ID A0A372GKI0_9ACTN Unreviewed; 325 AA.
AC A0A372GKI0;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:RFS85880.1};
GN ORFNames=D0T12_10130 {ECO:0000313|EMBL:RFS85880.1};
OS Actinomadura spongiicola.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Thermomonosporaceae; Actinomadura.
OX NCBI_TaxID=2303421 {ECO:0000313|EMBL:RFS85880.1, ECO:0000313|Proteomes:UP000262882};
RN [1] {ECO:0000313|EMBL:RFS85880.1, ECO:0000313|Proteomes:UP000262882}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LHW52907 {ECO:0000313|EMBL:RFS85880.1,
RC ECO:0000313|Proteomes:UP000262882};
RA Li L., Lin H.W.;
RT "Actinomadura spongicola sp. nov., isolated from marine sponge Leucetta
RT chagosensis.";
RL Submitted (AUG-2018) 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:RFS85880.1}.
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DR EMBL; QVNQ01000003; RFS85880.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A372GKI0; -.
DR OrthoDB; 3915799at2; -.
DR Proteomes; UP000262882; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:SF13; LD04361P; 1.
DR PANTHER; PTHR43671; SERINE/THREONINE-PROTEIN KINASE NEK; 1.
DR Pfam; PF00069; Pkinase; 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:RFS85880.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000262882};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:RFS85880.1};
KW Transferase {ECO:0000313|EMBL:RFS85880.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 305..324
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 35..292
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 325 AA; 34349 MW; C4A93762BCD149A7 CRC64;
MPDGHPARGH GARPAVPPGA RAPLAPDDPR GLGSYTLLGR LGEGGQGVVY LGRDADGELV
TVKLLRGGDS AGERAHRRFV KEADAARRVS GRHTARVLDA DMTGDRPYIV SEFVEGPPLQ
RVVEDRGPLP APKLRKLALR TAAALAAIHR AGIVHRDFKP GNVLLGPDGA KVIDFGIARL
DQEGADATPV TTGPVGTPAY MAPEQIEDEP VGPPADVFAW GATLVFAATG RPPFGTGPSA
AVIRRVTSRS PDLGDLQGPL RDLAARCLDK NPAARPTAPQ IVRALREGQG PMPKPRPTRI
PRYRWRMMVA LAVVVTGGFV LGLLF
//
