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Database: UniProt
Entry: A0A0J0UT99_9ACTN
LinkDB: A0A0J0UT99_9ACTN
Original site: A0A0J0UT99_9ACTN 
ID   A0A0J0UT99_9ACTN        Unreviewed;       351 AA.
AC   A0A0J0UT99;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Putative ATPase of the PP-loop superfamily implicated in cell cycle control {ECO:0000313|EMBL:KLR60110.1};
GN   ORFNames=IMCC26207_110356 {ECO:0000313|EMBL:KLR60110.1};
OS   Actinobacteria bacterium IMCC26207.
OC   Bacteria; Actinomycetota; Actinomycetes.
OX   NCBI_TaxID=1641811 {ECO:0000313|EMBL:KLR60110.1, ECO:0000313|Proteomes:UP000036180};
RN   [1] {ECO:0000313|EMBL:KLR60110.1, ECO:0000313|Proteomes:UP000036180}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMCC26207 {ECO:0000313|EMBL:KLR60110.1,
RC   ECO:0000313|Proteomes:UP000036180};
RA   Kim S., Cho J.-C.;
RT   "Genome sequence of freshwater Actinobacteria.";
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KLR60110.1}.
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DR   EMBL; LCZK01000010; KLR60110.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0J0UT99; -.
DR   STRING; 1641811.IMCC26207_110356; -.
DR   PATRIC; fig|1641811.3.peg.2669; -.
DR   OrthoDB; 9801054at2; -.
DR   Proteomes; UP000036180; Unassembled WGS sequence.
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:0006400; P:tRNA modification; IEA:UniProt.
DR   CDD; cd01993; Alpha_ANH_like_II; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR011063; TilS/TtcA_N.
DR   InterPro; IPR035107; tRNA_thiolation_TtcA_Ctu1.
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:UP000036180};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|PIRSR:PIRSR004976-50}.
FT   DOMAIN          50..221
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         53..55
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004976-51"
FT   BINDING         59
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004976-51"
FT   BINDING         79
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         286
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004976-50"
FT   BINDING         289
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004976-50"
FT   BINDING         298
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004976-50"
FT   BINDING         301
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004976-50"
SQ   SEQUENCE   351 AA;  38595 MW;  89CC9972F24360BA CRC64;
     MKCVVCRESA VIDVRRANSN FCSDHFLRFC QEQMSRAIRE FDMLSPTDRV LVAVSGGKDS
     LAVWDLLQRS GYEADGLYVG LGIDSYSDTS GDFARAFAES RGLKLIEIDL PTDYGYDIPT
     GARAARRAPC SACGTSKRHL FDKAALDGSY DVLVTGHNLD DEAAVLFGNV LRWQTEYLAR
     QMPVLQARVG FPKKVKPLIR LSERDTAAYC ILQGIDYMVE ECPMSAGNKH LGYKEALNSI
     ELASPGTKSD FYSGFLRKAS ALFRAEYLEK SQTDLNSPSV DELTYCVRCS APSTATLCAF
     CRLVDKAGGS VRVEQGRFTG ELEDNAAQSV RITTRAERLA SGTTREVEAG Q
//
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