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Database: UniProt
Entry: A0A1I0H3G9_9ACTN
LinkDB: A0A1I0H3G9_9ACTN
Original site: A0A1I0H3G9_9ACTN 
ID   A0A1I0H3G9_9ACTN        Unreviewed;       597 AA.
AC   A0A1I0H3G9;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
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=SAMN05421811_10499 {ECO:0000313|EMBL:SET78107.1};
OS   Nonomuraea wenchangensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Streptosporangiaceae; Nonomuraea.
OX   NCBI_TaxID=568860 {ECO:0000313|EMBL:SET78107.1, ECO:0000313|Proteomes:UP000199361};
RN   [1] {ECO:0000313|EMBL:SET78107.1, ECO:0000313|Proteomes:UP000199361}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.5598 {ECO:0000313|EMBL:SET78107.1,
RC   ECO:0000313|Proteomes:UP000199361};
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};
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DR   EMBL; FOHX01000004; SET78107.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I0H3G9; -.
DR   STRING; 568860.SAMN05421811_10499; -.
DR   OrthoDB; 9762169at2; -.
DR   Proteomes; UP000199361; 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; 3.
DR   CDD; cd14014; STKc_PknB_like; 1.
DR   Gene3D; 3.30.10.20; -; 3.
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; 3.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00740; PASTA; 3.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51178; PASTA; 3.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:SET78107.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199361};
KW   Serine/threonine-protein kinase {ECO:0000313|EMBL:SET78107.1};
KW   Transferase {ECO:0000313|EMBL:SET78107.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        327..348
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1..256
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          356..422
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   DOMAIN          423..487
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   DOMAIN          488..553
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   REGION          293..321
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          520..597
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        522..583
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   597 AA;  64164 MW;  9198BFF92F487930 CRC64;
     MAEVYRARDI RLDRIVAIKT LRSDLARDHT FQARFRREAQ SAASLNHPAV VAVYDTGEDV
     TDGAPVPYIV MEYVDGRTLR DLLRQDRRLL PERAVELVDG ILRALDYSHR GGIVHRDIKP
     ANVMITRAGD VKVMDFGIAR AMADSAATMT QTAQVIGTAQ YLSPEQARGE RVDARSDIYS
     TGCLLYELLT GQPPFTGDSP VAIAYQHVRE EPIPPSQIDP EIPAWADAIV LKSMAKDPAQ
     RYQSAGEMRA DIQRAMSGMP TDAQTMAMNA GGYGQGTRMM TATHAAAGPA TQRTNAVPPY
     EYGDGEGGGR GGRRRASGGG GNGVKTALWI IIPLLIIGAF VTVGYIVFGG GNSATSDTQV
     TIPSLVSQER AYAEEQLKTL ELKVEVVQEN SSEIDKGSVI RTDPPEDTKV EKGSAVKLYV
     SKGPAKKKVP DGLIGLSQED AMAALEKEGL RGTVKTKVSS KKQGTVIDTR PKAGEEIEEN
     GTVTLYVPKE LGEVPSVIGL TQEDASAQIK SAGFRVKVVP QPSDQPQGTV IQQNPGEGAK
     LAPNTTITIV VSTGPQQPTQ QPNEDFPQQP SDEPTSDNPI DDPPTNDNPI DDEPDGF
//
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