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Database: UniProt
Entry: J9FWY2_9SPIT
LinkDB: J9FWY2_9SPIT
Original site: J9FWY2_9SPIT 
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
//
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