ID A5CYS9_PELTS Unreviewed; 250 AA.
AC A5CYS9;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE SubName: Full=Predicted ATPase {ECO:0000313|EMBL:BAF60846.1};
GN Name=MesJ {ECO:0000313|EMBL:BAF60846.1};
GN OrderedLocusNames=PTH_2665 {ECO:0000313|EMBL:BAF60846.1};
OS Pelotomaculum thermopropionicum (strain DSM 13744 / JCM 10971 / SI).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfotomaculaceae;
OC Pelotomaculum.
OX NCBI_TaxID=370438 {ECO:0000313|EMBL:BAF60846.1, ECO:0000313|Proteomes:UP000006556};
RN [1] {ECO:0000313|Proteomes:UP000006556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13744 / JCM 10971 / SI {ECO:0000313|Proteomes:UP000006556};
RX PubMed=18218977; DOI=10.1101/gr.7136508;
RA Kosaka T., Kato S., Shimoyama T., Ishii S., Abe T., Watanabe K.;
RT "The genome of Pelotomaculum thermopropionicum reveals niche-associated
RT evolution in anaerobic microbiota.";
RL Genome Res. 18:442-448(2008).
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DR EMBL; AP009389; BAF60846.1; -; Genomic_DNA.
DR AlphaFoldDB; A5CYS9; -.
DR STRING; 370438.PTH_2665; -.
DR KEGG; pth:PTH_2665; -.
DR eggNOG; COG0037; Bacteria.
DR HOGENOM; CLU_026481_5_2_9; -.
DR Proteomes; UP000006556; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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; PTHR43686; SULFURTRANSFERASE-RELATED; 1.
DR PANTHER; PTHR43686:SF1; TRNA-CYTIDINE(32) 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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR004976-51};
KW Reference proteome {ECO:0000313|Proteomes:UP000006556};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 29..208
FT /note="tRNA(Ile)-lysidine/2-thiocytidine synthase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF01171"
FT BINDING 32..34
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR004976-51"
FT BINDING 38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR004976-51"
FT BINDING 64
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR004976-51"
FT BINDING 133
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR004976-51"
FT BINDING 138
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR004976-51"
SQ SEQUENCE 250 AA; 28119 MW; 8F6601E621643761 CRC64;
MVKDYRKWFL GRIKKAITDY GMIGAGDRVA VGMSGGKDST SLLHALHLIS RSAPVRFELE
AVFVDLGWPA DISLLEEFCR LRNVSLHVVK TGIAEIVFEA RKGENPCALC AHLRRGAFHG
KALELGCNKV ALGHHLDDAI ETFFMSLFYT GQLRTFSPCT FLDRTGLTMI RPLVYLPAED
IRTWVEMEGL PAITNPCPAS GKTKRQEARE LVAWLAGRYP DLKMRFLTAL QTFDRRNLWP
EIKGCRIGHN
//
