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Database: UniProt
Entry: J9IUC0_9SPIT
LinkDB: J9IUC0_9SPIT
Original site: J9IUC0_9SPIT 
ID   J9IUC0_9SPIT            Unreviewed;      1442 AA.
AC   J9IUC0;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   30-AUG-2017, entry version 27.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EJY83389.1};
GN   ORFNames=OXYTRI_18989 {ECO:0000313|EMBL:EJY83389.1};
OS   Oxytricha trifallax.
OC   Eukaryota; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC   Stichotrichia; Sporadotrichida; Oxytrichidae; Oxytrichinae; Oxytricha.
OX   NCBI_TaxID=1172189 {ECO:0000313|EMBL:EJY83389.1, ECO:0000313|Proteomes:UP000006077};
RN   [1] {ECO:0000313|EMBL:EJY83389.1, 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:EJY83389.1}.
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DR   EMBL; AMCR01005017; EJY83389.1; -; Genomic_DNA.
DR   EnsemblProtists; EJY83389; EJY83389; OXYTRI_18989.
DR   Proteomes; UP000006077; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   Gene3D; 2.60.120.10; -; 1.
DR   Gene3D; 4.10.60.10; -; 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   InterPro; IPR001878; Znf_CCHC.
DR   Pfam; PF00027; cNMP_binding; 1.
DR   Pfam; PF00520; Ion_trans; 1.
DR   PRINTS; PR01463; EAGCHANLFMLY.
DR   SMART; SM00100; cNMP; 1.
DR   SMART; SM00343; ZnF_C2HC; 1.
DR   SUPFAM; SSF51206; SSF51206; 1.
DR   PROSITE; PS50042; CNMP_BINDING_3; 1.
PE   4: Predicted;
KW   Complete proteome {ECO:0000313|Proteomes:UP000006077};
KW   Ion channel {ECO:0000256|SAAS:SAAS00091826};
KW   Ion transport {ECO:0000256|SAAS:SAAS00502700};
KW   Membrane {ECO:0000256|SAAS:SAAS00502630, ECO:0000256|SAM:Phobius};
KW   Potassium {ECO:0000256|SAAS:SAAS00807593};
KW   Potassium channel {ECO:0000256|SAAS:SAAS00807732};
KW   Potassium transport {ECO:0000256|SAAS:SAAS00807568};
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:SAAS00807693}.
FT   TRANSMEM    452    472       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    484    504       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    516    540       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    599    620       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    675    693       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN      780    876       Cyclic nucleotide-binding.
FT                                {ECO:0000259|PROSITE:PS50042}.
SQ   SEQUENCE   1442 AA;  168165 MW;  FE9C56D9EBCA51E3 CRC64;
     MQQYNSNKIP ENILEATNKL ITAKSKYDNG LLQRRQTRLF NYLHLQNNPD PLNQARSQHN
     NNINYINTQN SQIPQANVLG GILKNSHLNT VNNSNGVLQQ TSSQNISNNK QSDKGLILPT
     QTHSNATLQN NNYTQQYHSG NEQVGIGYIG QHLTQNNYSS NYQIQTKSDQ LLNSRITREN
     INDQTAFDND ISMLSVDENR GMLGSRSRGS ENNNFNFNTG IDPFNKNYYD QQQEQQINAK
     NRHSIIDVET NNHVLDIEEV NRNKRILRDY FKDQIKEQRR LTSSKLLVIN KFKKGLFSKQ
     DSLTKAIQQQ SAAAIRRSSV KNLTALLQGN EIPISPTKKV HKSMKKFFQQ KISKNQRDQK
     LNISNIWNQS QKPSQKIEDE NSYLDSNFTS QSSKIKHKKT MFQNAIDFMI QPKEEQAEDG
     INESQIRMIN RRSQNSCMIL YPDSNMRSLV DATSFALMII ISIYIPVVLA FNVDTSGSFD
     YFELFIDVWF LTEILFNFIT GYYHKGILIL ERSKIIWSYL MSWFFIDLFS SLPILIIFII
     SKDDAGNYQA VRSAKLLRIV RFARYARLIR LIKFLRLNKY LQPFEELIVT DYAHLGVRFL
     KITCAVVFIA HWAACVIYMI GVNDFNDQGT NWLTLQNLND SSIFEQYINS LYWTITTMCT
     VGYGDFHPVT SNERVISMVI MIISSGVFAF IIGDISRMVS SFNFLADQFR EKMIYVDKFL
     KQKYIPLNIR VQVKRYLEYN LQLKKHYKIE ERDVLGLLNE DLRTKLKVYF NGKILQNIDV
     LKKFPMEFLS NLSFILRKEI YIVDDNLIIE KENGDEMFFM QTGRVAVIHK KSKTHIAELE
     MEKYFGEIGF FTDLPRQSTI KARDFTEVLI LKRDDFLIMA RNIQSDASLA LFLRIRQSVA
     ENSKDMKLLM IKCYICNVIG HIAINCKQFH RLKGNLKRYL KKRYNTDHYQ TEEGFDNQMP
     QIKIVENPLL VSLESQENRN RKVSKKARKI KPPRKRMSIK KLQVRRNVSP KRTRTDIRDL
     DPVSKISNTN LVINLHFNDC VSSFIQSENQ TSVGDPQQNN FFEDVPQIHL NSGNIQSQKS
     LSDSDQSRLS VTFANLQNLN QYHKELSQVS SAPKLVENDF DGNLIPNMVH FDTPRKEQTN
     PKLLKRIQTK TKNQLKRKRS VKSKLREEVI QEDLLEDYQS SNNNENSVSS KESSSQSLRN
     HSRFQLNLSE RMNDNFINQQ NLCKEIQDTL SHDSQEEIQN SNNEEEKQPL IFKQKTIKSR
     AELITDDINQ LSKIVGQRKR FDSIEREETQ AQNLSRRQST FKLKRKIFIK PMVEISRKVS
     RGDANNLHKF NESLGSDLMQ TNNSRFYENY NQSTPQRREK KVFEDKYSEL IQSSIVSQNI
     DKTKSKKKLK EHLIQNSFKS AYSNIKSSYH SFKFDDQNKR KSIIKNQHNP NMIQDSLEGL
     DQ
//
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