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Database: UniProt
Entry: A0A1Q5UFA9_9EURO
LinkDB: A0A1Q5UFA9_9EURO
Original site: A0A1Q5UFA9_9EURO 
ID   A0A1Q5UFA9_9EURO        Unreviewed;      1713 AA.
AC   A0A1Q5UFA9;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=ATP-dependent bile acid permease {ECO:0000313|EMBL:OKP11168.1};
GN   ORFNames=PENSUB_3190 {ECO:0000313|EMBL:OKP11168.1};
OS   Penicillium subrubescens.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=1316194 {ECO:0000313|EMBL:OKP11168.1, ECO:0000313|Proteomes:UP000186955};
RN   [1] {ECO:0000313|EMBL:OKP11168.1, ECO:0000313|Proteomes:UP000186955}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 132785 {ECO:0000313|EMBL:OKP11168.1,
RC   ECO:0000313|Proteomes:UP000186955};
RA   De Vries R.P., Peng M., Dilokpimol A., Hilden K., Makela M.R.,
RA   Grigoriev I., Riley R., Granchi Z.;
RT   "Genome sequence of the ascomycete fungus Penicillium subrubescens.";
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the Cyclase 1 superfamily.
CC       {ECO:0000256|ARBA:ARBA00007865}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OKP11168.1}.
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DR   EMBL; MNBE01000293; OKP11168.1; -; Genomic_DNA.
DR   STRING; 1316194.A0A1Q5UFA9; -.
DR   OrthoDB; 3295317at2759; -.
DR   Proteomes; UP000186955; 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:0004061; F:arylformamidase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0019441; P:tryptophan catabolic process to kynurenine; IEA:InterPro.
DR   CDD; cd18596; ABC_6TM_VMR1_D1_like; 1.
DR   CDD; cd18604; ABC_6TM_VMR1_D2_like; 1.
DR   CDD; cd03250; ABCC_MRP_domain1; 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   Gene3D; 3.50.30.50; Putative cyclase; 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; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR007325; KFase/CYL.
DR   InterPro; IPR037175; KFase_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR24223; ATP-BINDING CASSETTE SUB-FAMILY C; 1.
DR   PANTHER; PTHR24223:SF368; BILE ACID TRANSPORTER, PUTATIVE (EUROFUNG)-RELATED; 1.
DR   Pfam; PF00664; ABC_membrane; 2.
DR   Pfam; PF00005; ABC_tran; 2.
DR   Pfam; PF04199; Cyclase; 1.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF90123; ABC transporter transmembrane region; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   SUPFAM; SSF102198; Putative cyclase; 1.
DR   PROSITE; PS50929; ABC_TM1F; 2.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE   3: Inferred from homology;
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:UP000186955};
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        327..350
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        362..384
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        390..410
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        503..524
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        544..565
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        674..692
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        698..718
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1143..1164
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1223..1253
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1302..1319
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1325..1343
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          504..837
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50929"
FT   DOMAIN          868..1092
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   DOMAIN          1189..1462
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50929"
FT   DOMAIN          1497..1713
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
SQ   SEQUENCE   1713 AA;  192528 MW;  29FB48D721A5E870 CRC64;
     MSASKNDQVI PFEALPLDPN GPRGNAWGRF GPNDELGTLN LLTPEVIVQA AKEICTGIRI
     SLDWPLSMPS YPSFDRNPFK QELVLRNPNC IYDDILSFNS QGSTQWDGFR HYANQKMRRF
     YNGHTTEEIE SSDVIGLHTV AEHGGMTGRG ILLDFADWAE SNSVSISALE SQAITLDSIK
     QVVKDHQLEF RKGDILFIRS GFTAAYNKLD DQQRRDMPNR PTPDFIGVEA TEGMVRWLWG
     HQFAAVAGDA PSFERAPIRG SHADPNFNLH EWVLAGWGTP IGEMFDLERL SQHCSVLRRW
     QPKWTVPFIS EQDEYQGFPL EGVKHSLGWT LALLTFTGIG FSAELATAAV VITVKRPRSC
     SVLLLVFYTL SFMVEIILAT ASYGKPEYQA ISRYIAASAA LMACFTILLM PFRKPSLPVI
     DISTVGQTPS SDFRSPEDNL RLWQFLTVSW MAPLISLGHK RQLNEPDVWL LGFEFQHSRL
     HEKFRRIRGS VLRRVLQANG LDVLIISVIA VVQMICTFST PVLLQQLLQA MQDPTKPKRV
     PLTYAVLALV LRLVAAQSQV LNLWYGRRCY ERSRGEMVMM VYEKALSRKN ILGLHVAGEQ
     KQPGGEETIE GDPTINEVEV LPTTKPGFWG RLFSVKRKPQ LKKPKEAATL GKIFNLLRGD
     VYDVAQRFWE IDVLIDKPLG LVIAVVLVWT LFGPSCFLGI LAVLIAQALN AVITRFLLRR
     ERLTRAATDA RLQITSQFVE AIRHLRWYGW QDHWLRQVME ARQHELNRRI ITKLCTTSIN
     FINAFASGVF PVVALYAYTM LAGHELRIDI IFPALQLFTM LETRLREIPS LITALINSSI
     ALGRIEDFMA EPDKEQFEPE QRPDETPFRL DSCSFAWPGK LSPVLRDINV TIPRGLTVVS
     GKVGAGKTAF LQALLGELDR LRGSCRLPNQ TIGYCAQTPW LQSMSIRDNI LFSAPYEEQR
     YKRTLDACAL LPDLSQFKHG DLTFIGENGV GLSGGQKARV ALARAVYSAS RVLLLDDPLS
     ALDHNTAEFV VRKCLSGPLM QNRTIVLVTH RTALVRDIAD QIIEIDESRA IVHSKAALSA
     STKRDGIGLL LNLNDSETET DEANEDEEAA AVPDKFFEEE HRAEWGVKAR VYWNYIRAGK
     YRWWALLVLV LAIYRLMAVG QSWFLKEWGE AYSQVSLSNS HLSVWQSHSV QTSLFSMSGV
     DAYFIPQNPI NQLPSPHEDV RPWLWTFFGI ICFQAAAVLV SQLLMLVIVY CAGRTLFHQV
     MVRVSHASFR FFDVTPVGRL MNRLTSDISV VDGNISAQFQ TIAFYAITWI SSILVIATAT
     PTFLVFSLIL TIAFVLIFLR FLPTSQSLRR LEMVSLTPLL SNFGELLHGL TTVRAFRAEE
     RFQNRVISVV DKFQGMDHFY WSLQAWLMYR FESLSALSTF CLTVLALYTN TTPGLVAFVL
     IAANNFVDST HALCKQYGQL QMDFVSVERI DELLHIEEEP KGTIDPPAAW PTYGSDVTFE
     NVTLRYAPHL DPALKEISLQ IPGGSTTAVI GRTGSGKSTL AVSLLSVVRP ETGRILIDGI
     NIADVNTQAL RTRVTFVAQD PVLFPGSVRL NLDPTEEFSD QQCADVLERL CGRHGWNLET
     HIEAGGKNLS QGQRQLIALT RAVLRRSPVV ILDEATASID HETSLEIQQI IREELQLSTV
     ITIAHRVEAV KDAEYFVELD QGRVLRYGSV RDL
//
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