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Database: UniProt
Entry: G0R5E7_ICHMG
LinkDB: G0R5E7_ICHMG
Original site: G0R5E7_ICHMG 
ID   G0R5E7_ICHMG            Unreviewed;       794 AA.
AC   G0R5E7;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   28-FEB-2018, entry version 31.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EGR27305.1};
GN   ORFNames=IMG5_198130 {ECO:0000313|EMBL:EGR27305.1};
OS   Ichthyophthirius multifiliis (strain G5) (White spot disease agent)
OS   (Ich).
OC   Eukaryota; Alveolata; Ciliophora; Intramacronucleata;
OC   Oligohymenophorea; Hymenostomatida; Ophryoglenina; Ichthyophthirius.
OX   NCBI_TaxID=857967 {ECO:0000313|Proteomes:UP000008983};
RN   [1] {ECO:0000313|EMBL:EGR27305.1, ECO:0000313|Proteomes:UP000008983}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G5 {ECO:0000313|EMBL:EGR27305.1,
RC   ECO:0000313|Proteomes:UP000008983};
RA   Coyne R., Brami D., Johnson J., Hostetler J., Hannick L., Clark T.,
RA   Cassidy-Hanley D., Inman J.;
RL   Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; GL984369; EGR27305.1; -; Genomic_DNA.
DR   RefSeq; XP_004024189.1; XM_004024140.1.
DR   EnsemblProtists; EGR27305; EGR27305; IMG5_198130.
DR   GeneID; 14903375; -.
DR   InParanoid; G0R5E7; -.
DR   Proteomes; UP000008983; 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   GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
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   InterPro; IPR001878; Znf_CCHC.
DR   InterPro; IPR036875; Znf_CCHC_sf.
DR   Pfam; PF00027; cNMP_binding; 1.
DR   Pfam; PF00520; Ion_trans; 1.
DR   Pfam; PF00098; zf-CCHC; 1.
DR   PRINTS; PR01463; EAGCHANLFMLY.
DR   SMART; SM00100; cNMP; 1.
DR   SMART; SM00343; ZnF_C2HC; 1.
DR   SUPFAM; SSF51206; SSF51206; 1.
DR   SUPFAM; SSF57756; SSF57756; 1.
DR   PROSITE; PS50042; CNMP_BINDING_3; 1.
DR   PROSITE; PS50158; ZF_CCHC; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008983};
KW   Ion channel {ECO:0000256|SAAS:SAAS00084808};
KW   Ion transport {ECO:0000256|SAAS:SAAS00502700};
KW   Membrane {ECO:0000256|SAAS:SAAS00502630, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00047};
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:UP000008983};
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};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00047};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00047}.
FT   TRANSMEM    212    237       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    249    271       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    283    303       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    323    341       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    362    383       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    438    456       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN      546    651       Cyclic nucleotide-binding.
FT                                {ECO:0000259|PROSITE:PS50042}.
FT   DOMAIN      680    696       CCHC-type. {ECO:0000259|PROSITE:PS50158}.
FT   COILED      456    483       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   794 AA;  95052 MW;  0E0581783ECCED8E CRC64;
     MLTEKPLKLE CIVKFEPFFQ KQGDNFVSCK ELELVNTKII QDLQISQNQI KVQLQEKLQQ
     KISFIDCKKE EDIYKNQIQV FSLGSEQLIR KEISKQITQF YQKQKNQLCK EINTQNDREK
     GNQIILNLLN NSENRIINIK NHVENFIKIL KNRYFQTKPI NLNHNDLSII NDKSYFLQKN
     QKQILFLQKI RKIINLLNIL GHIKVFMPTN RFLLFWNMLY CFIVSCFLYF YSILLFFNYD
     FEENIVSMRL FIVIICIFLI DILINFNTAF FQNDQLICYR KKIAFKYLQS FFFTDFLSSL
     VLFQKIIFQQ NNKCLVHNPE NELGLFLFDL IIFFKGFDIL RKKQNVECII TLKEYQKLIL
     KLIDLIILII VVAHLVCILW HGLGIYEEKY NFDISWLSKY SLVGQNWQIR YIYSLYWSIT
     TMTTIGYGDI TPQNPYEVFF VSVNMIFTSC LFAYSINNIG MILQEIEKQS KELNQNISII
     QRYLDRKNVN ANLKSRVRNY LIFLQEEQKD RDKESEDRIL DKLSNRLRDE ITQEINSNIL
     KKYNVFYENF TQQTIKKVIY IMNEILIQPN QVIFKDNEYD NQSIYFIQSG NIEIFHYNLF
     EKNHSVIKQL SSGDFFGEIS FFSGLPRKAS ARSLNLSTLY KIDRDQLIYI LNQNQTDFER
     FKMIQEQIVF QNDYSTIQMK CYSCKIPGHM AQNCPKLHQI FDKQFLILKN NFSQPQTRQN
     ISYQQFKKRK NIILSKQKTN NNNNNILYVR QLIKFNPDNI KKLKFNAQFM KSNIMALFES
     DEGDNEGTLY WIRK
//
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