ID M3E3B7_9ACTN Unreviewed; 547 AA.
AC M3E3B7;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:EMF28362.1};
GN ORFNames=H114_14266 {ECO:0000313|EMBL:EMF28362.1};
OS Streptomyces gancidicus BKS 13-15.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces; Streptomyces pseudogriseolus group.
OX NCBI_TaxID=1284664 {ECO:0000313|EMBL:EMF28362.1, ECO:0000313|Proteomes:UP000011732};
RN [1] {ECO:0000313|EMBL:EMF28362.1, ECO:0000313|Proteomes:UP000011732}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BKS 13-15 {ECO:0000313|EMBL:EMF28362.1,
RC ECO:0000313|Proteomes:UP000011732};
RX PubMed=23599292;
RA Kumar S., Kaur N., Singh N.K., Raghava G.P., Mayilraj S.;
RT "Draft Genome Sequence of Streptomyces gancidicus Strain BKS 13-15.";
RL Genome Announc. 1:E00150-13(2013).
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:EMF28362.1}.
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; AOHP01000058; EMF28362.1; -; Genomic_DNA.
DR RefSeq; WP_006132408.1; NZ_AOHP01000058.1.
DR AlphaFoldDB; M3E3B7; -.
DR PATRIC; fig|1284664.3.peg.2869; -.
DR OrthoDB; 9762169at2; -.
DR Proteomes; UP000011732; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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 InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR43671:SF116; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43671; SERINE/THREONINE-PROTEIN KINASE NEK; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:EMF28362.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000011732};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:EMF28362.1};
KW Transferase {ECO:0000313|EMBL:EMF28362.1}.
FT DOMAIN 8..276
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 302..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 391..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..368
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..405
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..465
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 547 AA; 59015 MW; 5DC3D17BAEEDD87C CRC64;
MRPVGSKYLL EEPLGRGATG TVWRARQRET AGAEAAVPGQ PGETVAIKVL KEELAGDADV
VMRFLRERSV LLRLTHPNIV RVRDLVVEGE LLALVMDLVE GPDLHRYLRE NGPFTPVAAA
LLTAQIADAL GASHADGVVH RDLKPANVLL KQQGGELHPM LTDFGIARLA DSPGLTRTHE
FVGTPAYIAP ESAEGRPQTS AVDIYGAGIL LYELVTGRPP FSGGSALEVL HQHLSAEPRR
PSTVPDPLWT VIERCLSKDP GRRPSAENLA RGMRVVAEGI GVHASSAQIS AAENVGALLA
PDPAPAPVPG APSAPGASDP TQVLPQNPPG AYDPNAATSV LPQTGPNGAA DPTAVMPPVP
PGGPGGGPED PHPWQNQLRA ARDRNEQTQV QYLDPHEDPL RRRPQRQVAR PQQPPQRPQQ
PQPGPGYGYP QQPPPQQYAP PPERQRRQQP QPPQRYAPPP EPQRPAREPR QPRQRSANPM
RIPGLGCLKG CLFTLLILFV ASWLIWELSP LQDWIGTGKG YWEQLSDWFG SVTGWIEDLG
GPSDPTN
//