ID A0A142YAG4_9PLAN Unreviewed; 1356 AA.
AC A0A142YAG4;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Serine/threonine-protein kinase Pkn1 {ECO:0000313|EMBL:AMV36154.1};
DE EC=2.7.11.1 {ECO:0000313|EMBL:AMV36154.1};
GN Name=pkn1_1 {ECO:0000313|EMBL:AMV36154.1};
GN ORFNames=VT85_01830 {ECO:0000313|EMBL:AMV36154.1};
OS Planctomyces sp. SH-PL62.
OC Bacteria; Planctomycetota; Planctomycetia; Planctomycetales;
OC Planctomycetaceae; Planctomyces.
OX NCBI_TaxID=1636152 {ECO:0000313|EMBL:AMV36154.1, ECO:0000313|Proteomes:UP000076365};
RN [1] {ECO:0000313|EMBL:AMV36154.1, ECO:0000313|Proteomes:UP000076365}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SH-PL62 {ECO:0000313|EMBL:AMV36154.1,
RC ECO:0000313|Proteomes:UP000076365};
RA van der Voort M., Raaijmakers J.M.;
RT "Genome minning of novel planctomycete species.";
RL Submitted (APR-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};
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DR EMBL; CP011273; AMV36154.1; -; Genomic_DNA.
DR RefSeq; WP_068409676.1; NZ_CP011273.1.
DR STRING; 1636152.VT85_01830; -.
DR KEGG; plh:VT85_01830; -.
DR PATRIC; fig|1636152.3.peg.445; -.
DR OrthoDB; 258731at2; -.
DR Proteomes; UP000076365; Chromosome.
DR GO; GO:0005871; C:kinesin complex; IEA:InterPro.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
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; 5.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR002151; Kinesin_light.
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; PTHR46082:SF6; AAA+ ATPASE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR46082; ATP/GTP-BINDING PROTEIN-RELATED; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF13374; TPR_10; 3.
DR Pfam; PF13424; TPR_12; 6.
DR PRINTS; PR00381; KINESINLIGHT.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00028; TPR; 14.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF48452; TPR-like; 6.
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:AMV36154.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000076365};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000313|EMBL:AMV36154.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 435..457
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 111..413
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 68..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 471..495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1331..1356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 141
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1356 AA; 147104 MW; 3EA6CD0DBE8E1F22 CRC64;
MAIEPGRVKF LFQAAIERDD PDDRRAFVER EAGGDAELLA RVLALLAAYD DPPDALDRPL
AADAQATVDT DPATPPDSAP SPGPPAVEEA TIGLRCGDGV ERIDDVIAGR YRLRQEIGEG
GMGAVYLAEQ TRPVRRQVAL KLIKPGMDSR AVLARFESER QALALMDHPH IAKVLDAGTT
EQGRPFFVME LVKGVPLTDF CDQHLLDVPA RLALFCQICS AVHHAHQKGI IHRDLKPSNI
LVESHDGRPM PRVIDFGLAK AVSGMQLSED PAFTGLGIVA GTPLYMAPEQ AGFNALDVDT
RADIYALGVI LYELLTGSTP IRRETLKRAA MEEMLRLIRE EEPATPSSRI STSEALPNLA
AHRQIEPGRL SRLVRGDLDW IVMKALSKER DRRYASAIGL ANDVERFTNH EPVSAGPPTA
AYRMRKFVRR NRGRVVAASL LLLALVGGIV GTTLGLLEAT RQRGFAETEA AQKEEARQAE
ADQRREAETQ RRAAVEQRRQ AEARLAQVEK ANAVLGSIFI DLNPRSAEKD GKPLSALLGE
RLDQATAQIE GDAIGDPLAV ARMQLVLGDS QAGLGYPEKA IALVTKARAT FLDRLGPDHL
HTLASLFALA ECYRALGKPD LALPLFQQAL AARTRVLGPD HPITLHSMNG LAMGYRDAGK
LDLALPLMER ALAAQKAKLG PDDPATFVSM NNLAAVHRDM GRIDLALPLM ERALAARETK
LGPDHPDTLT LMNNLATGYQ AVGKLDLALP LLERALAARE AKLGPDHPGT LLTMNNLAAG
YVDADKPGLA LPLMERALAA QKSKLGLDHP ETLLTMNNLA SVYRNVGKLD LAVPLLEQTL
EARKAKLGLD HPDTLRSMND LAALYRDAGK PDLARPMMEQ ALEARKAKLG LDHPDTLKSM
NDLAGLYRAA GKLDLARPLM EQALASARSK LGPDHPITLA AMNQLGLVYQ SADKFDLALP
MMEQALAMRK AKFGDDHPET VMSMNDLAAL YRIVGRIDLA LQLMERALAA RETKLGPDHP
DTLTLMNNLA TGYQTVGKLD LALPLLERTL AARKTKLGPD HPETLLTMNN LAAAYRDVGK
LDLALPLLEE ALAAARSKLG PDHPDTLLSM NNLASIYWSS RRLDRSIPLF EEVLKLRMAK
FGADHHETWL VKANLGVNYR DAGRLDEALP LLEGAAAASR RLPMLSWVAP ELLQLLARTG
RAEKARAVAE EVLAQGRAAM PAGSPQLAAH LCSISLALLA VKAYDQAEPL LREALAIREK
ADPDAWTTFN TKSMLGGALL GQAKSAEAEP LLRDGYDGMR RRTDKIPPQG KARVVEALDR
LIVLAEAAGK DEDAKAWRAE REKAAADAPK PEGDGK
//
