ID A0A0G3ADQ3_9ACTN Unreviewed; 671 AA.
AC A0A0G3ADQ3;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN ORFNames=ABB07_03570 {ECO:0000313|EMBL:AKJ09134.1};
OS Streptomyces incarnatus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=665007 {ECO:0000313|EMBL:AKJ09134.1, ECO:0000313|Proteomes:UP000035366};
RN [1] {ECO:0000313|EMBL:AKJ09134.1, ECO:0000313|Proteomes:UP000035366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL8089 {ECO:0000313|Proteomes:UP000035366};
RX PubMed=26159526;
RA Oshima K., Hattori M., Shimizu H., Fukuda K., Nemoto M., Inagaki K.,
RA Tamura T.;
RT "Draft Genome Sequence of Streptomyces incarnatus NRRL8089, which Produces
RT the Nucleoside Antibiotic Sinefungin.";
RL Genome Announc. 3:e00715-e00715(2015).
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};
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DR EMBL; CP011497; AKJ09134.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G3ADQ3; -.
DR STRING; 665007.ABB07_03570; -.
DR PATRIC; fig|665007.5.peg.789; -.
DR Proteomes; UP000035366; Chromosome.
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; 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; PTHR34512; CELL SURFACE PROTEIN; 1.
DR PANTHER; PTHR34512:SF30; OUTER MEMBRANE PROTEIN ASSEMBLY FACTOR BAMB; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF13360; PQQ_2; 2.
DR Pfam; PF13570; PQQ_3; 1.
DR SMART; SM00564; PQQ; 7.
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.
DR PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE 4: Predicted;
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}.
FT DOMAIN 15..273
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 296..318
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 671 AA; 70099 MW; D82CE12ED99471EC CRC64;
MEPLTPDDPR EVGRYRVLAR LGSGGMGRVY LARSPQNQQV ALKVIRPDLA EDPLFRRRFA
REVAASRSVS GPYTAGVVDA EPDGKPPWLA TTYIPGPSLQ DAVLAGGALP ESAVRELGLG
LVQALTAVHA AGVVHRDLKP GNVLLAADGP RVIDFGISRV VEASALTGTG TTMGSPGYMA
PEQIRGKGIG TAVDVFALGA VLVFASTGRG PFGEGTAHLL LYRIMHEEPY LGAVPERLRA
IAAGCLDKDA ARRPGLPEVG AALGRGRPAT ALFEPGWLPR PLAATPGTDP RHILVRAPGD
RGGTGDRLPT TGPGPHEVPA PANAASGRRR VLLAAAGLAA SAALGFTGWR LLDGDPPKAG
TRLWRFPLTG VLVNHPAVAG DLVYAASNDG TLYTVDAAKG ERRWSYTTKA ALGSAPYLVG
GVVYLGSDDG KLYALDARTG AQRWTFTTGG IVHSPVVTGG VAYVGSSDGY LYAVQVSDGR
RLWRFRTGHD THCPAVVEDT VYVGCSDTRL YAVNAYDGSK RWTFTTAGAI SWFPVVTGGL
VYFCSTDQTL YAVRAATGQE VWRAGGVAAK AGPAVARGLV YCGGGRELRA WDAGTGRQRW
SLSTGGDVGA PVVADGVVYA GSGDQRLYAV DAVDGQQRWT FTAGAEVHPP VATADAVYFG
GADSRLYAVR A
//
