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Database: UniProt
Entry: J9HXG5_9SPIT
LinkDB: J9HXG5_9SPIT
Original site: J9HXG5_9SPIT 
ID   J9HXG5_9SPIT            Unreviewed;      1261 AA.
AC   J9HXG5;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=Cyclic nucleotide-binding domain-containing protein {ECO:0000259|PROSITE:PS50042};
GN   ORFNames=OXYTRI_14712 {ECO:0000313|EMBL:EJY65138.1};
OS   Oxytricha trifallax.
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC   Stichotrichia; Sporadotrichida; Oxytrichidae; Oxytrichinae; Oxytricha.
OX   NCBI_TaxID=1172189 {ECO:0000313|EMBL:EJY65138.1};
RN   [1] {ECO:0000313|EMBL:EJY65138.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JRB310 {ECO:0000313|EMBL:EJY65138.1};
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:EJY65138.1}.
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DR   EMBL; AMCR01021656; EJY65138.1; -; Genomic_DNA.
DR   AlphaFoldDB; J9HXG5; -.
DR   EnsemblProtists; EJY65138; EJY65138; OXYTRI_14712.
DR   OrthoDB; 52684at2759; -.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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; 1.10.287.630; Helix hairpin bin; 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; PTHR10217:SF435; POTASSIUM VOLTAGE-GATED CHANNEL PROTEIN EAG; 1.
DR   PANTHER; PTHR10217; VOLTAGE AND LIGAND GATED POTASSIUM CHANNEL; 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        252..272
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        293..312
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        389..410
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          568..669
FT                   /note="Cyclic nucleotide-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50042"
FT   REGION          166..197
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1032..1055
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1261 AA;  146690 MW;  4E80D0DC7747D001 CRC64;
     MFGSKKNLSF YQSNNHLGAN LITPTARKKI GSIISNKTVK DLLMKHQMGG GGIGTPGLKF
     MNQQRKLSNI QDSYMNQNSI AGMSQSDFDY TQGMMTVRHK NNVVNHQDFG SSYAYSQEPG
     GMYDSPALHE MNQFDNSRHE NNMMNRATAL NNNREQITRN VSELKKIKKK KKNQKRQDSF
     RSRKSSTTVL HRNRKSKGGL SRITNILRNV TFKKDFETTS NGSDTDQEEE DPMQILIAIL
     VPFNMSFGLQ DFPISALILL EIIMIFDIFV IMNCGYYTKG MLIMQRNLII KRYLRSWFIL
     DFLAAIPAYS IYRQILKENI LMSSDQLLTG NHLQEIQKNK VEFSYYRSQV LSFLFLQFMK
     VLKIIKFTDL QSRVYDFIMT EVGEIFFKAF KLSFLIFMVA HWLGCFFWLI GGTQDHISAE
     TWIRPYLDLS LDEQYVNSIY WAITTMVTVG YGDIHPTNTY ERLATIVNML VASGMYAYII
     NEVATMVRLY NTLATKYEES MKYVNKFMKQ KGIPEDLRTK IVRYLEYNWE QKKKIKIEER
     EVYGLLNENL RDKITLYLNG KILRNIQIFE SFSIEFISRL TFVFKKQSFA VDEIIFNEDT
     IGQDMFFISS GKVYIIHKKT MSFVKELYKD DHFGEIGFFS DLPRQATIKA RDYTDTMILS
     KENFLKVAGD DFLALKLKGN LIPLIVKSEI QKFREEQNQN IFQMLTKSKN QKKPKNNANR
     FFQKRVQGNG TSPKGDKFEN SQRGLLKDIK DQNKNQEFEH LTEDKGDNFH QQSNSFDFNN
     EDKLREHIQM QLLRKNQEYN KVPHNSIKES LDSEYQISSD SQSRNIKKTT NSLDFNYEIQ
     ANLLDRQRVN AIRIEQLSQA NSFQFISQGT FINNNSGDEL NQYTAKNQPF KRRTHKISFN
     NDISQNQIIE ENSSSSSSIG AQKRIIAKSK KVLKTVTQKF SSLRNDRVPI DDLLRMSGEV
     IPQQQKNRDL DSPFKKIISP KKPSKIEKLV ESSLETENMD GIENFEMEID KLLLNDLKNE
     EQIMNEINML TTPKKTPQKK NEDQVSGLQN SNQREIISPL LRNNLTNNRP QTEDRINEQV
     LQQNEPKIAK NYTRLLREKT RTTEVNLQQM QTKSKNIHRN IKKRPKASRI QQKDLFSNKF
     FVEDFLEDIN SATILESENL NQIETPKSGL KYAKYNSTNM YQQPLAFKRT LSNKGNIGVN
     PFNFINQSRT SHNQNLKVNI SRFGLGDSSP LNSSIENLNQ IDDQNETDSQ DELMKSIEKA
     Y
//
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