ID A0A1H0GD83_9ACTN Unreviewed; 639 AA.
AC A0A1H0GD83;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=SAMN05428965_2572 {ECO:0000313|EMBL:SDO04885.1};
OS Geodermatophilus sp. DSM 45219.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Geodermatophilus.
OX NCBI_TaxID=1881103 {ECO:0000313|EMBL:SDO04885.1, ECO:0000313|Proteomes:UP000198730};
RN [1] {ECO:0000313|EMBL:SDO04885.1, ECO:0000313|Proteomes:UP000198730}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45219 {ECO:0000313|EMBL:SDO04885.1,
RC ECO:0000313|Proteomes:UP000198730};
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; FNIQ01000003; SDO04885.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H0GD83; -.
DR STRING; 1881103.SAMN05428965_2572; -.
DR OrthoDB; 9762169at2; -.
DR Proteomes; UP000198730; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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; IPR017441; Protein_kinase_ATP_BS.
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; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:SDO04885.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:SDO04885.1};
KW Transferase {ECO:0000313|EMBL:SDO04885.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 323..344
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 11..274
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 355..423
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 424..490
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 491..555
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 559..629
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 460..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 40
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 639 AA; 66108 MW; 0DEB14332A1FCDAA CRC64;
MTTPSVLGER YEIGGVLGRG GMAEVHRGRD LRLGREVAVK VLRSDLARDP SFQVRFRREA
QAAASLNHPA IVAVYDTGED RTSSGATPYI VMEYVEGETL RDVLRREGVL PPDRAMTLAA
DICAALDFSH RNGIVHRDVK PGNVMITPQG TVKVMDFGIA RAVSDSAATM TSTAAVIGTA
QYLSPEQARG ESVDARSDVY SLGCLLYELV TGAPPFTGDS PVSVAYQHVR EDPRLPSSVN
PAIPADLDAI VLKALSKNPA NRYQSAAEMR NDLLRSLAGQ RVEATPVMGD AEKTAIIGAP
PGGYGDADWD DEEADRKRRR NRIIAAVVAG LLLIGAVVGV ALLVNSGDEA PTEPAVAQVT
VPALTGEQQA AAEALITEAG LVVGEVTTQV TNDETQQGAV LESTPASGAQ VDEGTAVDLV
VGVGPDTIEV PAVIGLDADR AETTLENAGF TDVRTEEVDS LAPENQVTGV EPGEGESADP
ADTITLQVSS GSAEVPDVVG DEQSAATATL RDAGFTNVVP EEVESDQPEG TVIATDPAAG
QLASADDPVT LQVSSGPAEP ETVAVPRVAG QSANAALDAL EAAGFVDVRV VDATTGAEVD
PAQATAVSTN PPAGSQVTPD TRVTLAVQGP TPTEETTGE
//
