ID A0A1F8NIV0_9CHLR Unreviewed; 726 AA.
AC A0A1F8NIV0;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-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=A2Y53_02745 {ECO:0000313|EMBL:OGO10733.1};
OS Chloroflexi bacterium RBG_16_47_49.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1797639 {ECO:0000313|EMBL:OGO10733.1, ECO:0000313|Proteomes:UP000179729};
RN [1] {ECO:0000313|EMBL:OGO10733.1, ECO:0000313|Proteomes:UP000179729}
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. 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:OGO10733.1}.
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DR EMBL; MGNG01000129; OGO10733.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8NIV0; -.
DR Proteomes; UP000179729; Unassembled WGS sequence.
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; 3.
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; 4.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF69304; Tricorn protease N-terminal domain; 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 Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141}.
FT DOMAIN 13..265
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 170..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 407..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..432
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 42
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 726 AA; 79710 MW; 006F0C157269C02A CRC64;
MTLEPGSLLN NRYRIVEVLG QGGMAAVYRA IDENLSVEVA VKENLFTTDE YARQFRLEAT
ILAGLRQPNL PRVSDHFVIE PQGQYLVMDF IEGEDLRQRL DRLGPLPEQE VIIIGVAICD
AMAYMHSRKP MILHRDIKPG NVRITPSGHI YLVDFGLAKL VQGRETTHTG ARAMTPGYSP
PEQYGTARTD PRSDIYSLGA TLYSALTDVL PEDGLDRAMN RVGLTPILKH NLKASEHVTT
IIEKCLAIQT EDRYQSAEEL RFALMEARSI SRRKLPLELV LQPPPMILHD RLPIETGNQS
QNFIAVDASK SAIRDKKSTR PLYEGQDNIE LVPLKPKLHR KASTWLLLAL LPIIVLSGFG
IYATRPEFVK QAIGFVLPAL VPTDTAILGT PTNTPVPILA IVSKTPTQVN SPSPTATTTP
HPTLTSTQEP SPTITPSPLP TPMGGAAQIA FASNRSGAVE IYLMNLDGSK LEMITNIAEG
ACQPSWSPDG KRIVFISPCK RHLTSYPGAS MFMINADGSS LVPLPNVPGG DYDPSWSPDG
TKIAFTSLRK GGVPGIYILN INDHSVKSLV EDETRAISQP AWSPDGEQIA YVNSDNRIWL
MDVNGKNRHG LTIGGGDYMI NAPAWSPDGS VVIYTRTVFS DTTGSTLLMA VPYSETGAIP
VEVPNSQLVL DVSYSFDGYW LLFTSWFSGS HDLWVMRANG VDRHSIEADP AYDFDPVWRP
NPFNPP
//
