FUM19_GIBM7
ID FUM19_GIBM7 Reviewed; 1489 AA.
AC Q8J2Q1; W7L9F5;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=ABC transporter FUM19 {ECO:0000303|PubMed:12620260};
DE AltName: Full=Fumonisin biosynthesis cluster protein 19 {ECO:0000303|PubMed:12620260};
GN Name=FUM19 {ECO:0000303|PubMed:12620260}; ORFNames=FVEG_00329;
OS Gibberella moniliformis (strain M3125 / FGSC 7600) (Maize ear and stalk rot
OS fungus) (Fusarium verticillioides).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium fujikuroi species complex.
OX NCBI_TaxID=334819;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=M3125 / FGSC 7600;
RX PubMed=12620260; DOI=10.1016/s1087-1845(02)00525-x;
RA Proctor R.H., Brown D.W., Plattner R.D., Desjardins A.E.;
RT "Co-expression of 15 contiguous genes delineates a fumonisin biosynthetic
RT gene cluster in Gibberella moniliformis.";
RL Fungal Genet. Biol. 38:237-249(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M3125 / FGSC 7600;
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D.,
RA Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A.,
RA Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C.,
RA Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S.,
RA Galagan J., Cuomo C.A., Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
RN [3]
RP INDUCTION.
RX PubMed=25217721; DOI=10.1016/j.ijfoodmicro.2014.08.026;
RA Cruz A., Marin P., Magan N., Gonzalez-Jaen M.T.;
RT "Combined effects of benomyl and environmental factors on growth and
RT expression of the fumonisin biosynthetic genes FUM1 and FUM19 by Fusarium
RT verticillioides.";
RL Int. J. Food Microbiol. 191:17-23(2014).
CC -!- FUNCTION: ABC transporter that may provide the dual role fumonisin
CC export and self-protection by allowing the fungus to evade the harmful
CC effect of its own fumonisin production (PubMed:12620260).
CC {ECO:0000305|PubMed:12620260}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: Expression is strongly reduced by benomyl (PubMed:25217721).
CC {ECO:0000269|PubMed:25217721}.
CC -!- DISRUPTION PHENOTYPE: Does not affect the production of fumonisins B1
CC and B2, but strongly decreases the production of fumonisin B3
CC (PubMed:12620260). {ECO:0000269|PubMed:12620260}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCC family.
CC Conjugate transporter (TC 3.A.1.208) subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EWG36213.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF155773; AAN74822.1; -; Genomic_DNA.
DR EMBL; DS022242; EWG36213.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_018742404.1; XM_018886768.1.
DR AlphaFoldDB; Q8J2Q1; -.
DR SMR; Q8J2Q1; -.
DR TCDB; 3.A.1.208.40; the atp-binding cassette (abc) superfamily.
DR GeneID; 30058706; -.
DR KEGG; fvr:FVEG_00329; -.
DR eggNOG; KOG0054; Eukaryota.
DR OrthoDB; 138195at2759; -.
DR Proteomes; UP000009096; Chromosome 1.
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 GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR CDD; cd18579; ABC_6TM_ABCC_D1; 1.
DR CDD; cd18580; ABC_6TM_ABCC_D2; 1.
DR Gene3D; 1.20.1560.10; -; 2.
DR Gene3D; 3.40.50.300; -; 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; IPR044746; ABCC_6TM_D1.
DR InterPro; IPR044726; ABCC_6TM_D2.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00664; ABC_membrane; 2.
DR Pfam; PF00005; ABC_tran; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF90123; SSF90123; 2.
