ID A0A1Q2MAP1_9GAMM Unreviewed; 579 AA.
AC A0A1Q2MAP1;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Serine/threonine protein phosphatase {ECO:0000313|EMBL:AQQ69367.1};
GN ORFNames=Mag101_03770 {ECO:0000313|EMBL:AQQ69367.1};
OS Microbulbifer agarilyticus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Microbulbiferaceae; Microbulbifer.
OX NCBI_TaxID=260552 {ECO:0000313|EMBL:AQQ69367.1, ECO:0000313|Proteomes:UP000188219};
RN [1] {ECO:0000313|EMBL:AQQ69367.1, ECO:0000313|Proteomes:UP000188219}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GP101 {ECO:0000313|EMBL:AQQ69367.1,
RC ECO:0000313|Proteomes:UP000188219};
RA Jung J., Bae S.S., Baek K.;
RT "Genome of Microbulbifer agarilyticus GP101.";
RL Submitted (FEB-2017) 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; CP019650; AQQ69367.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q2MAP1; -.
DR STRING; 260552.Mag101_03770; -.
DR KEGG; maga:Mag101_03770; -.
DR eggNOG; COG0515; Bacteria.
DR eggNOG; COG0631; Bacteria.
DR Proteomes; UP000188219; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR CDD; cd00143; PP2Cc; 1.
DR CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR036457; PPM-type-like_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR11042:SF91; EUKARYOTIC TRANSLATION INITIATION FACTOR 2-ALPHA KINASE; 1.
DR PANTHER; PTHR11042; EUKARYOTIC TRANSLATION INITIATION FACTOR 2-ALPHA KINASE EIF2-ALPHA KINASE -RELATED; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF13672; PP2C_2; 1.
DR SMART; SM00331; PP2C_SIG; 1.
DR SMART; SM00332; PP2Cc; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF81606; PP2C-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51746; PPM_2; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000188219}.
FT DOMAIN 15..240
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT DOMAIN 273..540
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
SQ SEQUENCE 579 AA; 64836 MW; 181C43B9B129AE78 CRC64;
MSDSDQKASN SENLEFATAT ECGLRAYNDD AVAAYRATGS DLRYRGSIAA IADGVGSAEA
GGAAARAAIS GFISDYYSTP DSWSVKQASA RVLHALNSWL YRQSGGADEV QRGWLTTFSA
VILKGSTAHL IHIGDSRIYR LRDGNLECLT RDHSRALGPD RTFLSRALGM DAHIEVDYRR
EPLEAGDLFC VTTDGIHDFL PRSQFTELLI RHQMDAAKPL MAAALDNGSK DNLSLALCRV
NLVDAVQADD VMVATSQLPF PPALQPGNKI DGYEVLQELH ASSRSYLYLV RDMDADTDGQ
PEQLLALKAP SENFSDDPAY IERFIAEEWT GRRLEHPAIV QIYPPRKQRK FLYHVMEYVD
GQNLRQWMQL NPEPPLDQVR NLVEQLVSAL RRLQRLEIVH GDLKPENIMI DTAGRLKLID
LGGANAAGLQ ELLRYQDSAP PGSKNYCAPE YFFSDAASHR SDIFSLGVIA YEMLTGNYPY
KERFGSSHYQ LKNYASLRYI SARQYREDIP EWIDGALRQA CAPDPKNRYP ALSEFVHDLR
TPNKKFDTAE KPPLIQRNPL LFWQTVAVLA VLSHLLYFL
//
