ID A0A1H2AA85_9BACL Unreviewed; 736 AA.
AC A0A1H2AA85;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:SDT42868.1};
GN ORFNames=SAMN05444162_4251 {ECO:0000313|EMBL:SDT42868.1};
OS Paenibacillaceae bacterium GAS479.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae.
OX NCBI_TaxID=1882832 {ECO:0000313|EMBL:SDT42868.1, ECO:0000313|Proteomes:UP000198637};
RN [1] {ECO:0000313|EMBL:SDT42868.1, ECO:0000313|Proteomes:UP000198637}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GAS479 {ECO:0000313|EMBL:SDT42868.1,
RC ECO:0000313|Proteomes:UP000198637};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; LT629764; SDT42868.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H2AA85; -.
DR STRING; 1882832.SAMN05444162_4251; -.
DR OrthoDB; 9788659at2; -.
DR Proteomes; UP000198637; Chromosome i.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd06577; PASTA_pknB; 3.
DR CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 3.30.10.20; -; 3.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR005543; PASTA_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR NCBIfam; NF033483; PknB_PASTA_kin; 1.
DR PANTHER; PTHR43671:SF13; LD04361P; 1.
DR PANTHER; PTHR43671; SERINE/THREONINE-PROTEIN KINASE NEK; 1.
DR Pfam; PF03793; PASTA; 3.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00740; PASTA; 3.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51178; PASTA; 3.
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}; Kinase {ECO:0000313|EMBL:SDT42868.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000198637};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:SDT42868.1};
KW Transferase {ECO:0000313|EMBL:SDT42868.1}.
FT DOMAIN 10..270
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 372..440
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 441..511
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 512..581
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 298..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 665..736
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..327
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 677..691
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 709..727
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 736 AA; 79663 MW; 038B34D0DFA8A207 CRC64;
MIGRELGGRY EILTRIGGGG MALVYKAHDL LLSRNVAVKV LRQQYVHDEE FIRRFRREAQ
SAAALSHPNV VSIYDVGQED EVHYIVMEYV EGYNLNEVIQ ERASLQADEA VRIAAQIADA
LDHAHQNHII HRDIKPHNIL IGRNGRVKVT DFGIARAVTS STITQTGSVI GSVHYFSPEH
AKGVSTGEKS DIYSLGIVLY QMVTGKLPFL GESPISVALK HLQEPLEDPR TINPLIPQSV
ENIIIKAMRK NPSERYRTAG EMLVDLETAL SPDRINEPKR QFGANDFDET RVMPAIRPGR
DLKQSSSHTA ASDAAQEDTS FSTARQQAAN EEEEDEPKRR KAWLKPLIIV LTTLALLGVV
YGAFKLVSGS LDVADVTVPN VVGMTEADAK SALEEAGLLL EEPSIRAFKP DIPKDQVFAQ
SKSPDMRVKQ GAPVKLSISD GPELKRLGDY KGQKVADAVA ALQALGIPAE SIAQTEVFDD
SAEPGVVLSQ NPAADSELDP ATSKVTLTVS KGAETVKMPD LVGKSVEEAR KLVLQAGLQM
SDDNIVNEGS YKPEGEVLSQ FPYDAGSQVS KGAQVSVTVS SGLPRDALEF TFDLLISPAQ
AGKASEIRIV FTDATGKDIQ AHKRAIKETR SFPVKVVLAP NTEAFVSVYR DGQLVDTFSR
TYDEVKNGSD MGPSTVPGLD PTPPPDTSIG PSPSNDPSAG NPGEGDETAW NDRNGRDRDR
NDGDDRNGGG PNNDNG
//
