PKNX_STRCO
ID PKNX_STRCO Reviewed; 673 AA.
AC Q9XA16;
DT 04-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Probable serine/threonine-protein kinase SCO3848;
DE EC=2.7.11.1;
GN OrderedLocusNames=SCO3848; ORFNames=SCH69.18;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
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.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., 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 -!- 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;
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AL939118; CAB45215.1; -; Genomic_DNA.
DR PIR; T36717; T36717.
DR RefSeq; NP_628036.1; NC_003888.3.
DR RefSeq; WP_011029269.1; NZ_VNID01000003.1.
DR AlphaFoldDB; Q9XA16; -.
DR SMR; Q9XA16; -.
DR STRING; 100226.SCO3848; -.
DR DNASU; 1099284; -.
DR GeneID; 1099284; -.
DR KEGG; sco:SCO3848; -.
DR PATRIC; fig|100226.15.peg.3919; -.
DR eggNOG; COG0515; Bacteria.
DR HOGENOM; CLU_000288_135_2_11; -.
DR InParanoid; Q9XA16; -.
DR OMA; DPDYRYQ; -.
DR PhylomeDB; Q9XA16; -.
DR Proteomes; UP000001973; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
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 Pfam; PF03793; PASTA; 4.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00740; PASTA; 4.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51178; PASTA; 4.
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; Kinase; Nucleotide-binding; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..673
FT /note="Probable serine/threonine-protein kinase SCO3848"
FT /id="PRO_0000171237"
FT DOMAIN 11..277
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 379..445
FT /note="PASTA 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00528"
FT DOMAIN 446..511
FT /note="PASTA 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00528"
FT DOMAIN 512..580
FT /note="PASTA 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00528"
FT DOMAIN 581..649
FT /note="PASTA 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00528"
FT REGION 302..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 472..500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 613..641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 653..673
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 330..344
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 613..628
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 138
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 17..25
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 40
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 673 AA; 71488 MW; 42A0615E239722DE CRC64;
MEEPRRLGGR YELGPVLGRG GMAEVYHAHD TRLGRQVAVK TLRADLARDP SFQARFRREA
QSAASLNHPA IVAVYDTGED YIDNVSIPYI VMEYVDGSTL RELLHSGRKL LPERTLEMTI
GILQALEYSH RAGIVHRDIK PANVMLTRNG QVKVMDFGIA RAMGDSGMTM TQTAAVIGTA
QYLSPEQAKG EQVDARSDLY STGCLLYELL TVRPPFVGDS PVAVAYQHVR EEPQAPSVFD
PEITPEMDAI VLKALVKDPD YRYQSADEMR VDIEACLDGQ PVGATAAMGA MAAGGYGAYP
DDQPTTALRS DGGGGATTML PPMNPDDGGY GYDERPDRRR QQPRKKNTST IFLVLAGVLV
LVGAILIGKY AFSGDGGPGN DKVPVPAFIG LSKADAQQQA DNIDLVLTFK QQECEDQPKG
NICAQDPKQG TDVDKESTVN LVVSTGAPKV AVPNVIDKNI DEAKKQLEDK GFEVETKQTE
SSQDEGTILS QNPDPGKELE KGSTVTLEVA KAEEKATVPD VVGRTCDEAK AQVESGGDLT
AVCTDQPTND PNQVGKVIST TPQSSTQVDP GSKVTIVVGK AVEKTKVPEV RGKTLAEARQ
ILQQSGFTNV QVAQGSPGDD NAKVFASNPQ PGSEVDDPAA TPITLMTVPG DGGNGNGGNG
NGGAIAGLPG FGD
