protein {ECO:0000259|Pfam:PF01171};
GN ORFNames=QT06_C0001G0587 {ECO:0000313|EMBL:AJF61427.1};
OS Archaeon GW2011_AR15.
OC Archaea.
OX NCBI_TaxID=1579373 {ECO:0000313|EMBL:AJF61427.1, ECO:0000313|Proteomes:UP000031776};
RN [1] {ECO:0000313|Proteomes:UP000031776}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=25702576; DOI=10.1016/j.cub.2015.01.014;
RA Castelle C.J., Wrighton K.C., Thomas B.C., Hug L.A., Brown C.T.,
RA Wilkins M.J., Frischkorn K.R., Tringe S.G., Singh A., Markillie L.M.,
RA Taylor R.C., Williams K.H., Banfield J.F.;
RT "Genomic expansion of domain archaea highlights roles for organisms from
RT new phyla in anaerobic carbon cycling.";
RL Curr. Biol. 25:690-701(2015).
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DR EMBL; CP010425; AJF61427.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B5HT63; -.
DR STRING; 1579373.QT06_C0001G0587; -.
DR HOGENOM; CLU_026481_1_1_2; -.
DR Proteomes; UP000031776; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR GO; GO:0034227; P:tRNA thio-modification; IEA:InterPro.
DR GO; GO:0002098; P:tRNA wobble uridine modification; IEA:InterPro.
DR CDD; cd01993; Alpha_ANH_like_II; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR InterPro; IPR000541; Ncs6/Tuc1/Ctu1.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR011063; TilS/TtcA_N.
DR InterPro; IPR035107; tRNA_thiolation_TtcA_Ctu1.
DR InterPro; IPR020554; UPF0021_CS.
DR NCBIfam; TIGR00269; TIGR00269 family protein; 1.
DR PANTHER; PTHR11807; ATPASES OF THE PP SUPERFAMILY-RELATED; 1.
DR PANTHER; PTHR11807:SF12; CYTOPLASMIC TRNA 2-THIOLATION PROTEIN 1; 1.
DR Pfam; PF01171; ATP_bind_3; 1.
DR PIRSF; PIRSF004976; ATPase_YdaO; 1.
DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR PROSITE; PS01263; UPF0021; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PIRSR:PIRSR004976-51};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR004976-50};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR004976-51};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|PIRSR:PIRSR004976-50}.
FT DOMAIN 45..212
FT /note="tRNA(Ile)-lysidine/2-thiocytidine synthase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF01171"
FT BINDING 3
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR004976-50"
FT BINDING 6
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR004976-50"
FT BINDING 18
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR004976-50"
FT BINDING 21
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR004976-50"
FT BINDING 49..51
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR004976-51"
FT BINDING 55
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR004976-51"
FT BINDING 75
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR004976-51"
FT BINDING 150
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR004976-51"
FT BINDING 155
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR004976-51"
FT BINDING 268
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR004976-50"
FT BINDING 271
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR004976-50"
FT BINDING 280
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR004976-50"
FT BINDING 283
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR004976-50"
SQ SEQUENCE 291 AA; 32689 MW; 876CF32050314ED2 CRC64;
MKCGLCEKNA VFGNPAYCKE HFCGYIEKKV LGTIEKYNLI EKGQKVAVAA SGGKDSLSVL
YILNKYGYGV TALAIDEGIS GYRDRTLATL KKICGAHKIK LRIVSFKGKF SKSLDEILFT
NRERPCTVCG VFRRYLLNLH ARDYDVLATG HNMDDEAQVT LMNLIKNNLS AMQRMGPSAG
VVSSEKFTRR VKPLYFCTEK EIMTYAFINK LTADFNECPN VSRAFRLRVR DMLNEIEQEV
PGAKKNLIEW SLKSKTGMKT GEEGLRECRA CGELSSADVC MACRYMEKIS V
//
