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Database: UniProt
Entry: A0A1E7JRU7_9ACTN
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ID   A0A1E7JRU7_9ACTN        Unreviewed;       711 AA.
AC   A0A1E7JRU7;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN   ORFNames=AN215_03650 {ECO:0000313|EMBL:OEU91635.1};
OS   Streptomyces abyssalis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=933944 {ECO:0000313|EMBL:OEU91635.1, ECO:0000313|Proteomes:UP000176087};
RN   [1] {ECO:0000313|EMBL:OEU91635.1, ECO:0000313|Proteomes:UP000176087}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCSIO 10390 {ECO:0000313|EMBL:OEU91635.1,
RC   ECO:0000313|Proteomes:UP000176087};
RX   PubMed=27446038; DOI=10.3389/fmicb.2016.00998;
RA   Tian X., Zhang Z., Yang T., Chen M., Li J., Chen F., Yang J., Li W.,
RA   Zhang B., Zhang Z., Wu J., Zhang C., Long L., Xiao J.;
RT   "Comparative Genomics Analysis of Streptomyces Species Reveals Their
RT   Adaptation to the Marine Environment and Their Diversity at the Genomic
RT   Level.";
RL   Front. Microbiol. 7:998-998(2016).
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   -!- SIMILARITY: Belongs to the protein kinase superfamily. NEK Ser/Thr
CC       protein kinase family. NIMA subfamily. {ECO:0000256|ARBA:ARBA00010886}.
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:OEU91635.1}.
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DR   EMBL; LJGT01000037; OEU91635.1; -; Genomic_DNA.
DR   RefSeq; WP_070010244.1; NZ_LJGT01000037.1.
DR   AlphaFoldDB; A0A1E7JRU7; -.
DR   STRING; 933944.AN215_03650; -.
DR   PATRIC; fig|933944.5.peg.1943; -.
DR   Proteomes; UP000176087; 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; 2.40.10.480; -; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
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; PTHR43671:SF13; LD04361P; 1.
DR   PANTHER; PTHR43671; SERINE/THREONINE-PROTEIN KINASE NEK; 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; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   3: Inferred from homology;
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:UP000176087}.
FT   DOMAIN          27..275
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          264..287
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          306..338
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         55
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   711 AA;  74363 MW;  A533C2486A6900AA CRC64;
     MARPTPQQEG FALKPLGYGD PLRLGPYRII GTLGEGGMGK VYLGRDGSGE VAAVKVLRPE
     LAHETHMSQR FVREAQAAQA VRSKGVARVL TAQTDGGAPF IATEFLAGPT LDRAVERHGP
     FPEPEVRALG AALARTLGDI HAAGLVHRDL KPSNIVLTSG GPRIIDFGIA RPEHGLTLTT
     TGQAPVTPGY GAPEQVLGQR TGPPGDVFAL GAVLVFAASG ERAYQGDQIA VVQYEVVHGE
     PRLEGVPEAL VPLIAPCLTR DAAQRPQPAQ ITSALAPPRD GRQLWKKGGL GDDIAEAESA
     AKQLATFPPA PGSQNGTAAT GPAAGSAAPP PADSPTRRRV LTGLAAGGTL LVAGGGTAWW
     LTREEPPRRA HPWFALPLQD GEYEEGRAPE PLWGPRDVAF AQSPAPLVSR DLVVVGGKRD
     ARVTAFSVRD GKRKWVSEAA FYQPLFAASP RLIVTGGSDG QLFGVDARTG AVERRHPTGM
     SVLLAVDARA AYCLVEDEVR CVELVSGKVR WRKPAPLDEF SGGRGISATA AGGLLVLATA
     KDAAIALDVR TGGKVWSRPG GSTGAGVPPV TAGGEVYLGG QSLSAVRLRD GEEQWSVPAE
     VNEGWSGPAV QGDAVYASAG SEVRCRGRRD GREVWRREVD GGVFAGGRPV AEGNTVWVTL
     KETAGVAALD TRTGRAAWVR RHKDGGSVRM TGAGNRVFLL TEGKLTAMPV I
//
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