ID C5MCP3_CANTT Unreviewed; 1024 AA.
AC C5MCP3;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE SubName: Full=Chromatin remodelling complex ATPase chain ISW1 {ECO:0000313|EMBL:EER32323.1};
GN ORFNames=CTRG_03994 {ECO:0000313|EMBL:EER32323.1};
OS Candida tropicalis (strain ATCC MYA-3404 / T1) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=294747 {ECO:0000313|EMBL:EER32323.1, ECO:0000313|Proteomes:UP000002037};
RN [1] {ECO:0000313|EMBL:EER32323.1, ECO:0000313|Proteomes:UP000002037}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-3404 / T1 {ECO:0000313|Proteomes:UP000002037};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. ISWI subfamily.
CC {ECO:0000256|ARBA:ARBA00009687}.
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DR EMBL; GG692399; EER32323.1; -; Genomic_DNA.
DR RefSeq; XP_002549697.1; XM_002549651.1.
DR AlphaFoldDB; C5MCP3; -.
DR STRING; 294747.C5MCP3; -.
DR EnsemblFungi; CTRG_03994-t43_1; CTRG_03994-t43_1-p1; CTRG_03994.
DR GeneID; 8295842; -.
DR KEGG; ctp:CTRG_03994; -.
DR VEuPathDB; FungiDB:CTRG_03994; -.
DR eggNOG; KOG0385; Eukaryota.
DR HOGENOM; CLU_000315_0_2_1; -.
DR OrthoDB; 5482994at2759; -.
DR Proteomes; UP000002037; Unassembled WGS sequence.
DR GO; GO:0036436; C:Isw1a complex; IEA:EnsemblFungi.
DR GO; GO:0036437; C:Isw1b complex; IEA:EnsemblFungi.
DR GO; GO:0030874; C:nucleolar chromatin; IEA:EnsemblFungi.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:EnsemblFungi.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0031491; F:nucleosome binding; IEA:EnsemblFungi.
DR GO; GO:0000182; F:rDNA binding; IEA:EnsemblFungi.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IEA:EnsemblFungi.
DR GO; GO:0006354; P:DNA-templated transcription elongation; IEA:EnsemblFungi.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:EnsemblFungi.
DR GO; GO:1902275; P:regulation of chromatin organization; IEA:EnsemblFungi.
DR GO; GO:0001178; P:regulation of transcriptional start site selection at RNA polymerase II promoter; IEA:EnsemblFungi.
DR GO; GO:0007062; P:sister chromatid cohesion; IEA:EnsemblFungi.
DR GO; GO:0006363; P:termination of RNA polymerase I transcription; IEA:EnsemblFungi.
DR GO; GO:0006369; P:termination of RNA polymerase II transcription; IEA:EnsemblFungi.
DR CDD; cd17997; DEXHc_SMARCA1_SMARCA5; 1.
DR CDD; cd00167; SANT; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 2.
DR Gene3D; 1.20.5.1190; iswi atpase; 1.
DR Gene3D; 1.10.1040.30; ISWI, HAND domain; 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; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR044754; Isw1/2_DEXHc.
DR InterPro; IPR015194; ISWI_HAND-dom.
DR InterPro; IPR036306; ISWI_HAND-dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR017884; SANT_dom.
DR InterPro; IPR015195; SLIDE.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR PANTHER; PTHR45623:SF49; SWI_SNF RELATED, MATRIX ASSOCIATED, ACTIN DEPENDENT REGULATOR OF CHROMATIN, SUBFAMILY A, MEMBER 1; 1.
DR Pfam; PF09110; HAND; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF09111; SLIDE; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00717; SANT; 2.
DR SUPFAM; SSF101224; HAND domain of the nucleosome remodeling ATPase ISWI; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51293; SANT; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
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:UP000002037}.
FT DOMAIN 145..310
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 444..595
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 818..870
FT /note="SANT"
FT /evidence="ECO:0000259|PROSITE:PS51293"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 83..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 721..742
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 779..798
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 998..1024
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 721..738
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1024 AA; 119314 MW; 02CD6169BEBEB2C7 CRC64;
MSSTEATPSF DVTDGSETMN DFSFENNQRK YFTKSDKQQV DIEKTSNRFK YLLGLTSLFR
HFIEAKANKD PLFRKIVDDI HDSESKPGKK GSDASKRRRK TEKEEDAELL KDERLTSSIF
EFTESPGYVD GKLRPYQIQG LNWLISLYEN NLSGILADEM GLGKTLQTIS FLGYLRYMRG
INGPHLVITP KSTLDNWQRE FNRWIPDIKV LVLQGDKDER AELIKSKVMQ CEFDIIIASY
EIVIREKSTL KKFDWEYIVI DEAHRIKNEE SLLSQIIRMF HSKNRLLITG TPLQNNLREL
WALLNFILPD VFADNESFDE WFQKEDQEEE DQDKVISQLH KVLKPFLLRR IKADVEKSLL
PKKELNVYVK MAPMQKNLYK KILEKDIDAV NGSNGKKESK TRLLNIVMQL RKCCNHPYLF
EGMEPGPPYT TDEHLVFNSQ KMLILDQMLK KFQQEGSRVL IFSQMSRMLD ILEDYCYFRE
YQYCRIDGQT EHSDRINAID EYNKPGSEKF VFLLTTRAGG LGINLTTADI VILFDSDWNP
QADLQAMDRA HRIGQTKQVK VFRFITENAI EEKVLERATQ KLRLDQLVIQ QGRNTGGLDG
QQSSKAASKN ELLDLIQFGA ADMFHKDNSA APGGSGEGEA TVDIEDILKK SEEKTQELNE
KYAKLNLNAL QNFSNDDSVY NWNGEDFKKK ELGIQLPVVE LGKRERKENY SVDTYYRDVF
NAGSNKSSST TSRSGPKPPK QLNIYDHQFY PAKVLELYEL EKNYYRKQIN YKVPLKAADK
NTSQEELEKE QRLEQEEIDN SRPLTDEERA LKEELMQQGF STWNRRDFHH FISVCSKYGR
NSIRLISQEF EDKTEEEVRE YAQAFWKNYQ EIDGYERYIN QIEQGEEKII KGKVQKEALR
RKLSQYKYPL QELVLKYPPA STNKRVFSDE EDRFLLVQLY KYGLDSPDVY DNIREAIRQS
PLFQFDFFFQ TRNSGELSRR CTTLLGCVLK EINPENNVNY GAGSNNGKRS KDATPEPKSK
KQKK
//
