ID A0A0S8BEH9_9PROT Unreviewed; 843 AA.
AC A0A0S8BEH9;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN ORFNames=AMJ68_10510 {ECO:0000313|EMBL:KPK09992.1};
OS Acidithiobacillales bacterium SG8_45.
OC Bacteria; Pseudomonadota; Acidithiobacillia; Acidithiobacillales.
OX NCBI_TaxID=1703383 {ECO:0000313|EMBL:KPK09992.1, ECO:0000313|Proteomes:UP000053136};
RN [1] {ECO:0000313|EMBL:KPK09992.1, ECO:0000313|Proteomes:UP000053136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG8_45 {ECO:0000313|EMBL:KPK09992.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001433};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
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:KPK09992.1}.
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DR EMBL; LJTU01000070; KPK09992.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8BEH9; -.
DR PATRIC; fig|1703383.3.peg.2170; -.
DR Proteomes; UP000053136; 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:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR007890; CHASE2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR43671:SF13; LD04361P; 1.
DR PANTHER; PTHR43671; SERINE/THREONINE-PROTEIN KINASE NEK; 1.
DR Pfam; PF05226; CHASE2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM01080; CHASE2; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 375..394
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 401..420
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 426..444
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 572..833
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 601
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 843 AA; 94692 MW; 6476EE2436B22025 CRC64;
MNGGLLKKDW ALALAITLVY FVAMISDVPI LERMERVAYD TGVSLTNRNP GDADRIAIIA
IDDASLERIG RWPWSRAELA TMVDKMHRAR AKVVGLQFPL VDAQTDVGLD RVRDIRNYIS
SNSFPRAAQK KINVIKGKLW AAQREMDVDR QLANLMARGG NVFLPMEFDI GVPEGNPSSQ
LPSYVKENRL TRIYDSDDNS HLPVSTLAAT YPIAELGKKA SGIGHLNRTR DADGGVRKES
LVYEYFGQYY PSMALLMAAR SQNIRTSRID LNLGQGVGLG KLFVRTDKKM RFYHGFYSPA
NDTPPFAQYS FADVRDGKVS LRTFRNKIVL IGLTATDVAH SYLTPINPQM SDPELTANVI
ASILNQDYYT RPTTVVVVEV FLFLAVIFYL AFVLPRFRAN VGALFTFIVL LSLLIAGQYS
MVSQKVWLQS VAPALLLILG YIVLKTRRFL STEHQKESAD SDSAQSNRML GLTFQSQGQL
DMALDKFRKL PVDDSVLELF YNLALDFERK RHFNKAAACY ENILQHNRKF RDAKERRQRA
SQMEGTIIMG PRGSGTLVVD GGITENPTLG RYQVERELGR GAMGTVYYGK DPKINRVVAI
KTLDLSAEFE GKELDQVKER FFREAETAGR LNHPNIVTIY DAGEEHDLAY IAMEYLEGKD
LTDKIQEKKP LPVAWVLQIV MQVADALDYA HKLGVVHRDI KPANIMYNEK DSSIKVTDFG
IARITDSSKT RTGVVLGTPS YMSPEQFSGK RVDGRSDLYS LGVTMFEMLT GEQPFGGDSL
AELMYQITNK KHPNIMRIRD DVPTCVRTII DKALQKEPDD RYQTGEQFVQ AVRRCLVSIE
GNG
//
