ID J9J0I2_9SPIT Unreviewed; 1027 AA.
AC J9J0I2;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Cation channel family protein {ECO:0000313|EMBL:EJY78665.1};
GN ORFNames=OXYTRI_24173 {ECO:0000313|EMBL:EJY78665.1};
OS Oxytricha trifallax.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC Stichotrichia; Sporadotrichida; Oxytrichidae; Oxytrichinae; Oxytricha.
OX NCBI_TaxID=1172189 {ECO:0000313|EMBL:EJY78665.1};
RN [1] {ECO:0000313|EMBL:EJY78665.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JRB310 {ECO:0000313|EMBL:EJY78665.1};
RX PubMed=23382650; DOI=10.1371/journal.pbio.1001473;
RA Swart E.C., Bracht J.R., Magrini V., Minx P., Chen X., Zhou Y.,
RA Khurana J.S., Goldman A.D., Nowacki M., Schotanus K., Jung S., Fulton R.S.,
RA Ly A., McGrath S., Haub K., Wiggins J.L., Storton D., Matese J.C.,
RA Parsons L., Chang W.J., Bowen M.S., Stover N.A., Jones T.A., Eddy S.R.,
RA Herrick G.A., Doak T.G., Wilson R.K., Mardis E.R., Landweber L.F.;
RT "The Oxytricha trifallax Macronuclear Genome: A Complex Eukaryotic Genome
RT with 16,000 Tiny Chromosomes.";
RL PLoS Biol. 11:E1001473-E1001473(2013).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:EJY78665.1}.
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DR EMBL; AMCR01009391; EJY78665.1; -; Genomic_DNA.
DR AlphaFoldDB; J9J0I2; -.
DR EnsemblProtists; EJY78665; EJY78665; OXYTRI_24173.
DR OrthoDB; 52684at2759; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
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; IPR005821; Ion_trans_dom.
DR InterPro; IPR003938; K_chnl_volt-dep_EAG/ELK/ERG.
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; PF00520; Ion_trans; 1.
DR PRINTS; PR01463; EAGCHANLFMLY.
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 Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 215..238
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 258..277
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 376..401
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 426..446
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 458..480
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 569..660
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1027 AA; 119092 MW; 1FCA8945FB94150A CRC64;
MEELKQNGQR KRLSQLTEKN ISQITSRIGI TPRSGGGESP SQKPKMQFNS MMKYQNRQNQ
ALENKKKINQ TGGSDNFSPL SNVQKRSSNL ITINDASVRR KSMVGRLVDA IRGKPRESTY
FPQNDSSLNY LEQSIENESY DHPPLAQMSA LERRSYLLVQ WRRAFIMAHS CSRFLNVSQY
VKRKIEIFGK DLSKGYKRPQ EDGDQLEDRQ KLTMFLVMPH SIFNLFWCIV QILLQIYTAT
YMPYKICFDD EVNSGGSLVF EYFLDLMFGI DVLVNFFTVR QNQDGTQMTN LNDISRVYLR
STFILDVLCS LPSQVLEVGY DQNEGQKLSV TTSSSLRMIA KLYKVIRLVK FIYIWRRFKK
IRIIQVLKNK LKLSAAFFRM IFTLLTAFLS VHIVSCLWYL AAKYKNFSPE TWVVRLNKQD
QNPSRLYLEC LFWSLQTVAT VGYGNFGAST VPELLMSIIW MVFGVAFYSI IIGNLSLIIA
NESSSSQNLI DKMQSIDEFA SKTHMPDDLT YKLKAFLEKN YEDLYSHLDD HIFLKELPQA
LKDEIFQHRF HHLIDAFELL KNCPSKDFIK DCLQVMKRIK VDKDDVIYND GDLSEEIYFI
KKGTVKIYTK NGMPFIDFTD GQQFGEAEVV LSKTRDGKAV ALTDSVFYCL HKDDLEMILG
DHPPMVLFFE NLAEETSKSY VQKKEHVNKI TPIFGRKIFK EVSNEINFLD KSKLNKFGLV
NKKRFDSQTP LLPPQKRGLD KDLIIGNGDS TTKSAFSKGK KFNIFKDSKK QDFTKTQDPE
TNYQEEIKIN LRKKSSGQFL TSDIDNIQDI DSDYVKIVKK SNLNKKKKER LDTVLSKIDQ
EPEFTRSVAD LLQNEMVFQT NSNINTHQME TPKLKPRQDS SRIDSQGKIQ ELKTQFEKKN
KVSSRQSYDL HTSQFADQLS QAYQQSQNFD KSQALISTEK GKDIKILEEE EGDDLAEEGL
ENLAQFNQDM NMIARNVFEI YNLFDILEKD NQYAIERMHQ VESKTIELEE LQAENLKTIE
KLLNYDF
//
