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Database: UniProt
Entry: Q08Y28_STIAD
LinkDB: Q08Y28_STIAD
Original site: Q08Y28_STIAD 
ID   Q08Y28_STIAD            Unreviewed;       859 AA.
AC   Q08Y28;
DT   31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2006, sequence version 1.
DT   24-JAN-2024, entry version 73.
DE   SubName: Full=Serine/threonine kinase PKN8 {ECO:0000313|EMBL:EAU65377.1};
GN   ORFNames=STIAU_2165 {ECO:0000313|EMBL:EAU65377.1};
OS   Stigmatella aurantiaca (strain DW4/3-1).
OC   Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC   Archangiaceae; Stigmatella.
OX   NCBI_TaxID=378806 {ECO:0000313|EMBL:EAU65377.1, ECO:0000313|Proteomes:UP000032702};
RN   [1] {ECO:0000313|EMBL:EAU65377.1, ECO:0000313|Proteomes:UP000032702}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DW4/3-1 {ECO:0000313|EMBL:EAU65377.1,
RC   ECO:0000313|Proteomes:UP000032702};
RA   Nierman W.C.;
RL   Submitted (APR-2006) 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:EAU65377.1}.
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DR   EMBL; AAMD01000084; EAU65377.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q08Y28; -.
DR   PATRIC; fig|378806.16.peg.4383; -.
DR   Proteomes; UP000032702; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
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; 2.
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; 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; SM00028; TPR; 5.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF48452; TPR-like; 2.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS50005; TPR; 2.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:EAU65377.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW   Transferase {ECO:0000313|EMBL:EAU65377.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        298..316
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1..287
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REPEAT          585..618
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REPEAT          711..744
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
SQ   SEQUENCE   859 AA;  93950 MW;  B7634320A52361F8 CRC64;
     MGTVYAAYDP ELDRKVALKL LRPGKGDAED SEGRARLLRE AQAMARISHP NVITVHDVGT
     FGSQVFITLE FIQGQTLREW LRKARHPWQQ ILQRFLEAGQ GLVAAHQVGL VHRDFKPANV
     LIADSGRVYV TDFGLARLAE AAGQEEASFE AGSVSEEQMS AVLSSPLTSA GVIVGTPQYM
     PPEQYLGNAG DARLDQFSFC ASLYWALYGK RPFEPQQMAA MAAEVSQSLQ AQSPQEIRRR
     LGHGTIVQEP PRDTRVPSWV RRAVLRGLSL APEDRFPSMQ ALLTALSQQQ RRVRRRKVIA
     AVGAVAVAGA GVGLYFQHRS QLCTGAEPLM ASVWGAAPRQ KLEAAFSATG KPFAPESARQ
     VVQVLDGYAK GWTRMHTEAC VATRIQGMQT EALLSLRMVC LERRRRDLRA LVGLLTEADG
     KVVERSVDAV AALPSLKACQ DIESLAEQSP LPEDPARRAT IERLGEQLSQ IKALHDAGRY
     QAALKLARTI EPEVAATTYL PLQAELRYHL GWLLQQSGEA EEGLRELERA FDDAESSRSD
     RTRLEVLIKL IFTLANNGHP EQAQRWGEVA VAVLNRLGGE PSLAGDLMGN LGSVALMQGR
     YQEATGYFEK ARALRQDPLG TEDPKQAKVS YGLGLAALRQ GEHARAIQML GEALQQTQSS
     KGAQHPEMGS RHVMLATAYR EGGEPVQALA HAEAALKLRK AALGADHPAV ADALDELGEC
     LLLLKRYEEA MEAFRQAVDI KGEKLGMDHP DLSYSYDGMG KALLAQGKAE EAIVYLKQAL
     AYGNTEPEAL AGTGFRLAQA LWEAGKAPQS AREEALRARE GYAKLEKPQQ VAEINAWLKA
     REAPPVPALP GRPPRRLRR
//
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