ID W9WNY1_9EURO Unreviewed; 962 AA.
AC W9WNY1;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=F-box and leucine-rich repeat protein 7 {ECO:0008006|Google:ProtNLM};
GN ORFNames=A1O5_10493 {ECO:0000313|EMBL:EXJ66341.1};
OS Cladophialophora psammophila CBS 110553.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Cladophialophora.
OX NCBI_TaxID=1182543 {ECO:0000313|EMBL:EXJ66341.1, ECO:0000313|Proteomes:UP000019471};
RN [1] {ECO:0000313|EMBL:EXJ66341.1, ECO:0000313|Proteomes:UP000019471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 110553 {ECO:0000313|EMBL:EXJ66341.1,
RC ECO:0000313|Proteomes:UP000019471};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Cladophialophora psammophila CBS 110553.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:EXJ66341.1}.
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DR EMBL; AMGX01000020; EXJ66341.1; -; Genomic_DNA.
DR RefSeq; XP_007749259.1; XM_007751069.1.
DR AlphaFoldDB; W9WNY1; -.
DR STRING; 1182543.W9WNY1; -.
DR GeneID; 19195186; -.
DR eggNOG; KOG0500; Eukaryota.
DR eggNOG; KOG1947; Eukaryota.
DR HOGENOM; CLU_006113_0_0_1; -.
DR OrthoDB; 1330350at2759; -.
DR Proteomes; UP000019471; 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; 3.
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; PF16643; cNMPbd_u2; 1.
DR Pfam; PF13516; LRR_6; 1.
DR SMART; SM00100; cNMP; 2.
DR SMART; SM00256; FBOX; 1.
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; 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:UP000019471};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 66..183
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 268..404
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 565..612
FT /note="F-box"
FT /evidence="ECO:0000259|PROSITE:PS50181"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 195..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 425..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..220
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..249
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..446
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..474
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..548
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 962 AA; 106405 MW; 1078014552CE82C1 CRC64;
MRRHHGRALS PYHGRTAAPP SAEVSLVRSF DSKINPSRPA RQSPLATSQI QGMPLDLIER
IRSFPLFQST SDDFLADIGL LLKPQLHNTN DYIITEGEDA KAMYWLVRGA VAVTSRDGES
TFAELKPGAF FGEIGILMER PRTATVVART RCMVLVLKKE DLKKILPKYP DVEQAIRDEA
LERLTQLEKK KRQVLLGTED VPNHERRGSK RARATVGDDV YMRDSDGSVT SSSKRRKSPS
PGTNEVSTAS ALGHGLVNIR ATLKELPLFA SLPPDILHFL GLSAQPRSFA PFTDIVKQDT
RGREVYFIVR GEVEVLDERH VSIPKPHKAG EPNGVPGTPR VKARLRPGQY FGEVVSLSLA
DRRTATVRSV TQVECLMISE NVLADFWNRC PPSILRQIED TAKHRLRLAS DNDVVMNEAD
ATPDIHDLEI GDSKERRQKK VHNGPRVTFT DTEISSSTQP AQTEEPNNTL EPSDPDPFLS
EGLEKVRSRS RRGSLAPPPP DEPSKDQRRR SPRSSPTTTA SPSPKSSASG TPSPTSEYKG
SSSFPFSDPF SPGGRPKPRP RSSRGLNRGR IPDKLLPLIL EYLDLHELMS LQGVSLHWQN
VLNNSPNLLH CLDLARYNRK VTDDILINRI CPFVGDRPRF IDISNCFHIT DEGFAALVNI
CGANVQGWRM KSVWDVTAPA ILEMANKARG LKEVDLSNCR KVSDTLLARI IGWVVTAQPQ
APSSRTKVNS QRPVLNTKLS NYAPPQQPPP GTVIGCPELN SITLSYCKHI TDRTMAHIAT
HAHNRIVSID LTRCTTITDA GFQFWGNVKF ERLRRLCLAD CTYLSDQSIV WLVNGAGNGL
RQLDLSFCCA LSDTATEVLA LGCPNLTHLN LSFCGSAVSD PSLRSIGLHL TSLRELAVRG
CVRVTGLGVQ SVVEGCQKLK LFDVSQCKNL QPWLVSGGIE RWRSMGREVE FVVVSSGTKL
VR
//
