ID H6R8R1_NOCCG Unreviewed; 1238 AA.
AC H6R8R1;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN OrderedLocusNames=NOCYR_0268 {ECO:0000313|EMBL:CCF61089.1};
OS Nocardia cyriacigeorgica (strain GUH-2).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Nocardia.
OX NCBI_TaxID=1127134 {ECO:0000313|EMBL:CCF61089.1, ECO:0000313|Proteomes:UP000008190};
RN [1] {ECO:0000313|EMBL:CCF61089.1, ECO:0000313|Proteomes:UP000008190}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GUH-2 {ECO:0000313|EMBL:CCF61089.1,
RC ECO:0000313|Proteomes:UP000008190};
RX PubMed=22461543; DOI=10.1128/JB.00161-12;
RA Zoropogui A., Pujic P., Normand P., Barbe V., Beaman B., Beaman L.,
RA Boiron P., Colinon C., Deredjian A., Graindorge A., Mangenot S.,
RA Nazaret S., Neto M., Petit S., Roche D., Vallenet D., Rodriguez-Nava V.,
RA Richard Y., Cournoyer B., Blaha D.;
RT "Genome sequence of the human- and animal-pathogenic strain Nocardia
RT cyriacigeorgica GUH-2.";
RL J. Bacteriol. 194:2098-2099(2012).
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};
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DR EMBL; FO082843; CCF61089.1; -; Genomic_DNA.
DR RefSeq; WP_014348566.1; NC_016887.1.
DR AlphaFoldDB; H6R8R1; -.
DR STRING; 1127134.NOCYR_0268; -.
DR KEGG; ncy:NOCYR_0268; -.
DR eggNOG; COG0515; Bacteria.
DR eggNOG; COG2909; Bacteria.
DR HOGENOM; CLU_006325_2_0_11; -.
DR OrthoDB; 136365at2; -.
DR Proteomes; UP000008190; Chromosome.
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; cd14014; STKc_PknB_like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR041664; AAA_16.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
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; PTHR43289; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 20-RELATED; 1.
DR PANTHER; PTHR43289:SF32; SERINE_THREONINE-PROTEIN KINASE PKAB; 1.
DR Pfam; PF13191; AAA_16; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF17874; TPR_MalT; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:CCF61089.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000008190};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:CCF61089.1};
KW Transferase {ECO:0000313|EMBL:CCF61089.1}.
FT DOMAIN 99..365
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 380..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..414
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 128
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1238 AA; 133844 MW; AE30957E24DF94F3 CRC64;
MDPRARSDRA GREPGSVVSD TARWQPDLGT RTPGREPDAD AEPAEPDAAD SVADAAAGPG
AAARPAVSGN GDTGTRPEDR DTQENNPIAI EDELEAMGLS GAREIGHGGF GVVYRCVQRA
LDRVVAVKVL SSDIDDESRE RFLREEHAMG RLSGHPNIVD ILQVDVTATG RPFIVMPYAT
RGSLEVVVRD NGPLTWSDTL RAGVKLAGAI ESAHRAGILH RDVKPANVLL SSYGEPQLTD
FGIARVPGGF RTSSSMITGS PAFTAPEVLK GDEPTVRSDV YGLGATLFAL LTGHAAFERQ
AGEKVVAQFL RITTQPVPDL REQDIPADVA AAIEHAMAQH PDDRPASAYE FGEMLRAIQR
AHGQMADEMA LLDTTDEADA VPSQAGRTAV TARRSWPLNL SPPTPRPGYD PSPTATLPPT
AATKFRPPTP AREPIPRTRL LDILRTGGRR RLAVIHAPAG FGKSTLAAQW RAELTADGVA
VAWIGIDSDD DNEIWFLAHL IEAIRRVRPD IGTGLDQVLE EQPADAVAYA ITTLIDDVHA
GGATVVVVVD DWHRITDPGT RRVMDSLLDN GCHHLRFVVT SRDQSGLPIS RMRVRDELVE
IGSAQLRLTR EETRQILVER NRFSLTDDQI DDLYRATDGW PAAVQLISLA LRGNPDPAPL
IEHLAEGGHG IREYLAENVI DGLEPRMVDF LTAISIAEKV SGSLAAALSD DPGAEHLLEQ
AEQRELFVRR VEYDPEWFRV QPLFAEHLRA RLERSDPAQV KALHRKAARW YAEHQLLRKS
VDHAVAATDL KMALDLLESG GMDLIDGSRL ATLLGTVSKL PVQQVASRSK LLMAVARANV
NLQQSGAARS ALGRLSNVLS RGPSGDADVI RQRCQAAVLA AADQVARDHT EGVAEQIADC
LEHPDELPAW TVSTAANLIS FVRLCEFDFD GARAIQDWAA DYHERSKDPL GSVFGLCSRG
AVAYEQLDIA TAAQCFQQAF DIARARSGPR SHAVRVAAAL LGELHYRRGE LDAADRLLDE
SHQLVARVGP IDFLISTFVI GARVKAVRGD MGTAANRLAE GERIAVDQNL PRLAAQVRAE
RVRLGPAAEP SGPQAATARR HGDVIDDTAR AGHRFTGTAA LTLEAQEIAA IRELLAGGGI
EDQDRAVRRA RALYGRTHEQ HRPRAQLDTS LLLAECLAAA GWVGEAAAQL VPAVNTCADL
DWSRPLLDAG PGVVAILRVL RNDLPDELPV RFVDELLT
//
