ID A0A0N1CX10_9MICO Unreviewed; 652 AA.
AC A0A0N1CX10;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=AEQ27_11540 {ECO:0000313|EMBL:KPG80804.1};
OS Frigoribacterium sp. RIT-PI-h.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Frigoribacterium.
OX NCBI_TaxID=1690245 {ECO:0000313|EMBL:KPG80804.1, ECO:0000313|Proteomes:UP000037934};
RN [1] {ECO:0000313|Proteomes:UP000037934}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIT-PI-h {ECO:0000313|Proteomes:UP000037934};
RA Tran P.N., Lee Y.P., Gan H.M., Savka M.A.;
RT "Whole genome sequencing of endophytes isolated from poison ivy
RT (Toxicodendron radicans).";
RL Submitted (JUL-2015) 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:KPG80804.1}.
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DR EMBL; LHOZ01000079; KPG80804.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N1CX10; -.
DR PATRIC; fig|1690245.3.peg.851; -.
DR Proteomes; UP000037934; 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; cd06577; PASTA_pknB; 3.
DR CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 3.30.10.20; -; 4.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR005543; PASTA_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR NCBIfam; NF033483; PknB_PASTA_kin; 1.
DR PANTHER; PTHR45832:SF24; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR45832; SERINE/THREONINE-PROTEIN KINASE SAMKA-RELATED-RELATED; 1.
DR Pfam; PF03793; PASTA; 3.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00740; PASTA; 3.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51178; PASTA; 3.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:KPG80804.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000037934};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:KPG80804.1};
KW Transferase {ECO:0000313|EMBL:KPG80804.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 348..368
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 18..274
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 372..439
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 511..578
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 579..651
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 406..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..425
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 652 AA; 68459 MW; 24C7F64CFF4C7F57 CRC64;
MSVNQTDPMI GRLIEGRYEV RSRIARGGMA TVYLATDLRL ERRVAIKIMH GHLADDASFK
ERFIQEARSA ARLAHPNVVN VFDQGQDDDS AYLVMEYLPG ITLRELLQDH KVLTPEQAMD
ILEAVLAGLA AAHRAGIVHR DLKPENVLLA DDGRIKIGDF GLARAATANT ATGAALLGTI
AYLSPELVTR GIADTRSDIY ALGIMLYEML TGEQPYKGDQ PMQIAYQHAN DTVPTPSSAN
PRVPVELDEL VLWATARDPE QRPRDARALL DQLLDVQRVL ADPSGPPAHR TMVLPAAGAT
SVLPSGGTGE TQILPKARHR TGPVQAEPDD AATTLAAVAD RRRRRGRVLM ALVVVVALLA
GGVGWWFGSG PGAQASVPDV TGQDPAAASA ALTSAGFVVA PDPQSDFSPV VPTGQVTRTD
PDATSRVQKG STITLVVSQG PRQLPVPTVV GGTAKAATDA LSDFTLQPTS SQFDASAAGT
VLAISGVDDA GTPVDLAGAA QYGEQQPVTL TVSLGPVPDV AGLSVADAQS ALAGVQLTGV
ESGTEFSDGV TSGEVIRYEQ QAEGALRQGD TVNLVVSKGP PPITIPDVRG KTIDAATSQL
QGLGFRVSYP RCTAFTCAFY DWEASLPVTA TDPEAGLTAT KGATITLSYR VE
//
