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
//