DR PROSITE; PS50929; ABC_TM1F; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell membrane; Glycoprotein; Hydrolase; Membrane;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1489
FT /note="ABC transporter FUM19"
FT /id="PRO_0000441154"
FT TRANSMEM 33..53
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 116..136
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 143..163
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 264..284
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 302..322
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 373..393
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 397..417
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 482..502
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 511..531
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 890..910
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 945..965
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 977..999
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 1031..1051
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 1120..1140
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 1149..1169
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT DOMAIN 272..539
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 591..823
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 902..1187
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1214..1485
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 852..874
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 625..632
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1254..1261
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 612
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 616
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 670
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1489 AA; 165139 MW; 417DF1BBF09075EB CRC64;
MMNFEGCPSD ASFGPFVKGC RGDFDFTLKF ELIIFFIAPS CVFTALTFVR IFVLVSKSRI
MTGNRIPLNL IKNVYSPIQI RENCFSSSQV LGLVAGMTTA ALSYYEHWYS RRPSMLLSIY
LFLSLLLDIA HDRTLWLNAY STLEYGFSSV FSAAVAIKAF AVWLESRPLS KLPWGDSHVK
ETPDSTSGVY SLSSFMWLRG LLRLGYRKVL ALSDLPALHG NMLGVVYDRF RKCSVNHFTR
AEQSQERGKY KLVHALSTTL TLHLLLPVLP RIALIGLSLA QAFLTQAVLR YLEEDQPHSY
SWGLIGATVL IYGGISICTS LYWYFHERLL CLVRGCLASA IFHKTLELSL TSNARSASVT
LMSTDIDRIH KGFLNLHELW ANIVEAGLAA WFLWRQVGIA FIAPIGLVLL SFLGVSIVGN
YVGLYQKAWM GKIQNRVAIT ANVISNIKHL KVSGMTRPVE SIIQNTRESE LRASRGTRRL
QIASLIIAFA PDLTAPGIML AATKSQDFSS HKVYTAIALL TLLTVPLGSI FRSVSPLMSA
FACLERIQAF LELDTRKDPR LITHSTPDTS SASGDEKVYA DPLPMSRSSA VKVIQASFGW
QGKEQACLKN INLTVNYSAL TAIIGPVGSG KSTLCKALLG ETPFSAGKVV LERDASCKVG
YCDQTPFIRN CSIKENIVGF SKWNPVRYLE VVEASMLSYD LRELPEGDAT IVGSGGMTLS
GGQKQRIAIA RSLYLDTRLL ILDDILSGLD TQTEHHLFQH VLSPNGLLKK RENAPAIVFS
THSVKYARWA DHIFLLNEKG EMIEQGSWEE LSTYQSHLQS LCIQEKVQMT DLKQLEPVES
EQPLDVTMSE IEQTRSSRRG ADNQETIASG ADSSARQNGD LGVYRHYFRA VPPVAIISFV
TSSLSYGFLY SFPNIWLKWW LLDADSTRPH HPKAFWNGIY AMFQILALLS ELLTMYLALT
YFALISGATV HSSALRAITR APLYFFASVD LGTITNYFSQ DMTLVDGALP ASLIQFASDV
AASLGMAGNL AASSPYLAAS YPLCFFLLYF VTKYYLRTSR QLRLLDLEAK SPLYAHFLEL
ENGIATIRAA DWTGEYLVQS RLLLDVSQRP AYLLAMVQRW LLFILNTFVS LLALFTVALV
TQLNNHGTGF AGAGLISLMQ IGQFLTNVVR SYATLEVSMG AVSRLKALTE SPHRECIEGQ
EVVPPQEWPC RGSIKIDGVS ASYDSQNDQV NEKSFSLREL NLHIEAGQKV AICGRTGSGK
SSIILLLLHM LRPLRNTRED AITIDGISIQ NVDPPILRER IFAVPQDTIF LPQGSSWLEN
MEPFATNAAE CRSVLEDVNL WDVVIAQGGD LTAALDSDTL SQGQRQLFGL ARAVLRKRAK
AQSMSEPAPQ GGLLLLDEPS SAVDFETEGL MHRVIQREFC EYTVIMVTHR LEFITQIHSV
GQVSVDTQQG LFDRVLVVDA GTIVEDGHPA QLLESKEGKF RALWEASRV
