ID   Q9XAI1_STRCO            Unreviewed;       783 AA.
AC   Q9XAI1;
DT   01-NOV-1999, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1999, sequence version 1.
DT   27-MAR-2024, entry version 136.
DE   SubName: Full=Serine-threonine protein kinase {ECO:0000313|EMBL:CAB45488.1};
GN   OrderedLocusNames=SCO3621 {ECO:0000313|EMBL:CAB45488.1};
GN   ORFNames=SC66T3.32c {ECO:0000313|EMBL:CAB45488.1};
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226 {ECO:0000313|EMBL:CAB45488.1, ECO:0000313|Proteomes:UP000001973};
RN   [1] {ECO:0000313|EMBL:CAB45488.1, ECO:0000313|Proteomes:UP000001973}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145
RC   {ECO:0000313|Proteomes:UP000001973};
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.H.,
RA   Kieser T., Larke L., Murphy L., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(2002).
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; AL939117; CAB45488.1; -; Genomic_DNA.
DR   PIR; T35389; T35389.
DR   RefSeq; NP_627816.1; NC_003888.3.
DR   AlphaFoldDB; Q9XAI1; -.
DR   STRING; 100226.gene:17761244; -.
DR   PaxDb; 100226-SCO3621; -.
DR   PATRIC; fig|100226.15.peg.3679; -.
DR   eggNOG; COG0515; Bacteria.
DR   HOGENOM; CLU_000288_135_1_11; -.
DR   InParanoid; Q9XAI1; -.
DR   OrthoDB; 9762169at2; -.
DR   Proteomes; UP000001973; Chromosome.
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; IBA:GO_Central.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd14014; STKc_PknB_like; 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   PANTHER; PTHR43671:SF13; LD04361P; 1.
DR   PANTHER; PTHR43671; SERINE/THREONINE-PROTEIN KINASE NEK; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 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}; Kinase {ECO:0000313|EMBL:CAB45488.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000001973};
KW   Transferase {ECO:0000313|EMBL:CAB45488.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        595..616
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          25..295
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          314..589
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          619..682
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          739..783
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        534..548
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        571..586
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        631..655
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         53
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   783 AA;  75647 MW;  9C7F3A7614B5E8A5 CRC64;
     MRRLGDGDPV GVPPGVQHWG NIGVYRLLGR LGTGGMGHVY LARSDRGRTV AVKLVREELA
     ALEEFRERFR HEVESARRVG GHWTAPVLDA DTEAAVPWVA TGYVAGPSLQ QVVGHDHGAL
     PERSVRTLGA GLAHALQDIH AAGIVHRDLK PSNVLVTIDG PRVIDFGIAR ALQTVADGGL
     TRTGALVGSP GFMAPEQVRG DRVTPACDVF CLGSVLAYAA TGKLPFGSAN SGAHALMFRI
     AQEEPDLEGV PEGIADLVRD CLRKDPAARP ALADVLERTG AQDTVTGGRS RDPWLPSALV
     AQLGRHAVQL LDTENPEDPA HPAGGPDPSR TPGAAAATPG DALPDGASAP AAGVRPEGAG
     HGGVAPGSAG PGGGGRGGVG PGGAGPGGVG PGGVGPGGVG PGGVGSGGVG PGGAGPGGVG
     PGGAGSGGVG PGGAGSGGVG PGGAGSGGVG PGGAGSGSAG PDGADPGGVG PGGAWPGGGG
     ARGGGSGGEG AAQGADPASG GPPPPREPGS GGGAPLNHLP TQVAGRHPAT PPPGAHGHAQ
     PPAPGYDPAP AWHASQPGHQ HPYDGGGGLG PTPPQGPPPP YGPPHEPVRN GRSTALLIVV
     ALVVALGAGG SVYALMRGDD DGRAGGDPTP TRSTGAPQDP GTGASGSSGA TGGRSPSTGP
     AADEGTVPTG YLGDWSTSID NASGTHPRTL SIVPGEVGDT VLTLVADGPT DTGTYHCVFE
     AALTAEPGSG GPLRLGPSAV RTGPASSCAP GGPSTVTLRP DGSLERTSDD TGESLLYTRA
     QGY
//