ID H8G8N2_9PSEU Unreviewed; 659 AA.
AC H8G8N2;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 24-JAN-2024, entry version 41.
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=SacazDRAFT_01512 {ECO:0000313|EMBL:EHY88441.1};
OS Saccharomonospora azurea NA-128.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharomonospora.
OX NCBI_TaxID=882081 {ECO:0000313|EMBL:EHY88441.1};
RN [1] {ECO:0000313|EMBL:EHY88441.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NA-128 {ECO:0000313|EMBL:EHY88441.1};
RX PubMed=22768365; DOI=10.4056/sigs.2635833;
RA Klenk H.P., Held B., Lucas S., Lapidus A., Copeland A., Hammon N.,
RA Pitluck S., Goodwin L.A., Han C., Tapia R., Brambilla E.M., Potter G.,
RA Land M., Ivanova N., Rohde M., Goker M., Detter J.C., Kyrpides N.C.,
RA Woyke T.;
RT "Genome sequence of the soil bacterium Saccharomonospora azurea type strain
RT (NA-128(T)).";
RL Stand. Genomic Sci. 6:220-229(2012).
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; CM001466; EHY88441.1; -; Genomic_DNA.
DR RefSeq; WP_005440162.1; NZ_CM001466.1.
DR AlphaFoldDB; H8G8N2; -.
DR HOGENOM; CLU_000288_135_2_11; -.
DR OrthoDB; 9762169at2; -.
DR Proteomes; UP000004705; 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-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:SF6; SERINE/THREONINE-PROTEIN KINASE NEKL-3; 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:EHY88441.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:EHY88441.1};
KW Transferase {ECO:0000313|EMBL:EHY88441.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 372..393
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 17..290
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 395..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..598
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 599..659
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 292..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 425..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..338
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..439
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 659 AA; 69117 MW; 24C3011AFDB41538 CRC64;
MTRTETSLAG ALLDRRYRVG GLIARGGMSS VYRGVDTRLD RPVAVKVMDS RFAGDRSFVE
RFEREARSAA RLHHPHVVAV HDQGFDTSAG VDDPRAFLVM ELVDGGTLRD LLTERGRLDV
PLALTVAEQV LSALAAAHAA GLVHRDIKPE NVLIGAAGES GGVVKVADFG LVRAAASAGT
TSTSVILGTV GYLSPEQVST GASSARSDVY STGILLFEML TGQVPYHGDT ALSVAYRHVN
DDVPRPSTVV PELPSALDEL VERATRRDPE SRPADAEAFL AEIQRVRAEL GLPPAPIPRV
PAPRTATQPP AETDSELTVP ALPAVGTATS TTALPSDGGP RGTQALPRAA AQDHEQETDD
GPLASPRRRA PLAVLALVVL VLLGGVGAGV WWFSSGRYVD VPSVTGMSRE EAETALRQAE
LTPVVTEERH NTTPSGTVIR TEPDGGDRAL QGDEVTVVLS LGRPVVPDVR PGASVEEAER
AIEAVQLTPR VSEETDEYSS DVPEGAVVSL TPEPGSQANV GDAVTIVRSK GPPPTPVPDV
RGKSRDEAFQ ALRDAGFEPF EAGEEFAEGV AAGHVVRTDP AQGSTVDEGT RVGVVVSNAV
KVPSVVGRRT EKAVQILREA GFEVSGGDSR GPISFVIEQS PSGGSFVRPG TTVNLSVIP
//