ID A0A142X070_9PLAN Unreviewed; 432 AA.
AC A0A142X070;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN Name=stkP_5 {ECO:0000313|EMBL:AMV20305.1};
GN ORFNames=VT03_20575 {ECO:0000313|EMBL:AMV20305.1};
OS Planctomyces sp. SH-PL14.
OC Bacteria; Planctomycetota; Planctomycetia; Planctomycetales;
OC Planctomycetaceae; Planctomyces.
OX NCBI_TaxID=1632864 {ECO:0000313|EMBL:AMV20305.1, ECO:0000313|Proteomes:UP000076318};
RN [1] {ECO:0000313|EMBL:AMV20305.1, ECO:0000313|Proteomes:UP000076318}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SH-PL14 {ECO:0000313|EMBL:AMV20305.1,
RC ECO:0000313|Proteomes:UP000076318};
RA van der Voort M., Raaijmakers J.M.;
RT "Genome minning of novel planctomycete species.";
RL Submitted (APR-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};
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DR EMBL; CP011270; AMV20305.1; -; Genomic_DNA.
DR RefSeq; WP_075094679.1; NZ_CP011270.1.
DR AlphaFoldDB; A0A142X070; -.
DR STRING; 1632864.VT03_20575; -.
DR KEGG; pls:VT03_20575; -.
DR OrthoDB; 6111975at2; -.
DR Proteomes; UP000076318; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00060; FHA; 1.
DR CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 2.60.200.20; -; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR PANTHER; PTHR43289; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 20-RELATED; 1.
DR PANTHER; PTHR43289:SF6; SERINE_THREONINE-PROTEIN KINASE NEKL-3; 1.
DR Pfam; PF00498; FHA; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00240; FHA; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR PROSITE; PS50006; FHA_DOMAIN; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:AMV20305.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000076318};
KW Transferase {ECO:0000313|EMBL:AMV20305.1}.
FT DOMAIN 25..76
FT /note="FHA"
FT /evidence="ECO:0000259|PROSITE:PS50006"
FT DOMAIN 153..423
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 182
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 432 AA; 47840 MW; 8139528DC94D0ED8 CRC64;
MKIRLVVVKG PHLGEQFLFA HHEHFLVGRA PVAHFRLGDK DPYVSRLHFV IEANPPACRL
LDLNSSNGTL LNGTLTKTAD LKDGDLLQAG ETTFRLSLVL EPHETIEDTV VGLHPPRRPD
LGPGSRQDTA EVDNSFELIP EEAASVGWSP PGYRLLSRIG EGAMGTVYRA RRLADAAEVA
VKIVKQAYAT SPADRQRFLR EIEVMRQVNH RHIVTLLEGG CSDEELFLVM ELVEGDNLEQ
WTSQRKEKSA EPLPIATAVK LILPILDALH AAHTSGFVHR DVKPANIFLK REGRAIRPVL
GDFGLARAYQ ETQLSGLTLT GELRGTLRYM APEQITDARR AQPASDQYSA AATLYWLLAG
RHTHDFEAAV PRALCQVLLE DPVPLAGRRE GIPPGIVTAV HRALAKKTEE RFPSIAEFRR
ALLASLRRLS RS
//
