ID A0A0X3XVR1_9ACTN Unreviewed; 338 AA.
AC A0A0X3XVR1;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=GlmZ(SRNA)-inactivating NTPase {ECO:0000313|EMBL:KUL78433.1};
GN ORFNames=ADL34_07630 {ECO:0000313|EMBL:KUL78433.1};
OS Streptomyces sp. NRRL WC-3605.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1609103 {ECO:0000313|EMBL:KUL78433.1, ECO:0000313|Proteomes:UP000052945};
RN [1] {ECO:0000313|EMBL:KUL78433.1, ECO:0000313|Proteomes:UP000052945}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL WC-3605 {ECO:0000313|EMBL:KUL78433.1,
RC ECO:0000313|Proteomes:UP000052945};
RA Gilbert D.G.;
RL Submitted (OCT-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:KUL78433.1}.
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; LLZN01000039; KUL78433.1; -; Genomic_DNA.
DR RefSeq; WP_062674659.1; NZ_LLZN01000039.1.
DR AlphaFoldDB; A0A0X3XVR1; -.
DR OrthoDB; 9784461at2; -.
DR Proteomes; UP000052945; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_00636; RapZ_like; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005337; RapZ-like.
DR PANTHER; PTHR30448:SF0; RNASE ADAPTER PROTEIN RAPZ; 1.
DR PANTHER; PTHR30448; UNCHARACTERIZED; 1.
DR Pfam; PF03668; ATP_bind_2; 1.
DR PIRSF; PIRSF005052; P-loopkin; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00636};
KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00636};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00636};
KW Reference proteome {ECO:0000313|Proteomes:UP000052945}.
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..32
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 62..69
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00636"
FT BINDING 113..116
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00636"
SQ SEQUENCE 338 AA; 37067 MW; 0C60780BE2A7C27E CRC64;
MNEHDTGATA DRDPEPRDPH RSPGDDPAQQ DARQEDGAQV STGSEKAGVP DAAIPELVII
SGMSGAGRST AAKCLEDLGW FVVDNLPPAL IPTMVELGAR SQGNVARIAV VVDVRGRRFF
DNLRESLSDL DARGVTRRIV FLESSDDALV RRFESVRRPH PLQGDGRIVD GIAAERELLR
ELRGDADLVI DTSSLNVHEL RAKMDAQFAG EEEPELRATV MSFGFKYGLP VDADLVVDMR
FLPNPHWVPE LRPFTGLNEE VAAYVFNQPG AKEFLDRYAE MLQLVAAGYR REGKRYVTIA
VGCTGGKHRS VAMSEKLAAR LAAEGVETVV VHRDMGRE
//