ID D9VVX3_9ACTN Unreviewed; 412 AA.
AC D9VVX3;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Predicted protein {ECO:0000313|EMBL:EFL19176.1};
GN ORFNames=SSNG_06428 {ECO:0000313|EMBL:EFL19176.1};
OS Streptomyces sp. C.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=253839 {ECO:0000313|EMBL:EFL19176.1, ECO:0000313|Proteomes:UP000005763};
RN [1] {ECO:0000313|EMBL:EFL19176.1, ECO:0000313|Proteomes:UP000005763}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C {ECO:0000313|EMBL:EFL19176.1,
RC ECO:0000313|Proteomes:UP000005763};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Microbial Sequencing Center;
RA Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA Haas B., Nusbaum C., Birren B.;
RT "Annotation of Streptomyces sp. strain C.";
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; GG657750; EFL19176.1; -; Genomic_DNA.
DR RefSeq; WP_007268101.1; NZ_GG657750.1.
DR AlphaFoldDB; D9VVX3; -.
DR STRING; 253839.SSNG_06428; -.
DR eggNOG; COG0151; Bacteria.
DR HOGENOM; CLU_029016_6_3_11; -.
DR Proteomes; UP000005763; 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; 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; 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}.
FT DOMAIN 120..312
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 412 AA; 43815 MW; 36B550F07F0B4F9E CRC64;
MTPPREPGRL LMVMPYEQLV RKAVEAGFEV WSIWDPALRT PEYLDKVAAH SRELALVDFG
DEAALRALVA ELAHEHDVQH VLHLGSEATM APVLAEAEAL GLSPNTAESV RLLNDKHAMR
GLLNAHGVSA VRARRAETLG EVEPLLTEFG LPAVVKPTNT AGSRGIALVR TAADLAEWTE
RVKAGGFEGP FIIEDYLEGP EFSVETLTAG GTHHVVGITA KQTTGAPGFV ETGHIHPAPL
DPADAAAIRD TVTALLDLTG YAFGPAHTEV ILTPAGPRVV ESQARLGGDR IPLLVEVATG
YDIEAAVFRG LAGEDVTAPA PHRYAAIGFF QLPAGRLESV DGLDDLRARD HVHGVHFPYG
PGDVLPRTTD SGTRHGYAVV DAPTPAEAAD RIAAARTALR TTTTQTPKEA LR
//
