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Database: UniProt
Entry: R5QPR1_9FIRM
LinkDB: R5QPR1_9FIRM
Original site: R5QPR1_9FIRM 
ID   R5QPR1_9FIRM            Unreviewed;       198 AA.
AC   R5QPR1;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Guanylate kinase-like domain-containing protein {ECO:0000259|PROSITE:PS50052};
GN   ORFNames=BN526_00783 {ECO:0000313|EMBL:CCZ28359.1};
OS   Firmicutes bacterium CAG:194.
OC   Bacteria; Bacillota.
OX   NCBI_TaxID=1263008 {ECO:0000313|EMBL:CCZ28359.1, ECO:0000313|Proteomes:UP000018384};
RN   [1] {ECO:0000313|EMBL:CCZ28359.1, ECO:0000313|Proteomes:UP000018384}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:194 {ECO:0000313|Proteomes:UP000018384};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Essential for recycling GMP and indirectly, cGMP.
CC       {ECO:0000256|ARBA:ARBA00003531}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + GMP = ADP + GDP; Xref=Rhea:RHEA:20780,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:58115, ChEBI:CHEBI:58189,
CC         ChEBI:CHEBI:456216; EC=2.7.4.8;
CC         Evidence={ECO:0000256|ARBA:ARBA00000283};
CC   -!- SIMILARITY: Belongs to the guanylate kinase family.
CC       {ECO:0000256|ARBA:ARBA00005790}.
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:CCZ28359.1}.
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DR   EMBL; CAZT010000053; CCZ28359.1; -; Genomic_DNA.
DR   AlphaFoldDB; R5QPR1; -.
DR   Proteomes; UP000018384; Unassembled WGS sequence.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR008145; GK/Ca_channel_bsu.
DR   InterPro; IPR008144; Guanylate_kin-like_dom.
DR   InterPro; IPR020590; Guanylate_kinase_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR23117:SF13; GUANYLATE KINASE; 1.
DR   PANTHER; PTHR23117; GUANYLATE KINASE-RELATED; 1.
DR   Pfam; PF00625; Guanylate_kin; 1.
DR   SMART; SM00072; GuKc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00856; GUANYLATE_KINASE_1; 1.
DR   PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
PE   3: Inferred from homology;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018384};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          2..191
FT                   /note="Guanylate kinase-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50052"
SQ   SEQUENCE   198 AA;  23310 MW;  C1734E9FCF5EBF53 CRC64;
     MGKIFYLMGK SSSGKDTIYK QLMADEDLHL KNIVLYTTRP IRQGEQEGIE YHFITEEQLA
     NLEKEGRIIE LRAYDTCFGI WKYCTVDAHI DLDRENYLII GTIESFCKTK AFYGEEKVIP
     LMIELDDGIR LRRALDREMA QDQPKYDEMC RRYLADAADF SPEKKKEAGI EKEFLNDELD
     VCIAELKEYI LHEMRKRI
//
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