ID J9FWY2_9SPIT Unreviewed; 1402 AA.
AC J9FWY2;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Cation channel family protein {ECO:0000313|EMBL:EJY82491.1};
GN ORFNames=OXYTRI_19896 {ECO:0000313|EMBL:EJY82491.1};
OS Oxytricha trifallax.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC Stichotrichia; Sporadotrichida; Oxytrichidae; Oxytrichinae; Oxytricha.
OX NCBI_TaxID=1172189 {ECO:0000313|EMBL:EJY82491.1};
RN [1] {ECO:0000313|EMBL:EJY82491.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JRB310 {ECO:0000313|EMBL:EJY82491.1};
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 -!- 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:EJY82491.1}.
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DR EMBL; AMCR01005861; EJY82491.1; -; Genomic_DNA.
DR EnsemblProtists; EJY82491; EJY82491; OXYTRI_19896.
DR OrthoDB; 52684at2759; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005216; F:monoatomic ion 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; 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 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 246..272
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 325..345
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 435..520
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT REGION 632..663
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 878..899
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 632..652
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1402 AA; 162976 MW; DF41C9155EEA7400 CRC64;
MGSRYRKLMS NVFNDQEPIN MSPGKTQFLA VKNRSMTRNA QNLGSNSNSN SQIKKNRALS
FSKLEQNIED LRLQIMDEKK KYKEGRRIFR QMTIQQSSEQ NKSRWNCFQS CKRNYNDDDS
SAGSISSNEC EDNARYFKKM NEQQKVKHMQ KQCAFEESDG SIQHRPDYIA KKYFRGWFFI
DVISSFPFQH LQVQKQGFDY QKLLRLFRLP RLFRMLRLIK VVKQLKFLRE NQFFEKFERK
IKSNSAILRM IQFMVGAIIN THIIACFFYL AAKFDDFGPD TWVARMKLQD KDQGDQYLYA
FYWSTQTVLT AGFGDIHAQT ELEMILSLFW MVFGVGFYSF IIGNYSSIIA GNIQIEASIS
LKIKSIKDLA KRAQIPFDLL LKIKKFIENN FESMYNQEEE SQLIKVLPPS LRDEVLSNTF
GEIIETIKFF KDLKDPDFLW KILPLLRPVK LEKGDTLYWR GDHAEDIYFV LKGAIKLYTE
RGYPYIRYEE GSFFGDSDTL LNLPRDGKAI AMTHLKMMVL KADHMFEKLF ENQEKNFMEM
IFNARKKRNH HLRLIQTANR KYRWLQKKRT NLYKNSSQKI KQQSMNPNNE SAYFNNIQGN
SLDIQTDKID QTDVQEKTSI FKKLKNTIFS SFQKGNQQSQ SVQNQTKNKN ENQNKINDND
ILESERKRQQ YFVMLRQKAF KNDQMIYGGF QQKNNSSKKK ERSQQLEAFI NIAERDKQLP
ASSLSIQTSL THTPKHIQST QLQQLTLIGQ SSSNFNDQHR ANMIQDFNNT EHTRNESGLA
AGGQISLSQL SRQLASKQMS EQLGSDLAIT PKALLNTSNL QTPSQRKQKQ NEKIELIKNM
NLMGNIVEIV ESRVIQLKQK IKVDLTVGQP EKNQLFGKLD QSENPQSIQQ TSQDQSSRLN
LKNNKEIKLT FAHNNRKFDS LTNSDLSSPE VKPEPQLQFN RQATVIEVSQ LGVTKPPQRQ
KQSTTLLDKV MASAFGDEEL SHVYSYFDVL NEINKDEDKY RDSSMKPKYT KSIQKRRAEF
KSAAGSSTII LKLSDKKVLN QSSASNLTRY YLKRSKVPLS PSIAMAKNSS LRRYSQQQQV
MPGKTIKTSK RAQKVLHETK ININILKPKS SEKTSSEYLT SDSEDQELTY KQIDLVNKTD
EMNDQNESNQ QFEVNETLQG QLGKINSFKL NDDPLFESSL FNEKVINTTL KQQNSQETIQ
SDKKIIQNGE IQKKTPFLEI ISKHIQVKAI KLLNRQIITS IQSNQNFLLN IILHSRQLFA
VKEEEPNSKL IHNSLNKYNP KLLLKKQETT LQGQWHLDLH LESLNNLVQL IRLQSLETYT
FDLNDIGQQV LFNIRGSVYC SQKKILNTTK CIKSQQFKGK PNLLTTIINI PSIKPQLQDI
LRFNDYCFSS KWDKNKFSAN IL
//