ID A0A345XY31_9ACTN Unreviewed; 615 AA.
AC A0A345XY31;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:AXK36547.1};
GN ORFNames=DVA86_32205 {ECO:0000313|EMBL:AXK36547.1};
OS Streptomyces armeniacus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=83291 {ECO:0000313|EMBL:AXK36547.1, ECO:0000313|Proteomes:UP000254425};
RN [1] {ECO:0000313|EMBL:AXK36547.1, ECO:0000313|Proteomes:UP000254425}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15676 {ECO:0000313|EMBL:AXK36547.1,
RC ECO:0000313|Proteomes:UP000254425};
RA Labana P., Gosse J.T., Boddy C.N.;
RT "Draft genome of the type strain Streptomyces armeniacus ATCC 15676.";
RL Submitted (JUL-2018) 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; CP031320; AXK36547.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A345XY31; -.
DR Proteomes; UP000254425; 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; 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:AXK36547.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000254425};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:AXK36547.1};
KW Transferase {ECO:0000313|EMBL:AXK36547.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 372..394
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 15..270
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 278..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 397..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..468
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 44
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 615 AA; 64525 MW; 91627597640A456E CRC64;
MGQDVEDGRL VGGRYRLEGV LGRGGMGTVW RGRDETLGRT VAVKELRFPS SIDDEEKQRL
IMRTLREAKA IARIRSGSAI TVYDVVDEDD RPWIVMELIE GRSLADTIRQ DGPLSPRRTA
EVGLAVLDVL RAAHREGILH RDVKPSNVLM EEGTGRVVLT DFGIAKVQGD PSITSTGMLV
GAPSYISPER ARGNPPGPPA DMWSLGGLLY AAVEGRPPYD KGSAISTLTA VMTEPLPPLE
RAGALSEVIF GLLEKDPEKR LDVAGARVLL EMAAAVSDGM DTTGGGATPA DVTRSAAGMP
PVPPPGGSGS EPRTPPVRTA SGLPPIPSLN PPGGRAGSAA SGTGAGSGAG NGPGSWPAAR
QGFGGLGSRR TLAIIAAVVV LLVILGVVVA NAVGSDGGGS AAGSDGGTGQ QEQQGDKTGQ
DDGDDEAAEP SSKPEPDNGG KDDGKGEDKG EDGGKDKGKQ DGALPDGYRR VADGRFHFSM
AMPQDFKRTG TAGAGSGAKY GWPGGGYPKL QVDYNDSPLA DAVLAWKGLE PAVRKSSPGY
KLLDLQKVKW RGYPTVADWS FLRNEGDQRV RVLNRGFKVD DKRGYAIMVT CKADEWTGEQ
CRTLRQTAFK TFKPQ
//
