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Database: UniProt
Entry: A0A0B5HZH1_9ACTN
LinkDB: A0A0B5HZH1_9ACTN
Original site: A0A0B5HZH1_9ACTN 
ID   A0A0B5HZH1_9ACTN        Unreviewed;       715 AA.
AC   A0A0B5HZH1;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:AJF65786.1};
GN   ORFNames=SVTN_16675 {ECO:0000313|EMBL:AJF65786.1};
OS   Streptomyces vietnamensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=362257 {ECO:0000313|EMBL:AJF65786.1, ECO:0000313|Proteomes:UP000031774};
RN   [1] {ECO:0000313|EMBL:AJF65786.1, ECO:0000313|Proteomes:UP000031774}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GIMV4.0001 {ECO:0000313|Proteomes:UP000031774};
RA   Deng M.R., Guo J., Ma L.Y., Feng G.D., Mo C.Y., Zhu H.H.;
RT   "Complete genome sequence of Streptomyces vietnamensis strain GIMV4.0001, a
RT   genetic manipulable producer of the benzoisochromanequinone antibiotic
RT   granaticin.";
RL   Submitted (DEC-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   -!- SIMILARITY: Belongs to the protein kinase superfamily. NEK Ser/Thr
CC       protein kinase family. NIMA subfamily. {ECO:0000256|ARBA:ARBA00010886}.
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DR   EMBL; CP010407; AJF65786.1; -; Genomic_DNA.
DR   RefSeq; WP_041129809.1; NZ_CP010407.1.
DR   AlphaFoldDB; A0A0B5HZH1; -.
DR   STRING; 362257.SVTN_16675; -.
DR   KEGG; svt:SVTN_16675; -.
DR   HOGENOM; CLU_000288_135_1_11; -.
DR   Proteomes; UP000031774; Chromosome.
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; 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; 3.
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}; Kinase {ECO:0000313|EMBL:AJF65786.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000031774};
KW   Serine/threonine-protein kinase {ECO:0000313|EMBL:AJF65786.1};
KW   Transferase {ECO:0000313|EMBL:AJF65786.1}.
FT   DOMAIN          22..282
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          288..320
FT                   /note="Disordered"
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   715 AA;  75267 MW;  9F8FCFF6DADC467A CRC64;
     MPPLRSTGAD RDAEGPEYAG EYRLQACLGA GGMGVVHLAT SPSGLRLAVK VVHGQYAEDP
     EFRARFRQEV AAARRVSGAF TAPVVDADPD AVRPWMATLY VPGPTLADQV KRNGPLSPAE
     LRRLTAGLAE ALRDIHRAGV VHRDLKPSNV LLTDTGPKVI DFGISRPVDS DLHTETGKLI
     GSPPFMAPEQ FQRPREVGPA ADVFALGSVL VHAATGHGPF DSDSPYIVAY QVVHDEPDLT
     GVPADLTPLV ARCLAKEPAE RPTPGEIMTA LLPPSYEAAA FIPSQRRAPV LPTPAPRSPG
     SWDADTPVRV TTEQPRRRRP PRWPVTATAL LVLAGVGAFA AVQFSGDGAH TRDPHKAPVA
     KAFAGWQTPL QKDGDTVAPA CGYIADALFC SGRGIAIARV DPGAGRVLWS QPAADSENFS
     APAPMSGGLI GVSSADRGLR TYETDGNPGW YMKGAEHDSN VRFADETVLF AGGSGRLKAV
     AAATGEQRWS HSLQGHSEPR FGPYDPVSDL LPVFEASSGA SGRAHTLISA LRPLSGEIAW
     QKRLDGDLVP VGTGADGVLV LRSANRDSRT DAVVLYDPAK RSARRIPVPS LMDEPKVAVR
     GTTVYLLTPT GQLIALDTAS PGGRVLWTLE TAAGTVSVPV VGPGDRLYFS ASDGRLLAVD
     TARGALLGQT GPRLRDGRLG YATTIPAPVV AGDRVFGTAP DGSVFAVDAR DPAAW
//
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