ID   ADRC_PENRO              Reviewed;        1452 AA.
AC   A0A1Y0BRF0;
DT   10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2017, sequence version 1.
DT   03-AUG-2022, entry version 14.
DE   RecName: Full=ABC-type transporter adrC {ECO:0000303|PubMed:28529508};
DE   AltName: Full=Andrastin A biosynthesis cluster protein C {ECO:0000303|PubMed:28529508};
GN   Name=adrC {ECO:0000303|PubMed:28529508};
OS   Penicillium roqueforti.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=5082;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION, FUNCTION, AND DISRUPTION
RP   PHENOTYPE.
RC   STRAIN=CECT 2905;
RX   PubMed=28529508; DOI=10.3389/fmicb.2017.00813;
RA   Rojas-Aedo J.F., Gil-Duran C., Del-Cid A., Valdes N., Alamos P., Vaca I.,
RA   Garcia-Rico R.O., Levican G., Tello M., Chavez R.;
RT   "The biosynthetic gene cluster for andrastin A in Penicillium roqueforti.";
RL   Front. Microbiol. 8:813-813(2017).
CC   -!- FUNCTION: ABC-type transporter; part of the gene cluster that mediates
CC       the biosynthesis of the meroterpenoid compound andrastin A, a promising
CC       antitumoral compound (PubMed:28529508). Is required for the production
CC       of andrastin A but does not have a significant role in its secretion
CC       (PubMed:28529508). {ECO:0000269|PubMed:28529508}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- DISRUPTION PHENOTYPE: Drastically reduces the production of andrastin A
CC       but does not affect its secretion. {ECO:0000269|PubMed:28529508}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCG family.
CC       PDR (TC 3.A.1.205) subfamily. {ECO:0000305}.
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DR   EMBL; KY349137; ART41208.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y0BRF0; -.
DR   SMR; A0A1Y0BRF0; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   CDD; cd03233; ABCG_PDR_domain1; 1.
DR   CDD; cd03232; ABCG_PDR_domain2; 1.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR013525; ABC_2_trans.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR043926; ABCG_dom.
DR   InterPro; IPR034001; ABCG_PDR_1.
DR   InterPro; IPR034003; ABCG_PDR_2.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR010929; PDR_CDR_ABC.
DR   Pfam; PF01061; ABC2_membrane; 2.
DR   Pfam; PF19055; ABC2_membrane_7; 1.
DR   Pfam; PF00005; ABC_tran; 2.
DR   Pfam; PF06422; PDR_CDR; 1.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE   3: Inferred from homology;
KW   ATP-binding; Membrane; Nucleotide-binding; Repeat; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..1452
FT                   /note="ABC-type transporter adrC"
FT                   /id="PRO_0000446491"
FT   TRANSMEM        487..507
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        524..544
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        569..589
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        598..618
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        631..651
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        738..758
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1149..1169
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1181..1201
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1224..1244
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1264..1284
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1287..1307
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1322..1344
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1415..1435
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          116..378
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   DOMAIN          813..1055
FT                   /note="ABC transporter 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   REGION          1..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        15..33
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         849..856
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ   SEQUENCE   1452 AA;  162812 MW;  2A321434EA76E3E4 CRC64;
     MAPEEGDQAM SHEDKAACSS LNTTSSTELF DGAPSSENER LRIRQAAVDA MHHGSPKIDP
     QIWTDVTSHL SGSTTIDARQ RDIFFENLTV HGKGSSLQIQ KTVLSALLYP IAYPVKRLMS
     IVGNKKPHND RRTILHGFNG ILNSGELLLV LGRPGSGCST FLKSLCGYLE GLDLDPVSEI
     QYRGVPFRVM IEKYRGDLVY NQEADHHFPN LTVGQTLEFA AHARAPHNQV GNSSRDQYVK
     SVVKVVMDTF GLSHTYDTNV GNDFVPGVSG GERKRVRTDT IVGMNSIAET VLSRTSIAAW
     DNSTRGLDAA TAVDFVRSLR TSAKLAGSCH AVAVYQASEG LYNTFDKVIL LYEGREIYFG
     PRQGAVAYFE TMGWKRPPQQ VSADFLTAIT NPGERQPQVG MENAVPRTPV EFESYWKNSP
     EHAELETSMR QYKMKTPLDS SEEIKLDEIK RLEQSNHARI SSPYLLSVPM QIRLCIVRAW
     QRTRNDIPAL IATAVAQTVV SLIIGSLFYN IPENTAGLGQ RASVLFLAVL TNALISLLEI
     TTLYSQRLIV EKQAAYAFVH PFTEAIAEVI VDFPIKLFRC LLSAIIVYFL ANLRREASHF
     FIYIMFQLTA VMTMATIFRT LATVTRTIGQ AMALAGVVII CIAVYTGFTV PQFDMPPWFG
     WIRWLNPIFY TFEGIVSNEF HGRHFECVEY IPSLSFEQGL SFTCSYVGSI AGERYVSGDA
     YIAGSYDYSY DHVWRNYGIL VAFLVFFYVL YFWLTELIPG TTPAHEVLIF RHGGVLQRLV
     RGDLERGESI RLQEVKSLAS EVHSSKAEQK NTFSWKGLSY DIPVKGGEKR LLDDVSGWVK
     PGSLTALMGV SGAGKTTLMN VLARRMTIGV VTGDMFVNGR ELDASFARNI GYVQQQDLHV
     ETCTIREALR FSAALRQPQS VSMEEKYNFV EEVIQLLGMQ NFAEAVIGSP GDGLNMEQRK
     LLSIGVELAA KPQLLIFLDE PTSGLDSRSS WAICAFMRKL ADHGQPVLAT IHQPSAVLFE
     QFDRLLFLAK GGRTVYFGDI GKQARTVLEY LEDKGARHCG PTENPAEYML EVIGGGTQGQ
     STSIDWVQAW KRSTEYNKLL GELDILASSP SNGVSADPYM VGEFAMPLLV QFYHVMKRDL
     QQYYRQPEYI LAKFGAGVFC GVFIGFSFWK SDNSSQGFQN VLFSLFLLCT IFSTLVNQIM
     PKFLSRRTLY ELRERPARTY SWKVFILCQI LVELPWQTLL GICTWASFYF SVYGSGQSSQ
     RQGLVLLFTV QFFIFASTFA QLVVAAVPSV VLGSMLATFT FLLCLLFNGT MQPPSALPRF
     WIFMNRVSPL TYYVGGISAT ALHGRPIHCS NRELRVFDPP QGQNCGQYLA EYLKTAQGTL
     SNPLSTDQCQ YCPLRVADQY LAARDISWDD RWRNFGIFWV YIIFNVIGAV LLYYLFRVLP
     YIRRNRTQKS RN