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Database: UniProt
Entry: A0A136KWB4_9CHLR
LinkDB: A0A136KWB4_9CHLR
Original site: A0A136KWB4_9CHLR 
ID   A0A136KWB4_9CHLR        Unreviewed;       921 AA.
AC   A0A136KWB4;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
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=UZ15_CFX003003290 {ECO:0000313|EMBL:KXK13650.1};
OS   Chloroflexi bacterium OLB15.
OC   Bacteria; Chloroflexota.
OX   NCBI_TaxID=1617416 {ECO:0000313|EMBL:KXK13650.1, ECO:0000313|Proteomes:UP000070332};
RN   [1] {ECO:0000313|EMBL:KXK13650.1, ECO:0000313|Proteomes:UP000070332}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OLB15 {ECO:0000313|EMBL:KXK13650.1};
RA   Speth D.R., In T Zandt M., Guerrero Cruz S., Jetten M.S., Dutilh B.E.;
RT   "Genome based microbial ecology of anammox granules in a full-scale
RT   wastewater treatment system.";
RL   Submitted (NOV-2015) 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:KXK13650.1}.
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DR   EMBL; LMZS01000177; KXK13650.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A136KWB4; -.
DR   STRING; 1617416.UZ15_CFX003003290; -.
DR   PATRIC; fig|1617416.3.peg.3474; -.
DR   Proteomes; UP000070332; 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; cd00146; PKD; 1.
DR   CDD; cd14014; STKc_PknB_like; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
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; IPR013783; Ig-like_fold.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR022409; PKD/Chitinase_dom.
DR   InterPro; IPR000601; PKD_dom.
DR   InterPro; IPR035986; PKD_dom_sf.
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; PTHR43289; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 20-RELATED; 1.
DR   PANTHER; PTHR43289:SF32; SERINE/THREONINE-PROTEIN KINASE PKAA; 1.
DR   Pfam; PF03781; FGE-sulfatase; 1.
DR   Pfam; PF18911; PKD_4; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00089; PKD; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56436; C-type lectin-like; 1.
DR   SUPFAM; SSF49299; PKD domain; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50093; PKD; 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:KXK13650.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141};
KW   Serine/threonine-protein kinase {ECO:0000313|EMBL:KXK13650.1};
KW   Transferase {ECO:0000313|EMBL:KXK13650.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        327..346
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          14..277
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          575..658
FT                   /note="PKD"
FT                   /evidence="ECO:0000259|PROSITE:PS50093"
FT   REGION          427..498
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        427..457
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        477..496
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         43
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   921 AA;  98591 MW;  08B541E0492CFCC9 CRC64;
     MLDAKSGKQM LGQYELRELL GQGGMGSVYR AFQASLKREV AIKVLPAHLV ASPGYTERFT
     REAETAASLE HAHIVPVYDY GTSKEATYIV MRLLNGGTLS ERAQQHKLAG HETISLTEIA
     DILKQIASAL DYAHSRGVIH RDIKPGNIMF DNQGSAYLTD FGIARLMEAS TKLTSTGATL
     GTPLYMSPEQ WRGDAITPAS DQYAVAVMIY QLVTGHTPFE ADTPYALMNK HIHEPPTPPQ
     AYRSDIPEAV TTVLNRALSK NPAQRFPTVT SFAQAFSAAV ASNQEESTQF LLFKVTHTPP
     SMPLPVQTPA VSAALPPPNK PFYRSPMLWV AGVAVIVIAA LAALLISQEQ RAAALTDSLT
     QTAIAFVPTQ GATSTPTNEP VTTVNTETPV AAPTLTPTQV ETTALPTAAP TEAFTDTATN
     VPPTASPTEA FTDTATNVPP TASPTEAFTD TATNVPPTET ETPPPTLTFT ATRVPPSPTD
     TLPPPSNAPR PTNTPVSPTI NPLIAIQITY EYIQSATAKM WTPTPTNDAT AAFSPTLTAA
     FEEGLTQTAT LWTHTPEPVT PTNTPTNTPT TLPAPVAAFE AHPTSGTVPL TVTFTNQSRG
     NIVSYYWQFG DNSSSTDANP THTYGRIGTF NVLLIVTGPG GTSVAQTSIE TSAPTATSIP
     AALTTITRND DWTPIHQTFA GIDMVLVPAG CFNLGSSAIE VDAAYAQCEA DLGVGNCQHV
     WFEKETPQTQ ICFNQPFWIA YSETTNAQYG SISAAFTDTS ATMPRDSVSW FGAAEFCAAR
     GMRLPTEAEW EYAARGPDNL IYPWGNTFIS NNAAYVNNVS SPEHVGSRPS GISWVGAVDM
     AGNLREWTST IFTPYPYTPG DGRESLSDTV SDRVVRGGSW YVIPVSLRAA DRVNVPPITV
     DWNIGFRCVR DFQSSDLTGI G
//
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