(data stored in ACNUC7421 zone)

SWISSPROT: Q758Q0_ASHGO

ID   Q758Q0_ASHGO            Unreviewed;       895 AA.
AC   Q758Q0;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 2.
DT   11-DEC-2019, entry version 94.
DE   SubName: Full=AEL297Wp {ECO:0000313|EMBL:AAS52387.2};
GN   ORFNames=AGOS_AEL297W {ECO:0000313|EMBL:AAS52387.2};
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:AAS52387.2, ECO:0000313|Proteomes:UP000000591};
RN   [1] {ECO:0000313|EMBL:AAS52387.2, 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; AE016818; AAS52387.2; -; Genomic_DNA.
DR   RefSeq; NP_984563.2; NM_209916.2.
DR   STRING; 33169.AAS52387; -.
DR   EnsemblFungi; AAS52387; AAS52387; AGOS_AEL297W.
DR   GeneID; 4620739; -.
DR   KEGG; ago:AGOS_AEL297W; -.
DR   HOGENOM; HOG000204521; -.
DR   InParanoid; Q758Q0; -.
DR   KO; K10875; -.
DR   OMA; GMVICDE; -.
DR   Proteomes; UP000000591; Chromosome V.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0015616; F:DNA translocase activity; IBA:GO_Central.
DR   GO; GO:0006338; P:chromatin remodeling; IEA:EnsemblFungi.
DR   GO; GO:0032392; P:DNA geometric change; IEA:EnsemblFungi.
DR   GO; GO:0045003; P:double-strand break repair via synthesis-dependent strand annealing; IBA:GO_Central.
DR   GO; GO:0030491; P:heteroduplex formation; IEA:EnsemblFungi.
DR   GO; GO:0032079; P:positive regulation of endodeoxyribonuclease activity; IEA:EnsemblFungi.
DR   GO; GO:0007131; P:reciprocal meiotic recombination; IBA:GO_Central.
DR   GO; GO:0000722; P:telomere maintenance via recombination; IEA:EnsemblFungi.
DR   Gene3D; 3.40.50.10810; -; 2.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR013967; Rad54_N.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR000330; SNF2_N.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF08658; Rad54_N; 1.
DR   Pfam; PF00176; SNF2_N; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   4: Predicted;
DR   PRODOM; Q758Q0.
DR   SWISS-2DPAGE; Q758Q0.
KW   Reference proteome {ECO:0000313|Proteomes:UP000000591}.
FT   DOMAIN          317..497
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          657..810
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          157..203
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        160..191
FT                   /note="Polyampholyte"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   895 AA;  100339 MW;  6FE2AEFD6FA10286 CRC64;
     MAKRKLPDRP PNGSGAGERP SVRPRRLDSG RAYSTLTQPF RVPLNSERTR HGERYGVRAT
     RRAVTTYAEE GGARSEENDV GGKRIDALSA QRLSKDAQRL AGIERTLRRS FSVPIKGYVP
     RHNIPLALGM KMRVVAPPRP LHDPTEEFAI VLYDPTVDGE IPDETPREEP AQKENDGGNE
     EQARPTRRTA THPEKLSNGL RNKTLRELLG TVTETPKFPS VPVVIDPRLA RILRPHQVEG
     VRFLYRCVTG LAMKDFLDTQ AVLAAGEVQD DGTGKDPGSK DSEPIVVEVL EETPTPTPTP
     TPTPSPEILD ANAAMTRESN RGAYGCIMAD EMGLGKTLQC IALMWTLLRQ GSQGRPTIEK
     CIIVCPSSLV NNWANEIVKW LGPDALSPLA IDGRKSSLSN GSVAQSVRQW AIAQGRNVVK
     PVLIISYETL RRNVENLKGC KVGLMLADEG HRLKNGDSLT FTSLDSINCP RRVILSGTPI
     QNDLSEYFAL LNFSNPGLLG TRAQFRKNFE IPILRGRDAD ATDKEIAAGE VKLHELSQIV
     SKFIIRRTND ILSKYLPCKY EHILFVNLSP MQKAIYEHFV RSREVAKLMK GTGSQPLKAI
     GLLKKLCNHP DLLDLPDEIA GSTNLIPDDY QSAMTHNSRG GRSHVEVQTT HSSKFAILER
     FLFKIKHESN DKIVLISNYT QTLDLIEKMC RYNHYGVLRL DGTMTINKRQ KLVDKFNDPS
     GEEFIFLLSS KAGGCGINLI GANRLILMDP DWNPAADQQA LARVWRDGQK KDCFIYRFIT
     TGSIEEKIYQ RQSMKMSLSS CVVDEKEDVE RLFSSDNLRQ LFQFDSNTIC DTHATYHCKR
     CRDGKQMIKA PAMLYGDATT WNHLNHDALL KTNDHLLRNE HQFNDISYVF QYISH
//

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