ID A0A086N1D7_9ACTN Unreviewed; 746 AA.
AC A0A086N1D7;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:KFG74955.1};
GN ORFNames=FM21_02000 {ECO:0000313|EMBL:KFG74955.1};
OS Streptomyces mutabilis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=67332 {ECO:0000313|EMBL:KFG74955.1, ECO:0000313|Proteomes:UP000029095};
RN [1] {ECO:0000313|EMBL:KFG74955.1, ECO:0000313|Proteomes:UP000029095}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TRM45540 {ECO:0000313|EMBL:KFG74955.1,
RC ECO:0000313|Proteomes:UP000029095};
RA Luo X., Zhang L.;
RT "Complete genome sequence of the Streptomyces mutabilis TRM45540.";
RL Submitted (MAY-2014) 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:KFG74955.1}.
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DR EMBL; JNFQ01000001; KFG74955.1; -; Genomic_DNA.
DR RefSeq; WP_043371964.1; NZ_KN039946.1.
DR AlphaFoldDB; A0A086N1D7; -.
DR STRING; 1915400.FM21_02000; -.
DR HOGENOM; CLU_000288_135_1_11; -.
DR Proteomes; UP000029095; 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-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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; IPR018391; PQQ_beta_propeller_repeat.
DR InterPro; IPR002372; PQQ_repeat.
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 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; PF13360; PQQ_2; 2.
DR SMART; SM00564; PQQ; 6.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 2.
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:KFG74955.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:KFG74955.1};
KW Transferase {ECO:0000313|EMBL:KFG74955.1}.
FT DOMAIN 22..284
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 289..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..313
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 50
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 746 AA; 77916 MW; 8E16DB8343B42DCC CRC64;
MAPQPNTGAD AEAELPDYAG HYRLESCLGS GGMGVVHLAR STSGMRVAVK VVHTSYAKDP
EFRGRFRQEV AAARRVSGAF TAPVVDADPD AGRPWMATLY IPGPTLSEQV KRNGPMDPAQ
LRRLMAGLAE ALRDIHRVGV VHRDLKPSNV LLAEDGPKVI DFGISRPKDS EVRTETGKLI
GTPPFMAPEQ FRRPREVGPA ADVFALGSLM VHAATGRGPF DSDSPYVVAY QVVHDEPDLT
GVPEALAPLV LRCLAKEPGD RPTPDELMRE LRSAAAAYDT QVFIPAQRAR EEAGEPSEPR
GVPEAREARG AREALGARGA SGACEAPETR QAPEAPEAPA ESASGSRAHV PARWPVRRLG
RRTGLVAGVV GLAVLGGLTS VQVFGGAEPA RRAPAGQSEP SGFGVWEAAP ASDGGGMPQC
SYAARVLLCA RPGLVYALDP ADGGTLWRHG VADAARSEPP VVSGGLVQPS LDRIGELEAL
DPATGRQVWR EDVPEYDGVR AAGDTLLLTR SDGTVTGVDG ATGDVEWSHR IPGQAVPYFS
SFTGDASAYA VSPSGDGNRT RVTAVDPATG DVRWDVEPAG SLTPVGAADG SVYFVAAGAV
YGDAKAVVRY TPGTGEVRRV KLPVPVAQAE AGVHGDTVYL MGAGGSLVAV DMAAGRQRWR
LETGVSRGSA PASDGRHVYV TAPDGRLLGV DAREGRLLGQ TRPRLGAESD RVPAALPRPV
LAGGHVYAGA PDGTVFGVAG RDPADW
//