ID A0A086TLG1_9FUNG Unreviewed; 1678 AA.
AC A0A086TLG1;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Amino acid permease/ SLC12A domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=MVEG_11314 {ECO:0000313|EMBL:KFH62788.1};
OS Podila verticillata NRRL 6337.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mortierellomycotina;
OC Mortierellomycetes; Mortierellales; Mortierellaceae; Podila.
OX NCBI_TaxID=1069443 {ECO:0000313|EMBL:KFH62788.1, ECO:0000313|Proteomes:UP000243308};
RN [1] {ECO:0000313|EMBL:KFH62788.1, ECO:0000313|Proteomes:UP000243308}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 6337 {ECO:0000313|EMBL:KFH62788.1,
RC ECO:0000313|Proteomes:UP000243308};
RG The Broad Institute Genome Sequencing Platform;
RA Russ C., Cuomo C., Burger G., Gray M.W., Holland P.W.H., King N.,
RA Lang F.B.F., Roger A.J., Ruiz-Trillo I., Young S.K., Zeng Q., Gargeya S.,
RA Alvarado L., Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C.,
RA Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., White J., Yandava C., Haas B., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Mortierella verticillata NRRL 6337.";
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; KN042430; KFH62788.1; -; Genomic_DNA.
DR OrthoDB; 5490251at2759; -.
DR Proteomes; UP000243308; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015377; F:chloride:monoatomic cation symporter activity; IEA:InterPro.
DR Gene3D; 1.20.1740.10; Amino acid/polyamine transporter I; 1.
DR InterPro; IPR004841; AA-permease/SLC12A_dom.
DR InterPro; IPR018491; SLC12_C.
DR InterPro; IPR004842; SLC12A_fam.
DR PANTHER; PTHR11827:SF72; GH08340P; 1.
DR PANTHER; PTHR11827; SOLUTE CARRIER FAMILY 12, CATION COTRANSPORTERS; 1.
DR Pfam; PF00324; AA_permease; 1.
DR Pfam; PF03522; SLC12; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000243308};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 246..267
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 273..298
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 319..343
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 365..386
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 393..413
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 459..480
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 492..513
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 533..562
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 607..630
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 642..662
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 668..685
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 245..724
FT /note="Amino acid permease/ SLC12A"
FT /evidence="ECO:0000259|Pfam:PF00324"
FT DOMAIN 736..818
FT /note="SLC12A transporter C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03522"
FT REGION 1..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 135..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1134..1302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1321..1371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1390..1461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1529..1575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..185
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1134..1148
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1189..1207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1232..1247
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1269..1302
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1332..1348
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1390..1420
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1440..1461
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1533..1560
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1678 AA; 183523 MW; 81CB97BAA5125DA8 CRC64;
MAHRDRDHRN EPAADPRQVA NAIRTRTNRP YSSPSVPTAN SLQGMTNTTP TPAASSSQNT
PPGSAASSIR TRRPPNAVLT GAGSTAGTGG AIRSATTRPK TAYQAVTWKE NLDAFNRRLR
RGSLSLDATA QEEEFASQTM ARAKAQQQAQ YHHDQGNYNG ENEQTSLLGD PSSKSLGSSF
SNGKAYGATG LPKGDAPEHH HNHSQHHQQP QQEQQDGSSY EPVFPTQLNP ALATTKSSKL
GVFSGVFIPC VLSIWGIILF LRFGFIIGQA GVLGTMGMFV IGYAINILTT FSLSAVSTNG
TVRGGGPYYL VSRSLGPEFG GSIGVIYFFG TVIGCGMNVL GFVEPLMSNF GESSGTVYRV
LPEGAVWGFI YGTILLVLCT LVCLVGSKLF SRASLVLAVI ILLSTLSIFV SFATMPAFSI
PERNIEYTGW SWETLQENMW PAFTVTTGPD GSKESFQTVF GVLFPACIGI LAGASMSGDL
EDPSKSIPSG TLWAVGTTFC AYTCIVILMG GSISRSTMYT DLSVLQDISI SPLFIASGAL
AASVFATLGS VIGAAKILQA IARDNLLPVL SIFGQGTPRT DEPTLAVLLT YILCQFCLFL
TDMNSIATFV SMITLLTFLI INLACFLLKI GSAPNFRPSF RFFHWWTAFT GMVLCAIVMG
FVDLGKSLLS GLMVAVIFVW IHYWSPPKRW GDVTQSLIYH QVRKYLLRLD SRKEHVKFWR
PQILLLVHHP RSEYHLIQFC NHLKKGALYV LGHVIQGDLR DVLQEYRRQQ VNWLKFVDVL
QIKAFVNLSV ADSICIGARN LLIGTGLGGM RPNIVVMGSF NLQRYLQEME LQQSTDQRPL
SPFLGKKAPV TPLTPGFAPY QVQGHGDHTI NIPVSLPIDN IRIEKPIKIT EYVSIIEDVL
SLNKAVAIGY GFDRLEFPDE HPKSSWKLFN FASMLSPSSS RRSSLHHGEP KKKKYIDLWP
MQMSVAPLPF DVAPGQQPFG TKRASRDMGS PYSPMVGHSA TFSESQPGAK VEANLTNFDT
YTMVLQMGCI LHMVPHWKEN YLLRVMVFVE YKEDVEEEKQ RLADLLENLR IPAEIKVMCL
DGGDSETYDR LVKGEVFEFS PVESTNGFAD SLVKDQSAKV PLVPYLYREL QQMAPLQQPQ
PKNTHSRWTS EPVMEEEELE PSGDEVPTVN KDGEQSSHEI GPYSGIAGQV SDRTRTLSSS
GNNDTDIQPL HYPAFEASGP PPQRRRTISH PDPPSHISQS GPKQAPLRVN TALSPRMRQG
PIGISSAHPR QLHHSSSTGV RYRSVGAPGS TSPQETRLGT SVPLGASMNF RIAVPLPRQY
FDPNSIDSES ESDSISSEDD EDDYDRNDDD LVYGAHHPRS TSLGQHRTPP TTMVQRRASM
VLPLSRTPTL EQQRLRQPQL QQQQPTQQSQ IASTSIGSPS GLGIGLGLPT VHSEPDIIGH
PTPTTLSSQS ISFSQGQLHP QKQQPYTLPY QHHQQPSSSS LGIGSSNPWA TDKLSISPSN
SVARNDLSSS PGAMYDWSRE VIVSAAAAAN TEQGPPLDSS LSSTVTTTSE PTSTLGQQLH
TPVDKHGHEG EASQRPEEPY FLDYPKASPA SPGPAVPVQF DHLGPEAQLM ILNELMRIHS
SPETTSIVLT TMPAPEPGTC LHEESSYAYL ENLDVLMDQL EVPVLLIHAK SLTVTMTL
//
