ID A0A177CW53_9PLEO Unreviewed; 518 AA.
AC A0A177CW53;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Purine-cytosine permease FCY21 {ECO:0008006|Google:ProtNLM};
GN ORFNames=CC84DRAFT_1139866 {ECO:0000313|EMBL:OAG10959.1};
OS Paraphaeosphaeria sporulosa.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Didymosphaeriaceae;
OC Paraphaeosphaeria.
OX NCBI_TaxID=1460663 {ECO:0000313|EMBL:OAG10959.1, ECO:0000313|Proteomes:UP000077069};
RN [1] {ECO:0000313|EMBL:OAG10959.1, ECO:0000313|Proteomes:UP000077069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP3s5-JAC2a {ECO:0000313|EMBL:OAG10959.1,
RC ECO:0000313|Proteomes:UP000077069};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the purine-cytosine permease (2.A.39) family.
CC {ECO:0000256|ARBA:ARBA00008974, ECO:0000256|PIRNR:PIRNR002744}.
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; KV441549; OAG10959.1; -; Genomic_DNA.
DR RefSeq; XP_018041324.1; XM_018176263.1.
DR AlphaFoldDB; A0A177CW53; -.
DR STRING; 1460663.A0A177CW53; -.
DR GeneID; 28759749; -.
DR InParanoid; A0A177CW53; -.
DR OrthoDB; 65220at2759; -.
DR Proteomes; UP000077069; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR Gene3D; 1.10.4160.10; Hydantoin permease; 1.
DR InterPro; IPR001248; Pur-cyt_permease.
DR InterPro; IPR026030; Pur-cyt_permease_Fcy2/21/22.
DR PANTHER; PTHR31806; PURINE-CYTOSINE PERMEASE FCY2-RELATED; 1.
DR PANTHER; PTHR31806:SF5; PURINE-CYTOSINE PERMEASE FCY21; 1.
DR Pfam; PF02133; Transp_cyt_pur; 1.
DR PIRSF; PIRSF002744; Pur-cyt_permease; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR002744};
KW Reference proteome {ECO:0000313|Proteomes:UP000077069};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|PIRNR:PIRNR002744}.
FT TRANSMEM 84..108
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 114..133
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 154..173
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 193..212
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 221..238
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 258..277
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 289..311
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 347..372
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 384..406
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 412..434
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 455..480
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 492..511
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..31
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 518 AA; 55782 MW; 4928BB8DA4158130 CRC64;
MAPTDADAES VISVPPEEEG HHARQEQVQK EKKGASVYAF GDGSRTSSLL SILDVLEKRA
GVELRGCQPV PWDKRTVTQY ANIFTLWFSM SCNLLPITTG MVGTLSFGLG LRDASLVILF
FTLLSTIPVA YMCTWGPRTG MRQLIQARFV YGKYFVSLFI LLNLATLTGF SIVDSIIGGQ
ALSAVSSGTT INATVGIVII ALLSLLVSFA GFKTLHKYEK YAWVPALVAI IIATGCGGKD
LKNQTTVPPA TVQQVLSFGG LVASFMLPWA ALASDFSTYM HPSAPPLRIA AYTYIGLALP
TILLMVLGAA IGGATPNIPS WQAGYESNAA SGVLAAMLHP AGGFGRFVTV VLAFSMVGNL
SATMYSITLN FQMLLPWLFR VQRILFSIVI TAIVIGVAIK AASSFFTNLE NFLGLIGYWA
AAFIGVVVTD HLWFRWGNFA AYTEDEGLWD DGKRLSTGWA AMGASVGCLG LVVPCMYQIW
FTGPIAEWTG DLGFEVAFVL SAGLYVPLRY LEKRACGR
//
