(data stored in SCRATCH zone)

SWISSPROT: Q6BMG3_DEBHA

ID   Q6BMG3_DEBHA            Unreviewed;      1161 AA.
AC   Q6BMG3;
DT   16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT   04-NOV-2008, sequence version 2.
DT   08-MAY-2019, entry version 108.
DE   SubName: Full=DEHA2F05676p {ECO:0000313|EMBL:CAG88933.2};
GN   OrderedLocusNames=DEHA2F05676g {ECO:0000313|EMBL:CAG88933.2};
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC
OS   0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592 {ECO:0000313|EMBL:CAG88933.2, ECO:0000313|Proteomes:UP000000599};
RN   [1] {ECO:0000313|EMBL:CAG88933.2, ECO:0000313|Proteomes:UP000000599}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968
RC   {ECO:0000313|Proteomes:UP000000599};
RX   PubMed=15229592; DOI=10.1038/nature02579;
RG   Genolevures;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.F., Straub M.L., Suleau A.,
RA   Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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DR   EMBL; CR382138; CAG88933.2; -; Genomic_DNA.
DR   RefSeq; XP_460608.2; XM_460608.1.
DR   STRING; 4959.XP_460608.2; -.
DR   EnsemblFungi; CAG88933; CAG88933; DEHA2F05676g.
DR   GeneID; 2903381; -.
DR   KEGG; dha:DEHA2F05676g; -.
DR   InParanoid; Q6BMG3; -.
DR   OMA; RNKSAFG; -.
DR   OrthoDB; 132523at2759; -.
DR   Proteomes; UP000000599; Chromosome F.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   CDD; cd00079; HELICc; 1.
DR   Gene3D; 3.30.40.10; -; 1.
DR   Gene3D; 3.40.50.10810; -; 1.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR000330; SNF2_N.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00176; SNF2_N; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
DR   PRODOM; Q6BMG3.
DR   SWISS-2DPAGE; Q6BMG3.
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000599};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000599};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT   DOMAIN      484    682       Helicase ATP-binding.
FT                                {ECO:0000259|PROSITE:PS51192}.
FT   DOMAIN      873    925       RING-type. {ECO:0000259|PROSITE:PS50089}.
FT   DOMAIN      994   1147       Helicase C-terminal.
FT                                {ECO:0000259|PROSITE:PS51194}.
FT   COILED      320    340       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   1161 AA;  132148 MW;  80E4F9A62995EA35 CRC64;
     MASDEPSQNI INLSSDDDEE VDENVSLKDI QINGHEIHER GNNQDWRQAN SNSNTTHINQ
     PPKRQRLDSL YSNNGPFRSP SKQGNDLSHI GNSNHIQQRQ LYPKTLPNAV LDRTVFGPRS
     VSSNTTIQNH PRQSEPQSIP KNNLIQNQYM QADPQSIPNN NTIQYQSRQA DPQEDVIILS
     SEDEDMDSDG DIMILDAEEA SRIGKFKTSS FERNANRSSR DMGNYEAPAN TGPYYSVPAV
     NPNEMHVTYN NPAPVPHFTK DDGPEVEKLN FQRAQETLEE NVRRKDELLY KHEQLTSDFT
     KSSRQANELL QHLTLLQSHL KREEIQENRD ENTILSLKNE ISFKGAEYHN FRRSKDATAT
     SLSGIASKLS WLTVSIRDAK SRIHNYGKHR NGVNIIDNPF VLNNNSGRNN SDYENESIMN
     NPFGNIPGFS ANVYSDNDQQ HLQNLLNNIR PDEELDEEGL SLTPSELAIT LLKHQRMGLA
     WLLRMEESKS KGGILADDMG LGKTVQTIAL IMAHKSDDDN RKTNLVIAPV SLLRQWAAEI
     ESKIKPNAQI KIAIYHGSVK KNLRTFNSLK KYDVVLTSYG TLSSEWKKHY QGPLEEARLS
     RNQNVIPDLD AGGTSYTSPF FATDAVFYRI ILDEAQNIKN KSAIASKASY CIKGIHRFCL
     SGTPIQNNVE ELYPILRFLR IKPYNDESKF RSDIVLPIRS KSSGYDDFDK KKSMQKLRAL
     LRAILLRRSK NSLIDGKPIL SLPDKLVTED TVQMEDEELT YYRELEQGIQ KKAKTLLASE
     KLGSTSSILT LLLRLRQACC HSFLVEMGRM KAAESEATKT LITRDWKSMY VNIQKFDEDT
     INRIRNEVHQ GNLLKGENEG ESNTNSDEDL FTCPICYDVL GYESIVLFSG CGHMICNNCI
     ENFFERFETG DGSEGNRLAS CFSCSKSIKE NELIDYNMFH MIHQEGYDRD KIAEFYNINY
     SSNGKTTNMQ KIRQLIQENK GFTPSAKMEK CMHLIKDVLE NYPDEKIIIF SQFLSLFDLM
     KLVLANEKIP FLRYDGSMSL DEKNSTIKQF YQGSTKVLLI SLRAGNVGLT LTCASHVIIM
     DPFWNPYVEE QAMDRAHRIG QQRDVRVHRI LTEGSVEGRI MTLQNEKKEI ISGALDEKGM
     KSVSKLGRQE LGFLFGLNEL R
//

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