ID K1XIN3_MARBU Unreviewed; 902 AA.
AC K1XIN3;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE SubName: Full=General amino-acid permease GAP1 {ECO:0000313|EMBL:EKD12344.1};
GN ORFNames=MBM_09519 {ECO:0000313|EMBL:EKD12344.1};
OS Marssonina brunnea f. sp. multigermtubi (strain MB_m1) (Marssonina leaf
OS spot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Drepanopezizaceae; Drepanopeziza.
OX NCBI_TaxID=1072389 {ECO:0000313|EMBL:EKD12344.1, ECO:0000313|Proteomes:UP000006753};
RN [1] {ECO:0000313|EMBL:EKD12344.1, ECO:0000313|Proteomes:UP000006753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MB_m1 {ECO:0000313|EMBL:EKD12344.1,
RC ECO:0000313|Proteomes:UP000006753};
RX PubMed=22876864; DOI=10.1186/1471-2164-13-382;
RA Zhu S., Cao Y.-Z., Jiang C., Tan B.-Y., Wang Z., Feng S., Zhang L.,
RA Su X.-H., Brejova B., Vinar T., Xu M., Wang M.-X., Zhang S.-G.,
RA Huang M.-R., Wu R., Zhou Y.;
RT "Sequencing the genome of Marssonina brunnea reveals fungus-poplar co-
RT evolution.";
RL BMC Genomics 13:382-382(2012).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; JH921459; EKD12344.1; -; Genomic_DNA.
DR RefSeq; XP_007297408.1; XM_007297346.1.
DR AlphaFoldDB; K1XIN3; -.
DR GeneID; 18765454; -.
DR KEGG; mbe:MBM_09519; -.
DR eggNOG; KOG1286; Eukaryota.
DR HOGENOM; CLU_321334_0_0_1; -.
DR InParanoid; K1XIN3; -.
DR OrthoDB; 1438808at2759; -.
DR Proteomes; UP000006753; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:UniProt.
DR GO; GO:0006865; P:amino acid transport; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1740.10; Amino acid/polyamine transporter I; 1.
DR InterPro; IPR004841; AA-permease/SLC12A_dom.
DR InterPro; IPR004762; Amino_acid_permease_fungi.
DR InterPro; IPR004840; Amoino_acid_permease_CS.
DR NCBIfam; TIGR00913; 2A0310; 1.
DR PANTHER; PTHR43341; AMINO ACID PERMEASE; 1.
DR PANTHER; PTHR43341:SF1; GENERAL AMINO-ACID PERMEASE GAP1; 1.
DR Pfam; PF00324; AA_permease; 1.
DR PROSITE; PS00218; AMINO_ACID_PERMEASE_1; 1.
PE 4: Predicted;
KW Amino-acid transport {ECO:0000256|ARBA:ARBA00022970};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000006753};
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|ARBA:ARBA00022448}.
FT TRANSMEM 397..418
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 424..457
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 502..523
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 535..558
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 578..599
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 620..642
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 662..687
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 722..742
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 748..774
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 795..815
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 835..855
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 393..863
FT /note="Amino acid permease/ SLC12A"
FT /evidence="ECO:0000259|Pfam:PF00324"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 79..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 266..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 319..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..98
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 902 AA; 97993 MW; 0B94497B81B44FCF CRC64;
MTLHSEGKCT SFPSKSRVRK IAERSPEQVR CNVESCNNGF HRTDVSLRGT LFGVSRPKSR
RHPGAFDACI HVKLRSSSGS TDRRLLPHTP TLPSGTRRSH TDVCGVPPHL QSISRGCIHD
LVAAIGGQLA KDPRIEKKPP VRLAPRGVRV VQAPNEVMHA QDLSSRSAFH TRPSDSNLLE
TAASLGEIML VQNTPGISFD DDSSYSVGTA AARRDIVQRD RRLTVTRRSL SRSAVAMIHK
LPWPIVRLRI GFFEGAANVR KRKGVGPYLQ PTRKKPPCHA STSDKNKALR LSGPIYISSS
PSPFDTSRAS EDVEKAIYDN DKYSGETSPS QPGYEHGDVK EHHESFFSAF AVNSFKRNHN
ARVVTEATDS EGRPLPDQPP AEPALAMKLK GRHLQMIAIG GAIGTGLFVG SGSALATGGP
ASLIIAYGLI GIMVYCTVHA LGELAVAFPI AGAFSVYSSR FIDPAWGFAM GWNYATNWLV
TLPLELTAAS ITVSYWPGAK DINPAAFVVI FWIVVVTINL FGVRGYGEAE FVFSIVKVIA
VVGFILLGII IAAGGVPGSP QGYLGAGYWY NPGAFNHGFK GLCSVFVTAA FSFGGTEMVG
LTAAETENPR KSLPSAVKQV FWRITLFYMV SLTIVGCLVP YTDPELLNGT GSQDANASPF
VIAVKNAGIS VVPSIMNVVI LIAVLSVGNS SVYGSSRTLA ALADRGQAPK ILGYIDNSGR
PLVSILLASF IGLFGFIVAA GTDVRVQAFN WMLAISGLSS IFTWMSICAC HIRFRHAWKY
NGHTLDELAF TSQPGYYGSW IGVIMNGLIL VAQFWTAVWP VGYAAETPAE IAKGFFQAYL
AMPIVILFYV GFKVIKKTKF KRLKDIDVTS GRREMNLPAI LAEERAEQAT WPWYKRWWNI
AF
//
