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Database: UniProt
Entry: A0A1C6RGA0_9ACTN
LinkDB: A0A1C6RGA0_9ACTN
Original site: A0A1C6RGA0_9ACTN 
ID   A0A1C6RGA0_9ACTN        Unreviewed;       663 AA.
AC   A0A1C6RGA0;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
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=GA0070616_0949 {ECO:0000313|EMBL:SCL16175.1};
OS   Micromonospora nigra.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=145857 {ECO:0000313|EMBL:SCL16175.1, ECO:0000313|Proteomes:UP000199699};
RN   [1] {ECO:0000313|EMBL:SCL16175.1, ECO:0000313|Proteomes:UP000199699}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 43818 {ECO:0000313|EMBL:SCL16175.1,
RC   ECO:0000313|Proteomes:UP000199699};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-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; FMHT01000003; SCL16175.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C6RGA0; -.
DR   STRING; 145857.GA0070616_0949; -.
DR   OrthoDB; 308915at2; -.
DR   Proteomes; UP000199699; 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; 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:SCL16175.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199699};
KW   Serine/threonine-protein kinase {ECO:0000313|EMBL:SCL16175.1};
KW   Transferase {ECO:0000313|EMBL:SCL16175.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        378..398
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          18..306
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          404..467
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   DOMAIN          468..535
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   DOMAIN          536..602
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   DOMAIN          603..663
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   REGION          333..355
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   663 AA;  70213 MW;  47FA4831CFC48B1F CRC64;
     MDTQVADTLP GSLIDGRYRI RGRVARGGMA TVYTATDERL ERTVAVKIIH SSQATGARAR
     PADFLDRFTD EAKAIARLTH PNVVAVYDQG THAGLPYLVM EYVRGRTLRE VLSERRRLNP
     DESLAIAEQM LAAIAAAHRA GLVHRDIKPE NVLVAEAPTG GPANLVDSVV KVADFGLARA
     VEASTDEQDG SQLMATVAYV APELVTDGHA DARTDVYSAG IVLFEMLTGR VPYDGDRPVD
     VAWQHVDRDV PTPSTLVPGL PRVLDDLVAR ATRRDPGARP TDAGALLAEV QVARDDLGNP
     NTHTAVLSRI TDESAVSQPT MVVAAVAPSQ RPAWARLPEG GGGSGRGRRR AAPTRGGDLW
     SRLAALRTQV MGSPRGRLAV AAAVVALGLV AALGGWWFGV GRYTVAPQLV SMSQADAEAQ
     AARAGFTVAY DEPRHDEQIP RDGVVAQNPA PAARILKGDT IRLTLSLGPE RFPVPDVVGK
     EFELAEADLT SLRLEVVKGN ARYDDNLPEG VVVATDPAVG AEVKPGDKVT VVLSRGRAPI
     TVPNLVGKNL NEARATIAQL GLVLVEPTYK DSDKPRDEVL GQSPADGAGV VKGTQVRLEV
     SKGPPLVAVP KVVGLPCPQA KQVLEAQGHP VTVQFNPNGV ARFQNPAENT QVNPGSAVTI
     GCF
//
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