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Database: UniProt
Entry: A0A1I5AYC4_9GAMM
LinkDB: A0A1I5AYC4_9GAMM
Original site: A0A1I5AYC4_9GAMM 
ID   A0A1I5AYC4_9GAMM        Unreviewed;       641 AA.
AC   A0A1I5AYC4;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
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=SAMN05216289_1461 {ECO:0000313|EMBL:SFN67427.1};
OS   Dokdonella immobilis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Rhodanobacteraceae; Dokdonella.
OX   NCBI_TaxID=578942 {ECO:0000313|EMBL:SFN67427.1, ECO:0000313|Proteomes:UP000198575};
RN   [1] {ECO:0000313|EMBL:SFN67427.1, ECO:0000313|Proteomes:UP000198575}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.7659 {ECO:0000313|EMBL:SFN67427.1,
RC   ECO:0000313|Proteomes:UP000198575};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; FOVF01000046; SFN67427.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I5AYC4; -.
DR   STRING; 578942.SAMN05216289_1461; -.
DR   OrthoDB; 9801841at2; -.
DR   Proteomes; UP000198575; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
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; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 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:SFN67427.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000198575};
KW   Serine/threonine-protein kinase {ECO:0000313|EMBL:SFN67427.1};
KW   Transferase {ECO:0000313|EMBL:SFN67427.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        352..373
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          8..272
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          309..333
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          406..453
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        406..431
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         37
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   641 AA;  67923 MW;  7CE9B309838A3D13 CRC64;
     MKTRLGHYDI VAELGRGGMG VVYKGHESSL NRYVAIKVLA DSLAHDEGVK ERFLREARSM
     AALNDPHIIQ IYYIGDDEGQ TYFVMEFVEG ESLGTLLKRE HKVPVGPAAK IIYQTAMGLA
     TAHDKGVIHR DIKPGNLMVS SRGTIKIADF GIALSNQDIS KKLTSTGEFV GTPGYLSPEV
     CLGKQVDRRS DIFSLGIVLF EMLAGRMPFT DESPLGLMLE VVRAEIPDVR QLNGEVDEQI
     AWILSKMIAK EPEDRYQSCH ELAEDLAAHP LVAKGGPITI VPKVSAAAAT LIGQRTPVPN
     AAVANTRITP SAQPMPPAHT PAATAPGSAQ PAFERQSVLD RPTDVGGKRS SAALPIAIAA
     ILVLCLIGGA WAFRDKIPGL SGLGSNPVAA TDANTANAMA STATVTNTPA TTGQNDSLPS
     SNTNGVPDSS TDMPATDAVA DNGAEGPGPR ASQADVDALR DLPAARASED APDSVPMPRA
     EEATDVAMVA PKKTVTTPPR PHVPTIAVVV GGDDVITEPA RDAIVSLLQR RGFRVIEAGE
     ASGSKPNMGS LRGRADAVVF VQAKPIGSQQ LNYYGQSSTL YTVQMGVKAY RVSDGSTLWS
     SGMEQVNFST LNATEKAQEA VEPLLDAVDS RLDEFRSRRR G
//
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