ID A0A0B5HZC2_9ACTN Unreviewed; 810 AA.
AC A0A0B5HZC2;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
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=SVTN_16220 {ECO:0000313|EMBL:AJF65711.1};
OS Streptomyces vietnamensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=362257 {ECO:0000313|EMBL:AJF65711.1, ECO:0000313|Proteomes:UP000031774};
RN [1] {ECO:0000313|EMBL:AJF65711.1, 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP010407; AJF65711.1; -; Genomic_DNA.
DR RefSeq; WP_041129737.1; NZ_CP010407.1.
DR AlphaFoldDB; A0A0B5HZC2; -.
DR STRING; 362257.SVTN_16220; -.
DR KEGG; svt:SVTN_16220; -.
DR HOGENOM; CLU_000288_135_1_11; -.
DR Proteomes; UP000031774; Chromosome.
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; 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; PF13360; PQQ_2; 1.
DR Pfam; PF13570; PQQ_3; 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; 1.
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:AJF65711.1};
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:0000256|ARBA:ARBA00022527,
KW ECO:0000313|EMBL:AJF65711.1}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 15..270
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 295..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 383..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..324
FT /note="Pro residues"
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 810 AA; 84801 MW; 571CC2C9B53B11A8 CRC64;
MEQLTQHDPR RIGPFEVLGR LGAGGMGLVY LARSASGRRV AIKTVRTELA EDQLFRVRFT
REVEAARAVS GFYTAAVVDA DPRAAVPWLA TAYVPAPSLE EIVNECGPLP AQAVRWLAAG
VAEALQSIHG AGLVHRDLKP SNVLVVEDGP RVIDFGIASG VSNTRLTMTN VAVGTPAYMS
PEQARDSRSV TGASDVFSLG SMLVFAATGH APFHGANPVE TVFMLLREGP DLEGLPDELR
PLIDSCMQMD VTRRPTPADL QAQLAPHLFG PGSDDSGTAS AWLPQSATAM IERRRGGGRQ
LPGPTAPPPP ADPPGPPGPR QDPRFPEQAP ERPDRAPVGG RHAGPSESAG GPVRLGGATV
PIGPGPRVAD TRAAVAVGRS ADAGPATGWI RPPGSGPHGA EPAPQQGARP VSVPPQGADQ
AAPQPPPEPG HWRPWRFRMS NDVWGTPVVD GDLLYVTSFE VHALDTGSGR RQFKTRDVAW
SMAVASGRIH ASDGPTLYAL DAGDGSERWR LHTDAYVYSL KVDRGTVVTG TRGGGVQGWE
ASNGAKLWEL TGAQTDFETA EAGPAVHGDT VYVWRDARLQ ALDARTGVER WSYPIGDAAS
CAGVPVRVAP AEDGCVYVSA GTRVLSIDIA AGHVRWHFEA PAVFLSPPTF APGPAVTGGG
VYLSDHLGTV YALDATTGQD RWRIATEPRQ STEPVLVADG NVHVGSGSAL YTLDAVTGTP
RWRFAAGGEL VGSPVVADGR VHFGSADHVL YTLDATGGQL RWKLATGGEI TGSPVAKGGV
VYACSKDRCV YALDAVKGTA TGRGAAAPRA
//
