ID A0A0V0R9N3_PSEPJ Unreviewed; 1200 AA.
AC A0A0V0R9N3;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=Protein kinase-like domain {ECO:0000313|EMBL:KRX11179.1};
GN ORFNames=PPERSA_10111 {ECO:0000313|EMBL:KRX11179.1};
OS Pseudocohnilembus persalinus (Ciliate).
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Scuticociliatia; Philasterida; Pseudocohnilembidae;
OC Pseudocohnilembus.
OX NCBI_TaxID=266149 {ECO:0000313|EMBL:KRX11179.1, ECO:0000313|Proteomes:UP000054937};
RN [1] {ECO:0000313|EMBL:KRX11179.1, ECO:0000313|Proteomes:UP000054937}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=36N120E {ECO:0000313|EMBL:KRX11179.1};
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:KRX11179.1}.
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DR EMBL; LDAU01000005; KRX11179.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0R9N3; -.
DR EnsemblProtists; KRX11179; KRX11179; PPERSA_10111.
DR InParanoid; A0A0V0R9N3; -.
DR Proteomes; UP000054937; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00009; AAA; 1.
DR CDD; cd05123; STKc_AGC; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 1.20.272.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR008921; DNA_pol3_clamp-load_cplx_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR013748; Rep_factorC_C.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR045270; STKc_AGC.
DR PANTHER; PTHR24351:SF240; KINASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF08542; Rep_fac_C; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF48019; post-AAA+ oligomerization domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
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}; Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KRX11179.1};
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 DOMAIN 79..341
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 342..412
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT REGION 412..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 453..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 730..766
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 622..649
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 453..471
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 112
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1200 AA; 139916 MW; E6D1213B364477B5 CRC64;
MGLCQSKEET LNEKKETQCT IQSYENNIKK SFQIMPEREF ESQVMPKESL ENIKDSRFCS
LIDPEQNDNT RVKICIDDFE ILKNLGKGSF GKVLLVRYKE NQQFYAMKII LKEKITNQKQ
KTHAITERYI LEKIDFPFIV QLHYSFQNKT KLYLAVDYMS GGELFFHLKK NKGMKFSETQ
TRFYAAEILL ALEHLHKNNI IYRDLKPENI LLDEKGHIKV TDFGLSKQIL NFKQHAHSMC
GTPEYLAPEI LLSGPQGHDK TCDWWSFGSV IYEMLCGAPP HYCEDKKLMF KRNCQVPIPY
PRQYFSDKAI SLLSQLLVVN PKKRLGYGEQ DAKSIKEHEF FNGIDFDKLL KKEITPPIDI
TKMNSFQFFD QNFVKQQPKD TPVDSSKYNF PKSIEQFPDF TYCREVLNNK DNSMAKKSSD
NSYDKLKTNE KQQSSIQNQI NSIKIQLNFQ NTDKDSLNNN RHSNNVNNNQ QHDEIQEEDE
EQNFSTKKNT RDLQSPLKLA SVLKNQSNLM KPQILVHSQT LNLQKDKENE NKQENPLIKL
EKNNSNLFHN SLQNDFNMKE QLAQKEQIEQ ENLYIGQEFH KLNIQNSEQN YNLMKSQDDS
IMNSVENSKL TPLNSNKSLS YVNSYKKKNN NQNKNKNQYN INSEQKQQNS LNKNQNMQNN
VQKNEFVLDT DFDDLSPNNI YNSESENGNV LNECKQSNIN KKKQQNQIQQ DQYLQQNINN
TKKNVILQND ENKDNSNNND TGSNQQENTN YAYKSSKEKS ESQQTLSLDY SKRKFQKVKL
SKKETDYTQD EKKTQTPVLE NFNQFFAENK LIPNGKKSEI ISEKEKWEYE QYFQNKKNNM
DKIKYLKNKT NSKSLSPMQT NKQDNLPWVE KYRPSKLEDL IAHESIVQTI EKFVDENRLP
NLLFYGPPGT GKTSTIIALA KQIYGDAYKS NVLEMNASDE RGINSVREVI KDFVSTSQIS
FKKVVGPRRP KLVILDEADN MTNAAQFALR RLIEKFSNNA RFCLICNYVS KIIPALQSRC
TRFKFRHLDL QQAKPRIQEI CENEGINCTE KGVIAAFALC EGDMRRVVNM LQSLSLSQSK
SKANVVIDDQ YVYNYTGNIT PQDIEQINNI LMTENIQNAY KLIKEMQIVK GISLQVIIKD
LNLFLIEVDM DTRMKEFIIQ RLADIEYRMS INGDEKVQLL SLIGAYVETR QTVDYNRQKN
//