ID D2RXG9_HALTV Unreviewed; 319 AA.
AC D2RXG9;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=PP-loop domain protein {ECO:0000313|EMBL:ADB61693.1};
GN OrderedLocusNames=Htur_2822 {ECO:0000313|EMBL:ADB61693.1};
OS Haloterrigena turkmenica (strain ATCC 51198 / DSM 5511 / JCM 9101 / NCIMB
OS 13204 / VKM B-1734 / 4k) (Halococcus turkmenicus).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Haloterrigena.
OX NCBI_TaxID=543526 {ECO:0000313|EMBL:ADB61693.1, ECO:0000313|Proteomes:UP000001903};
RN [1] {ECO:0000313|EMBL:ADB61693.1, ECO:0000313|Proteomes:UP000001903}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51198 / DSM 5511 / JCM 9101 / NCIMB 13204 / VKM B-1734 /
RC 4k {ECO:0000313|Proteomes:UP000001903};
RX PubMed=21304683; DOI=10.4056/sigs.681272;
RA Saunders E., Tindall B.J., Fahnrich R., Lapidus A., Copeland A.,
RA Del Rio T.G., Lucas S., Chen F., Tice H., Cheng J.F., Han C., Detter J.C.,
RA Bruce D., Goodwin L., Chain P., Pitluck S., Pati A., Ivanova N.,
RA Mavromatis K., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA Jeffries C.D., Brettin T., Rohde M., Goker M., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of Haloterrigena turkmenica type strain (4k).";
RL Stand. Genomic Sci. 2:107-116(2010).
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DR EMBL; CP001860; ADB61693.1; -; Genomic_DNA.
DR RefSeq; WP_012943962.1; NC_013743.1.
DR AlphaFoldDB; D2RXG9; -.
DR STRING; 543526.Htur_2822; -.
DR GeneID; 8743438; -.
DR KEGG; htu:Htur_2822; -.
DR eggNOG; arCOG00042; Archaea.
DR HOGENOM; CLU_026481_1_1_2; -.
DR OrthoDB; 33422at2157; -.
DR Proteomes; UP000001903; 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 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.
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 56..231
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 22
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR004976-50"
FT BINDING 25
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR004976-50"
FT BINDING 59..61
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR004976-51"
FT BINDING 65
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR004976-51"
FT BINDING 90
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR004976-51"
FT BINDING 169
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR004976-51"
FT BINDING 174
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR004976-51"
FT BINDING 297
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR004976-50"
FT BINDING 300
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR004976-50"
FT BINDING 309
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR004976-50"
FT BINDING 312
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR004976-50"
SQ SEQUENCE 319 AA; 35646 MW; A789EA990A480E14 CRC64;
MDCNRCDEEA VMHAAYSGAH LCADHFRESV EKRVRRRVRR DDLVPRDATP EAPQTWVIGL
SGGKDSVVLT QILHDTFAED PRIELVGLTI HEGIEGYRDK SVDACVELAD DLDIRHELVS
YEEEFGVRMD DVVEDDPENM AACAYCGVFR RDLLEKYAEK LEADLLLTGH NLDDEAQTAL
MNFLEGDVEQ IAKHFDASLG ALSEREDQAE FVPRAKPLRD VPEKEVALYA HINDLPAHIT
ECPHASEAYR GEIQQLLYGL EENHPGTRHS ILAGYEELAS IAADEFSGDD GAELQECTQC
GSTTTREICR KCSLLESLA
//
