ID B6QSY8_TALMQ Unreviewed; 1458 AA.
AC B6QSY8;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 13-SEP-2023, entry version 81.
DE SubName: Full=Multidrug resistance-associated protein, putative {ECO:0000313|EMBL:EEA19551.1};
GN ORFNames=PMAA_003390 {ECO:0000313|EMBL:EEA19551.1};
OS Talaromyces marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333)
OS (Penicillium marneffei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441960 {ECO:0000313|EMBL:EEA19551.1, ECO:0000313|Proteomes:UP000001294};
RN [1] {ECO:0000313|Proteomes:UP000001294}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18224 / CBS 334.59 / QM 7333
RC {ECO:0000313|Proteomes:UP000001294};
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; DS995905; EEA19551.1; -; Genomic_DNA.
DR RefSeq; XP_002152488.1; XM_002152452.1.
DR VEuPathDB; FungiDB:PMAA_003390; -.
DR HOGENOM; CLU_000604_27_5_1; -.
DR OrthoDB; 1829487at2759; -.
DR PhylomeDB; B6QSY8; -.
DR Proteomes; UP000001294; 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; cd18579; ABC_6TM_ABCC_D1; 1.
DR CDD; cd18580; ABC_6TM_ABCC_D2; 1.
DR CDD; cd03244; ABCC_MRP_domain2; 1.
DR Gene3D; 1.20.1560.10; ABC transporter type 1, transmembrane domain; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
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; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR044746; ABCC_6TM_D1.
DR InterPro; IPR044726; ABCC_6TM_D2.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR24223:SF404; ABC MULTIDRUG TRANSPORTER (EUROFUNG)-RELATED; 1.
DR PANTHER; PTHR24223; ATP-BINDING CASSETTE SUB-FAMILY C; 1.
DR Pfam; PF00664; ABC_membrane; 1.
DR Pfam; PF00005; ABC_tran; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF90123; ABC transporter transmembrane region; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS50929; ABC_TM1F; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
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:UP000001294};
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 36..57
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 69..90
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 102..121
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 133..151
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 163..182
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 265..289
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 309..332
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 406..427
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 458..478
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 490..517
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 529..547
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 903..925
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 937..964
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1013..1034
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1040..1060
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1115..1139
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 277..555
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 610..835
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 903..1182
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 1221..1453
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
SQ SEQUENCE 1458 AA; 160878 MW; 31FAFF83C1EEC039 CRC64;
MAAAASTCPF GSDNQFGPRV NVACRLFDFT LLFEDAFFGI LPAALFLLLL ASRLQYLRTA
PVKLASYKLA VYKLGLLALL FVLQVVYTAV QLRTASLHTQ LSTTSGVLNI LAIFAAALLS
FMEDQRSVKP SDLIVIYFSV SSILSIARLR SLWLISSAPA CRGLWTAVYI LTVLTLLLES
VTKTRLLRPV YRSLTNEQLI GFWGRSFFVW VLPIFRTGYS KVFEVEDLPN VDEALQGSSA
EKKLQASWNQ TKGPRRLLKA TIDAYMWPLV SGIGPRLCVT VFTFCQPFLI NATVNFMATT
TTTPETKSYG QALVGAYALV YLGLTISTAV YWRQTFRLAT MIRAGLISMI YRQTSLLKSS
SMRGNEAITL HGTDVEVIVT SVKVIHEAWV SLLEVGVALW LLERQIFAAC VVPAIICIVC
VIAAGPLSTL SVGAQKAWVE QIEKRLAVTS TVLGDMKAVK MLGLTDLVFS IISALRKVEL
KTSTKLRKLI LLQVSISNVP IDLAPFATFV VYAIIAAVKK DETLLASRAF TALSLISILT
SPLLTFIQSL PSLVRALGCF QRIEEYCLIE PAVVSDDQDT TLPLPGSRTN DVEFSIRNIG
VNDDTCLFKF RNANISWSPE TETVLENLRL DIGNGITIII GPVGSGKSAL LESIIGETHL
KDGTTTKPLT RVAYCSQNPW IINNTIKFNI TNGSEHIDQK WYDFTIWACA LEEDLKSIPG
GDQFQTGSNG VSLSGGQKQR VALARAVYSR LPIVILDDVF SGLDSHSTML ISTRLFDQDG
HFRKTGTSVV LATHTQRMLP YADRIIALNN GFVVNDGPYQ KILAETPEIA AKSMISSIKP
SISSEDGHSE IEKDSLGRKA TKTGINGSEE ALVIKKQDLS RRNGTWDVYK YYVKSAGYKT
TGLFIFSILV SAFFSSFAIL WLQWWSDANE TQPNGRLGYY LGVYAAIFVL NFMGLVSACQ
LLFVNIINNT GSGMHSDLLR ATLGAPFSFF LKTDTGTTTN RFSQDINLID MDLPIASINF
AANLSMSIFS LAILCIAGKY LAITVPFLGL AVFFLQLYYL RTSRQVRLLD IEAKSPLYTH
FIETIGGIAT VRAYGWESIF QDECEQKLNQ SQKPFYMLMC IQIWLTLVLD LIVGIMAVIL
MATTTSLKDN FSPGSVGVGL NLVLLFGLSL KNCIRSWTQL ETSIGAVSRV KSFVADTPSE
NRHLGTTEWI PPQEWPSQGA IIFEEVTATH SDDSPPILKN LSLKINAGEK VAICGPSGSG
KTSLVMALLQ MINLQSGRIE IDSRDLSAIE CADLRTRINV IPQEPFFMPG TVRFNMDPSE
NKVSDETIEA ALAKVGLWKR ISANGGLEMA LVMSDWSVGE RQLLALARAL TMKSSILVLD
EVTSSVDWET EAIMQDVIEK EFSTQTVIAV VHRFRYIDRF DRVVLLNKGE LVESDSPKKL
LESDSEFKAL YMALQKPR
//
