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Database: UniProt
Entry: A0A1E4TJ14_9ASCO
LinkDB: A0A1E4TJ14_9ASCO
Original site: A0A1E4TJ14_9ASCO 
ID   A0A1E4TJ14_9ASCO        Unreviewed;       990 AA.
AC   A0A1E4TJ14;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Cyclic nucleotide-binding domain-containing protein {ECO:0000259|PROSITE:PS50042};
GN   ORFNames=CANCADRAFT_30072 {ECO:0000313|EMBL:ODV91736.1};
OS   Tortispora caseinolytica NRRL Y-17796.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Trigonopsidaceae; Tortispora.
OX   NCBI_TaxID=767744 {ECO:0000313|EMBL:ODV91736.1, ECO:0000313|Proteomes:UP000095023};
RN   [1] {ECO:0000313|Proteomes:UP000095023}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL Y-17796 {ECO:0000313|Proteomes:UP000095023};
RG   DOE Joint Genome Institute;
RA   Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goker M.,
RA   Salamov A., Wisecaver J., Long T.M., Aerts A.L., Barry K., Choi C.,
RA   Clum A., Coughlan A.Y., Deshpande S., Douglass A.P., Hanson S.J.,
RA   Klenk H.-P., Labutti K., Lapidus A., Lindquist E., Lipzen A.,
RA   Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J., Peng Y.,
RA   Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C., Stielow J.B.,
RA   Sun H., Kurtzman C.P., Blackwell M., Jeffries T.W., Grigoriev I.V.;
RT   "Comparative genomics of biotechnologically important yeasts.";
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; KV453841; ODV91736.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1E4TJ14; -.
DR   OrthoDB; 1330350at2759; -.
DR   Proteomes; UP000095023; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0034220; P:monoatomic ion transmembrane transport; IEA:UniProtKB-KW.
DR   CDD; cd00038; CAP_ED; 2.
DR   Gene3D; 2.60.120.10; Jelly Rolls; 2.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 2.
DR   InterPro; IPR018488; cNMP-bd_CS.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR018490; cNMP-bd_dom_sf.
DR   InterPro; IPR036047; F-box-like_dom_sf.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR006553; Leu-rich_rpt_Cys-con_subtyp.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   PANTHER; PTHR45638; CYCLIC NUCLEOTIDE-GATED CATION CHANNEL SUBUNIT A; 1.
DR   PANTHER; PTHR45638:SF11; CYCLIC NUCLEOTIDE-GATED CATION CHANNEL SUBUNIT A; 1.
DR   Pfam; PF00027; cNMP_binding; 2.
DR   Pfam; PF13516; LRR_6; 2.
DR   SMART; SM00100; cNMP; 2.
DR   SMART; SM00367; LRR_CC; 8.
DR   SUPFAM; SSF51206; cAMP-binding domain-like; 2.
DR   SUPFAM; SSF81383; F-box domain; 1.
DR   SUPFAM; SSF52047; RNI-like; 2.
DR   PROSITE; PS00889; CNMP_BINDING_2; 1.
DR   PROSITE; PS50042; CNMP_BINDING_3; 2.
PE   4: Predicted;
KW   Ion channel {ECO:0000256|ARBA:ARBA00023303};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW   Ligand-gated ion channel {ECO:0000256|ARBA:ARBA00023286};
KW   Reference proteome {ECO:0000313|Proteomes:UP000095023};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          88..205
FT                   /note="Cyclic nucleotide-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50042"
FT   DOMAIN          273..374
FT                   /note="Cyclic nucleotide-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50042"
FT   REGION          1..67
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          434..461
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          477..533
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        15..40
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        510..533
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   990 AA;  108278 MW;  11E65C8F874C0A9B CRC64;
     MRSDSGRRGP RKSHTRGYSN ASSTYDRHSI SINSNAYYRP TDPGSGVVKP RRSSSDPKLY
     APIRPSPLST ASNGMPLEIF ERISEFPLFK SAPESFLLEV AGKLRPHQAG PGDSIIIEGT
     EAKAMYWIVR GSVSVSSRDG ESIYSTLQPG SFFGEIGILF NCPRTATVSA QSRCLLVVLT
     AEALHSILPS YPDVEKSLRN EAEVRLVLTQ KFKDRKKGRL SSDISSSSLT DSNDGHSQTA
     MANVSSFTDS EIPGKPIFLH VSQVTSRLKE SPLFSHLPDD ALHSLALAVE PRRFGPFEVI
     LQEGTRGQAI YFITDGEVEV IRQGLLKALS RLGPNTYVGE IGFLDMSRTR TATVRTISDV
     QCLCLSRNAL NNVLDKYPAL QAQIQETAQT RLQALVSENN SQALEGVSPQ EMLMSGESAS
     SPSDYSLSVL PEHEELSPTA MPADPVSMPE SQIPEADLGP TDTCTVTIKR PFTVVEPASI
     PLDPDPYSNV AGANDAQDMT KARTPGRRSS LAPKTDDNEQ GSSNTDKTEE RDIMMVDNSD
     VSTIDTQSSE SVPLVYNPAF SMTGDTKQEE QSFFYERSGS VFSVLDNGVP KRPRLVNSFS
     SMTKDIDMYS SQPLINSNLS VLGKILSYLP LLEKIRKQRV CRTWKKVLLS APEVGEVLDL
     SPYNTVIYDT IIPHIVAFMN GRKPRYIDLS NCFHLSDAGF RMLACNCIGP ATLVLKMKSV
     WDISGSAITE IAAKARGLAI EELDFSNCRK IGDSSLARII GWNYPGLLAG LEGKKGQDRI
     ELLEQLAAES EEAGIGFLGC TSLRRLTLSY CKHISDRSMH HISLHASHRL EHLDLTRCTT
     ITDHGFGYWA MKPFPNLRSI CLSDCTFLTD NAIVSLAGAA KNLEYLNLNF CCALSDVAVE
     VLALGCTNLK SLNLSFCGSA VSDSSLKTVA LHLLNLEYLS VRGCVRVTGI GVDTILGGCV
     MLKKFNVSQC RNLSTYNKGL AKRQGVEMIF
//
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