CLZ9_COCLU
ID CLZ9_COCLU Reviewed; 919 AA.
AC A0A345BJN8;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 07-NOV-2018, sequence version 1.
DT 25-MAY-2022, entry version 17.
DE RecName: Full=MFS-type transporter clz9 {ECO:0000303|PubMed:28605916};
DE AltName: Full=Squalestatin S1 biosynthesis cluster protein clz9 {ECO:0000303|PubMed:28605916};
DE AltName: Full=Zaragozic acid A biosynthesis cluster protein 9 {ECO:0000303|PubMed:28605916};
GN Name=clz9 {ECO:0000303|PubMed:28605916};
OS Cochliobolus lunatus (Filamentous fungus) (Curvularia lunata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Curvularia.
OX NCBI_TaxID=5503;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC 74067;
RX PubMed=28605916; DOI=10.1021/acs.orglett.7b01534;
RA Liu N., Hung Y.S., Gao S.S., Hang L., Zou Y., Chooi Y.H., Tang Y.;
RT "Identification and heterologous production of a benzoyl-primed
RT tricarboxylic acid polyketide intermediate from the zaragozic acid A
RT biosynthetic pathway.";
RL Org. Lett. 19:3560-3563(2017).
CC -!- FUNCTION: MFS-type transporter; part of the gene cluster that mediates
CC the biosynthesis of squalestatin S1 (SQS1, also known as zaragozic acid
CC A), a heavily oxidized fungal polyketide that offers potent cholesterol
CC lowering activity by targeting squalene synthase (SS).
CC {ECO:0000305|PubMed:28605916}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. CAR1 family.
CC {ECO:0000305}.
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DR EMBL; MF806533; AXF50651.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A345BJN8; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR Gene3D; 1.20.1250.20; -; 1.
DR Gene3D; 3.30.420.10; -; 1.
DR InterPro; IPR004875; DDE_SF_endonuclease_dom.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR Pfam; PF03184; DDE_1; 1.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS50850; MFS; 1.
PE 3: Inferred from homology;
KW Glycoprotein; Membrane; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..919
FT /note="MFS-type transporter clz9"
FT /id="PRO_0000452628"
FT TRANSMEM 69..89
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 192..212
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 222..242
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 303..323
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 333..353
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 393..413
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 418..438
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 465..485
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 641..809
FT /note="DDE-1"
FT /evidence="ECO:0000255"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 840..897
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..29
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 859..889
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 260
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 461
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 915
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 919 AA; 101381 MW; 9948C244AF1C3666 CRC64;
MAASTKPTTK LSTEEDDVSR RDSESSADFM KSNEELQATM IPEDDGANPA TGQPTWTILS
DTEIKSVLVV ASFAAAISPF STSTYYPVVT AIARDLGVSV SKINLTMSSY QIFQGVAPTI
TAAFADTYGR RPMFLVCFVT YFVANVGLAL QNDFTTLLVL RCLQSTGSSG TFALAQAVTA
DITTRAERGR YLIYATLGST LGPFIGPVIG GLLVKFLGWR SVFWFLLCMG TVFALLIFIF
FGETARPIVG DGSIPPQSWN RSYLQMRSKG VSNLKPNLAS LERRKSRPNP LTSLALLWDR
ENFILSVSGG LLYAGYSSVT SVLASQLQQR YKYDAVQVGL CYLPVGFGSL LAYRTTVRLM
DWNFEREAKK QGLVIVKNRQ TDISRFDLEK ARLGFVFPMI LVCSGLLVAY GWQMHYHAPL
APILVTMFLI AIILTGVMNA IAALLTDVNR ENAAAVGAAM NLTRLLLGAG AVAVVGPLNK
SAGIGWTATV TAGFSYNVNT KGIQTKRRAA AIFEVSRATL HRRCDGKRAR RDCQPNSKKL
IQQEEEVILK YILDLDTRGF LPTYAAERGM ADKLLSTRGG SPVGRDWPRN FVKHKAKYSI
LDEDVYSFDE AGFMMGKITT QLAVTGSERR GRPKAIQPEN REWVTLIQGI NAAGWAISPF
VVFAGQHHLS AWYEEDIPRD WAIAVSDNGW TTNEIGVEWL EHFIKYTDGK AVGVRRLLIF
DGHESHHSLK SRELCKENNI YTLYMPPHSS HLLQPLDIGC FSPLKRAYSR EIEALICHHI
NHITKLEFLP AFKAAFQRSF TSANICSSFR GAGLVPLQPD IVLSKLDVRL LTHIPAASPE
APWEAKTPSN RKKKQIQKRG TLTKGEGEDT LAQKEADQQI EREQRQGGEQ SGRSRQALAR
SLEALEVGGV AHSLNGSFV
