ID A0A286H660_9ACTN Unreviewed; 661 AA.
AC A0A286H660;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN ORFNames=SAMN06272739_3779 {ECO:0000313|EMBL:SOE02819.1};
OS Blastococcus haudaquaticus.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Blastococcus.
OX NCBI_TaxID=1938745 {ECO:0000313|EMBL:SOE02819.1, ECO:0000313|Proteomes:UP000219482};
RN [1] {ECO:0000313|Proteomes:UP000219482}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44270 {ECO:0000313|Proteomes:UP000219482};
RA Varghese N., Submissions S.;
RL Submitted (SEP-2017) 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};
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DR EMBL; OCNK01000005; SOE02819.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A286H660; -.
DR Proteomes; UP000219482; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd06577; PASTA_pknB; 4.
DR CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 3.30.10.20; -; 4.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR005543; PASTA_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR NCBIfam; NF033483; PknB_PASTA_kin; 1.
DR PANTHER; PTHR43289; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 20-RELATED; 1.
DR PANTHER; PTHR43289:SF32; SERINE_THREONINE-PROTEIN KINASE PKAB; 1.
DR Pfam; PF03793; PASTA; 4.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00740; PASTA; 4.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF54184; Penicillin-binding protein 2x (pbp-2x), c-terminal domain; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51178; PASTA; 4.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:SOE02819.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000219482};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:SOE02819.1};
KW Transferase {ECO:0000313|EMBL:SOE02819.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 374..394
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 14..279
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 394..461
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 462..530
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 531..599
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 600..661
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 282..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..306
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 661 AA; 69966 MW; 74642F371826353D CRC64;
MTDPVVGLVL EGRYRLEERL ARGGMSTVYA ATDLRLHKTV AVKVMAEHLA HDPTFVDRFT
REARAAAMLS HTNVVGVSDQ GSDQGLVFLV MELVRGRTLR DLLTARGRLT VAEAFAVLEP
MLAGLTAAHR AGIVHRDIKP ENVLIGVDGV VKVADFGLAR AVVGTGTAQA SQTGGVLIGT
VAYLSPEQLE RGRADARSDI YAAGIVLYEM LTGHPPYGGD TPLAVAYQHV HHDVPAPSAE
VTGLPWAVDE LVARTTRRDP SGRPLDAGAF LAELGHVRKD LGIEPVPVPT GRSTAGPQTL
RPTNRPTRPR HPSDPGTAVL GSQRTDRTDR TGRTSMLPAV GAGPTMNVNG RRPAGLERPR
PGVPQHIRRR RARFAVALVL LLVITIGAIG WWLGSGRWTE IPELVGKDQA AAIDLLQQSG
LDPDCCEEVW SEEFPAGAVM SIDPEPGEAI RGTDVRLTVS KGPERFVVPT EMVSRPYDEV
VAQLQETVPI QLTKADEYDD TLAPGQVIRF EPPAGTKLPR DSVVTVVVSA GRAPVAVPDV
TGQSPEQAQA NLESLGFTVA RGPDARSTAV DKGEVMAVSP GPADGPVAHG SEITIVVSAG
VPLVAVPNVV GMKEDEAAAA LRAAGLTVDA TKFFGNKVRQ QTPAAGESVE QGTSVKILVA
F
//
