GenomeNet

Database: UniProt
Entry: A0A1I4Y2U1_9GAMM
LinkDB: A0A1I4Y2U1_9GAMM
Original site: A0A1I4Y2U1_9GAMM 
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};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
//
DBGET integrated database retrieval system