ID A0A1Q4X3Z6_9ACTN Unreviewed; 703 AA.
AC A0A1Q4X3Z6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN ORFNames=A6A08_06950 {ECO:0000313|EMBL:OKI16999.1};
OS Nocardiopsis sp. TSRI0078.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Nocardiopsaceae; Nocardiopsis.
OX NCBI_TaxID=1718951 {ECO:0000313|EMBL:OKI16999.1, ECO:0000313|Proteomes:UP000185866};
RN [1] {ECO:0000313|EMBL:OKI16999.1, ECO:0000313|Proteomes:UP000185866}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TSRI0078 {ECO:0000313|EMBL:OKI16999.1,
RC ECO:0000313|Proteomes:UP000185866};
RX PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL MBio 7:e02104-e02116(2016).
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:OKI16999.1}.
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DR EMBL; LWLB01000023; OKI16999.1; -; Genomic_DNA.
DR RefSeq; WP_073703301.1; NZ_LWLB01000023.1.
DR AlphaFoldDB; A0A1Q4X3Z6; -.
DR STRING; 1718951.A6A08_06950; -.
DR OrthoDB; 3915799at2; -.
DR Proteomes; UP000185866; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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; 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; PF00069; Pkinase; 1.
DR Pfam; PF13432; TPR_16; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF81901; HCP-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.
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};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}.
FT DOMAIN 15..269
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 297..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..317
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 703 AA; 77020 MW; A32379A09C58130F CRC64;
MSDILPWPLV PVGGYRPLKL LGRGGYGIVY LGSRDSGEQA AVKLLRTDRF DSGQAQQRFV
REIEQLSRVS GPCVASILDA DPEAPIPWIA TEYIEGPTLQ KFIEANGPCT GPDLYRLAVR
TAEALTGIHA AGVIHRDLKP ENILLASEGP RVIDFGISRA LESTGMLPSM PLGSVGYAAP
EQLKDVPLSP RTDVFAWGAV MVFAATGRKA FPAAEKLAWM HQVMNREPET YGVREPLLSV
VLSCLDKRPE RRPTSARLMQ TLVESHSSGG WTRLTGEVAA AGTGREPSST RLTPTRLFTT
RPMTDLQDGS PESPAPSSRE ETARGEATVN PHTHQRRPHR PHALAHSLAR TVTDLARAGL
PTVSNDLLAK AHTVHLHDVH LPEGMSFIEE LNWACLPVPR GGGLLVSAQG TRWRPADHLL
AEAGGPVPRE LWFTAAANAS GEVGPADVAM NALRMDEYEI ALSILIQASE HDDLAARGLL
GLLSAQARDY RRAEPLLREV VGENGSAAYR FELGALLHRT GRVDEAEQWY LDAAESGSGR
AMAHLGMLYS QRAEEEQAQH WLRQSAESAE DPLGMVLWSF DLSLRGRPAD ARHWYDRALE
ESGPQVLVEA GDLLRDLGNP EAEDFYRAAA RHDEDFGHER WEQTHRKGAD TVQLHVPRAA
TGNGHPTEPD WYIRQVARDE VSQVFTEFFG NDGPWVEPNG KGP
//
