(data stored in SCRATCH zone)

SWISSPROT: Q750B0_ASHGO

ID   Q750B0_ASHGO            Unreviewed;      1492 AA.
AC   Q750B0;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 2.
DT   11-DEC-2019, entry version 124.
DE   SubName: Full=AGR047Wp {ECO:0000313|EMBL:AAS54536.2};
GN   ORFNames=AGOS_AGR047W {ECO:0000313|EMBL:AAS54536.2};
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811 {ECO:0000313|EMBL:AAS54536.2, ECO:0000313|Proteomes:UP000000591};
RN   [1] {ECO:0000313|EMBL:AAS54536.2, ECO:0000313|Proteomes:UP000000591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Pohlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2] {ECO:0000313|Proteomes:UP000000591}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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DR   EMBL; AE016820; AAS54536.2; -; Genomic_DNA.
DR   RefSeq; NP_986712.2; NM_211774.2.
DR   STRING; 33169.AAS54536; -.
DR   EnsemblFungi; AAS54536; AAS54536; AGOS_AGR047W.
DR   GeneID; 4623012; -.
DR   KEGG; ago:AGOS_AGR047W; -.
DR   InParanoid; Q750B0; -.
DR   KO; K05665; -.
DR   OMA; NEWRVDA; -.
DR   Proteomes; UP000000591; Chromosome VII.
DR   GO; GO:0005623; C:cell; IEA:GOC.
DR   GO; GO:0000324; C:fungal-type vacuole; IBA:GO_Central.
DR   GO; GO:0000329; C:fungal-type vacuole membrane; IEA:EnsemblFungi.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATPase activity; IEA:InterPro.
DR   GO; GO:0015431; F:ATPase-coupled glutathione S-conjugate transmembrane transporter activity; IEA:EnsemblFungi.
DR   GO; GO:0044604; F:ATPase-coupled phytochelatin transmembrane transporter activity; IEA:EnsemblFungi.
DR   GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0015127; F:bilirubin transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:EnsemblFungi.
DR   GO; GO:0098849; P:cellular detoxification of cadmium ion; IEA:EnsemblFungi.
DR   GO; GO:0006749; P:glutathione metabolic process; IEA:EnsemblFungi.
DR   GO; GO:0071996; P:glutathione transmembrane import into vacuole; IEA:EnsemblFungi.
DR   GO; GO:0036246; P:phytochelatin 2 import into vacuole; IEA:EnsemblFungi.
DR   GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR   GO; GO:0042144; P:vacuole fusion, non-autophagic; IEA:EnsemblFungi.
DR   Gene3D; 1.20.1560.10; -; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR011527; ABC1_TM_dom.
DR   InterPro; IPR036640; ABC1_TM_sf.
DR   InterPro; IPR003439; ABC_transporter-like.
DR   InterPro; IPR017871; ABC_transporter_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   4: Predicted;
DR   PRODOM; Q750B0.
DR   SWISS-2DPAGE; Q750B0.
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00434};
KW   Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00434};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000591};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        33..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        67..90
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        96..113
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        125..145
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        157..176
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        327..348
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        429..450
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        511..534
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        546..571
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        929..950
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        970..994
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1058..1084
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1154..1175
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          278..572
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50929"
FT   DOMAIN          608..835
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   DOMAIN          930..1213
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50929"
FT   DOMAIN          1250..1485
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   NP_BIND         645..652
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00434"
FT   NP_BIND         1284..1291
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00434"
FT   COILED          450..470
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1492 AA;  167381 MW;  F7CC7D079AB0A6B8 CRC64;
     MGTMRAERGS RPDWGGGPIS FYGDLELTFI DGVLLRGTAL LMLAVGSARV WRLIARPHPG
     VKYRQDWLLM ARLGCSAVFL ALCAAAGATV QGDASIYWLT AASTAVAIVL QWISFMRAPV
     SDGVLLFYWL FEALVHVARS VNFTIRHFYE DQWPAGHRAF VFEILLVASA LLVLALEAGP
     QKRKKPYQEI RELHSSRRRN PLEKAHIFQR ITFSWMSEMM SNGYRRYLTE RDLYQLPAEH
     DARTLSEDME KRWQRELNKR ARPSLAWVLF SSFSHKILLA VLFKICHDIL AFTQPQLLRL
     LIKFVTEYSK ARGDISAEED VPLVRGFMLA VGMFLVSVVQ TTVLQQYFLQ AFDTGTDLRS
     GITSLIYKKA LHLSNEASGT SATGDIVNLM SVDAQRLRDL TQWGNVIWSG PFQLCLCLYS
     LHRLLGPCIW VGVVLLLFTL PLNSYISRVL KRLQKEQMKN KDERTRLISE ILNNIKSLKL
     YAWEIPYKEK LDYVRNQKEL KTLRKMGLTT AFANFQYNII PFLVSCSTFA VFVLTQKGRP
     LTTDLVFPAL TLFNLLSFPL AVLPIAITSF IEASVAIGRL TNFLTAEELQ RDAITREPAV
     KAPGGVAVAL ADNATFLWQR KPEYKVALKN INFRAKKSEL TCIIGKVGSG KSALIQAMLG
     DLFRVNGSAV VRGNVAYVSQ VAWIMNGTVR DNILFGHKYD AKFYQQTIKA CALTVDLSIL
     PDGDNTFVGE KGISLSGGQK ARLSLARAVY ARADTYLLDD PLAAVDEHVA KHLLQNVFGP
     NGLLKSKARV LTTNKITALE IADHIVLLEN GEIVQQGTFS EVISDEDSAI SKLVLHHGKK
     QNGAPTSGES SSPSSSAFEY DVVEPDLDLE KLADEELQVQ DVFSLRRPSD ATFKSISFAE
     TAHEEHREQG KVKWSIYLEY AKACNPRHVV VFLCVLTLSM FLSVMGGVWL KHWSEVNTRY
     GYNPNVALYL GVYFMFGLGA SLSTLIQSAI LWIYCSIHAS VYLHESMLAA VLRAPMSFFE
     TTPIGRILNR FSNDIYKVDE LLARTFSQFF ANTTRVSFTI IVICVTTWQF TFFVIPLAML
     YIYYQQYYLK TSRELRRLDS VTKSPVYAHF QETLNGVSSI RGYGQLDRFI HINQARINNN
     TSAYYPSMNV NRWLAYRLEF IGSCIIFFAA TLSVFRLASG SLTSGMVGLS LSYALQITQS
     LNWIVRMTVE VETNIVSVER IKEYAELEPE APQFIANSVP SGDWPKDGEI KFENYSTRYR
     PGLDLILRGI NLHIKPHERV GIVGRTGAGK SSLALSLFRI IEAAEGHISI DGVPIDTIGL
     TDLRKKLSII PQDSQVFEGT VRDNIDPTKQ YTDEQIWKAL ELSHLADHVK GMGSDGLDTP
     LTEGGKNLSV GQRQLMCLAR ALLIPSRILV LDEATAAIDV ETDKVIQDTI RSSFNDRTIL
     TIAHRINTIM DSDKIVVLDK GTVAEFDTPE NLLKKKEESI FYTLCKEAGL TS
//

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