ID A0A372JN64_9ACTN Unreviewed; 629 AA.
AC A0A372JN64;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=DZF91_11840 {ECO:0000313|EMBL:RFU41455.1};
OS Actinomadura logoneensis.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Thermomonosporaceae; Actinomadura.
OX NCBI_TaxID=2293572 {ECO:0000313|EMBL:RFU41455.1, ECO:0000313|Proteomes:UP000261811};
RN [1] {ECO:0000313|EMBL:RFU41455.1, ECO:0000313|Proteomes:UP000261811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEAU-G17 {ECO:0000313|EMBL:RFU41455.1,
RC ECO:0000313|Proteomes:UP000261811};
RA Shi L.;
RT "Actinomadura jelena sp. nov., a novel Actinomycete isolated from soil in
RT Chad.";
RL Submitted (AUG-2018) 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};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RFU41455.1}.
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DR EMBL; QURH01000211; RFU41455.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A372JN64; -.
DR OrthoDB; 951193at2; -.
DR Proteomes; UP000261811; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
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; PF00069; Pkinase; 1.
DR Pfam; PF00400; WD40; 2.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00320; WD40; 3.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 3.
DR PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000261811};
KW WD repeat {ECO:0000256|PROSITE-ProRule:PRU00221}.
FT DOMAIN 15..274
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REPEAT 427..459
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 551..592
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 593..629
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REGION 262..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..279
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 43
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 629 AA; 64275 MW; DCEBE89AFC63E31F CRC64;
MPPLGPGDPR EVGPYRLEER LGAGGMGEVF LGVSPGGRRV AVKLIRAEFA ADARFRARFA
REIEAARKVG GFHTAQVVDA DAEAASPWMA TAFVPGPSLR QVVLRQGPLP PHEVRRLGAG
LAEGLAAIHG SGLVHRDLKP GNVVMAPDGP RIIDFGIARA ADATSLTSAG AVVGTFSFMS
PEQVCAEETG PPGDVFSLGC LLTYAATGHG PFDAPTIPAI VHRITDGPPT LDGLTGDLRE
IVAACLRKDP AARPTVPDLI ERLTAPEPPR PPALPTAPDS EPVPGGVSRR GVLIGGAAAA
VAAAVGVPAA VLLWPDGGTG SALPETPLAV PVPTVLPNTA VDMLQLAYGA NGGRLTGAAF
DQIWHWDLAT GKGSSTTFQF DDWTRPQTLS ADGRIAAGAT RNGPFTIRDA LTGKAIGGLP
SGTRPRTVAL GPDGRLLAYL GDDGALHIWD VAAKRIVKSE PAPAGGADTG SRLLFSRDGR
DVLRLDQGRT TRTRVTGKPV AGAPAAVPSP AAEIGVPVAA VSPDGSTLAL AAGSDSTISL
GPPDGSPVRT LEGHTGRVTA VAFSPDGRVL ASGGEDGTVR LWHVPTGRPV AAVHGDPRKV
ECVAFAPDGR SFASGGASGV TKLWTFPAH
//
