ID A0A0V0QXB4_PSEPJ Unreviewed; 803 AA.
AC A0A0V0QXB4;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Protein kinase-like domain {ECO:0000313|EMBL:KRX06836.1};
GN ORFNames=PPERSA_11481 {ECO:0000313|EMBL:KRX06836.1};
OS Pseudocohnilembus persalinus (Ciliate).
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Scuticociliatia; Philasterida; Pseudocohnilembidae;
OC Pseudocohnilembus.
OX NCBI_TaxID=266149 {ECO:0000313|EMBL:KRX06836.1, ECO:0000313|Proteomes:UP000054937};
RN [1] {ECO:0000313|EMBL:KRX06836.1, ECO:0000313|Proteomes:UP000054937}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=36N120E {ECO:0000313|EMBL:KRX06836.1};
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Folate-
CC biopterin transporter (TC 2.A.71) family.
CC {ECO:0000256|ARBA:ARBA00007015}.
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:KRX06836.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LDAU01000091; KRX06836.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0QXB4; -.
DR EnsemblProtists; KRX06836; KRX06836; PPERSA_11481.
DR InParanoid; A0A0V0QXB4; -.
DR OrthoDB; 191528at2759; -.
DR Proteomes; UP000054937; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR039309; BT1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR PANTHER; PTHR24347:SF412; CALCIUM_CALMODULIN DEPENDENT PROTEIN KINASE I; 1.
DR PANTHER; PTHR24347; SERINE/THREONINE-PROTEIN KINASE; 1.
DR Pfam; PF03092; BT1; 2.
DR Pfam; PF00069; Pkinase; 1.
DR SUPFAM; SSF103473; MFS general substrate transporter; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Kinase {ECO:0000313|EMBL:KRX06836.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Reference proteome {ECO:0000313|Proteomes:UP000054937};
KW Transferase {ECO:0000313|EMBL:KRX06836.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 592..611
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 617..638
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 688..710
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 187..437
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 216
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 803 AA; 93389 MW; 09B00C1E23C25307 CRC64;
MEGIMPNYQR YCQTQRNAQQ TINFESNNNK NELQQRFSLN LPQKDNNIKK LQKNNHLSST
QFNLKNSFQQ PSPQQNYLKQ NQIPQKKYSQ QLLEKNYLVE NNTQNQRSDY MMQKQNYQFF
KKTQNETKKK LNKTLNSSPE IIENIFDDKC DQFNLSLKLQ KIQSGESVLT NISQNQEIIQ
DKFQQNYLEF HQIGEGMHGI VKVCQNKFNG CEYVVKLIKS KDPEIIQAVF EEYQILQSLN
HPSIVKAIDY FHNEKRGHIR LIMEYIQYPN LAEYLQKQKT IREEQIKNIF YKLLNAIKYI
HQKQISHRDI NPSNILIDIQ NQDIKLIDFG IAKNFQQKLW TPTGTPSYKA PEILRSEPYT
EQVDIWSAGV VLYQCLSGKL PFQSDKSLAK MQNGEFDIQT GIWQNISNEA KNLIYFMLKP
IASERPTSHQ VLSHPWFFNC KFQDIKQQVS NFDKIGLFQQ KPLKLQISIS NQEQKNQENN
LISPKEIKYQ YSSGKKANNK FQSKFLNQEN QQPSSETQPN KTRIFYFESP SILKKSKYTQ
KTFSDKRTIQ DFQLSPSQLQ IVNGLIHIPF VLKPFLGFFT DTYPILGYRR KPYLIMCAII
AFICWNLEAF VVQKNNINLG VFCIFIIKIT TSFKSVIAGK YNLENKNDKY KVSVFFFIDA
IIIEVSQKRS KVQDLNLSEQ QKDAGKNVSI YFIAKYSGII LTAQLGGFLL EIMDKHTIKA
SQIMLVTGHN LEIGIPNKIF CLSDSLIIEV FYQVNILPML ILACQLCPKN IEGTVYAIIM
SAINFGGLLG QQIGGTYYDF GII
//
