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Database: UniProt
Entry: A0A0V0QF51_PSEPJ
LinkDB: A0A0V0QF51_PSEPJ
Original site: A0A0V0QF51_PSEPJ 
ID   A0A0V0QF51_PSEPJ        Unreviewed;      1029 AA.
AC   A0A0V0QF51;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   SubName: Full=Protein kinase-like domain {ECO:0000313|EMBL:KRX00795.1};
GN   ORFNames=PPERSA_01974 {ECO:0000313|EMBL:KRX00795.1};
OS   Pseudocohnilembus persalinus (Ciliate).
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC   Oligohymenophorea; Scuticociliatia; Philasterida; Pseudocohnilembidae;
OC   Pseudocohnilembus.
OX   NCBI_TaxID=266149 {ECO:0000313|EMBL:KRX00795.1, ECO:0000313|Proteomes:UP000054937};
RN   [1] {ECO:0000313|EMBL:KRX00795.1, ECO:0000313|Proteomes:UP000054937}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=36N120E {ECO:0000313|EMBL:KRX00795.1};
RX   PubMed=26486372; DOI=10.1038/srep15470;
RA   Xiong J., Wang G., Cheng J., Tian M., Pan X., Warren A., Jiang C., Yuan D.,
RA   Miao W.;
RT   "Genome of the facultative scuticociliatosis pathogen Pseudocohnilembus
RT   persalinus provides insight into its virulence through horizontal gene
RT   transfer.";
RL   Sci. Rep. 5:15470-15470(2015).
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:KRX00795.1}.
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DR   EMBL; LDAU01000181; KRX00795.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V0QF51; -.
DR   EnsemblProtists; KRX00795; KRX00795; PPERSA_01974.
DR   InParanoid; A0A0V0QF51; -.
DR   OrthoDB; 179354at2759; -.
DR   Proteomes; UP000054937; Unassembled WGS sequence.
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; cd05123; STKc_AGC; 1.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR045270; STKc_AGC.
DR   PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR   PANTHER; PTHR24351:SF234; SERINE/THREONINE-PROTEIN KINASE YPK2/YKR2; 1.
DR   Pfam; PF00023; Ank; 1.
DR   Pfam; PF12796; Ank_2; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00248; ANK; 3.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 3.
DR   PROSITE; PS50088; ANK_REPEAT; 3.
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   ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KRX00795.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000054937};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   REPEAT          231..263
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          264..286
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          297..329
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   DOMAIN          704..959
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          960..1029
FT                   /note="AGC-kinase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51285"
FT   REGION          114..172
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          361..426
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          577..625
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          639..694
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        121..137
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        142..172
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        361..421
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        579..625
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         743
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1029 AA;  119518 MW;  CD54F72E2A862BC1 CRC64;
     MRVIIQYITS TLQKRTDRIT IPQEQDTDTL IKLVAKKVNA KPNQISLKFK RDGVELRVIK
     GWPLDHYQIR NNSILQVEQR ETQTDINNQY RQKIFQKYQQ YGIKDIMPKV QPKLSVLKEN
     TEEEEDEYGE ENSENEEKEE QNIGSNNNLN SNNNQSNYSQ KSQESFGKPQ RLSQISKQKI
     MDITLEKLLV ETKQGNLQNI KDLFEQNFPD IFDDNQLKQV QIQLVNENGY GGWNSLHFAI
     FQNHLEIVKY LMDRGADVNS VTKDGWTPLQ LAVYRKNLSI VEQLLKDEEL FVNQVTSRDT
     ALHQACKVQS LEIVKLLMEH DADPDILNDK AESPIDLCQD KEVQEKITKI LLKYSEINEQ
     SSPELGSKKQ SEQEKLNQQQ NQQQMNNHIQ QKQQQIIQQQ VQQQHQQKSQ QHSNSLPVRQ
     ARGIATPQRP PIVKGMAYKH GNWTLTLRKR FFVLNPDQGT LVRYKEKKYY PMKPMEVIPL
     KDIQNVQHID RSWYMKGNIH YFEFKYNHQV YQMGYTYPET CRSWNFFLKE SIRYSSYLEK
     QIDRTTNEPN QEIELIDNPE IDEQVAKEFK FYLLGKHNSK RPQSPSPPSN NTINQVQQKD
     QASPTKIRQN SNQAPQAPSL PDKSQELPAN ISTIRRNQVH QLQTPAQKQQ NQQKQQQQNN
     NNQKNIANKQ NSQGSNKSGN SDSTDTENIN LGNLQNNNVN FESFKIQKLL GRGAFGKVFL
     VKKKDDGKIY ALKALKKKQL ILKKQLKYAV TEANVLKMCN HPFVLKLHYA FQTPNYMYLV
     LEYCPGGDLS LHLAQRTTFD EYSAKYYTAE LILAIEHIHE KDIVYRDLKP ENILIDKEGH
     IKLADFGLSK DGVADADNTR SFCGSPAYLS PEMLTHQGAG KPSDIYGIGC VLYEMITGDP
     PYYNDDIPKM YANIKNGVLK YPKNITPEAK DLIQKLLDRS PKTRIGVKSK QELKSHPFFK
     GIDWVKLGNK EIQPPKYDLQ LDDDDDDEDD ELQYLQPNQP IFQDTDYTEN NKRINRVINY
     TFHRPATAD
//
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