ID A0A319CIN8_9EURO Unreviewed; 851 AA.
AC A0A319CIN8;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Abc transporter {ECO:0000313|EMBL:PYH84320.1};
GN ORFNames=BO82DRAFT_351900 {ECO:0000313|EMBL:PYH84320.1};
OS Aspergillus uvarum CBS 121591.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448315 {ECO:0000313|EMBL:PYH84320.1, ECO:0000313|Proteomes:UP000248340};
RN [1] {ECO:0000313|EMBL:PYH84320.1, ECO:0000313|Proteomes:UP000248340}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121591 {ECO:0000313|EMBL:PYH84320.1,
RC ECO:0000313|Proteomes:UP000248340};
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 (DEC-2016) 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; KZ821684; PYH84320.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A319CIN8; -.
DR STRING; 1448315.A0A319CIN8; -.
DR VEuPathDB; FungiDB:BO82DRAFT_351900; -.
DR OrthoDB; 2876209at2759; -.
DR Proteomes; UP000248340; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR CDD; cd18583; ABC_6TM_HMT1; 1.
DR Gene3D; 1.20.1560.10; ABC transporter type 1, transmembrane domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011527; ABC1_TM_dom.
DR InterPro; IPR036640; ABC1_TM_sf.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR039421; Type_1_exporter.
DR PANTHER; PTHR24221; ATP-BINDING CASSETTE SUB-FAMILY B; 1.
DR PANTHER; PTHR24221:SF672; HEAVY METAL TOLERANCE PROTEIN; 1.
DR Pfam; PF00664; ABC_membrane; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF90123; ABC transporter transmembrane region; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50929; ABC_TM1F; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000248340};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..28
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 106..125
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 131..154
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 369..392
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 398..420
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 261..534
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 578..832
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 174..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..221
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 851 AA; 93875 MW; 3E1D50F38348FD79 CRC64;
MALERVAQPL WVVTTTVTLL FVFSSFLLNY KSKTHVKPSV LRKTALRVII FQCISASYIS
EVIILSGQRH GPDPTPDHIF AAVTTASAWA TTCLRKDILV AEATGLSVIA LLFGIPGLAL
DAIALDRHAV HRTLIILESV RLLLVSGVLA NCLFHTRSQR SPLKSEEDED MIPCLGEANG
HSAPSPISYG TTRTDDLESS CSTDESVSEI SDDEEESDES DESRTSQLRK TGSWIAYLQN
FKIFLPFLIP RKDRKVQACL LVCILCLIAD RVLNVLVPRQ LGIVADKLFA RESPTTELGV
YIALSLLHGQ SGVELALALA KIPIKQFSYR QLTTTAFSHV MDLGMDFHSD RDSAEVMKAM
EQGEALTNLL EVALLEIALA VLDTAVAFVF LYRKFTSTAA LSMLVATLAF TTVEVITADW
NVDNRRRQTR AERAEARVLH QAIQGWPTVF IFNMFHHERA RFGGAVDRHL RATRAWSQRD
AYTTALTEAF FPATFALLAT LVAREVQAGR ASPGDFVFLV QYWDYLIWPI KYLSKEYRWL
VSEVVSAERL LDLLLTTPSV TDAPDAIALS PATVEGRVEF KNVNFSYTPQ HNQPQHHLNH
DPQTLKNITL TATPGQTIAL VGATGAGKSS LTKLLLRAYD LSSGRITLDT HDIRSLTQSS
LRSAIGVVPQ TPLLFNTSVL ENLRYARRSA SILEIHAACR SAAIHEKILS FPRGYATKVG
EQGVKLSGGE VQRLAIARVL LKDPAVLVLD EATSAVDTET EGAVQRALFA ADDSGSGSGN
RKKRTTFVIA HRLSTVVRAD LICVLHEGRV VERGTHEGLL KERGRYFGLW QRQLIREEEG
QEVSLGEVDG D
//
