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Database: UniProt
Entry: A0A1M6TJ68_9AQUI
LinkDB: A0A1M6TJ68_9AQUI
Original site: A0A1M6TJ68_9AQUI 
ID   A0A1M6TJ68_9AQUI        Unreviewed;       304 AA.
AC   A0A1M6TJ68;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=TIGR00269 family protein {ECO:0000313|EMBL:SHK57132.1};
GN   ORFNames=SAMN05444391_1491 {ECO:0000313|EMBL:SHK57132.1};
OS   Thermocrinis minervae.
OC   Bacteria; Aquificota; Aquificae; Aquificales; Aquificaceae; Thermocrinis.
OX   NCBI_TaxID=381751 {ECO:0000313|EMBL:SHK57132.1, ECO:0000313|Proteomes:UP000189810};
RN   [1] {ECO:0000313|EMBL:SHK57132.1, ECO:0000313|Proteomes:UP000189810}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19557 {ECO:0000313|EMBL:SHK57132.1,
RC   ECO:0000313|Proteomes:UP000189810};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; LT670846; SHK57132.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M6TJ68; -.
DR   STRING; 381751.SAMN05444391_1491; -.
DR   OrthoDB; 9801054at2; -.
DR   Proteomes; UP000189810; Chromosome i.
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:SF27; TRNA-5-METHYLURIDINE(54) 2-SULFURTRANSFERASE; 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   Reference proteome {ECO:0000313|Proteomes:UP000189810};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|PIRSR:PIRSR004976-50}.
FT   DOMAIN          51..219
FT                   /note="tRNA(Ile)-lysidine/2-thiocytidine synthase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01171"
FT   BINDING         4
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004976-50"
FT   BINDING         7
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004976-50"
FT   BINDING         23
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004976-50"
FT   BINDING         26
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004976-50"
FT   BINDING         54..56
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004976-51"
FT   BINDING         60
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004976-51"
FT   BINDING         80
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004976-51"
FT   BINDING         156
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004976-51"
FT   BINDING         161
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004976-51"
FT   BINDING         275
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004976-50"
FT   BINDING         278
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004976-50"
FT   BINDING         287
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004976-50"
FT   BINDING         290
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004976-50"
SQ   SEQUENCE   304 AA;  35134 MW;  54B462778C79226E CRC64;
     MRKCVKCNKK AEVYLPQYRL SLCREHYIEW FENRVEGTIR EFRMFSKKDR ILVAVSGGKD
     SLSLWNTLHK LGYQADGLYI DLGIGQYSED SKNLAIKFAN NIGRELHTVS LKEEVLSIPE
     IKKEDPRPAC SFCGTLKRYY MNHYAKKLGY NVVATGHNLD DEVAVLFSNV LSWNLDYLKR
     QYPVLEEGKG FVRKVKPLCK MSEKESALYA FMAGIEYIEY ECPFSEGSTS IEYKKLLSEL
     EERHPGTKLR FYMEFLRKIY PLLNQEQEQT NLRPCKVCGE PTSRDVCPVC ALKAKVGKVT
     EPNV
//
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