ID FD123_TRAVE Reviewed; 283 AA. AC O74631; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 23-FEB-2022, entry version 68. DE RecName: Full=Protein FDD123; DE AltName: Full=CvHSP30/1; GN Name=FDD123; OS Trametes versicolor (White-rot fungus) (Coriolus versicolor). OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes; OC Polyporales; Polyporaceae; Trametes. OX NCBI_TaxID=5325; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=ATCC 62976 / IAM 13013 / NBRC 30340 / FES 1030 / Ps-4a; RX PubMed=9256254; DOI=10.1016/s0014-5793(97)00807-7; RA Iimura Y., Tatsumi K.; RT "Isolation of mRNAs induced by a hazardous chemical in white-rot fungus, RT Coriolus versicolor, by differential display."; RL FEBS Lett. 412:370-374(1997). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane CC protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the archaeal/bacterial/fungal opsin family. CC {ECO:0000305}. CC -!- CAUTION: Lacks the conserved Lys residue in position 228 required for CC covalent retinal binding. {ECO:0000305}. 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; AB003518; BAA33053.1; -; mRNA. DR EMBL; AB018406; BAA76590.1; -; mRNA. DR SMR; O74631; -. DR TCDB; 3.E.1.4.9; the ion-translocating microbial rhodopsin (mr) family. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005216; F:ion channel activity; IEA:InterPro. DR CDD; cd15239; 7tm_YRO2_fungal-like; 1. DR InterPro; IPR001425; Arc/bac/fun_rhodopsins. DR InterPro; IPR043476; Yro2-like_7TM. DR PANTHER; PTHR28286; PTHR28286; 1. DR Pfam; PF01036; Bac_rhodopsin; 1. DR PRINTS; PR00251; BACTRLOPSIN. DR SMART; SM01021; Bac_rhodopsin; 1. PE 2: Evidence at transcript level; KW Membrane; Transmembrane; Transmembrane helix. FT CHAIN 1..283 FT /note="Protein FDD123" FT /id="PRO_0000196287" FT TRANSMEM 24..44 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 52..72 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 97..117 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 122..142 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 148..168 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 185..205 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 217..237 FT /note="Helical" FT /evidence="ECO:0000255" SQ SEQUENCE 283 AA; 30992 MW; E9E777C00D24818D CRC64; MGNSALDLNP PNATFHLSTH GSDWLWAAFS VFGVSLLTVV AWTFTRPRGA RLFHQIAIVV LTTGSLAYFS MASDLGATPV PVEFRGEGTR QIWFVRYIQW FITFPLLLLE LLLATGLSLS DIFTTLFMSI VLVITGLVAA LVPSTYKWGY YTFGVSALFY IWYVLLWHGP HTTFAAGGVL RRGYILAAGY LSFLLLLYPI AWACAEGGNV ISVTSEMIWY GILDIFAGPI FLFFFLWELR GVDYATFGLH SGKYTDKSAY APNTAQAAGT VPATTSTGAA GNV //