ID A0A0D2UH43_CAPO3 Unreviewed; 1890 AA.
AC A0A0D2UH43;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Cyclic nucleotide-binding domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=CAOG_005083 {ECO:0000313|EMBL:KJE94441.1};
OS Capsaspora owczarzaki (strain ATCC 30864).
OC Eukaryota; Filasterea; Capsaspora.
OX NCBI_TaxID=595528 {ECO:0000313|EMBL:KJE94441.1, ECO:0000313|Proteomes:UP000008743};
RN [1] {ECO:0000313|Proteomes:UP000008743}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 30864 {ECO:0000313|Proteomes:UP000008743};
RA Russ C., Cuomo C., Burger G., Gray M.W., Holland P.W.H., King N.,
RA Lang F.B.F., Roger A.J., Ruiz-Trillo I., Young S.K., Zeng Q., Gargeya S.,
RA Alvarado L., Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C.,
RA Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., White J., Yandava C., Haas B., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Capsaspora owczarzaki ATCC 30864.";
RL Submitted (FEB-2011) 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; KE346367; KJE94441.1; -; Genomic_DNA.
DR RefSeq; XP_004346768.1; XM_004346718.2.
DR STRING; 595528.A0A0D2UH43; -.
DR EnsemblProtists; KJE94441; KJE94441; CAOG_005083.
DR GeneID; 14897561; -.
DR eggNOG; KOG0498; Eukaryota.
DR eggNOG; KOG4341; Eukaryota.
DR InParanoid; A0A0D2UH43; -.
DR OrthoDB; 1330350at2759; -.
DR Proteomes; UP000008743; 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 CDD; cd09917; F-box_SF; 1.
DR Gene3D; 1.20.1280.50; -; 1.
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; IPR001810; F-box_dom.
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; PF12937; F-box-like; 1.
DR Pfam; PF13516; LRR_6; 1.
DR SMART; SM00100; cNMP; 2.
DR SMART; SM00256; FBOX; 1.
DR SMART; SM00367; LRR_CC; 10.
DR SUPFAM; SSF51206; cAMP-binding domain-like; 2.
DR SUPFAM; SSF81383; F-box domain; 1.
DR SUPFAM; SSF52047; RNI-like; 2.
DR PROSITE; PS00888; CNMP_BINDING_1; 1.
DR PROSITE; PS00889; CNMP_BINDING_2; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 2.
DR PROSITE; PS50181; FBOX; 1.
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:UP000008743};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 304..421
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 499..616
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 1525..1571
FT /note="F-box"
FT /evidence="ECO:0000259|PROSITE:PS50181"
FT REGION 1..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 130..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 243..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 627..682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 694..759
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 824..852
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1020..1041
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1123..1257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1290..1311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1366..1463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 655..682
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 700..759
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 828..852
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1124..1162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1192..1252
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1407..1430
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1440..1463
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1890 AA; 196623 MW; 7FBAC3C8C59AE279 CRC64;
MSGGGAQTRT EPATPPSPSS LRSMAAGLEV HHRKGHVPEP LKLDSAATAA RPASHQQHQQ
QHILTTSSST SSTLSTSSSS SSSSSSSLVA GHATITAAAA GVAAPLGGSN AAGVGSASAI
PSRNAALNLA SPLPSPTTRR RLASQLGPAA SVPSAPNSAG SPSTGTSSSA EPQVFGSPLT
SSLLASSSSS LSSSASYPPP LSPRSLMASM PPALFSTPSS LSSSGSAGRS LLSGGAVTTA
SATASSAAGN SAHTTPATST ASRSRASSFG STSAAAAAAA ASESGEDVSS PVRLLSLQLK
ESPLFHSSSN AFLERLVETM KPRLYKASDV IISFGDSGRA MFFIYKGVVE IISADRETVA
ATLGEGKFFG EIGLLFGVPR TATVRALTPC ILFAITHDKV SEVFQEFPEM RAQIEMEAQS
RFSMVRGRVQ ASPVLAPTAD SAAADSAPPA IASTVAPAFS TTTAAALMRA EGGHSKQASF
DDLEELLRAN EALVRQIPMF AHCDAGFVRM AAARVRPRTF PATSIIFHYN EPGDEIFFLL
SGSVSVFGRD DEVEFEILMP GSFFGEIAVL YNTTRFTTAV AREDIETFSL SKADMNDLAP
LYPEMKERIE KISNRRYRDW LRAKQLETAA SPSRSPDRKS PVQTPAPSPV PSRKFGANSD
ATTAVGNGSP RQPTTAQTSA TGVGTVLFST PLLGASAPMT GSPGSMSAPV SQRGSPGSRS
PLLSGGTPPN NSSTANLANS GLAPQLQQQQ QQQQPSHQLS HLVHHNGLLN QLPKLQVGSF
GSSNARAISA PVTSTNSTNG SPNNSLQNQN TTLAFAVSGR RSFSEKDRPS YLQSQQQLAQ
QARPIFSPPA QRSTSITNIS DILLLPASDP AASQLGGGIS SPPTAGSVLN LANANGPSPG
SGLASKLSSS LGFSQGLGLG SMAASVSMPS LRDITATEAR EMSPGGVVFP PTILTMANRR
SFSAMAQHQS FDATADGQPM THAQLEQLLL QQDENNQAEL SRQATSHLAA ASLSAMPRFG
NNPDLRPHQV IESPVPHHSS TSAFPFASAS NSALNTSAAA AAAAAAIAAA AGTTAAGAPA
TVGPAEPVDL SQYRPVAGPF APPRKAFSME DMSRRLTAMA AGGSPLATSM SGTPGSATRS
PTASSTGLDT LQLEAMASPT SNYHRRTHRR TPSADLASLK ESADENSNEL RKRASMMGQA
SQSPNQEGSP RNLSPSSSSH PSRQNSRSTL AKSSSVDLRQ TGSPQSPQLL SPHLSPALAP
PSGNVVVSEF HLDSQQGAAD LAVPVPARGL PHQSSSLKES SPKLAVLPAP TSPVVTPTIT
VESTPVTDEV VAPSSSVDEV AYDANAAAAA AAAAAAAAAS GMMSASRHRG GFAPSLPPHL
LGKMSEPETV DEDGSDGATS TAEVTSQENS DEEDEDDDAD DDDDDDDDGP AVNPFANFGA
GGWGTTSTAA APGTSAPTTM SNPAVDRLVA QSVGRRRASV AVWLPTVMTD IPQDESRSRT
LPDDVRKAFL AEQERRAAAD SGLTVSNIVE LPVTVTMRIF SWLDFPDLVR VSRVCQMWHR
LAFAPEVVST IDLSSVHKKV TDTVLDNLTE KLGDSVRKLS LHNCWLITDN GLRIVVERCP
KLEYLSLFSC WDITTESLIL LGSHCPNIQY LDISNCRKIT DDSLIQLTAS CSTIRWLELS
YCKNISDAAM VEVLGTCSNT LQHLNLQRCT RLTKEAFAPL RVTPALRLTK LILSDLFALD
DQTVADIAAG CPQLQHLDMS FCFGLTEAAL SHLARHCKAL VHLDLASCAG AVTDASVDAL
VASPSELRVT LQWLNLRNCS SITDDALRCL NENCAVLQHV NLSNCKHVTA GCAERSTNIA
TVVLNASVRP PAVALASSNA AGAAVPMLHG
//
