ID A0A165SU22_9APHY Unreviewed; 519 AA.
AC A0A165SU22;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Purine-cytosine permease {ECO:0008006|Google:ProtNLM};
GN ORFNames=DAEQUDRAFT_704836 {ECO:0000313|EMBL:KZT72490.1};
OS Daedalea quercina L-15889.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Daedalea.
OX NCBI_TaxID=1314783 {ECO:0000313|EMBL:KZT72490.1, ECO:0000313|Proteomes:UP000076727};
RN [1] {ECO:0000313|EMBL:KZT72490.1, ECO:0000313|Proteomes:UP000076727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L-15889 {ECO:0000313|EMBL:KZT72490.1,
RC ECO:0000313|Proteomes:UP000076727};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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; KV429040; KZT72490.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165SU22; -.
DR STRING; 1314783.A0A165SU22; -.
DR OrthoDB; 65220at2759; -.
DR Proteomes; UP000076727; 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:SF1; PURINE-CYTOSINE PERMEASE FCY2-RELATED; 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:UP000076727};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR002744}.
FT TRANSMEM 78..102
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 108..126
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 147..167
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 187..208
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 215..232
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 252..273
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 285..307
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 344..365
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 377..400
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 412..431
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 452..473
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 493..512
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 519 AA; 56755 MW; 000E261EACB8191C CRC64;
MSESIEKQVS DSASHDTKNR DVEHYVEPVS ASDAAVPRSK FKKLWAIVDK LDAYGVEAQG
IERVPPDARP QTSALAPFWL WLAANMTTST FSLGTLASSI FYLGLRDACL VILFFNLLCT
IPVAYFSTWG PKLGLRQLTL SRFSFGYFTS LIPIVLNCIA CVGWSVVNSI VGAQTLRAVS
DSHQIPTAAA IVVIAIGTIA VSFMGYRFVH LYEKYSWIPV AIIFIIYLGQ IARFADAGPW
GGSGPVEAGN VLSYGAAVAG FALGWTSVAA DYTVRMPEDM SAVKIFIWTY IGLNIPLILV
ECLGAAAMTT FTAKTTWADA YDASNVGGLL GAGLTGPMHG FGRFLLVIIS LSIIANNIPN
IYSLALTFQN IHPYAQAIPR VFIVIISSVV YIVLAIVGAS HFEDWLDTLL TILSYWLAIF
TTILVQEHLI FRRGRWANYE PDDYNNWRKL PLGVASFIAL GCGVAGAVLG MAQTWYVGQI
ARHIGDPVYG GDIGFELSFA FTAVVFPPLR YLEKKWWGY
//
