ID A0A1G9ED53_9ACTN Unreviewed; 591 AA.
AC A0A1G9ED53;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:SDK74089.1};
GN ORFNames=SAMN05421806_11191 {ECO:0000313|EMBL:SDK74089.1};
OS Streptomyces indicus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=417292 {ECO:0000313|EMBL:SDK74089.1, ECO:0000313|Proteomes:UP000199155};
RN [1] {ECO:0000313|EMBL:SDK74089.1, ECO:0000313|Proteomes:UP000199155}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.5727 {ECO:0000313|EMBL:SDK74089.1,
RC ECO:0000313|Proteomes:UP000199155};
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; FNFF01000011; SDK74089.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G9ED53; -.
DR STRING; 417292.SAMN05421806_11191; -.
DR OrthoDB; 9762169at2; -.
DR Proteomes; UP000199155; 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-KW.
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:SDK74089.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000199155};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:SDK74089.1};
KW Transferase {ECO:0000313|EMBL:SDK74089.1}.
FT DOMAIN 99..353
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..91
FT /note="Disordered"
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 591 AA; 62462 MW; CBD29A2B7E9B782F CRC64;
MSNDGGAPYG TGEPTSFSLR PPDQPQGPYA GHPYGTPGTP PAPGTPNPYA QAETQAVPNG
GPATPGAPQP PAEPQGHAVP TQVVSEPDPG AGRLIAGRYR LLSKLGHGGM GTVWRAKDET
VDREVAVKEP RVPDHLPERE RATAFERMRR EARAAARLDH PAVVNVHDVA VEDGQPWIVM
EFVQGRSLGA ALQEGTLGAR DAARIGLEVL GALEAAHKAG ILHRDVKPDN VMLGQYDRVV
LTDFGIAQIE GETNLTDTGG FVGSPEFIAP ERVLGQRPGP ASDLWSLGVV LYAATEGVSP
FRRSNTPATL QSVLNATPAA PASATGPLAE AINGLLHKDP SHRPDAATVR RLLEQAAKPP
APQVPTQVMT SGGAPSGAGD GIRVGKKALI GVGAAFVALA LALGLVIADP FAAGPTDGFV
TRDVKNLDAS ISVPGHYLDS KPEEDNIGTP EHWIQYTDPS GSVWVWLQLF KASDDKTGEI
ASSADAEMYD DEKTYKASGS TDLGMPANPE SKTEASLDYE GKKAAKNTLT YNSADEGEQE
RPRELKIFYY RTTDGDMYKL AIGYPGGESD FAERGRQVAD EVIKSLKVKN L
//
