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Database: UniProt
Entry: A0A1F9YNN1_9BACT
LinkDB: A0A1F9YNN1_9BACT
Original site: A0A1F9YNN1_9BACT 
ID   A0A1F9YNN1_9BACT        Unreviewed;       323 AA.
AC   A0A1F9YNN1;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=GHMP kinase {ECO:0000313|EMBL:OGS41206.1};
GN   ORFNames=A2506_00890 {ECO:0000313|EMBL:OGS41206.1};
OS   Elusimicrobia bacterium RIFOXYD12_FULL_66_9.
OC   Bacteria; Elusimicrobiota.
OX   NCBI_TaxID=1797972 {ECO:0000313|EMBL:OGS41206.1, ECO:0000313|Proteomes:UP000176958};
RN   [1] {ECO:0000313|EMBL:OGS41206.1, ECO:0000313|Proteomes:UP000176958}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
CC   -!- SIMILARITY: Belongs to the GHMP kinase family.
CC       {ECO:0000256|ARBA:ARBA00038121}.
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:OGS41206.1}.
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DR   EMBL; MGVR01000137; OGS41206.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F9YNN1; -.
DR   Proteomes; UP000176958; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.230.120; -; 1.
DR   InterPro; IPR001174; Galkinase.
DR   InterPro; IPR013750; GHMP_kinase_C_dom.
DR   InterPro; IPR036554; GHMP_kinase_C_sf.
DR   InterPro; IPR006204; GHMP_kinase_N_dom.
DR   InterPro; IPR014606; Heptose_7-P_kinase.
DR   InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR   PANTHER; PTHR32463; L-FUCOSE KINASE; 1.
DR   PANTHER; PTHR32463:SF0; L-FUCOSE KINASE; 1.
DR   Pfam; PF08544; GHMP_kinases_C; 1.
DR   Pfam; PF00288; GHMP_kinases_N; 1.
DR   PIRSF; PIRSF036406; Hept_kin; 1.
DR   PRINTS; PR00960; LMBPPROTEIN.
DR   SUPFAM; SSF55060; GHMP Kinase, C-terminal domain; 1.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:OGS41206.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:OGS41206.1}.
FT   DOMAIN          96..154
FT                   /note="GHMP kinase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00288"
FT   DOMAIN          225..303
FT                   /note="GHMP kinase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08544"
SQ   SEQUENCE   323 AA;  35465 MW;  012FD11A44CB4021 CRC64;
     MIISRTPFRI SLVGGGTDLA AFYRRRAGAV VSTAIDKYMY VTVNRYFDDS IILKYSRTEL
     VRRVSDIRHP ILRECLKLVG IERGIEITSM ADVVGGTGLG SSSSFTVGVL HALHAFKGEY
     RTAEELAREA CRVEIELLKE PIGKQDQYIA AYGGFQSIEF MPDETVRVDP IVLSEKARAA
     LAERTLLLYT GVTRKAGPVL RRFRAKFEAK DRQMTRLRDL AYEARESLRD GDIDAIGPML
     HEGWELKKGI SGGITSPGID RAYEAARKAG ASGGKILGAG GGGFLLLLAP PAKRGAVRRA
     LASWREIPFG LEPEGSKIVY VSR
//
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