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Y3714_MYCGI
ID   Y3714_MYCGI             Reviewed;         327 AA.
AC   A4TC20;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Nucleotide-binding protein Mflv_3714 {ECO:0000255|HAMAP-Rule:MF_00636};
GN   OrderedLocusNames=Mflv_3714;
OS   Mycolicibacterium gilvum (strain PYR-GCK) (Mycobacterium gilvum (strain
OS   PYR-GCK)).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=350054;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PYR-GCK;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Miller C., Richardson P.;
RT   "Complete sequence of chromosome of Mycobacterium gilvum PYR-GCK.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Displays ATPase and GTPase activities. {ECO:0000255|HAMAP-
CC       Rule:MF_00636}.
CC   -!- SIMILARITY: Belongs to the RapZ-like family. {ECO:0000255|HAMAP-
CC       Rule:MF_00636}.
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DR   EMBL; CP000656; ABP46186.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4TC20; -.
DR   SMR; A4TC20; -.
DR   STRING; 350054.Mflv_3714; -.
DR   PRIDE; A4TC20; -.
DR   EnsemblBacteria; ABP46186; ABP46186; Mflv_3714.
DR   KEGG; mgi:Mflv_3714; -.
DR   eggNOG; COG1660; Bacteria.
DR   HOGENOM; CLU_059558_0_0_11; -.
DR   OMA; TVMSFGF; -.
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; -; 1.
DR   HAMAP; MF_00636; RapZ_like; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005337; RapZ-like.
DR   PANTHER; PTHR30448; PTHR30448; 1.
DR   Pfam; PF03668; ATP_bind_2; 1.
DR   PIRSF; PIRSF005052; P-loopkin; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   3: Inferred from homology;
KW   ATP-binding; GTP-binding; Nucleotide-binding.
FT   CHAIN           1..327
FT                   /note="Nucleotide-binding protein Mflv_3714"
FT                   /id="PRO_0000383266"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..24
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         50..57
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00636"
FT   BINDING         101..104
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00636"
SQ   SEQUENCE   327 AA;  35699 MW;  9F2F2FB2F0CBC257 CRC64;
     MTRQGMRDDL RGEADSVVHD GTDDIDNEND IDNGIDNENG NGIDVVLVTG LSGAGRGTAA
     KVLEDLGWYV ADNLPPELIA QMVDLGLAAG SRITQLAAVM DVRSRGFTGD LDWVRSELAT
     RNIVPRVVFL EASDDILVRR YEQNRRSHPL QGNQTLAEGI AAERAMLAPV RASADLVIDT
     SALSVHGLRD SIERAFAAET VAHTNVTVES FGYKYGLPMD ADTVMDVRFL PNPHWIDRLR
     PHTGQNADVR DYVLGQPGAD EFLDSYHQLL NVVIDGYRRE GKRYMTVAIG CTGGKHRSVA
     MAEALAARLA GSDALTVRVL HRDLGRE
 
 
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