ALT5_ALTAL
ID ALT5_ALTAL Reviewed; 1576 AA.
AC A0A3G9H9H1;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 13-FEB-2019, sequence version 1.
DT 03-AUG-2022, entry version 14.
DE RecName: Full=ABC transporter ALT5 {ECO:0000250|UniProtKB:Q8J2Q1};
DE AltName: Full=AAL-toxin biosynthesis cluster protein 5 {ECO:0000303|Ref.1};
GN Name=ALT5 {ECO:0000303|Ref.1};
OS Alternaria alternata (Alternaria rot fungus) (Torula alternata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Alternaria;
OC Alternaria sect. Alternaria; Alternaria alternata complex.
OX NCBI_TaxID=5599;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=As-27;
RA Akagi Y., Akamatsu H., Takao K., Tsuge T., Kodama M.;
RT "AAL-toxin biosynthetic genes cluster in the tomato pathotype of Alternaria
RT alternata.";
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION.
RX PubMed=19749175; DOI=10.1128/ec.00135-09;
RA Akagi Y., Akamatsu H., Otani H., Kodama M.;
RT "Horizontal chromosome transfer, a mechanism for the evolution and
RT differentiation of a plant-pathogenic fungus.";
RL Eukaryot. Cell 8:1732-1738(2009).
CC -!- FUNCTION: ABC transporter that may provide the dual role AAL-toxin
CC export and self-protection by allowing the fungus to evade the harmful
CC effect of its own AAL-toxin production. {ECO:0000250|UniProtKB:Q8J2Q1,
CC ECO:0000305|PubMed:19749175}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- MISCELLANEOUS: Gene clusters encoding host-selective toxins (HSTs) are
CC localized on conditionally dispensable chromosomes (CDCs), also called
CC supernumerary chromosomes, where they are present in multiple copies.
CC The CDCs are not essential for saprophytic growth but controls host-
CC selective pathogenicity. {ECO:0000269|PubMed:19749175}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCC family.
CC Conjugate transporter (TC 3.A.1.208) subfamily. {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; AB969680; BBG74265.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3G9H9H1; -.
DR SMR; A0A3G9H9H1; -.
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; 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; 1.
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 3: Inferred from homology;
KW ATP-binding; Cell membrane; Membrane; Nucleotide-binding; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..1576
FT /note="ABC transporter ALT5"
FT /id="PRO_0000449858"
FT TRANSMEM 27..47
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 72..92
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 267..287
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 289..309
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 321..341
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 387..407
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 417..437
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 500..520
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 525..545
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 915..935
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 957..977
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 981..1001
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 1035..1054
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 1060..1078
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 1142..1162
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 1171..1191
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT DOMAIN 289..556
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 602..834
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 919..1199
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1236..1567
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 636..643
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1278..1285
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 1576 AA; 173102 MW; B39DAABF6743A79D CRC64;
MDFAKCIGDE FFGPVVDGCR GGFDFTLKFE LLFFATIPPA IFLILAVPRI ASLYSEPTIV
AWRSWLYASK QILGFVNLVL QVTLLVMTTQ GTAQFKLSGL FLSARIVTTS STLLSVIVCH
YEHSRCRRPS TILDVYLGLT LFLDIAHNRT LWLSVSSSLD AIFVRFHTTT VACKAVLAIL
ESLSKKRLFV LHNRTTQSLD GTRGSYSLST FSWLSRLLLS GYQNPLRLDS LPLLDEAMAV
ETLYARFLEN TKGYLGESSG SDQKSRLPLS QALAKTLLLP LLLPILPRLV LIGLSISQAF
LIQAVTGFLS AKNKADEVGY GLIGATILIY VGIALSTSLY WYYHQRFLYM ARSCLTSGIF
RKTTELSEAT LAESQAITLM STDIERVLAG FLNLHELWAS LIQAVIVSWI LWTRLKGFFA
LPVGLTVACF VALATVGRYI GGFQKTWMQE TQKRVAMIAS VLASMKQVKV SGLAATIDKK
VQQARKTELR ASHGVRMLQI TAMTLSLLPE LIAPVITLAA TSESVATSNI FTIVALISLL
TAPLGQLFQS VAPLMSGLAC LDRIQTYLEL EPVRERRGHN KSRLERIVDG PASSDEDYSY
AFRVVNGSFR WQKDSPHCLQ NVNLTVKHAA FTMIVGPVGS GKSTLCKALL GEISLSAGRV
LVGKESEGKI AYCGQTPFLS NSTIRDNIVH FSQWNTSRYI EVIEASGLSY HLARLPDGHD
TLVGSNGLLL SGGQRQLIAI ARALYSDAHT LIFDDVLSGL DARTEDHVFR HIFGPSGLLR
KRHDRPAVIL CTQSVMYLPL ADHIIVLSEQ GDIAEQGKWE VLNSNGGYLQ SLCVRDADAT
TPKVELGVEG ESERNHWHTT ESDEMRTKET LEQQLVVSEN DEATVSGPAS SGPSHVVAWS
GGLANYRYYL KAVSVVALVA FLASAICYGF FFAFPTLWLN FWVRDATSKH RSHTNAFWVG
IYGLFHALSL LGGFLTMYLA VTSISLVSGA SLHSSIFAAI MRAPLSLFRT IDQGTLTNYF
SQDITLVDGE LPRSLIQFVC DLAISLSMAG VLAASSPYLA AMYPIAIALM YATVKLYLRT
SRQLRILALE AKSPLYMHFL DVGRGIATLR AARLLKQYEN QNDQLLEISQ RPAYLLAMVQ
YWLLFILNII VMFLAIFVVT LVTQLRNHGT GFAGSGLVML LQFGQILASA MQSYAKLETS
MGAVHRLKSL FEHVVSDTVG EKGISPPLSW PSKGYIKLDG VSASYMSTNE ETDNTLGGLA
LRNIRLVVEP GQHVAICGRS GSGKSSLVLL LLGLLEPLQS TGCDAITIDG LDIRTIKQAV
LSERIIAVSQ DTIFLPAGAS WQENLDLLGT CTTSEVKSVL ENMNLWSLIE SQDGGLTAAM
KPEELSSGQK QLFSVARAVL RKRVKDREIR QASSIEIPST SQLRLASDAQ ECKKTESDCE
AVEGDSDLYC LPQLEPSNDT RLAAGREDVL GGVLLLDEFN SSMDLLTEQR YFNRIQSEFP
GYTIIAITHS LASFIKDQEC RQEGEAQVYR GGFFDRIIVL DSGMIVEDGH PTTLLETSHS
KFRALCEAAA RGEVST
