ID A0A178E7C3_9PLEO Unreviewed; 1742 AA.
AC A0A178E7C3;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=ATP-dependent bile acid permease {ECO:0008006|Google:ProtNLM};
GN ORFNames=IQ07DRAFT_586578 {ECO:0000313|EMBL:OAL50993.1};
OS Pyrenochaeta sp. DS3sAY3a.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Cucurbitariaceae;
OC Pyrenochaeta.
OX NCBI_TaxID=765867 {ECO:0000313|EMBL:OAL50993.1, ECO:0000313|Proteomes:UP000077535};
RN [1] {ECO:0000313|EMBL:OAL50993.1, ECO:0000313|Proteomes:UP000077535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS3sAY3a {ECO:0000313|EMBL:OAL50993.1,
RC ECO:0000313|Proteomes:UP000077535};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-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; KV441643; OAL50993.1; -; Genomic_DNA.
DR STRING; 765867.A0A178E7C3; -.
DR InParanoid; A0A178E7C3; -.
DR OrthoDB; 3295317at2759; -.
DR Proteomes; UP000077535; 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; 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; 3.
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; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR24223:SF353; ABC TRANSPORTER ATP-BINDING PROTEIN_PERMEASE VMR1-RELATED; 1.
DR PANTHER; PTHR24223; ATP-BINDING CASSETTE SUB-FAMILY C; 1.
DR Pfam; PF00664; ABC_membrane; 2.
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; 2.
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:UP000077535};
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 27..47
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 116..137
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 181..203
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 215..232
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 321..341
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 361..384
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 486..506
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 512..531
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 591..617
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1015..1039
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1114..1133
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1188..1209
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1215..1235
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1300..1323
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1329..1349
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 328..655
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 691..940
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 1019..1354
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 1394..1713
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 68..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 442..461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 935..984
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1513..1537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..456
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1513..1527
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1742 AA; 192628 MW; 13C9B10B01A0238F CRC64;
MFAHCKGPTW GQDDFSKCFE REYLQTLFPL VVCGVSVVYL SIQLYFATTS RTSYHGYSAL
DDPRNVYSLP APQRDSDDTD SDSEDGFDHT DEAALLPTKS RQTMSTIAVT KPRGEVTVVV
LEEVAVLAQL AIHIAVYMTN AWGKHGKSAA ISSIAVWAYV ATLASLRLLF SSTHRFSFPR
LWYHTAFIYG FQWVFTVLLF RSAIIHPRSD LHQKLIIISF VLTSLLFLIA LCSRKGNKAV
ELEYEGDIAP AREPTASVLS LATFGWVDSI VWTGYKKTYE LSDVWNLAPR DKAAAVIANY
RQVKKTSTLA FHLLKHFKRG LIIQASWAAI SGFLTFAPTL LLKAILEYVE SPELTPVNAA
WFYVILLFVS GSLSALADGQ ALWIGRKICI RLRAVIIGEL YAKALKRRAA SGTDKVLGEE
KKKKEGEEEE PKMLKRIMTF GRKKKKATET PNREGAAKPD SDAQVTTGAI INLMAVDAFK
VSEISAYLHF LWANTPVQVV VAVYLLYRIL GYSSIAGIGM MVVLLPINMY VAKQFAKIQK
LILAATDARI HTTNEVLTNI RIIKFFAWEQ RFIGLVNDKR YTELKHLRRR YILWAVAATI
WSGSPVFITF LSFFVYTNVE NKALIPSVAF TALSLFQILR IPLDQLADMI AHVQESKVSV
DRIEEYLNEP ETEKYSQLVT RKKDEHGQAI IGFKNGTFSW GGKDMTDKAA ADAFKLMDLN
VKFAVGKLNV VVGPTGSGKT SLLMGLLGEM TKLKGDVYLP GGLSREDLRA DPETGLTESV
AYCAQQAWLV NGTVKDNIVF ASEWDEKRYD EVIIACSLKR DLEILDAGDQ TIVGEKGVTL
SGGQKQRISL ARALYSKARH VLLDDVLSAV DSHTAKWIFD YALYGQLMVN RTCILVTHNV
SLCLPHAEFA VVLENGKVVS QGTADDVISS GKLTEDLSKS RPASRGASKA PSRVPSDVGG
EEAEGEVSHA NGNGTVDKSK DAKKAAAAAS QEEKKAEGGV KLSIIVMYLK AMGPWYYWVG
ATIAFVAAQI SSVSTNLWIR TWANAYADKG YTTMGHHNRS PVTHAPTLSG MGTCMKSGTC
SWNIPFFDQQ KQDVYTYNSM QTTFQYGDSD VDSAYFLGVY AVLGLIFMFI TFLREGFLFG
GSLAASRRVH ERLIQKVTHA KFRFFDQTPL GQLMNRFSKD IESVDQEVAP VAIGVVHCFA
SIITIVILIS VITPAFLIAA SVISVLYFLI GRFYINSSRD LKRLESVHRS PLYQQFGETL
SGMTTIRAYG DERRFIRENL TKINTQHRPF IYLWAANRWL AFRVDVVGAM VAFFAGMFVV
LSVGRIDAGA AGLALTYAVT FTENVLWFVR LYSANEQNMN SVERIKEYLD VDQEAPSVIP
NNRPANNWPS KGSVEFIGYS TRYRTDFDLV LKNVTFKILP GEKVGVVGRT GAGKSSMALA
LFRALEAEKG KILVDDVDIG LIGLQDLREN IVMVPQDPTL FTGTIRSNLD PFSLFTDEEI
FTALREVHLI SSSSLPSSGS VTPTESATPP KAIAIPNPTT GAVTADVNAS YSASTVNPGS
ILANRDWERG ETQDDTIVVM PNGHLATDEE AAQAAMQADN KNPFRNLNSP VTESGSNLSQ
GQRQLLCLAR ALLKAPKVLL MDEATASIDY ATDAKIQETI RQIKNTTITI AHRLQTIIDY
DKVLVLDKGE VIEYGDPYDL VRKEGGNFRS MCETSGEMEA LVKTAKTAYE SRQTPAVDEE
SA
//
