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Database: UniProt
Entry: A0A086N1D7_9ACTN
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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
//
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