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Database: UniProt
Entry: J9J394_9SPIT
LinkDB: J9J394_9SPIT
Original site: J9J394_9SPIT 
ID   J9J394_9SPIT            Unreviewed;      1329 AA.
AC   J9J394;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   25-OCT-2017, entry version 29.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EJY87384.1};
GN   ORFNames=OXYTRI_03887 {ECO:0000313|EMBL:EJY87384.1};
OS   Oxytricha trifallax.
OC   Eukaryota; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC   Stichotrichia; Sporadotrichida; Oxytrichidae; Oxytrichinae; Oxytricha.
OX   NCBI_TaxID=1172189 {ECO:0000313|EMBL:EJY87384.1, ECO:0000313|Proteomes:UP000006077};
RN   [1] {ECO:0000313|EMBL:EJY87384.1, ECO:0000313|Proteomes:UP000006077}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SB310 {ECO:0000313|Proteomes:UP000006077};
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.,
RA   Fulton R.S., Ly A., McGrath S., Haub K., Wiggins J.L., Storton D.,
RA   Matese J.C., Parsons L., Chang W.J., Bowen M.S., Stover N.A.,
RA   Jones T.A., Eddy S.R., Herrick G.A., Doak T.G., Wilson R.K.,
RA   Mardis E.R., Landweber L.F.;
RT   "The Oxytricha trifallax Macronuclear Genome: A Complex Eukaryotic
RT   Genome with 16,000 Tiny Chromosomes.";
RL   PLoS Biol. 11:E1001473-E1001473(2013).
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EJY87384.1}.
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DR   EMBL; AMCR01001327; EJY87384.1; -; Genomic_DNA.
DR   EnsemblProtists; EJY87384; EJY87384; OXYTRI_03887.
DR   Proteomes; UP000006077; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
DR   CDD; cd00038; CAP_ED; 1.
DR   Gene3D; 2.60.120.10; -; 1.
DR   InterPro; IPR018490; cNMP-bd-like.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR003938; K_chnl_volt-dep_EAG/ELK/ERG.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   Pfam; PF00027; cNMP_binding; 1.
DR   Pfam; PF00520; Ion_trans; 1.
DR   PRINTS; PR01463; EAGCHANLFMLY.
DR   SMART; SM00100; cNMP; 1.
DR   SUPFAM; SSF51206; SSF51206; 1.
DR   PROSITE; PS50042; CNMP_BINDING_3; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000006077};
KW   Ion channel {ECO:0000256|SAAS:SAAS00904115};
KW   Ion transport {ECO:0000256|SAAS:SAAS00502700};
KW   Membrane {ECO:0000256|SAAS:SAAS00502630, ECO:0000256|SAM:Phobius};
KW   Potassium {ECO:0000256|SAAS:SAAS00903208};
KW   Potassium channel {ECO:0000256|SAAS:SAAS00904256};
KW   Potassium transport {ECO:0000256|SAAS:SAAS00903350};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006077};
KW   Transmembrane {ECO:0000256|SAAS:SAAS00137614,
KW   ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAAS:SAAS00137754,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|SAAS:SAAS00502637};
KW   Voltage-gated channel {ECO:0000256|SAAS:SAAS00903851}.
FT   TRANSMEM    355    373       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    427    446       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN      533    632       Cyclic nucleotide-binding.
FT                                {ECO:0000259|PROSITE:PS50042}.
FT   COILED      137    164       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   1329 AA;  154390 MW;  F818DECD480EC6CE CRC64;
     MQTPINITTL RVPNTPQVQR KILHNLITDE RMMQATGLRS PMVNQKRRDT LVSMGQNPPF
     AKQTSIAGQS QRMSNHGGGQ IPRISNSNSV ANNRRKNFIA SSQLSMDIHS NADYIAPQQV
     NLQQNQEQIN RNVRALKAVF KDQKKDKKKE KQKLENQVVK RKTNLQNKKT GVLDGGIQRK
     KTGKSLGQID RKHSMSSIFT NNKSKNGETQ SRGSQSSDED DDQQFQNLKR RINRSTFKEI
     SIMSLYAECI IEVFFYVDVF MCFNTGFYDK GVLIMNRKLI AKKYMHSTLI VDILSNLPIN
     FLLVFKDFTI LDHQTLNLIR VVKLFRIYKM GFFGQKIFDY IASDFLNLIV NFTKMMFNIL
     LIAHWSACLF YFAGTVSSNE HNNTWLKDQG LIDTSDVEKY VNAMYFSITT MTTIGYGDIK
     PQNSQEYMIV CFLELLAGIT FAYMIGKIGS LFQRYNLLAV TYKEKVQFVL QFLTLRNIPK
     ELKLKIKRYL DYNLEMKKDL KIEEEEVYGF LNEDLKSKLT VFMNGKILKS VSVFSEFPLE
     FLSNLTFIFI KKSFSTEEYV FNEGDDGKDI YFITQGKVCL IHRQTYTYII DLEKEQSFGE
     IGFFSDCQRQ VTVKSRDYTD VLTVNLIDFL NIANTFSEHA ITIYHKINSS IDTWKKDFST
     LKIKCYICSS SKHISIDCPQ FKNKMKGNIA NFIKQQTKKG DTMDGSDVTQ RTPHRYRSTT
     KMPVVSPALS RQITYKVRDE LGAEDRLGNW RSIINLQPLK IERLSQFHHN LDNQMEMIED
     YMIDEDNNIN NNQPNFRDEF SSQSSFDDSG NQDDLRQYHI DIDEIPHDQP EYFQYELEMQ
     TINESQDLQL AEIEEIKEEN ESLYSEHDDY TRTRRRGTLG GFDQGRAKYH KMKKESKNEL
     SQQNLSQNRF KKSQTHLELT SSSFAQNSKN SFQTPQTPDV ILPIHAERYG EVQKVVYKDI
     EKNSNNNFKN QESRTSKNKN SNYQSNIFDE EKYRRIDQNS ESQFNHIEQQ SGRKKSSNTI
     TITPKNLNST VKKLRDFERV ETKVKFENDY EKKQSTKRKM GDSMEQQLQD LSVSSDNGGL
     DQPVSSDDGS STMSYKNHKN KVFSKQKIAM AIKPIVGIKK RQHRNLNRAF QNDEYTIHED
     DNSQQSKKQW QQSDSKKRRA ENISSQNSKN KFTKMLSDSS ESQYKIRTYP RQKSQEKVLS
     SRHSKHYRSI NVIKPTDEQE DDVYGQSNQI NNQRFQINSV GTSSPDNSIV NQLNINHSNN
     NNQMEDPMEF QFQNFVNFRI TMADLENDDD TSSNQSAAVA SHQNQTLLEN IGNQERTNLP
     RINTGDPCQ
//
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