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Database: UniProt
Entry: A0A1V6QTY2_9EURO
LinkDB: A0A1V6QTY2_9EURO
Original site: A0A1V6QTY2_9EURO 
ID   A0A1V6QTY2_9EURO        Unreviewed;      1261 AA.
AC   A0A1V6QTY2;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=ABC transporter {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PENSOL_c041G01160 {ECO:0000313|EMBL:OQD92412.1};
OS   Penicillium solitum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=60172 {ECO:0000313|EMBL:OQD92412.1, ECO:0000313|Proteomes:UP000191612};
RN   [1] {ECO:0000313|Proteomes:UP000191612}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 29525 {ECO:0000313|Proteomes:UP000191612};
RX   PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA   Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA   Frisvad J.C., Workman M., Nielsen J.;
RT   "Global analysis of biosynthetic gene clusters reveals vast potential of
RT   secondary metabolite production in Penicillium species.";
RL   Nat. Microbiol. 2:17044-17044(2017).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:OQD92412.1}.
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DR   EMBL; MDYO01000041; OQD92412.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V6QTY2; -.
DR   STRING; 60172.A0A1V6QTY2; -.
DR   OrthoDB; 1067095at2759; -.
DR   Proteomes; UP000191612; 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; cd18577; ABC_6TM_Pgp_ABCB1_D1_like; 1.
DR   CDD; cd18578; ABC_6TM_Pgp_ABCB1_D2_like; 1.
DR   CDD; cd03249; ABC_MTABC3_MDL1_MDL2; 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; 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; IPR027417; P-loop_NTPase.
DR   InterPro; IPR039421; Type_1_exporter.
DR   PANTHER; PTHR24221:SF420; ABC MULTIDRUG TRANSPORTER ATRC; 1.
DR   PANTHER; PTHR24221; ATP-BINDING CASSETTE SUB-FAMILY B; 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:UP000191612};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        41..68
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        88..115
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        164..182
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        188..209
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        268..291
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        306..328
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        688..711
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        731..758
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        810..830
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        836..854
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        913..937
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        949..972
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          41..332
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50929"
FT   DOMAIN          367..612
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   DOMAIN          693..978
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50929"
FT   DOMAIN          1013..1256
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
SQ   SEQUENCE   1261 AA;  138407 MW;  792F021C87313222 CRC64;
     MEKQSEKDSI DNQGSKEETD AFGAYLRIFH YGSSKDYTLQ AIATACALGS GVGMALVNLV
     FGQFITLITD YTAGHTDASK FRSESARLSL FFFVIGLCRF CLTYGYSTLF TLAAYRITRN
     IRRRYLKAGL SQEIAFFDSG TSGSIAMQAT SNGRLVQAGI SEKLGLIVQG LSAFISAFVL
     AFVTQWKLTL ICCCIAPSML LAVGISSTFE ASIEAQILKV QAQAGSFAES ILSSARTVQA
     FGLRNQLVCD FDKFLQVSRK LGNKKSPLFG CLFATEYTII FAGFGLCFWQ GIKMVSTGEV
     EQSGDIFIVL MSVIVAATSL TAIMPYLIDF VRAGSAAAEL FRLMDRKSRI DPFDDSGERP
     TDVMGYLDFS GISFAYPTRP DVKVLNDFSL HIPAGKTTAL VGASGSGKST IVGLIERWYD
     PLSGTIKLDG QPIELFNLKW LRQQVRLVQQ EPVLFDGTVA ENIANGLVGT PWENESPAER
     LARIQDAAKI SFAHDFITQL PNGYDTVIGE RGGLLSGGQK QRVAIARSIV SQPRFLLLDE
     ATSALDPHAE EVVQRALNNV SKGRTTITIA HKLATIRDAD NIVVMEHGRI LEQGTHNSLL
     ESNGAYARLV RAQDLSVVTQ DPESASDSQD ETDKEDHVIL AGELTRHSTT TRSTSEKQLS
     RDDFDNWKRF GLLHTIWRLV KSTPELNWTL MMMVLACLTG AAAYPGQAIL MSKFIEVFQY
     TGAAMRTKGN FFALMFFVLG LGSFVVYFII GWTSNIVAQT MNHKYRKQVI NDIMKQDLQF
     FDRAENTTGA LASRADSYPQ SVLELMGFNI ALMLVAATGV FSCSILAIVY AWKLGLVIVL
     AGLPPMLAAG YARIRMEGAM DHKISKLFSK SASIASEAVT AIRTVSSLAI EPSVLERYTH
     ELDQAVATST RPVLLIMLPF AFTQTVEYSF QALGFWYGCR LVSFGDVSMV NFFICFLSVF
     FSGQQASILF GFSSSMTKAT NAANYIFWLE QLQPTIQETD ENREIGPGDF KSLHLENLQF
     SYPMRPHARV LRGIDLHIKK GQFVAFVGAS GCGKSTMIGI LERFYDPVAG HIRIDAHTLE
     SMNPWLYRAQ VALVQQEPTL YPGTIRENIS MGTPTGSPST VSDNDIEAAC RAANAWEFIS
     SLPDGLMTLC GTNGTQLSGG QRQRIAIARA LLRNPRLLLL DEATSALDTQ SERIVQDALN
     EAASQGDRIT IAVAHRLSTI RHADMICVFD GGRIVESGTH EELLAKGRLY PKMCEAQNLG
     T
//
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