ID A0A1I4Y2U1_9GAMM Unreviewed; 973 AA.
AC A0A1I4Y2U1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:SFN32357.1};
GN ORFNames=SAMN05216289_11457 {ECO:0000313|EMBL:SFN32357.1};
OS Dokdonella immobilis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Dokdonella.
OX NCBI_TaxID=578942 {ECO:0000313|EMBL:SFN32357.1, ECO:0000313|Proteomes:UP000198575};
RN [1] {ECO:0000313|EMBL:SFN32357.1, ECO:0000313|Proteomes:UP000198575}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.7659 {ECO:0000313|EMBL:SFN32357.1,
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; FOVF01000014; SFN32357.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I4Y2U1; -.
DR STRING; 578942.SAMN05216289_11457; -.
DR OrthoDB; 9783151at2; -.
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; 1.25.40.10; Tetratricopeptide repeat domain; 3.
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 InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
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 Pfam; PF13424; TPR_12; 2.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00028; TPR; 6.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF48452; TPR-like; 4.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50005; TPR; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000313|EMBL:SFN32357.1}; 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:SFN32357.1};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW Transferase {ECO:0000313|EMBL:SFN32357.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 399..420
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 86..374
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REPEAT 622..655
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT COILED 417..449
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 117
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 973 AA; 104981 MW; E65845864C612C8B CRC64;
MSTATERWAE VAALFDELAE LEHAVRAQRL AALDESDPAL AAEVRALLAA DDTPNPLLDG
ELAGVVVGIP GVESPASAPA GKTGPWRLLR PLGEGGMGVV WLAERIDGAY EQQVAVKVLK
RGMDTQAILR RFLQERRILA RLNHPNIVRL VDGGMGEDER PYYVMDYVDG QSITRHAADH
HLDVSARMRL LARVADAVAY AHAQLVIHRD LKPSNVLVDH QGEPRVLDFG IAKLIEESGE
QTQTGTGLRV MSPAYAAPEQ ILGEPIGTAT DVYALGLMLC ELLVGQLPRQ RRGSTPAQLA
LEASQEVTDR ASTLAARLTG AQLQALYGET ADPRQLSRML SGDLDLIVAT ALQREPARRY
ATAAAFADDL RRWLDGRPIA ARADSPGYRL KKFMRRHRLG VAASVIVAFS LIGGLGVALW
QAQLARAEAQ RADLERGKAE RQLARSERVK DFILTLFREQ DPISRASATA RTPVALIRDG
IAQIDSSLAG EPELRAQLLK DLGEIQISLD DREAARATLK RAWELQSSLS GADSIATAEV
LAAYGDAVYA VGDVPASAAL LRDALTKLRQ AGAGNLPRAA LAESSLANIE LVEGSNAEAE
KLARHGVEVF RETYGAEDIR VASRLGVLGK VQQEAGNYPD ALASYREALA IVARNNGEDH
VRTAMLRTNV GDILRVQHKY DEARVEYETA LRIERAQLPD DHLFVGGTLL RLGDLQRRMG
NLEAAEASFA ESIAILGKTP SGQYAQALQT YGTLARAQGR FELAAQRYRK SFEAFQAATG
DSVYTWITAL LEVSALTAAE RFVEADRLGA DALAALARVS PDDRYNNTFA ASVVGSLRLA
ESRFDDATPL LRRALEGVQA IYDKDHAEIA QARVALAAAL LGQQESALRG EAAALIETAI
ETLTRAGDAG SEPMLGAAYL ERSRFHEQGG NLDAARADVV AAMARLRTPE YAPKLRQAEA
LARKLGAPVG GRA
//