ID A0A0N8GQF3_9CHLR Unreviewed; 664 AA.
AC A0A0N8GQF3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN ORFNames=ADN01_08075 {ECO:0000313|EMBL:KPL83538.1};
OS Levilinea saccharolytica.
OC Bacteria; Chloroflexota; Anaerolineae; Anaerolineales; Anaerolineaceae;
OC Levilinea.
OX NCBI_TaxID=229921 {ECO:0000313|EMBL:KPL83538.1, ECO:0000313|Proteomes:UP000050501};
RN [1] {ECO:0000313|EMBL:KPL83538.1, ECO:0000313|Proteomes:UP000050501}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIBI-1 {ECO:0000313|EMBL:KPL83538.1,
RC ECO:0000313|Proteomes:UP000050501};
RA Hemp J., Ward L.M., Pace L.A., Fischer W.W.;
RT "Genome sequence of Levilinea saccharolytica DSM 16555.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. NEK Ser/Thr
CC protein kinase family. NIMA subfamily. {ECO:0000256|ARBA:ARBA00010886}.
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:KPL83538.1}.
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DR EMBL; LGCM01000030; KPL83538.1; -; Genomic_DNA.
DR RefSeq; WP_062418896.1; NZ_LGCM01000030.1.
DR AlphaFoldDB; A0A0N8GQF3; -.
DR STRING; 229921.ADN01_08075; -.
DR Proteomes; UP000050501; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR011659; PD40.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR PANTHER; PTHR43671:SF13; LD04361P; 1.
DR PANTHER; PTHR43671; SERINE/THREONINE-PROTEIN KINASE NEK; 1.
DR Pfam; PF07676; PD40; 3.
DR Pfam; PF00069; Pkinase; 1.
DR SUPFAM; SSF82171; DPP6 N-terminal domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Reference proteome {ECO:0000313|Proteomes:UP000050501};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 292..316
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 14..283
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 366..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..395
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 43
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 664 AA; 71864 MW; A33D9FD74D7E693C CRC64;
MPSYQPNDIL LDKYRIERLL GQGAFGEVYL ATHIKLNGQR AVKVLRADAP GFSAPQRLQD
ARERFELEAR LYELFHGSDL VQVFDFEEDH GILLLSMEYM PGGSLAARIE AADREGTPIP
VDEVVRIGGQ IAEALAALHQ RDVIHRDLHP GNILFDRDGR ARLADLGLAQ VPGVFSERYG
VSSALLSIHP GHPNFRSPEH NLGSQALKPP SDIYMLGACL FLALTGRDYH NQRPGTRVRS
LRPDAPVWLD DLLTVMLAED PRQRPWDGVE VAKKLRRDPS PLPRSAGKKP SAWWLALGAA
AVVLLFALIA VPILWLTSNR QTQKLQTTQT ALALQAVQAG PTDQQSAALL PAPAARAAAP
EIPVEPTDLS VQQSSLSNDG KTPTAFKTQE KSSSAGEAAH PVGWEQGKLV FTARLDAGAA
LTLLDLASKQ STVLQTGKSE NYLLGPALSP DGTRIAYYSL PNILYQSPLS PQFSPVQTDQ
CKSPSWASDS SSIVCSASGN RLKWAGGDSI SSIYGLIPAL SPNGKDLVYA VFEDQATKIY
RSSVNGDAPL LLAGSSSENY APAISPDGKW IAYQSNEGSA NSEIWLMNIN GAEKQRLTES
GSGNWSRGPA WSPDGQWLAY VSSQAGSLGA DFGEVFIRSV DTGESHQVTH TNGKVYDWRV
SWGP
//
