ID A0A0V0QUA4_PSEPJ Unreviewed; 2453 AA.
AC A0A0V0QUA4;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Protein kinase-like domain {ECO:0000313|EMBL:KRX05809.1};
GN ORFNames=PPERSA_02341 {ECO:0000313|EMBL:KRX05809.1};
OS Pseudocohnilembus persalinus (Ciliate).
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Scuticociliatia; Philasterida; Pseudocohnilembidae;
OC Pseudocohnilembus.
OX NCBI_TaxID=266149 {ECO:0000313|EMBL:KRX05809.1, ECO:0000313|Proteomes:UP000054937};
RN [1] {ECO:0000313|EMBL:KRX05809.1, ECO:0000313|Proteomes:UP000054937}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=36N120E {ECO:0000313|EMBL:KRX05809.1};
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:KRX05809.1}.
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DR EMBL; LDAU01000104; KRX05809.1; -; Genomic_DNA.
DR EnsemblProtists; KRX05809; KRX05809; PPERSA_02341.
DR InParanoid; A0A0V0QUA4; -.
DR Proteomes; UP000054937; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030553; F:cGMP binding; IEA:UniProtKB-KW.
DR GO; GO:0005216; F:monoatomic ion channel activity; IEA:InterPro.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00038; CAP_ED; 1.
DR CDD; cd14003; STKc_AMPK-like; 1.
DR Gene3D; 1.10.287.70; -; 1.
DR Gene3D; 1.10.287.630; Helix hairpin bin; 1.
DR Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR018490; cNMP-bd_dom_sf.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR001878; Znf_CCHC.
DR PANTHER; PTHR24345; SERINE/THREONINE-PROTEIN KINASE PLK; 1.
DR PANTHER; PTHR24345:SF0; SERINE_THREONINE-PROTEIN KINASE PLK1; 1.
DR Pfam; PF00027; cNMP_binding; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00100; cNMP; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF51206; cAMP-binding domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF81324; Voltage-gated potassium channels; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; cGMP {ECO:0000256|ARBA:ARBA00022535};
KW cGMP-binding {ECO:0000256|ARBA:ARBA00022992};
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:KRX05809.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000054937};
KW Transferase {ECO:0000313|EMBL:KRX05809.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00047}.
FT TRANSMEM 1134..1159
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1201..1223
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1244..1270
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1300..1320
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1332..1355
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 712..975
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1457..1572
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 1606..1621
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT REGION 199..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 355..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 527..556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1031..1051
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1897..1940
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2024..2045
