ID A0A0F9Z9D6_9BACT Unreviewed; 344 AA.
AC A0A0F9Z9D6;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Carbamoyl phosphate synthase-like-protein, carbamoyl-phosphate synthase large subunit {ECO:0000313|EMBL:KKP40274.1};
DE EC=6.3.5.5 {ECO:0000313|EMBL:KKP40274.1};
GN ORFNames=UR30_C0005G0055 {ECO:0000313|EMBL:KKP40274.1};
OS Candidatus Peregrinibacteria bacterium GW2011_GWC2_33_13.
OC Bacteria; Candidatus Peregrinibacteria.
OX NCBI_TaxID=1619061 {ECO:0000313|EMBL:KKP40274.1, ECO:0000313|Proteomes:UP000034765};
RN [1] {ECO:0000313|EMBL:KKP40274.1, ECO:0000313|Proteomes:UP000034765}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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:KKP40274.1}.
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DR EMBL; LBOR01000005; KKP40274.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F9Z9D6; -.
DR STRING; 1619061.UR30_C0005G0055; -.
DR PATRIC; fig|1619061.3.peg.601; -.
DR Proteomes; UP000034765; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR Gene3D; 3.40.50.20; -; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013651; ATP-grasp_RimK-type.
DR PANTHER; PTHR21621:SF4; GLUTATHIONE SYNTHETASE; 1.
DR PANTHER; PTHR21621; RIBOSOMAL PROTEIN S6 MODIFICATION PROTEIN; 1.
DR Pfam; PF15632; ATPgrasp_Ter; 1.
DR Pfam; PF08443; RimK; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Ligase {ECO:0000313|EMBL:KKP40274.1};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409}.
FT DOMAIN 120..311
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 344 AA; 38143 MW; 7DD776157C91DE0B CRC64;
MNKKIKVLIT GIAGASLGTE ILKCLQLAKN YCIFGCDISN LAFGHYQEGF KETFVADPNN
YVESVIDICK KNDIKYIIPG GEQPMTILGN SSELIKGNGI TLVSNSQGII NKFSDKEETF
KTLANLGFSI PLTIRVKTIN DLNEMVFPCI VKPAKDSGGS SFVFLAGNKE EAWIYAEYLI
KNNKIPLLQE YIDEKDGEFT VGVLSLPNEH IVGSIALRRT FNSKLSIFSK TATGLISSGY
SQGLIDKFPD ICKAAENIAK KIKSVGPINI QGRIKNGIFV PFEINPRFSA STYLRAMAGF
NEIDIYLKYL IDGSINYSSE IKYGYYMRSF SEIFVNRGDI IQND
//
