GenomeNet

Database: UniProt
Entry: A0A0V0R9N3_PSEPJ
LinkDB: A0A0V0R9N3_PSEPJ
Original site: A0A0V0R9N3_PSEPJ 
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
//
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