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1810..1889
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 527..546
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1900..1914
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 741
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 2453 AA; 290604 MW; 3D9BD6DEBB3D7697 CRC64;
MKIAKYLNQS FIQDPYKKND AYKVKDFEQE GGFMLHTERR AKQKMQQYLR EKELQTIQKD
KNDTINVNYE NFYDDESKNY QQPGTQYQSP LQKQFQTHKG YYNSAKYLDK ENLNICQNDD
LDTQLEELFD KYLEKEENNS KPQKTIKFQK KNLNEFDALE YNQNYLNFSS NNKPQNNSHL
TKYQQQKMNQ KLMEIKQKYQ PTQKNNHLKR PSTGIKRPQT ASSNKQSINI QKGQLLAVGN
GLNSKINNQN FIDKNNFLDE NQNQQDCDMI WQQQNQELIN KYLPKQQQYQ HENQNNQSHV
TSTTDSPKID VENQLKNFGQ QKQYQKQKNE DKKSDSNQLM QVDDFDGFIA NQDVNNENYN
QNKNNNETEE ESNEQEKQKE IQKTIQVGVY RKKNRVQSFK NSDHNLSNQY DQEVEDMNED
EQNLKNNQLF NVYSKQKTYN PQQFNQKKNI HKIERPQTGC KRYPITQNYK GKISNLNSSN
NIHRNSCDKN SFNQGNKPVK KSDDLEKLVD GMFDKIAIKE FQDTHIEKNT ANQKNSEKEL
QHRKSNKNNR SPSKIQHLKG GVYETGHINY GNYYNQTKTK QIYGNKYNYK GNMVSGNIAQ
ILENQARLKK ERKPPVPRFS NPNQQLNIEK REQELEVQKH QLKHVQNIML GDPKKIDRNS
NKQLTFQAKR PTTALQRQSD KNNINNNKLG FINNLIGETF YKNSGGTGLD NYKIGQAIGK
GSYAVVKFAE NQVTNKKVAI KTYDKFKLID HNRRANLRRE IQLLQQIEHK NIIKLYETID
TRTNINLIME YIGSVTLRQY IKEQQDKRIS EDEVKVIFTQ VVDAINYLHS HNINHRDIKL
ENIMICPKTL NLKLIDFGFA IRSDSKLTIF CGTPSYMSPE IVKKQDYYGK PSDVWALGIL
LFAMLFGKFP FRGNNDSELY RKIGKCDLRI PQNSISGGAQ NLISKILKVN AKDRPTARDP
NQEHNSSLEL SEPLLQKNYS QNKFEYNSDQ ERYLEGASKS DFKYSRFQNK SYHQKYGQSI
SFSGKTQFSQ NFNQSAQKSR NRGKQKERNL EFLNNTNGKE IVYQAKSNVR NQKTEKEIKN
FKQILEKIFS DLLPNKEQKD PEYDMKAEKK ESRKMNFFDL FIFKLHPIKS ENQLIIFWEI
LVSFTYIVQF FQIPLVIFFK FGTKDRTYVN EASIAITNRS QIIQHYLKGL FILDTVVLVS
YILQFTIIAQ WFPLIYLVFY LKIENLSKFN QKILRMFQLH RKLKAIYLLL RLMLVVMIIS
HLFASLYYAI HDYVYFNMPN TQTWVTDCDV SPDLIDEPWY VKYAFALYWA VTTMSTVGYG
DVHPVNNYEI TYATFAMLNS CIFFAYAINS IYQIFENTRE GQKRYERNYD AIGRFMRDKQ
VEKKLQLQVG AFLEFNNKEK NRERDVEEQV IKSLPPVLKN KLIYRVYGKN FLGRVPWLKQ
QNIPKENYQN PNFNKKSLYI FSKDFLYELS NQVEEQYYSK DEIVYSVNDR YDQNDDDYSH
SFYFVAKGEF QECFDNFPLY NNGQGINLRS YKLNDWFGDL EFLTGENRRF SIKATNYSLV
YKISRSNFLE TLKDFPDDYE KYCNLRDQLM FSKMNKDKFQ KLQMQCYFCG YKNHLANRCP
KTHYYITPAK YQFICKEYDI KQVQNQRIQY LNEMESFLQK ESSSEFDIQD NYDSEQDIFY
DSEEKRKNSS TRKKFKFLNS DSHKTQQNYE YDEDESELDE EDDFDEKLYN EQISFFNQKQ
SDENWQSNDQ MGKNQDFQIQ NEIELNEEEN ESDSSSLDKK KAIDFQQIQS LQKISDFKES
SESPQKGNQK FNLNQENQQL IEEKIQENQQ DQNKNMDELD LGKIKLVQSQ QLKQSEEIKI
LENQKQFLNQ NSNENIITYR KTKDILENEN NKIKKMSYDS VKNKSQMSLS KISKKSKQSK
NESKISLEKQ RSLPATGFKK NLKKKSADTI LDNYNMPKMS IGAQNMFQKM NKNQDYNYAQ
NFSEKQKKQS QFLQKKIKNY NLRRIGTSYL SSQSDENEEK NIQVQNQKEE QVQNIQNRKR
SSTNRVQQRF LKGSFNEDDE GQKIDKNKGK LSYFKQTGRK MTQDGLNDSQ NLQKKSFQSK
IQKHKKSQIS QIEEVEDRYL ENQVNQQKLQ FLKQQKCLEN QFNNYKSTIN NIGNVNGNLY
DDILNHKKFQ YAKHLSTMMQ LDDQNKFLNS SIQNKNQMSN QQMKYPEQFQ HLEQAQNLNF
IQPRKRVHKQ SANLTNIQAQ QQVQQQPQSQ LQAQQQIQLD QDGKTQIVKH LAQQLVSLLN
GQNDDKQNQN YYQQYQQINS QQIPYQKEEN FNNNNFNNNN NNNNINNNIN FDHIVDYLDY
NDLLFSEYGY QNIREPVNLD IDIQQDYGTY CQADNIKLVL KRYGKQRKHN LYQNFSNASI
GFPSRAKIMK NSNLFISKNS SFGKGFSSFN HEKIQNYNNN INASNKSKTN NNK
//
