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Database: UniProt
Entry: A0A0F0H322_9ACTN
LinkDB: A0A0F0H322_9ACTN
Original site: A0A0F0H322_9ACTN 
ID   A0A0F0H322_9ACTN        Unreviewed;       805 AA.
AC   A0A0F0H322;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 32.
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=UK14_13950 {ECO:0000313|EMBL:KJK50114.1};
OS   Streptomyces sp. NRRL F-4428.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1609137 {ECO:0000313|EMBL:KJK50114.1, ECO:0000313|Proteomes:UP000033569};
RN   [1] {ECO:0000313|EMBL:KJK50114.1, ECO:0000313|Proteomes:UP000033569}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL F-4428 {ECO:0000313|EMBL:KJK50114.1,
RC   ECO:0000313|Proteomes:UP000033569};
RA   Ju K.-S., Doroghazi J.R., Metcalf W.;
RL   Submitted (FEB-2015) 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:KJK50114.1}.
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DR   EMBL; JYJI01000102; KJK50114.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F0H322; -.
DR   PATRIC; fig|1609137.3.peg.2961; -.
DR   OrthoDB; 9762169at2; -.
DR   Proteomes; UP000033569; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
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:0016043; P:cellular component organization; IEA:UniProt.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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; 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; PTHR22983; PROTEIN KINASE RELATED; 1.
DR   PANTHER; PTHR22983:SF6; SERINE_THREONINE-PROTEIN KINASE 36; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF01011; PQQ; 1.
DR   Pfam; PF13360; PQQ_2; 2.
DR   SMART; SM00564; PQQ; 9.
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};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KJK50114.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000033569};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW   ECO:0000313|EMBL:KJK50114.1}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          15..270
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          296..375
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          396..433
FT                   /note="Disordered"
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   805 AA;  84019 MW;  DF7F8B97BBCF212A CRC64;
     MEQLTQHDPR RIGPFEVLGR LGAGGMGLVY LARSASGRRV AIKTVRTELA EDQLFRVRFT
     REVEAARAVS GFYTAAVVDA DPRAAVPWLA TAYVPAPSLE EIVNECGPMP AQAVRWLAAG
     IAEALQSIHG AGLVHRDLKP SNVLVVEDGP RVIDFGIASG VSNTRLTMTN VAVGTPAYMS
     PEQAKDSRSV KGASDVFSLG STLVFAATGH PPYHGANPVE TVFMLLREGP NLEGLPEELR
     PLIESCMQMD ASLRPTPADL QAQLAPHLFD GGDDSGTASA WLPGRAVALI EARRAGNRTP
     AAAVPAPGRD GGAGGGRARG PVSEQATHRR PRGAEGWVDP RTGQAVPQRP HHPPRSPVPS
     GEPVRLGGSP VPIGPGPFAT AAASAASAAH SAAADSATGW VRSPDGSVPA HATGPAAPPV
     PGSGPAPDSG RWRPWRFRMS NEVWGTPTVA GNLLYVTSFE VHALDVASGR RQFKTRDVAW
     SMAVADGRIH ASDGPSLYAL DGSDGSERWR LSTDAWVYAL RAERGTVVTA TRGGGVQAWE
     ASNGHKLWEL TGAQSDFETP EAAPVLHDGT VYVWQDARLR ALDARSGRES WSYPVGDAGS
     CGNVPVRVTP APDGNVYVAA GTRVLSVDRA SGRVRWHFEA PAVFLAPPAF APGAAVTGGG
     VYLADYLGTV YALDAATGQD RWRIATESRQ SSDPVLVVGG NVHLGAGSAL YTLDAVTGTP
     KWRFAAGGEI TGLPAVADGR VHFGSADHCL YTLDAAGGQL RWKLATGGEI AGAPVAEAGV
     VYACSKDRCV YALDAAKGTG TRTSG
//
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