GenomeNet

Database: UniProt
Entry: A0A257M5Z6_9BACT
LinkDB: A0A257M5Z6_9BACT
Original site: A0A257M5Z6_9BACT 
ID   A0A257M5Z6_9BACT        Unreviewed;       864 AA.
AC   A0A257M5Z6;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN   ORFNames=CFE26_03290 {ECO:0000313|EMBL:OYV07002.1};
OS   Verrucomicrobiales bacterium VVV1.
OC   Bacteria; Verrucomicrobiota; Verrucomicrobiae; Verrucomicrobiales.
OX   NCBI_TaxID=2015575 {ECO:0000313|EMBL:OYV07002.1, ECO:0000313|Proteomes:UP000216473};
RN   [1] {ECO:0000313|EMBL:OYV07002.1, ECO:0000313|Proteomes:UP000216473}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VVV1 {ECO:0000313|EMBL:OYV07002.1};
RA   Kojadinovic M., Villain A., Puppo C., Fon Sing S., Prioretti L., Hubert P.,
RA   Gregori G., Zhang Y., Sassi J.-F., Claverie J.-M., Blanc G., Gontero B.;
RT   "A metagenomic investigation of the 'star' freshwater diatom Asterionella
RT   formosa and its bacterial cohort.";
RL   Submitted (JUN-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};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OYV07002.1}.
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; NKJB01000064; OYV07002.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A257M5Z6; -.
DR   Proteomes; UP000216473; 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-EC.
DR   Gene3D; 3.90.1580.10; paralog of FGE (formylglycine-generating enzyme); 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR016187; CTDL_fold.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR013229; PEGA.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR005532; SUMF_dom.
DR   InterPro; IPR042095; SUMF_sf.
DR   PANTHER; PTHR23150:SF19; FORMYLGLYCINE-GENERATING ENZYME; 1.
DR   PANTHER; PTHR23150; SULFATASE MODIFYING FACTOR 1, 2; 1.
DR   Pfam; PF03781; FGE-sulfatase; 1.
DR   Pfam; PF08308; PEGA; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56436; C-type lectin-like; 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}; Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000216473};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        285..303
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          15..298
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         43
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   864 AA;  95313 MW;  BD89E497F8F46B94 CRC64;
     MPPIKNRPDP VVPDHEVLRK IGGGAYGEVW LARGVTGALR AVKVVWREDF DDARGFEREF
     EGILKFEPIS RTHPGLVNIL HVGRSPDGTS FYYYVMELGD DVRTGAEINA IEYEPRTLRA
     DTKLACGIRL ETNLCIDVGL RLAEALDHLH ELGLAHRDVK PANVIFVNGK AKLADIGLVA
     TRGQRTFVGT EGFVPPEGPG SAPADVYSLG KVLYEIATGK DRLDFPELPD EAPPPEEKKR
     WLELNRIICD ICDPQLSRRK ITTAAELADA LRRLQRGKRR RQTGLAAWMT AIVLGVFIAL
     GTWEALKDSP VMGWFSTPDP IVTVPDVVEK FGQIRVVSYP EGAEVIGPDE QWLGVTPLTL
     KAAVGSDVEY LIRKPGFRPM TVRGKVPPSA VNEPLPLGSE LGIFSPPEIG ASWEDHQGGS
     YQPVANEHLA SLLVSEASWR RFVNVTKRKI EAVEFFPISQ NGRPIQSVLA SKGEANAYCA
     WLREAAIKEG YLTADHEMLA KFDDGFNDPA ASERARNEGL KPFRILVRLI PYGRIILTTT
     PPGAAVYLNN GPLVGDTTPL EIDKVKPGPV TLTIVLDGYK PLTLNLEMKP DDLITLDKPL
     QENQGVRFDK PWKNGLGMKF VPYGSEGELM VSIWETRISD YDAFVADKNS GAKPLRKPDF
     AQTKDHPVIY VTRDDARNFC TWLTKRERTE ERISVAHTYR LLTDLEWSRI AGIAEVAGQG
     PGWRDIRKPL VFQWGSSWPP PANYANLADS AAAKAPGVPA NRTIEGYDDQ FETTAPVGSF
     PPNAAGLHDL CGNVHEWVND DYTTAQPGHA TYGVLRGGGW NSFQPDNLYT GARNAVPPNR
     SDNIYGFRVV LAKVPSKPDN ITDP
//
DBGET integrated database retrieval system