ID   PKPA_PHYB8              Reviewed;         613 AA.
AC   Q01577;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Serine/threonine-protein kinase pkpA;
DE            EC=2.7.11.1;
GN   Name=pkpA;
OS   Phycomyces blakesleeanus (strain ATCC 8743b / DSM 1359 / FGSC 10004 / NBRC
OS   33097 / NRRL 1555).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Phycomycetaceae; Phycomyces.
OX   NCBI_TaxID=763407;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 8743b / DSM 1359 / FGSC 10004 / NBRC 33097 / NRRL 1555;
RX   PubMed=8590476; DOI=10.1007/bf00326428;
RA   Ruiz-Perez V.L., Murillo F.J., Torres-Martinez S.;
RT   "PkpA, a novel Phycomyces blakesleeanus serine/threonine protein kinase.";
RL   Curr. Genet. 28:309-316(1995).
CC   -!- FUNCTION: Serine/threonine protein kinase that probably participates as
CC       an intermediate in an intracellular system controlling nuclear
CC       proliferation.
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   -!- 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;
CC   -!- DEVELOPMENTAL STAGE: Mainly expressed during the vegetative growth, the
CC       level decreased when the mycelium can differentiate and form
CC       sporangiophores.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR   EMBL; Z46636; CAA86606.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q01577; -.
DR   SMR; Q01577; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Kinase; Nucleotide-binding; Serine/threonine-protein kinase;
KW   Transferase.
FT   CHAIN           1..613
FT                   /note="Serine/threonine-protein kinase pkpA"
FT                   /id="PRO_0000086555"
FT   DOMAIN          17..269
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          424..475
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          589..613
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        425..443
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        444..475
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        592..606
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        140
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         23..31
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         50
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   613 AA;  69594 MW;  E988308E39101A1E CRC64;
     MPDYEKVIEA SGNGRYSKLN TVLGKGAYKV VYKAIDREEA INDNEITNVK VTRQEFKDLG
     HEIDILKSVR HPNIITFHDA WYNETEFVFI TELMTSGTLR EYIRKLTPLP NIKIVKRWCR
     QILKGLAYLH GHEPPIIHRD IKCDNIFING AHGEIKIGDM GTAEMKNGKK YTVIGTPEFM
     APEMYEEQGY NEKVDIYAFG MCLLEMATGE YPYGECTNAV QVFKKVTQTI KPECLSRVQD
     PELLTLVNIC LTPEDERMTA QEILEHRFLA VEPEVVLVSK DMTMKLLTLQ VVFKGMDKLS
     VKFEFNADTD TAADVVAEMI EEQVLQNCYQ QLITCEINRI LRDIARNQGP PDKGEDEKIV
     WRRENDIRSE LERAKKDLAL AVERVFEAEK KCELLEQHNI IAEERCKETI FALEQAKFQI
     PDLLQPQPQP QPQPQPQPQP QPQFQLQPQL QYLSPQSTTS PGPTSDDNST NSTMLSSLES
     ELSKLCVSGD EQVETTTHSA LMENVLAGKA KYYEYSNDTS IDKFVMDTAG ATNRSKDKQK
     QWAAKLQDQD IMTVGDLRDL HDEDWSGIGL TVFALRALKN MLAGKKAAVT QRGLQGTRSG
     ASTPVEEQEQ ELM