ID A0A1S2JWP6_9ACTN Unreviewed; 773 AA.
AC A0A1S2JWP6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:OII60374.1};
GN ORFNames=BJP40_10600 {ECO:0000313|EMBL:OII60374.1};
OS Streptomyces sp. CC53.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1906740 {ECO:0000313|EMBL:OII60374.1, ECO:0000313|Proteomes:UP000179639};
RN [1] {ECO:0000313|EMBL:OII60374.1, ECO:0000313|Proteomes:UP000179639}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC53 {ECO:0000313|EMBL:OII60374.1,
RC ECO:0000313|Proteomes:UP000179639};
RA Cruz-Morales P., Ramos-Aboites H.E., Barona-Gomez F.;
RT "Functional and evolutionary genomics of ferrioxamines biosynthesis and
RT transport.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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:OII60374.1}.
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DR EMBL; MKXB01000206; OII60374.1; -; Genomic_DNA.
DR RefSeq; WP_071283161.1; NZ_MKXB01000206.1.
DR AlphaFoldDB; A0A1S2JWP6; -.
DR STRING; 1906740.BJP40_10600; -.
DR Proteomes; UP000179639; 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-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR46082:SF6; AAA+ ATPASE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR46082; ATP/GTP-BINDING PROTEIN-RELATED; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF13374; TPR_10; 1.
DR Pfam; PF13424; TPR_12; 4.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF48452; TPR-like; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Kinase {ECO:0000313|EMBL:OII60374.1};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Reference proteome {ECO:0000313|Proteomes:UP000179639};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:OII60374.1};
KW Transferase {ECO:0000313|EMBL:OII60374.1}.
FT DOMAIN 11..278
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 303..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 378..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..329
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..397
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 40
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 773 AA; 83225 MW; 1E56ED4AD4C22B8F CRC64;
MADTRLIHGR YRLLEVIGRG GMGEVWRATD EALGRRVAVK CLKPLGPQHD PGFVRVLRER
FRREARVAAA LQHRGVTVVH DFGECDGSLF LVMELLEGRN LSQLLEDNRH HPLPLPDVVD
IAEQVADALA YTHRRGIVHR DLKPANIVRL ADGGVKICDF GIARPGADTG AASRLTSGGI
AMGTPHYMSP EQISGGQVDH RSDLYSLGCV LYEIATGAPP FDQDDAWAVL VGHRDTPPVP
LRVHRAELPP VFERIVLDLL AKAPDARPAD AGDLHRRITG ARGVAIPALH GAPGAVAPHL
LAPSAGPLGA TPHPSPSPSP LPSLPSAPTP AAPGDHTAWT RSLTPGPGAV GAPRPVPPED
PAAALTGEWT SATAAPPRSA AFPFAAPPEP RRPSPPPELL AVLAGRHSAG LGLGRLGRWE
EAGEVHRSVA AQRAHLLGPD HPDTLASRYE AASTLSRTGR TADALREFTE VAEGRARTLG
PDHPDTLKAR QEVAYVLGRL GRHFEAHQAY ADVLAARERT AGPDHPDTLR CRHNLAFTLG
RLGRLEESYR MAYGVVAART RTLGPDHPDT LVTLYEVAHT LGRLGRWTDA LRTYREVAAA
RGRALGAEHP DTLAAHYEVG ISLGRLGRGQ EALDLFHDLV AARTRTGGPA HPETLRARHG
YGVNLGRLGR WEEALAEARD VAAARDGALG PDHPDALVSH REAAVCLGWL GRWQEALDAY
RRVARARERL LGPDHPDTLA GRHDEARCLE RLGRHDEAAA IYRRAAAPSR RHP
//