ID A0A2C6MF97_9FIRM Unreviewed; 345 AA.
AC A0A2C6MF97;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=ATP-grasp domain-containing protein {ECO:0000259|PROSITE:PS50975};
GN ORFNames=P378_10920 {ECO:0000313|EMBL:PHJ38335.1};
OS Desulforamulus profundi.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC Desulforamulus.
OX NCBI_TaxID=1383067 {ECO:0000313|EMBL:PHJ38335.1, ECO:0000313|Proteomes:UP000222564};
RN [1] {ECO:0000313|EMBL:PHJ38335.1, ECO:0000313|Proteomes:UP000222564}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bs107 {ECO:0000313|EMBL:PHJ38335.1,
RC ECO:0000313|Proteomes:UP000222564};
RA Aullo T., Berlendis S., Lascourreges J.-F., Dessort D., Saint-Laurent S.,
RA Schraauwers B., Mas J., Magot M., Ranchou-Peyruse A.;
RT "Biodegradation of hydrocarbons in the deep terrestrial subsurface :
RT characterization of a microbial consortium composed of two Desulfotomaculum
RT species originating from a deep geological formation.";
RL Submitted (SEP-2013) 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:PHJ38335.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AWQQ01000054; PHJ38335.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2C6MF97; -.
DR OrthoDB; 9803907at2; -.
DR Proteomes; UP000222564; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003824; F:catalytic activity; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR Gene3D; 3.40.50.20; -; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR048764; PylC_PurT_N.
DR Pfam; PF15632; ATPgrasp_Ter; 1.
DR Pfam; PF21360; PylC-like_N; 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:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Reference proteome {ECO:0000313|Proteomes:UP000222564}.
FT DOMAIN 123..300
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 345 AA; 39345 MW; 5FBB87C21D37F948 CRC64;
MYEKDSCINL RVRFPLRRCI IQSLLKSDLA LKLVACDINP RTLGLHLAHR GYIVPPVHQE
EQYLKQLSNI IEKENINAIF VASSKEISFF SNHKAQIEEN TGARVFVNPP GVLEICCDKW
HTVNFLKEQG FYFPRTLRYP EDWEQIDAFI EAVHFPIIVK PRRGAGSQDL YTVNSLNELN
SLITGKKDIV LQQYLPGDLG EFTTGICTGA KGNVLSGITL KRYLQDGMTI AADFDDFTEI
TNYCKEVARV LKPYGPCNFQ SRLLEGKPYI FEINPRFSSS TGMRSLLGVN EAEILLRSEI
LGQKILEPPI LKCSVIRQYT DYLVSTEQIM KLKKENFCIN HSEEN
//
