GenomeNet

Database: UniProt
Entry: R9XK78_ASHAC
LinkDB: R9XK78_ASHAC
Original site: R9XK78_ASHAC 
ID   R9XK78_ASHAC            Unreviewed;      1423 AA.
AC   R9XK78;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   SubName: Full=AaceriAGR123Cp {ECO:0000313|EMBL:AGO13982.1};
GN   ORFNames=AACERI_AaceriAGR123C {ECO:0000313|EMBL:AGO13982.1};
OS   Ashbya aceri (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=566037 {ECO:0000313|EMBL:AGO13982.1, ECO:0000313|Proteomes:UP000016920};
RN   [1] {ECO:0000313|Proteomes:UP000016920}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; CP006026; AGO13982.1; -; Genomic_DNA.
DR   HOGENOM; CLU_000315_29_2_1; -.
DR   OrthoDB; 5482994at2759; -.
DR   Proteomes; UP000016920; Chromosome VII.
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; cd18665; CD1_tandem_CHD1_yeast_like; 1.
DR   CDD; cd17993; DEXHc_CHD1_2; 1.
DR   CDD; cd11660; SANT_TRF; 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; IPR009057; Homeobox-like_sf.
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; SSF46689; Homeodomain-like; 1.
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   Coiled coil {ECO:0000256|SAM:Coils};
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   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          175..237
FT                   /note="Chromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50013"
FT   DOMAIN          265..330
FT                   /note="Chromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50013"
FT   DOMAIN          368..542
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          679..840
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          14..102
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          136..160
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          955..984
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1243..1333
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1035..1073
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        24..40
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        42..62
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        63..82
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        136..150
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1291..1307
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1313..1333
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1423 AA;  162596 MW;  5BBE1DB8754661AE CRC64;
     MAKDLPDEVL ANPELYGLRR SHRTPAGVST QATYYESNDD EDSVVVSGRG RKRKKAIDMD
     SYSEEELADN ESTNEDISGD EDEEFGAPVR RRRKKGRREA SVEEDIMLPT RFSSRNNKAV
     NYNIDYSDDD LLESAEEDYE GDEGDEGEDD AYAQTPQIPD EHGIDFVVTH RLREGYAEPV
     EWDVPECKEC YEFLIKWNNE SHIHNTWETA ESLGSVRGVK KVDNYIKQYI LLDHELRTDK
     YTTREDIEVM DLEHERRCDE FDEFKKVERI IDSDRVTLED GSSQLQYLVK WKRLNYDEAT
     WENASVIVKM APEEVKRFQS RSSSKILPQH SSNYGSQRPG FEKLSVQPSF IKGGELRDFQ
     LTGINWMAFL WSKSDNGILA DEMGLGKTVQ TVSFISWLIF ARRQNGPHLV VVPLSTMPAW
     QETFEKWAPD LNCVYYMGNQ KSRDVIRDYE FYTNPHTKGK KNIKFNVLLT TYEYILKDRL
     ELGSIKWQFL AVDEAHRLKN AESSLYESLS SFKVANRMLI TGTPLQNNIK ELAALVNFLM
     PGKFTIDQEI DFENQDEKQE NYIRDLHKRL QPYILRRLKK DVEKSLPSKT ERILRVELSD
     VQTEYYKNIL TKNYNALTAG SKGAHFSLLN IMNELKKASN HPYLFGNAEN RVLAKFGDGN
     RSRENILRGL IMSSGKMVLL DKLLTRLKKD GHRVLIFSQM VRMLDILGDY LSIKGINFQR
     LDGTVPSSQR RISIDHFNAP DSNDFVFLLS TRAGGLGINL MTADTVIIFD SDWNPQADLQ
     AMARAHRIGQ KNHVMVYRFV SKDTVEEEVL ERARKKMILE YAIISLGVTD GNKYTSKSKA
     EPSAGELSEI LKFGAGNMFK AHDNQKKLED LNLDDVLNHA EDHVTTPDLG ESHLGGEEFL
     KQFEVTDYKA DVEWDDIIPE DELRKLKDEE QKRKDEEYVQ EQLQMMNRRN VALNKIKNSV
     NGDGTQSLSD KEDSRSKKRA KSNNLNSIGE REIRALYKAI LKYGDLTERL ADLIADGTLP
     VKSLEKYSEL YDELMSIARK QINDEESKRN EAISKLERAV EEYKTKVKSG EIKPDDNAKD
     LPIARLAAKR REKRAVLFEF YEIKGLNAET IVNRTDDLRF LHSFLKSNYP SDPMKFRFLN
     RLPKPITNWN CTWTQEDDEK LLVGVDKYGY GSWSQVRDDP FLGLSDKIFL NEPGTQANDS
     SAADADAADK KTRLANAAKK VPGSVHLGRR VDYLLTVLRE EAKGTDSAAA PQAALAAKKR
     ARKSSGSSKS ATPDVRPEDS PSIKRARALQ PSASRPSSGS PGPQLKRNGK KQASPKAPVE
     REYESMDEDE CRRTMHSVRA SLKRLKRGGA GLDRNEWAAI LKRELLAVGN YIERHKGDSA
     DRDRAQFKRH LWSYSAQFWP AQVKSSKIMA MYDKLAASAA APR
//
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