ID   Q1QB51_PSYCK            Unreviewed;       700 AA.
AC   Q1QB51;
DT   16-MAY-2006, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2006, sequence version 1.
DT   27-MAR-2024, entry version 92.
DE   SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:ABE75102.1};
GN   OrderedLocusNames=Pcryo_1321 {ECO:0000313|EMBL:ABE75102.1};
OS   Psychrobacter cryohalolentis (strain ATCC BAA-1226 / DSM 17306 / VKM B-2378
OS   / K5).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Psychrobacter.
OX   NCBI_TaxID=335284 {ECO:0000313|EMBL:ABE75102.1, ECO:0000313|Proteomes:UP000002425};
RN   [1] {ECO:0000313|Proteomes:UP000002425}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1226 / DSM 17306 / VKM B-2378 / K5
RC   {ECO:0000313|Proteomes:UP000002425};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., Bruce D.,
RA   Han C., Tapia R., Sims D.R., Gilna P., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Richardson P.;
RT   "Complete sequence of chromosome of Psychrobacter cryohalolentis K5.";
RL   Submitted (MAR-2006) 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; CP000323; ABE75102.1; -; Genomic_DNA.
DR   RefSeq; WP_011513654.1; NC_007969.1.
DR   AlphaFoldDB; Q1QB51; -.
DR   STRING; 335284.Pcryo_1321; -.
DR   KEGG; pcr:Pcryo_1321; -.
DR   eggNOG; COG0515; Bacteria.
DR   eggNOG; COG0631; Bacteria.
DR   HOGENOM; CLU_393740_0_0_6; -.
DR   Proteomes; UP000002425; Chromosome.
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; 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; PTHR24345; SERINE/THREONINE-PROTEIN KINASE PLK; 1.
DR   PANTHER; PTHR24345:SF0; SERINE_THREONINE-PROTEIN KINASE PLK1; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF13672; PP2C_2; 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   Kinase {ECO:0000313|EMBL:ABE75102.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Serine/threonine-protein kinase {ECO:0000313|EMBL:ABE75102.1};
KW   Transferase {ECO:0000313|EMBL:ABE75102.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        679..699
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          26..311
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51746"
FT   DOMAIN          364..666
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          320..342
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        320..338
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   700 AA;  77530 MW;  523CC57CD239EF86 CRC64;
     MKKGSTQDFK TTDKTSRHSA DNALWQLDFH SMQGRKSENQ DSLLITTCLP YGQFTATING
     GVQCPHAPLL VLMADGVSAC QFPKQASQLV VNTVTHHLTL ALKNGALKNE AIEEMVLAEN
     QSQSANIDFD DNQVAILIRE AVNKANDALY FPQVYERVPP LLSTLSGLLC IGDRIHLFHT
     GDSRIYRVGL ESIKVLSKDH RIHHGQDKGA LSAAIGADTM VELQQSVFTL HQNECLALMT
     DGVYESIAAS ELQFELCSAV KALCQPSQTI DTTDNSSNDG AVNSLSISQS ICEQAFNEGS
     HDNLSMVILG MNAQALHKKK TANSAHTKNN SNNKNASLHD PMPHDIHRYQ LLTGLEVGAR
     IDGFIVKHII ARTARSEVYL VEDENHHLFA LKSPSLNAIT DGHYLREFLK ERKIGLSLSK
     HRRAGEPAYN QADPNNLSSD SSLTGISSIK PYLDASSALS ASGLLRYYPI PASSAYLYHL
     TEYIEGESLR DFMDRHAPCD VWQTYDLLTK IGMAVRVMHR NYLLHQDIKP ENILLTTSGA
     VKLIDFGSAS SSILKDSTRP PNGDLHYAAP EYYTDAPKGV HSDLFSIAVI GYELLTGELP
     FSSQALMHSH QANHTLTLPT QLLRQYRVPA ASQQALMRAL LANTQARYQA IGEFLQDFNP
     ENHNYISDPE PLIIRNPLLV WHSICFIQFV LIFSLLAYFL
//