(data stored in SCRATCH zone)

SWISSPROT: Q750J4_ASHGO

ID   Q750J4_ASHGO            Unreviewed;       405 AA.
AC   Q750J4;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   11-DEC-2019, entry version 120.
DE   SubName: Full=AGL043Cp {ECO:0000313|EMBL:AAS54447.1};
GN   ORFNames=AGOS_AGL043C {ECO:0000313|EMBL:AAS54447.1};
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:AAS54447.1, ECO:0000313|Proteomes:UP000000591};
RN   [1] {ECO:0000313|EMBL:AAS54447.1, 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).
CC   -!- SIMILARITY: Belongs to the AAA ATPase family.
CC       {ECO:0000256|RuleBase:RU003651}.
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; AE016820; AAS54447.1; -; Genomic_DNA.
DR   RefSeq; NP_986623.1; NM_211685.2.
DR   STRING; 33169.AAS54447; -.
DR   EnsemblFungi; AAS54447; AAS54447; AGOS_AGL043C.
DR   GeneID; 4622922; -.
DR   KEGG; ago:AGOS_AGL043C; -.
DR   HOGENOM; HOG000225143; -.
DR   InParanoid; Q750J4; -.
DR   KO; K03066; -.
DR   OMA; MALDTFF; -.
DR   Proteomes; UP000000591; Chromosome VII.
DR   GO; GO:0031597; C:cytosolic proteasome complex; IBA:GO_Central.
DR   GO; GO:0031595; C:nuclear proteasome complex; IBA:GO_Central.
DR   GO; GO:0008540; C:proteasome regulatory particle, base subcomplex; IBA:GO_Central.
DR   GO; GO:0034515; C:proteasome storage granule; IEA:EnsemblFungi.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR   GO; GO:0019904; F:protein domain specific binding; IEA:EnsemblFungi.
DR   GO; GO:0017025; F:TBP-class protein binding; IBA:GO_Central.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:EnsemblFungi.
DR   GO; GO:0006338; P:chromatin remodeling; IEA:EnsemblFungi.
DR   GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; IEA:EnsemblFungi.
DR   GO; GO:0070651; P:nonfunctional rRNA decay; IEA:EnsemblFungi.
DR   GO; GO:0006289; P:nucleotide-excision repair; IEA:EnsemblFungi.
DR   GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IEA:EnsemblFungi.
DR   GO; GO:0045899; P:positive regulation of RNA polymerase II transcriptional preinitiation complex assembly; IBA:GO_Central.
DR   GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IEA:EnsemblFungi.
DR   GO; GO:0070682; P:proteasome regulatory particle assembly; IEA:EnsemblFungi.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:EnsemblFungi.
DR   InterPro; IPR005937; 26S_Psome_P45-like.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR041569; AAA_lid_3.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR003960; ATPase_AAA_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR032501; Prot_ATP_ID_OB.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF17862; AAA_lid_3; 1.
DR   Pfam; PF16450; Prot_ATP_ID_OB; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR01242; 26Sp45; 1.
DR   PROSITE; PS00674; AAA; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q750J4.
DR   SWISS-2DPAGE; Q750J4.
KW   ATP-binding {ECO:0000256|RuleBase:RU003651};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU003651};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000591}.
FT   DOMAIN          180..320
FT                   /note="AAA"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   COILED          26..60
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   405 AA;  45234 MW;  E060CAF70AD1DE15 CRC64;
     MAAIQVSTVP VNTHDSGVKP YFEQKIQETE LRIRTKTANL RRLEAQRNAL NDKVRFIKDE
     LRLLQEPGSY VGEVVKVVSD KKVLVKIQPE GKYIVDIAKD INVKDLKVSQ RVCLKSDSYV
     LHKVLENKVD PLVSLMMVEK VPDSTYDMVG GLTKQIKEIK EVIELPVKHP ELFESLGIAQ
     PKGVILYGPP GTGKTLLARA VAHHTDCKFI RVSGAELVQK YIGEGSRMVR ELFVMAREHA
     PSIIFMDEID SIGSSRVEGG SGGGDSEVQR TMLELLNQLD GFETSKNIKI IMATNRLDIL
     DPALLRPGRI DRKIEFPPPT VAARTEILRI HSRKMNLTRG INLRKIAEKM NGCSGADVKG
     VCTEAGMYAL RERRIHVTQE DFELAVAKVM NKNDETAISV AKLFK
//

If you have problems or comments...

PBIL Back to PBIL home page