ID A0A0D2E4L4_9EURO Unreviewed; 962 AA.
AC A0A0D2E4L4;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Unplaced genomic scaffold supercont1.1, whole genome shotgun sequence {ECO:0000313|EMBL:KIW84991.1};
GN ORFNames=Z517_00379 {ECO:0000313|EMBL:KIW84991.1};
OS Fonsecaea pedrosoi CBS 271.37.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX NCBI_TaxID=1442368 {ECO:0000313|EMBL:KIW84991.1, ECO:0000313|Proteomes:UP000053029};
RN [1] {ECO:0000313|EMBL:KIW84991.1, ECO:0000313|Proteomes:UP000053029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 271.37 {ECO:0000313|EMBL:KIW84991.1,
RC ECO:0000313|Proteomes:UP000053029};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Fonsecaea pedrosoi CBS 271.37.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KN846969; KIW84991.1; -; Genomic_DNA.
DR RefSeq; XP_013288799.1; XM_013433345.1.
DR AlphaFoldDB; A0A0D2E4L4; -.
DR STRING; 1442368.A0A0D2E4L4; -.
DR GeneID; 25299869; -.
DR VEuPathDB; FungiDB:Z517_00379; -.
DR HOGENOM; CLU_006113_0_0_1; -.
DR OrthoDB; 1330350at2759; -.
DR Proteomes; UP000053029; 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; SM00367; LRR_CC; 7.
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:UP000053029};
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..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 221..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 448..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..249
FT /note="Polar 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..542
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 962 AA; 106556 MW; 551881C0667DCF21 CRC64;
MRRHHGRALS PYHGRTASPP SAEVSLVRSF DSKINPSRPA RQSPLATSQI QGMPLDLIDR
IRSFPLFQAT SDDFLADIGL LLKPQLHNTN DYIITEGEDA KAMYWLVRGA VAVTSRDGES
TFAELKPGAF FGEIGILMER PRTATVVART RCMVLALKKE DLKKILPKYP DVEHAIRDEA
LERLTQLEKK KRQVLLGMED VPNHERRGSK RARTTVGEDI YMRDNDGSVT SSNKRRKSPS
PGTNEVSTAS ALGHGLVNIR ATLKELPLFA SLPSDILHFL GLSAQPRSFA PFTDIIKQDT
RGREVYFIVR GEVEVLDERN VSSPKPHKAG EPNGVLGTPR VIARLRPGQY FGEVVSLSLA
DRRTATVRSV TQVECLMISE NVLADFWHRC PTSVLRQIEE TAKHRLQLAS DNDVIMNDAD
TTPDIHDLEI RDSKEMRQRK VVTGPRVTFT DTEISASTPI VATDEPNNTL EPSDPDPFLS
EGLEKVRSRS RRGSLAPPPP DEPSKDQRRR SPRSSPTTTT HPSPRSSVSG TPSPTSEYKG
SSGFPFSDPL SPGSRPKPRP RSSRGLNRGR IPDRLLPLIL EYLDLHDLMR LQGVSLHWQN
VLSTAPNLLH HLDLSRYNRK ITDDILISRI CPFVAERPRF VDISNCFHIT DEGFSALVNT
CGANVQGWRM KSVWDVTAPA ILEMANKARG LKEVDLSNCR KVSDTLLARI VGWVVTAQPP
TPSNRTKVNS HRPVLNTKLS NNAPPQQPPP GTVIGCPELS SITLSYCKHI TDRTMAHIAT
HAHDRIVSMD LTRCTTITDA GFQFWGNVKF ERLRKLCLAD CTYLSDQSIV WLVNGAGSGL
RQLDLSFCCA LSDTATEVIA LGCPNLTHLN LSFCGSAVSD PSLRSIGLHL TSLRELAVRG
CVRVTGLGVQ SVVEGCQKLK LFDVSQCKNL QPWLVSGGIE RWRSMGRDVE FVVVSSGTKL
VR
//
