ID   A1SLA3_NOCSJ            Unreviewed;       658 AA.
AC   A1SLA3;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 84.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   OrderedLocusNames=Noca_3086 {ECO:0000313|EMBL:ABL82588.1};
OS   Nocardioides sp. (strain ATCC BAA-499 / JS614).
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Nocardioides.
OX   NCBI_TaxID=196162 {ECO:0000313|EMBL:ABL82588.1, ECO:0000313|Proteomes:UP000000640};
RN   [1] {ECO:0000313|Proteomes:UP000000640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-499 / JS614 {ECO:0000313|Proteomes:UP000000640};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Mattes T., Gossett J.,
RA   Richardson P.;
RT   "Complete sequence of chromosome 1 of Nocardioides sp. JS614.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ABL82588.1, ECO:0000313|Proteomes:UP000000640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-499 / JS614 {ECO:0000313|Proteomes:UP000000640};
RX   PubMed=21551312; DOI=10.1128/JB.05109-11;
RA   Coleman N.V., Wilson N.L., Barry K., Brettin T.S., Bruce D.C., Copeland A.,
RA   Dalin E., Detter J.C., Del Rio T.G., Goodwin L.A., Hammon N.M., Han S.,
RA   Hauser L.J., Israni S., Kim E., Kyrpides N., Land M.L., Lapidus A.,
RA   Larimer F.W., Lucas S., Pitluck S., Richardson P., Schmutz J., Tapia R.,
RA   Thompson S., Tice H.N., Spain J.C., Gossett J.G., Mattes T.E.;
RT   "Genome Sequence of the ethene- and vinyl chloride-oxidizing actinomycete
RT   Nocardioides sp. strain JS614.";
RL   J. Bacteriol. 193:3399-3400(2011).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000509; ABL82588.1; -; Genomic_DNA.
DR   AlphaFoldDB; A1SLA3; -.
DR   STRING; 196162.Noca_3086; -.
DR   KEGG; nca:Noca_3086; -.
DR   eggNOG; COG0515; Bacteria.
DR   eggNOG; COG2815; Bacteria.
DR   HOGENOM; CLU_000288_135_2_11; -.
DR   Proteomes; UP000000640; Chromosome.
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-EC.
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:ABL82588.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000640};
KW   Transferase {ECO:0000313|EMBL:ABL82588.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        368..389
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          31..290
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          390..457
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   DOMAIN          458..525
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   DOMAIN          526..593
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   DOMAIN          594..658
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          338..363
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   658 AA;  69209 MW;  D73B8CB443294C5E CRC64;
     MPPDRQSDRH AHAGADAAGD PMTGRLLEGR YRIGARIARG GMASVYEATD IRLDRTVAVK
     VMHPGLGDDD EFAARFVREA RSAARLSHPN VVAVYDQGDD HGTVFLAMEL VEGVTLRDVI
     RKESPMPPAR ALALIEPVLS ALAAAHRAGI IHRDVKPENV LIAADGRVKV ADFGLARAVS
     ADTQHTATGG VLIGTVSYLA PELVVDGRAD ARADVYAAGV VLFELLTGGK PHEGETPIQV
     AYKHVHEDVP APSTLEPGIP AYVDALVARA TARDRGLRPA DAGVLLHQLH RVSHALAEGV
     HDDPDLTADL TPLLLQTQPV ELAIPDEAVV DRTTPIQLLE RPSASPPSAG PERRTPPPRR
     PRRSRRGLVL LLAALLLVAG AGAGAWWFLD GRYTSTPGVL GLTKAAAEQR LDEAGLDVAW
     GDKAYSETVP AGRVVATDPE PGSKVLDGGT VTVVLSLGKE RYDVPKLKGL TVDQAQDALA
     ETHLAFGTST EKWSDTVEKG VVISSSPKAG TTLRPDAAVD LVVSKGPKPV TLKDWVGKDA
     DEAMAWAEGK GLDAAVASEE YNDDVAAGDV ISMDPPAGTT LHRGDSVSFV VSKGPHLVEV
     PSVRAQGVDA ATATLEALGF RVVTEKASGY LGLGYVFSQD PGGGEMVPFG STITLTLI
//