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Database: UniProt
Entry: A0A0A2JXJ6_PENEN
LinkDB: A0A0A2JXJ6_PENEN
Original site: A0A0A2JXJ6_PENEN 
ID   A0A0A2JXJ6_PENEN        Unreviewed;      1539 AA.
AC   A0A0A2JXJ6;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   SubName: Full=ABC transporter, integral membrane type 1 {ECO:0000313|EMBL:KGO59373.1};
GN   ORFNames=PEX2_073280 {ECO:0000313|EMBL:KGO59373.1};
OS   Penicillium expansum (Blue mold rot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=27334 {ECO:0000313|EMBL:KGO59373.1, ECO:0000313|Proteomes:UP000030143};
RN   [1] {ECO:0000313|EMBL:KGO59373.1, ECO:0000313|Proteomes:UP000030143}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MD-8 {ECO:0000313|EMBL:KGO59373.1,
RC   ECO:0000313|Proteomes:UP000030143};
RX   PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA   Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA   Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT   "Genome, transcriptome, and functional analyses of Penicillium expansum
RT   provide new insights into secondary metabolism and pathogenicity.";
RL   Mol. Plant Microbe Interact. 28:232-248(2015).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Vacuole membrane
CC       {ECO:0000256|ARBA:ARBA00004128}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004128}.
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:KGO59373.1}.
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DR   EMBL; JQFZ01000096; KGO59373.1; -; Genomic_DNA.
DR   RefSeq; XP_016600569.1; XM_016744598.1.
DR   STRING; 27334.A0A0A2JXJ6; -.
DR   GeneID; 27680018; -.
DR   HOGENOM; CLU_000604_27_3_1; -.
DR   OrthoDB; 3295317at2759; -.
DR   PhylomeDB; A0A0A2JXJ6; -.
DR   Proteomes; UP000030143; Unassembled WGS sequence.
DR   GO; GO:0000329; C:fungal-type vacuole membrane; IEA:UniProt.
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; cd18595; ABC_6TM_MRP1_2_3_6_D1_like; 1.
DR   CDD; cd18603; ABC_6TM_MRP1_2_3_6_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   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; ATP-BINDING CASSETTE SUB-FAMILY C; 1.
DR   PANTHER; PTHR24223:SF456; BILE PIGMENT TRANSPORTER 1-RELATED; 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:UP000030143};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
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};
KW   Vacuole {ECO:0000256|ARBA:ARBA00022554}.
FT   TRANSMEM        57..78
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        90..112
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        127..146
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        158..174
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        186..205
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        343..365
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        438..459
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        968..989
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1009..1036
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1095..1121
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          304..588
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50929"
FT   DOMAIN          624..849
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   DOMAIN          969..1253
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50929"
FT   DOMAIN          1290..1525
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   REGION          854..875
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1539 AA;  171107 MW;  F6282F0AA264D209 CRC64;
     MLDGQSQVVL EASRPGHLLH SLGSALDSRR QPFCTDSEGW GPVSSLRFDL TPCFLDAVVA
     VVAVWGTLSG LGALWLLLRK RIPQPVSKNW HFYTKLAVLA ALIVVTALQA AIQVESDPKR
     FWSDFRFWSS VLTIISLGVI TSVQYLEHWR SRQPNGVVLF YWLFFIIAYA VKLRSLVARK
     EYVGQLPYFI CFNISLGLAL FEFVLEYFVP KKQSAYDALG DEDECPYNYA DIFSVLTFGW
     MTPMMKYGYK NYLTQDDLWN LRSRDTTRAT GNALKEAWDE QLEKKNPSLW TALFKAFGAP
     YVRGAIIKSG SDVLAFVQPQ LLRLLIAFID SYRRPDPQPI IRGVAIALSM FVVSVCQTSF
     LHQYFQRAFD TGMRVKSALT AMIYAKSLKL SNEGRSTKTT GDIVNHMAVD QQRLADLTQF
     GTQLISAPFQ ITLCMISLYQ LLGASMFAGI GVMILMIPLN GVIARMMKKL QIIQMKNKDS
     RTRLMTEILN NIKSIKLYAW NTAFMNKLSH IRNDLELNTL RKIGATQSVA NFTWQSTPFL
     VSCSTFTVFV LTNDKPLTTE IVFPALTLFN LLTFPLSILP MVITSIIESS VAVTRLVEYF
     TAEELQTNAV ILQDAVAHPG DESVRVRDAT FTWNRHSGET VLENIDLSAR KGELSCIVGR
     VGAGKSSLLQ SLLGDLWKNQ GEVVVRGRIA YVAQAPWVMN ASVRENIVFG HRWDPSFYDL
     TVEACALLDD FKNLPDGDQT EVGERGISLS GGQKARLTLA RAVYARADIY LLDDILSAVD
     QHVGRHIINR VLGKNGLLGG KTRILATNAI TVLKEADFIG LLRDKTIIEE GTYEQLMAMK
     GEISNLVRST MVDSDDEGTV SGSEDLASPE SSVTTTIIQN SGASDSEEAE QLGDLIPIRA
     GGGGEARRRT STVTLRRAST VSWQGPRRKL GDEENVLKSK QTQEVSEQGK VKWGVYLQYA
     KDSNVMAVVV YLVAMMAAQT AQVVGNFWLK RWTEWNEAHG TNAQVGKFIG VYLGLGLGSS
     LLVIVQNLIL WIFCSIEASR KLHERMAFAI FRSPMSFFET TPSGRILNRF SSDIYRVDEV
     LARTFNMLFA NSARAMFTVI VISATTPAFL IFVLPLGYIY LSYQKYYLST SRELKRLDSV
     TRSPIYAHFQ ESLGGISTIR AYRQENRFAL ENEWRMDANL RAYFPSISAN RWLAVRLEFI
     GSIIILASAG LAITSVATGT KLAPGMVGLA MSYALQITQS LNWIVRQTVE VETNIVSVER
     VLEYANLPSE APEVIFKRRP AIGWPAQGAV EFNNYSTRYR PGLDLVLKDI SLNIKPKEKI
     GVVGRTGAGK SSLTLALFRI IEGVEGNINI DGLDVSTIGL TDLRGRLAII PQDPAMFEGT
     LRDNLDPRHV HDDTELWSVI DHARLKDHVS RMDGQLDAQI QEGGSNLSQG QRQLVSLARA
     LLTPSNILVL DEATAAVDVE TDALLQRTLR SSIFSDRTII TIAHRINTII DSDRIVVLDK
     GRVAEFDTPA ELIKGGGQFY ELAKEAGLLD SDGGIASSQ
//
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