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Database: UniProt
Entry: A0A1G1F9B4_9BACT
LinkDB: A0A1G1F9B4_9BACT
Original site: A0A1G1F9B4_9BACT 
ID   A0A1G1F9B4_9BACT        Unreviewed;       566 AA.
AC   A0A1G1F9B4;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN   ORFNames=A2X56_02800 {ECO:0000313|EMBL:OGW28328.1};
OS   Nitrospirae bacterium GWC2_57_13.
OC   Bacteria; Nitrospirota.
OX   NCBI_TaxID=1801697 {ECO:0000313|EMBL:OGW28328.1, ECO:0000313|Proteomes:UP000177780};
RN   [1] {ECO:0000313|EMBL:OGW28328.1, ECO:0000313|Proteomes:UP000177780}
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 protein kinase superfamily. ADCK protein
CC       kinase family. {ECO:0000256|ARBA:ARBA00009670}.
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:OGW28328.1}.
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DR   EMBL; MHDZ01000050; OGW28328.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G1F9B4; -.
DR   STRING; 1801697.A2X56_02800; -.
DR   Proteomes; UP000177780; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   CDD; cd05121; ABC1_ADCK3-like; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR004147; ABC1_dom.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   PANTHER; PTHR10566; CHAPERONE-ACTIVITY OF BC1 COMPLEX CABC1 -RELATED; 1.
DR   PANTHER; PTHR10566:SF129; PROTEIN KINASE UBIB-RELATED; 1.
DR   Pfam; PF03109; ABC1; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        14..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        165..184
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        496..515
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        535..553
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          128..434
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
SQ   SEQUENCE   566 AA;  64651 MW;  B1460049130E0CE6 CRC64;
     MGLIRTHLRG MKRLLTICLI LFRQFMILIP YKFLFAPSAK FEKAIGRYLS TKKPRMSAPE
     IAKETLEMLG PTYVKFGQFL SIRPDLVPPD FCEEFKKLQD RVPPFPFAQV KRELRNELKK
     DTTEIFSELD ETAMAAASVS QVHRARLRTG EEVAVKVQRP GIQDAMISDL FIMLRFAYLI
     VRFIPSLRKN RPVMLVQEFS RWTERELYFR QEGKNALLFS HNFKDHPEVR IPKVYREYTT
     RKILVMEHIR GVNIFNAAGH DIDKQAVARL IADSMLQQIF IHGFFHGDPH AGNILLVDNN
     TIAYLDFGIV GYLSEDLRAW IFDILYGMSE GDVTRVIGSF LELCNVREDE IDLAGYRREM
     NEVLSELPIY EVVGIPFSQM MERFLNTSLE FGIHIPHDFV LASKALTTFE GTCLTLDPQI
     KIVEHLRSFV QKYITTSLEF DDVLKQLKAG PFETARLKRL VLKHGTRVLR FFEDPTVRIA
     GEGTGTAAKN GDTSGLSLAH GFIIGALVLF AALVSNESDL ERWLRSFISL PPLPVLSLAS
     LAGAAFLWIG LAFRNRLKKN TRDATR
//
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