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OBLD_EMEVA
ID   OBLD_EMEVA              Reviewed;        1473 AA.
AC   A0A1V1GB10;
DT   07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2017, sequence version 1.
DT   03-AUG-2022, entry version 19.
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};
OS   Emericella variicolor (Aspergillus stellatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1549217;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=GF10;
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|PubMed:27116000};
CC       Multi-pass membrane 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; LC127211; BAX09285.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V1GB10; -.
DR   SMR; A0A1V1GB10; -.
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; IPR017871; ABC_transporter-like_CS.
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; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE   3: Inferred from homology;
KW   ATP-binding; Cell membrane; Glycoprotein; Membrane; Nucleotide-binding;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..1473
FT                   /note="ABC-type transporter oblD"
FT                   /id="PRO_0000451175"
FT   TRANSMEM        480..500
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        514..534
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        560..580
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        589..609
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        622..642
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        733..753
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1153..1173
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1189..1209
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1234..1254
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1277..1297
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1312..1332
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1425..1445
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          115..370
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   DOMAIN          808..1050
FT                   /note="ABC transporter 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         844..851
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   CARBOHYD        62
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        294
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        319
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        1371
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        1470
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   1473 AA;  164454 MW;  DBC253FFFAC5552F CRC64;
     MTDFNAIDLD EGTSKGSPSP EKRDAEVQQL AKQYTQQSAS SIYGQNPFCA DAGSALDPNG
     DNFSARAWCK AMLQLQTEDD KAHPPRTLGV AFGNLNVHGF GSDTDYQKSV GNVWLQALGL
     LRKALPGQRQ RKIDILHGLD GLVEAGEMLV VLGPPGSGCS TFLKTIAGET HGFYIDKASH
     LNYQGATAKH IANDFRGEAI YTAEVDVHFP RLTVGDTLFF AARARAPRHI PGGVTINEYA
     AHMRDVIMAM FGISHTRDTI IGNDFVRGVS GGERKRVTIA EASLSMAPLQ CWDNSTRGLD
     SANAIEFCKT LRMQADINNT TACVSLYQAP QAAYDNFDKV LVLYKGRQIY FGPTATAKQY
     FLDMGFECPD RQTDADFLTS MTSPKERVVR PGSEHQVPHT PDEFAARWKD STERARLLGA
     IEAYNAKFSD GQQLDKFRQS RRAQQAKIQR VSSPYTLSYT QQIQLCLWRG WLRLKADPSI
     TISSLFGNSI VALILGSMFY DLNGDTSSFF QRGALLFFAV LINALGCGLE MLTLYAQRGI
     VEKHARYALY HPSSEAFASM LMDLPYKILN TIIFNLILYF MTNLRREAGA FFFFLFVNFI
     LTLTMSMFFR SIASLTRTLV QALPAAAIFI LGLTMYTGFA IPTDYMLGWA KWIRFINPIN
     FGFESLMVNE FHNRDFPCVN FVPSGLGYAD IGSGNQVCST VGSVAGQGFV NGDAYVESLY
     DYTNSHKWRN VGIIFVFMIG LMFVYLAATE LILEKRSKGE ILVFRHGHSA LTGKSHDDEE
     DAGGRTVAMA EKTESDDLAI IERQTAIVQW KDVCYDIKVG KENRRILDHI DGWVKPGTLT
     ALMGVSGAGK TTLLDALATR TTMGVISGEI LVDGKQRDES FQRKTGYAQQ QDLHLSTSTV
     REALTFSAVL RQPAHVPRQE KVDYVTEVIK LLDMTEYADA VIGVPGEGLN VEQRKRLTIG
     VELAARPALL LFLDEPTSGL DSQTSWSILD LLDKLKKNGQ AILCTIHQPS AMLFQRFDRL
     LFLKSGGQTV YFGDVGENSH ILIDYFVRNG GRPCPPAANP AEWMLEVIGA APGSHTDIDW
     FSTWRKSPEY ARVQEHLQEL KLERSQLTDL ARTESGQKRQ NKADYREFAA PFYEQLCEVQ
     YRVFQQLWRS PMYIYSKTVL CSSSALFVGF SLFRSPNSIQ GCQNQLFSIF MLLTIFGQLI
     QQIMPHFVAQ RDLYEVRERP AKTYSWKAFM VSNILVELPW NSLMSLIMFL CWYYPVGLYR
     NAEPTDAVTL RGAQMWLFIW AFLLFSSTFA HFMIAAFDSA ENAGNMGNLL YILCLLFCGV
     LATPDQFPGF WIFMYRVSPF TYLVSGMLGV GLANTHVTCA ANEYLHFDPV NGSTCAEYME
     AYRTTMGGYV LNGDATSDCS FCPMDDTNAY LATVSANYGD VWRNFGIMWV YIVFNAVAAC
     ALYWWVRVPK GKKEAVETGA GAEAQKKTQN GSA
 
 
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