OBLD_ASPCL
ID OBLD_ASPCL Reviewed; 1446 AA.
AC A1C8C8;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=ABC-type transporter oblD {ECO:0000303|PubMed:27116000};
DE AltName: Full=Ophiobolin biosynthesis cluster protein D {ECO:0000303|PubMed:27116000};
GN Name=oblD {ECO:0000303|PubMed:27116000}; ORFNames=ACLA_076900;
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
RN [2]
RP FUNCTION.
RX PubMed=27116000; DOI=10.1021/acs.orglett.6b00552;
RA Narita K., Chiba R., Minami A., Kodama M., Fujii I., Gomi K., Oikawa H.;
RT "Multiple oxidative modifications in the ophiobolin biosynthesis: P450
RT oxidations found in genome mining.";
RL Org. Lett. 18:1980-1983(2016).
CC -!- FUNCTION: ABC-type transporter; part of the gene cluster that mediates
CC the biosynthesis of the sesterterpenes ophiobolins, fungal phytotoxins
CC with potential anti-cancer activities (PubMed:27116000). Acts as a
CC specific transporter involved in ophiobolins secretion (By similarity).
CC {ECO:0000250|UniProtKB:M2UCE5, ECO:0000269|PubMed:27116000}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
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; DS027045; EAW14649.1; -; Genomic_DNA.
DR RefSeq; XP_001276075.1; XM_001276074.1.
DR AlphaFoldDB; A1C8C8; -.
DR SMR; A1C8C8; -.
DR STRING; 344612.A1C8C8; -.
DR EnsemblFungi; EAW14649; EAW14649; ACLA_076900.
DR GeneID; 4708211; -.
DR KEGG; act:ACLA_076900; -.
DR VEuPathDB; FungiDB:ACLA_076900; -.
DR eggNOG; KOG0065; Eukaryota.
DR HOGENOM; CLU_000604_35_0_1; -.
DR OMA; TFAHFMI; -.
DR OrthoDB; 37708at2759; -.
DR Proteomes; UP000006701; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma 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 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; IPR029481; ABC_trans_N.
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; PF14510; ABC_trans_N; 1.
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; Cell membrane; Glycoprotein; Membrane; Nucleotide-binding;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1446
FT /note="ABC-type transporter oblD"
FT /id="PRO_0000451173"
FT TRANSMEM 468..488
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 502..522
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 548..568
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 577..597
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 610..630
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 719..739
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1147..1167
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1177..1197
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1217..1237
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1265..1285
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1301..1321
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1412..1432
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 104..357
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 796..1038
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 832..839
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 9
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 28
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 222
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 281
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 305
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1344
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1359
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1446 AA; 162111 MW; 73F2BE0A73A1C62E CRC64;
MNEDHEAGNS SREAEVHQLA RQFTDQSNYS AAGQNPFAVE AGSALDPNGE HFNARAWCKA
MLQMHTGDKQ AHPLRTLGVA FSNLNVHGFG SDTDYQKSVG NVWLEVLSLV SKAFGQKQRK
IEILQNMEGL VEAGEMLVVL GPPGSGCSTF LKTIAGETYG FHVDKNSNIN FQGIAKQMAH
EFRGEAIYTA EVDVHFPKLT VGDTLYFAAR ARAPRHIPGG VNATQYASHM RDVIMAMFGI
SHTKNTIVGN DFIRGVSGGE RKRVSIAEAC LSNAPLQCWD NSTRGLDSAN AIEFCKTLRM
QADINGTTAC VSLYQAPQAA YDYFDKALVL YEGREIYFGR TSMAKQYFLD MGFVCPDRQT
DADFLTSMTS HLERVVQPGY EGRVPRTPDE FAARWRASPQ RAQLLQDIKC YNAKFALDGE
YLDKLKQSRR AQQAKAQRVS SPYTLSYVQQ VELCLWRGYQ RLKADPSVTI SSVFGNTIIS
LVIASIFYNL KADTSTFFQR GALLFFAVLM NALGCGLEML TLYAQRGIIE KHSRYALYHP
SAEAFSSMIM DLPYKIINAI TSNIVLYFMT NLRREPGAFF FFVFTSFVLT LTMSMFFRSM
ASLSRSLVQA LPFSAVLLLG LSMYTGFTIP TGYMLGWARW IAYINPISYG FESLLINEFH
NRDFPCMNYV PSGPGYTDLG LNNRVCSTVG SVPGQAFVNG DAYIESAYIY TASHKWRNIG
VIFAYMFLLA AVYLVATDFI TEKKSKGEIL VFPRGHEALK KGKSDEDLEE GSGRSVTVEK
TGSDGLTMIE RQTAIFQWKD VCFDIKIGKE NRRILDHVDG WVKPGTLTAL MGVSGAGKTT
LLDVLATRTS VGIISGEILV DGQPRDDSFQ RKTGYAQQQD LHLSTATVRE ALEFSALLRQ
SAHVPRQEKI DYVTEVIKLL DMTEYADAVI GVPGEGLNVE QRKRLTIGVE LAARPQLLLF
LDEPTSGLDS QTSWAILDLL DKLKKNGQAI LCTIHQPSAM LFQRFDRLLF LQAGGRTVYF
GEVGENSQIL IDYFVRNGGP PCPPAANPAE WMLDVIGAAP GSHTNINWFE TWRKSPEYAR
VQEHLAELKR ERPEQTNLFR TTSSQKREDK ASYREFAAPF CAQLCEVQVR VFQQIWRSPT
YIYSKTALCV LSALFVGFSL FHTPNTIQGL QNQMFGIFML LTVFGQLIQQ IMPHFVAQRA
LYEVRERPAK TYSWKAFIIS NIVVELPWNS LMSVLMFLCW YYPIGLYRNA EPTDAVSLRG
TQMWLMVWTF LLFSSTFAHF MIAAFDAAEN AGNLGNLLFL LCLIFCGVLA TPGQLPGFWI
FMYRVSPFTY LVSGMLSVGI SNTNATCADN EYLRFDPVNG TCGKYMDSYI SNMGGYLEDE
MATSDCSFCP IKETNVFLSS VSSSYSEIWR NFGLMWVFIV FNIFAACLLY WWVRVPRVKK
PVAKTE
