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Database: UniProt
Entry: A0A0J6XKZ8_9ACTN
LinkDB: A0A0J6XKZ8_9ACTN
Original site: A0A0J6XKZ8_9ACTN 
ID   A0A0J6XKZ8_9ACTN        Unreviewed;       417 AA.
AC   A0A0J6XKZ8;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=ATP-grasp domain-containing protein {ECO:0000259|PROSITE:PS50975};
GN   ORFNames=ACS04_24210 {ECO:0000313|EMBL:KMO95358.1};
OS   Streptomyces roseus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=66430 {ECO:0000313|EMBL:KMO95358.1, ECO:0000313|Proteomes:UP000035932};
RN   [1] {ECO:0000313|EMBL:KMO95358.1, ECO:0000313|Proteomes:UP000035932}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31245 {ECO:0000313|EMBL:KMO95358.1,
RC   ECO:0000313|Proteomes:UP000035932};
RA   Cruz-Morales P., Martinez-Guerrero C., Morales-Escalante M.A.,
RA   Yanez-Guerra L.A., Kopp J.F., Feldmann J., Ramos-Aboites H.E.,
RA   Barona-Gomez F.;
RT   "Recapitulation of the evolution of biosynthetic gene clusters reveals
RT   hidden chemical diversity on bacterial genomes.";
RL   Submitted (JUN-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:KMO95358.1}.
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DR   EMBL; LFML01000102; KMO95358.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0J6XKZ8; -.
DR   STRING; 66430.ACS04_24210; -.
DR   PATRIC; fig|66430.4.peg.325; -.
DR   OrthoDB; 6964321at2; -.
DR   Proteomes; UP000035932; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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; IPR041472; BL00235/CARNS1_N.
DR   InterPro; IPR040570; LAL_C2.
DR   PANTHER; PTHR43585:SF2; ATP-GRASP ENZYME FSQD; 1.
DR   PANTHER; PTHR43585; FUMIPYRROLE BIOSYNTHESIS PROTEIN C; 1.
DR   Pfam; PF13535; ATP-grasp_4; 1.
DR   Pfam; PF18130; ATPgrasp_N; 1.
DR   Pfam; PF18603; LAL_C2; 1.
DR   SMART; SM01209; GARS_A; 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|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000035932}.
FT   DOMAIN          124..328
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   417 AA;  43734 MW;  8FAABBA2FFB12EC8 CRC64;
     MTIGAGPRGP GVLVIEPMGN AGRFLVEAAD RLGVRLYAAT HEDVHDGYPD RLRAALAGVC
     ATDLTDTPRA LADMEAFCRQ HAIAGVAPCF ELFTPLAALL AERTGLPGND PRLARAARNK
     ILMGEAFAAV GIPAPRWALA HDDAEAHRAA REHGLGWPLV VKPAEQGGSW GVSVVDGPER
     LADAVGAARQ YAYARPHGLA LDTRVLLQEY VPGEEYSCDT VVADGVAYPL PVVAKDTTGG
     RYRIETGHTC PSGLPAPLVR AVQHTAARAA LAVGVRNGIA HTELKIPPGT RTPYVIESGA
     RLPGDNLCEI VEAATGVSEA AAQLRAVLGL VPDTVPSRTD AASIRFLLPE HGGVLREVVV
     PDLPGTHSEV YLRPGEAVPE PADSTCRIAH VVARARTAEQ ARGLAGRVAA RSRVEVG
//
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