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Database: UniProt
Entry: G8YLA7_PICSO
LinkDB: G8YLA7_PICSO
Original site: G8YLA7_PICSO 
ID   G8YLA7_PICSO            Unreviewed;      1377 AA.
AC   G8YLA7;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   SubName: Full=Piso0_001627 protein {ECO:0000313|EMBL:CCE88841.1};
GN   Name=Piso0_001627 {ECO:0000313|EMBL:CCE88841.1};
GN   ORFNames=GNLVRS01_PISO0F10543g {ECO:0000313|EMBL:CCE88841.1};
OS   Pichia sorbitophila (strain ATCC MYA-4447 / BCRC 22081 / CBS 7064 / NBRC
OS   10061 / NRRL Y-12695) (Hybrid yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Millerozyma.
OX   NCBI_TaxID=559304 {ECO:0000313|EMBL:CCE88841.1, ECO:0000313|Proteomes:UP000005222};
RN   [1] {ECO:0000313|Proteomes:UP000005222}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4447 / BCRC 22081 / CBS 7064 / NBRC 10061 / NRRL
RC   Y-12695 {ECO:0000313|Proteomes:UP000005222};
RX   DOI=10.1534/g3.111.000745;
RA   Leh Louis V., Despons L., Friedrich A., Martin T., Durrens P.,
RA   Casaregola S., Neuveglise C., Fairhead C., Marck C., Cruz J.A.,
RA   Straub M.L., Kugler V., Sacerdot C., Uzunov Z., Thierry A., Weiss S.,
RA   Bleykasten C., De Montigny J., Jacques N., Jung P., Lemaire M., Mallet S.,
RA   Morel G., Richard G.F., Sarkar A., Savel G., Schacherer J., Seret M.L.,
RA   Talla E., Samson G., Jubin C., Poulain J., Vacherie B., Barbe V.,
RA   Pelletier E., Sherman D.J., Westhof E., Weissenbach J., Baret P.V.,
RA   Wincker P., Gaillardin C., Dujon B., Souciet J.L.;
RT   "Pichia sorbitophila, an interspecies yeast hybrid reveals early steps of
RT   genome resolution following polyploidization.";
RL   G3 (Bethesda) 2:299-311(2012).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; FO082054; CCE88841.1; -; Genomic_DNA.
DR   STRING; 559304.G8YLA7; -.
DR   eggNOG; KOG0384; Eukaryota.
DR   HOGENOM; CLU_000315_29_2_1; -.
DR   InParanoid; G8YLA7; -.
DR   OMA; WVQIRDD; -.
DR   Proteomes; UP000005222; Chromosome F.
DR   GO; GO:0000123; C:histone acetyltransferase complex; IEA:UniProt.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   CDD; cd17993; DEXHc_CHD1_2; 1.
DR   CDD; cd18793; SF2_C_SNF; 1.
DR   Gene3D; 2.40.50.40; -; 2.
DR   Gene3D; 6.10.140.1440; -; 1.
DR   Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR   InterPro; IPR041150; Cdh1_DBD.
DR   InterPro; IPR025260; CHD1-like_C.
DR   InterPro; IPR016197; Chromo-like_dom_sf.
DR   InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR   InterPro; IPR023780; Chromo_domain.
DR   InterPro; IPR023779; Chromodomain_CS.
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; IPR049730; SNF2/RAD54-like_C.
DR   InterPro; IPR000330; SNF2_N.
DR   PANTHER; PTHR45623:SF14; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 1; 1.
DR   PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR   Pfam; PF18196; Cdh1_DBD_1; 1.
DR   Pfam; PF13907; CHD1-like_C; 1.
DR   Pfam; PF00385; Chromo; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   SMART; SM00298; CHROMO; 2.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM01176; DUF4208; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF54160; Chromo domain-like; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS00598; CHROMO_1; 1.
DR   PROSITE; PS50013; CHROMO_2; 2.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005222};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          154..225
FT                   /note="Chromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50013"
FT   DOMAIN          253..317
FT                   /note="Chromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50013"
FT   DOMAIN          356..524
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          659..817
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          19..109
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          921..961
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1190..1274
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        19..55
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        56..73
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        90..109
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        931..961
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1377 AA;  158835 MW;  D26620F02DB03E5F CRC64;
     MVKPLIPDEV ALNPELYGLR RSHRERKVPA MVESDGSDEE LAPRGRKAKD NNYNFEDGYD
     EDDYDEDLPD DDDDFSVSTK KRKSNTKNSK PTVKKSNIPT PPSEVRFSAR NNKQVNYVVD
     YDDDNDLLES DVDEENGEGG AAYYYDYDNE QEERAIEQVM DHNLNEENAE ITNDPKLDYL
     FKIKWSDTSH LHNTWEACST LKNYKGFRRV ENYIKQYIVL DQEIRKDPST TSEDIEAMDI
     ELERRRDEQE EYTKVERIVD SERVEVDGQS KLQYFCKWRR LYYDECSWED AERIAEIAPE
     QVTKYQQRLN SKILPHLSAN YPHNQRPRFE KLVKQPLFIK NGELRDFQLT GLNWMAFLWS
     RNENGILADE MGLGKTVQTV SFLSWLIYAR RQNGPHLVVV PLSTITSWQE TFEKWAPDVN
     CVYYLGNSAA RKTIRDYEFY QNKKLKFNIL LTTYEYVLKD RSELGSIKWQ FLAVDEAHRL
     KNEESSLYES LKSFKVGNRL LITGTPLQNN IKELNALCNF LMPGRFNIGQ EIDFETPNRE
     QEQYIKDLQK NIQPFILRRL KKDVEKSLPS KSERILRVEL SDLQTEYYRN ILTKNYSALN
     AGNKGSQISL LNVVSELKKA SNHPYLFDGA EERALAKASS TSRDNILRGI IMSSGKMVLL
     EQLLNRLKKE GHRVLIFSQM VRMLDILGDY LSIKGLQFQR LDGGVPSSQR RISIDHFNAP
     DSKDFVFLLS TRAGGLGINL MTADTVIIFD SDWNPQADLQ AMARAHRIGQ KNHVSVYRFV
     SKDTIEEEIL ERARKKMILE YAIISLGITD KTSQKSKSEP STGELSEILK FGAGNMFKAN
     DNQKKLEDLN LDDVLKHAED HVTTPDLGES NLGSEEFLKQ FEVTDYKADI EWDDIIPQEE
     LAKLKEEEKK RADEEFLQEQ IAMNSRRKTA SRNLQEIDES DDDNSTSENQ RSKARKKNSE
     NYQLSEKEVR GIYRSILRLG DLSGKWEQLV EEGSISNKNP VLIKHAYNEI INISRRMVKE
     EDARRTKVLQ ELERKAKESK DGSIANPDGS GSMALWVAKK KEKRAVLFEY QGVKNINAEL
     VLARPKDMKL LESVIPKDDM LSFHFPKTPK PVKDWNCEWT VKNDAMLLVG VYKFGYGSWM
     QIRDDPLLGL QNKFFLENPK DNKDEKSKKV PGSVHLGRRV DYLFSLLKEE EQPSDKTSSS
     NGNAASKKRP VKKTKSETPV TAKKKSVKSQ SPEVNRKTKP KKAKSKASPT PASDANKEHG
     NHSSNPVKNE PVDDKELEYD SMDEAYCKST LKPVSKSLMK LHKGNTGFEK SEWATILRKE
     LVTIGDFIDE KSNEPEGASD RLKKHLWSYA SLYWPAKVPS KKINEMYNRL KTQEKKP
//
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