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
//