CICA_EMENI
ID CICA_EMENI Reviewed; 1396 AA.
AC A0A1U8QTJ9; C8V0E1; Q5AZ37;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2017, sequence version 1.
DT 03-AUG-2022, entry version 28.
DE RecName: Full=ABC-type transporter cicA {ECO:0000303|PubMed:24244835};
DE AltName: Full=Cichorine biosynthesis cluster protein A {ECO:0000303|PubMed:24244835};
GN Name=cicA {ECO:0000303|PubMed:24244835}; ORFNames=AN6443, ANIA_06443;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
RN [3]
RP FUNCTION.
RX PubMed=22510154; DOI=10.1021/ja3016395;
RA Ahuja M., Chiang Y.M., Chang S.L., Praseuth M.B., Entwistle R.,
RA Sanchez J.F., Lo H.C., Yeh H.H., Oakley B.R., Wang C.C.;
RT "Illuminating the diversity of aromatic polyketide synthases in Aspergillus
RT nidulans.";
RL J. Am. Chem. Soc. 134:8212-8221(2012).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24244835; DOI=10.1039/c2md20055d;
RA Sanchez J.F., Entwistle R., Corcoran D., Oakley B.R., Wang C.C.;
RT "Identification and molecular genetic analysis of the cichorine gene
RT cluster in Aspergillus nidulans.";
RL Med. Chem. Commun. 3:0-0(2012).
RN [5]
RP BIOTECHNOLOGY.
RX PubMed=30708999; DOI=10.3390/molecules24030515;
RA Liao L., Zhang X., Lou Y., Zhou C., Yuan Q., Gao J.;
RT "Discovery of three new phytotoxins from the fungus Aspergillus nidulans by
RT pathway inactivation.";
RL Molecules 24:0-0(2019).
CC -!- FUNCTION: ABC-type transporter; part of the gene cluster that mediates
CC the biosynthesis of cichorine, a phytotoxin active against knapweed,
CC corn, and soybeans (PubMed:24244835). CicA is probably involved in the
CC secretion of cichorine (Probable). {ECO:0000269|PubMed:24244835,
CC ECO:0000305|PubMed:24244835}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:24244835};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Abolishes the production of cichorine.
CC {ECO:0000269|PubMed:24244835}.
CC -!- BIOTECHNOLOGY: Cichorine and its derivatives are promising in the
CC course of developing novel herbicides. {ECO:0000269|PubMed:30708999}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCC family.
CC Conjugate transporter (TC 3.A.1.208) subfamily. {ECO:0000305}.
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DR EMBL; BN001301; CBF69461.1; -; Genomic_DNA.
DR EMBL; AACD01000108; EAA58465.1; -; Genomic_DNA.
DR RefSeq; XP_664047.1; XM_658955.1.
DR AlphaFoldDB; A0A1U8QTJ9; -.
DR SMR; A0A1U8QTJ9; -.
DR STRING; 162425.CADANIAP00006532; -.
DR EnsemblFungi; CBF69461; CBF69461; ANIA_06443.
DR EnsemblFungi; EAA58465; EAA58465; AN6443.2.
DR GeneID; 2871340; -.
DR KEGG; ani:AN6443.2; -.
DR eggNOG; KOG0054; Eukaryota.
DR HOGENOM; CLU_000604_27_1_1; -.
DR OMA; FVKFFGW; -.
DR OrthoDB; 138195at2759; -.
DR Proteomes; UP000000560; Chromosome I.
DR Proteomes; UP000005890; 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 GO; GO:0062032; P:cichorine biosynthetic process; IMP:GO_Central.
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; 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 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Glycoprotein; Membrane; Nucleotide-binding;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1396
FT /note="ABC-type transporter cicA"
FT /id="PRO_0000450883"
FT TRANSMEM 142..162
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 191..211
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 300..320
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 324..344
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 409..429
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 440..460
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 816..836
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 852..872
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 930..947
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 951..970
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 1036..1056
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 1065..1085
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT DOMAIN 143..466
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 525..751
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 816..1093
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1131..1380
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 510..543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 751..787
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 563..570
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1165..1172
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 321
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 604
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 880
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1096
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1150
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1154
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1396 AA; 155892 MW; F4A720ACD473A5B6 CRC64;
MRLSSEAKIA ESGGQPPTAG SRSETGSEST EAESADPKAQ KWYQRSLNPL RWQKIPPVPE
ERTVSREYGA SFFSIASFQW MAPLMKVGYL RPLELQDIWT VNPDREVDVL TKRFEVSLEK
RTNAGAKRPL LWALYDTFRF EFLLGGFCHL ISSLLIVFAP YLTRYQIAFA TEAYVAQRSG
QPAPRIGRGM GFVVGITVMQ AIQSLCTNQF LYRGQMVGGQ IRAVLILQIF NKAMKLSGRA
KAGGVQSPEQ QEKIKELKAA KDQALKKPGS PPADDKGWGN GRIVALMSID VDRINLACGM
FHISWTAPVS IIVALILLLV NLTYSALAGF GLLVIGMPFL TYAVRFLFKR RRNINKLTDQ
RVSLTQEILQ GVRFVKFFGW ESSFLDRLKE IRHHEIRSIQ TLLAVRNGIL CVSMAIPVFA
SMLSFITYAL SNHVLDPAPI FSSLALFNSL RMPLNLLPLV LGQITDAWTA LNRIQEFIVA
EEQKEDIERD EHMPEAVRMD RASFTWERKA ADKEAEKVEK KANPRRTEPK SEAPTDSAES
DEPFQLRDMT LDIRRDELVA VIGTVGSGKS SLLAALAGDM RLTDGSVRLS TSRAFCPQYT
WIQNTSLRDN ILFGKDYDEK WYDQVIDACA LKPDLEILPN GDATEIGERG ITISGGQKQR
LNIARAIYFN AELVLLDDPL SAVDAHVGRH IMDKAICGLL KGRCRILATH QLHVLSRCDR
IVVMDDGRIH AVGTFDELSR DNDLFKQLMS TASQDSKEDE EEATEVVEEE AEKQAQQEPT
KPAAALMQQE EKATDSVGWT VWKAYIRASG SYFNALAILF LLAFANVVNV WTNLWLSYWT
SNHYPSLSTG QYIGIYAGLG AGSALTMFIF STYMSTAGTN ASRQMLQLAM TRVLRAPMSF
FDTTPLGRIT NRFSKDIGVM DNELCDAMRM YAITITMIVS IMILIIVFYH YFAIALVPLF
LLFLTASNYY RSSAREMKRH ESILRSAVYA RFSEAITGTA SIRAYGVQNQ FRSSLRDSVD
TMNGAYFLTF SNQRWLSVRL DAVAVLLVFV TGVLVVTSRF DVSPSISGLV LSYILAIAQM
LQFTVRQLAE VENNMNATER VHYYGTQLEE EAPAHIPSNP VPESWPPHGE ITFDNVAMRY
RPGLPLVLKN LSMNISGGER IGIVGRTGAG KSSIMSALFR LTELSSGRIT IDGVDISTIG
LHDLRSRLAI IPQDPTLFRG SIRSNLDPFN EHSDLELWDA LRKAHLIDSD TKDSAVDASN
PNGNANAQRL TLDTAVDEEG LTFSLGQRQL MALARALVRN ARIIICDEAT SSVDFATDQR
IQETMAQGFE GKTLLCIAHR LKTIIHYDRI CVMDQGSIAE IDTPLNLWEK EDGIFRAMCE
RSGISREDIV GQVEKE
