ID A0A0V0R7I0_PSEPJ Unreviewed; 1104 AA.
AC A0A0V0R7I0;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Cyclic nucleotide-binding protein {ECO:0000313|EMBL:KRX10444.1};
GN ORFNames=PPERSA_08746 {ECO:0000313|EMBL:KRX10444.1};
OS Pseudocohnilembus persalinus (Ciliate).
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Scuticociliatia; Philasterida; Pseudocohnilembidae;
OC Pseudocohnilembus.
OX NCBI_TaxID=266149 {ECO:0000313|EMBL:KRX10444.1, ECO:0000313|Proteomes:UP000054937};
RN [1] {ECO:0000313|EMBL:KRX10444.1, ECO:0000313|Proteomes:UP000054937}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=36N120E {ECO:0000313|EMBL:KRX10444.1};
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:KRX10444.1}.
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DR EMBL; LDAU01000027; KRX10444.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0R7I0; -.
DR EnsemblProtists; KRX10444; KRX10444; PPERSA_08746.
DR InParanoid; A0A0V0R7I0; -.
DR OMA; WICITAP; -.
DR OrthoDB; 180795at2759; -.
DR Proteomes; UP000054937; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR CDD; cd00038; CAP_ED; 1.
DR Gene3D; 1.10.287.70; -; 1.
DR Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR018490; cNMP-bd_dom_sf.
DR InterPro; IPR013099; K_chnl_dom.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR PANTHER; PTHR47823; ION_TRANS DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR47823:SF9; K+-CHANNEL ERG AND RELATED PROTEINS; 1.
DR Pfam; PF00027; cNMP_binding; 1.
DR Pfam; PF07885; Ion_trans_2; 1.
DR SMART; SM00100; cNMP; 1.
DR SUPFAM; SSF51206; cAMP-binding domain-like; 1.
DR SUPFAM; SSF81324; Voltage-gated potassium channels; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000054937};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 549..572
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 584..606
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 626..645
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 697..718
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 743..763
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 775..797
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 892..1000
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 95..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 158..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1055..1076
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 979..1041
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 8..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1055..1072
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1104 AA; 129948 MW; 5A180C079FD1345C CRC64;
MKKNKPELIN SKNNTQKSPK NSQLPQKSIL VIKKKQETNL DANQTFVNGN ESNQKQNKTP
KIQLIDQTNN ITLISGQQSL LSPDSLTEYF KQLGTETEES DDEYDYDGLT SSQEIKNDSQ
NDSYLRLNRN NKRVTLYDLE VLEKHILNEE MKKNNIDKNI NDGQKLKTSK SQNDNNLNKN
QGQNNNFLKV QNNYNNSKTN KLNQENQFKT KLKSSEDTSE NQNLISQNLQ NFSKSIQQSF
FKKTNINSDF DTAQRKNQIM ELDSNQILDK DHESTREFIN KGLNTQKQKT INTFSKHQKS
QNNFLKQNPQ DLNQNQDLDQ INEQNEYNEI DDIKLANSEQ YQERKNKSNQ QTLQEQNDPQ
YQIDKDIHIN QNKNQNIYSQ SNINIIKSED NINQYKYSQN LTKKNSKSEN LAPIQQNITE
QDMISQQIQD NQIQKESNIK QVQSIQPSNI LKNKKEILAN NIQKWRKATI KIVTIKQLSK
VISDIRKYGT NMSQDIGLTE NFLQKVKKQI ISKYKKKKTD QSKYILKHNL AQQQDNECQK
RQLKLHSKFM GFFYNYFLIF LYVWICITAP WLGFIWSHSE ISQGYVILFK IIDVIIFLDI
FLQLNLSYID KEGKIILLRS KIVRKYIFRG LILDFLSCFP FEWFFNQSEI LNTSQIRPEY
YNQYFKILKL PILYRRARNG KYFLDQVKFS SSSIFRFYRF ISNSLLGTHI AGCFYFFVAK
LSDPNQNWID HVDPERQLSE VDYYIFGLYW AIQTLTTVGF GDIMGFTDEE RIVSMLWMTF
GIGIYSYTLG AISTMIIETD SRMNNLEHGI ILLDEFCRET GINMKLKFRI KKALQFNTSK
TILSENEKEV FFEELDNRLK SDLSAQIFQN RMESNKRALP FIFSLTDDYN FLSKFIKYLK
PLQQKKGEIV YRKGEYPTDL YFITKGRVNF TLFKKNQAFR TFVQGSYFGE LEIFSKKKRL
YTVVCDTDCE FLTIQSDSYT NILDDFQDIQ KKIKNLAEKR AKIFLQNAQE KATKILEAKK
KQKEQNKKKF LAELAQEYQK NSNVSFPIKD LKESPVKKNQ VNQKEKENEF LMKKNLLPLN
SEESQNKLTT LEINSPSNLL QQSI
//
