ID A0A3F3PU56_9EURO Unreviewed; 672 AA.
AC A0A3F3PU56;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=HCO3 transporter family-domain-containing protein {ECO:0000313|EMBL:RDH30490.1};
GN ORFNames=BDQ94DRAFT_181148 {ECO:0000313|EMBL:RDH30490.1};
OS Aspergillus welwitschiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1341132 {ECO:0000313|EMBL:RDH30490.1, ECO:0000313|Proteomes:UP000253729};
RN [1] {ECO:0000313|EMBL:RDH30490.1, ECO:0000313|Proteomes:UP000253729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 139.54b {ECO:0000313|EMBL:RDH30490.1,
RC ECO:0000313|Proteomes:UP000253729};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (JUL-2018) 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; KZ852060; RDH30490.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3F3PU56; -.
DR STRING; 1341132.A0A3F3PU56; -.
DR OrthoDB; 1013180at2759; -.
DR Proteomes; UP000253729; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005452; F:solute:inorganic anion antiporter activity; IEA:InterPro.
DR GO; GO:0006820; P:monoatomic anion transport; IEA:InterPro.
DR Gene3D; 1.10.287.570; Helical hairpin bin; 1.
DR InterPro; IPR011531; HCO3_transpt-like_TM_dom.
DR InterPro; IPR003020; HCO3_transpt_euk.
DR PANTHER; PTHR11453; ANION EXCHANGE PROTEIN; 1.
DR PANTHER; PTHR11453:SF82; SOLUTE CARRIER FAMILY 4 MEMBER 11; 1.
DR Pfam; PF00955; HCO3_cotransp; 2.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000253729};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 124..142
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 154..180
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 200..220
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 227..247
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 267..287
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 299..319
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 350..371
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 392..414
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 475..499
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 531..551
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 557..578
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 92..256
FT /note="Bicarbonate transporter-like transmembrane"
FT /evidence="ECO:0000259|Pfam:PF00955"
FT DOMAIN 266..529
FT /note="Bicarbonate transporter-like transmembrane"
FT /evidence="ECO:0000259|Pfam:PF00955"
FT REGION 1..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 607..672
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 639..660
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 672 AA; 74045 MW; 9A6243BD0D2C01B3 CRC64;
MQGPTASTSG SHSGGGGGGV GETLPPSSSH SRRPWQSQSQ SQHLRPTSSI RSQHSTHVHH
DHRYQSSVVG SGAGNAAPSG NEKDEKWYKI HLFRGMIQDV KRRAPFYWSD WTDAWDYRVV
PATVYMYFAN ILPALAFSLD MFEKTNQSYG VNEVLLASVL AAVVFSVFAA QPLVIVGVTG
PITVFNYTVY DIISPRGTNY LAFMCWIGIW SLIMHWLLAI TNACNGLTYV TRFSCDIFGF
YVAFIYLQKG IQVLTRQWGT AGETSAYLSI MVALLVLMSG WICGELGNSS LFKRWVRKFL
EDYGTPLTIV FFTGFVHIGH MRDVEVARLP TSKAFFPTEE RPWLVHFWDI NVGDVFLAIP
FAVLLTILFY FDHNVSSLIA QGTEFPLRKP AGFHWDLWLL GITTFVAGLL GIPFPNGLIP
QAPFHTAALC VTRDVADEDD TNKGKAIRVT DHVVEQRVSN FAQGLMTLGT MTGPLLIVLH
LIPQAVLAGL FFIMGVQALQ GNGITQKLIF LAQDSGLTPA SNPLKRIKRR LSIWVFVILE
LIGFGATFAI TQTIAAIGFP VIILLLIPVR SFLFPWWFTQ EELSVLDAPT ASPFTMESVG
GTHGLSDAAA AAASGRDEDH RDSKNGGGGN GVMMRRDESS SESAVEDDLE RGEAYEMQRL
GVRRRSTTGG VE
//
