ID A0A0V0QNN4_PSEPJ Unreviewed; 802 AA.
AC A0A0V0QNN4;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 28-JUN-2023, entry version 24.
DE SubName: Full=Protein kinase-like domain {ECO:0000313|EMBL:KRX03961.1};
GN ORFNames=PPERSA_12408 {ECO:0000313|EMBL:KRX03961.1};
OS Pseudocohnilembus persalinus (Ciliate).
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Scuticociliatia; Philasterida; Pseudocohnilembidae;
OC Pseudocohnilembus.
OX NCBI_TaxID=266149 {ECO:0000313|EMBL:KRX03961.1, ECO:0000313|Proteomes:UP000054937};
RN [1] {ECO:0000313|EMBL:KRX03961.1, ECO:0000313|Proteomes:UP000054937}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=36N120E {ECO:0000313|EMBL:KRX03961.1};
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 -!- SIMILARITY: Belongs to the protein kinase superfamily. ADCK protein
CC kinase family. {ECO:0000256|ARBA:ARBA00009670}.
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:KRX03961.1}.
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DR EMBL; LDAU01000122; KRX03961.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0QNN4; -.
DR EnsemblProtists; KRX03961; KRX03961; PPERSA_12408.
DR InParanoid; A0A0V0QNN4; -.
DR OrthoDB; 668390at2759; -.
DR Proteomes; UP000054937; Unassembled WGS sequence.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd13970; ABC1_ADCK3; 1.
DR InterPro; IPR004147; ABC1_dom.
DR InterPro; IPR034646; ADCK3_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR PANTHER; PTHR43851; -; 1.
DR PANTHER; PTHR43851:SF3; COENZYME Q8; 1.
DR Pfam; PF03109; ABC1; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000313|EMBL:KRX03961.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054937};
KW Transferase {ECO:0000313|EMBL:KRX03961.1}.
FT DOMAIN 444..683
FT /note="ABC1 atypical kinase-like"
FT /evidence="ECO:0000259|Pfam:PF03109"
FT REGION 62..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 137..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 279..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 315..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..92
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..182
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 802 AA; 93956 MW; 4F6F0607E0AF06C1 CRC64;
MKKLIQTVSD SQNLKDATAI GRGLYRCVQG LSETHSNSVS NAFFEEQKQY MTQDIKEKAD
TLKQKKQAEN NNKNQSEQQK QAKEHAKEFQ SLNYKSQEKV AQEYQDYQNK LYEEMKQKAF
NQMSEIRKEQ ELKNKKIQEK IQKQDSQQDL KTNQYQQQQK EKILNQNISK QESNQYQQAK
DKTIQGEQDK QKIQENVEKT EKAEKSQFQQ MNEEASQNIF DSVDNKSQNQ SELEKIQKEV
KNKKLDYDLS KYQSIKENYV PQYENTFKVK NPLEGLNFQQ RKKQQQQEAQ KNQDKNQNLS
ENLENNQDKK FAFQNLEKQD KNNQKNDLKK EKVEEENELD FDEVFGYQGQ VGREQKVPDG
SFSRAYNFGI LGLNLAGSTI SSWVTSPFSK EKPKSHIFNE KNAAKISDNL CKMRGAALKI
GQFLSIQDDS MVPKEIKMAF EKARKSADIM PKSQLYYMLE TELGENWKDN FLKFDEMPIA
AASIGQVHRA QLKNGKFVAI KIQYPGVKES IDSDLNNFKR VFAWTGLAPK SMFIDQMIAN
HRVELLEECD YKSELLKQDH MRNLVQEDRR YYVPKIYEEL STERVFTQEF IVGDSFEKIC
NSYSQEKRNE IGSRIMNLTL QELFDWHYMQ TDPNPSNFFF NEKKDVLYLL DFGACHTYSE
EFMDGYIELV HGAIQNDIQT IVDKSIQLGF LNGKEAKEMV DAQIKTIQSV AEPFMKNEEF
NFHGTDITSK TKGLMPVIMK YRIKSPPPET YSLHRKFSGA FLLNIRLGSK INCHKQFMDL
YQKHQQKKKL KSQQQKQSQN LQ
//
