ISW2_CANAL
ID ISW2_CANAL Reviewed; 1056 AA.
AC Q5A310; A0A1D8PKM1;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=ISWI chromatin-remodeling complex ATPase ISW2;
DE EC=3.6.4.-;
GN Name=ISW2; OrderedLocusNames=CAALFM_C306310CA; ORFNames=CaO19.7401;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [4]
RP FUNCTION.
RX PubMed=14663094; DOI=10.1099/mic.0.26640-0;
RA Nobile C.J., Bruno V.M., Richard M.L., Davis D.A., Mitchell A.P.;
RT "Genetic control of chlamydospore formation in Candida albicans.";
RL Microbiology 149:3629-3637(2003).
RN [5]
RP INDUCTION.
RX PubMed=16339080; DOI=10.1091/mbc.e05-06-0501;
RA Enjalbert B., Smith D.A., Cornell M.J., Alam I., Nicholls S., Brown A.J.P.,
RA Quinn J.;
RT "Role of the Hog1 stress-activated protein kinase in the global
RT transcriptional response to stress in the fungal pathogen Candida
RT albicans.";
RL Mol. Biol. Cell 17:1018-1032(2006).
RN [6]
RP INDUCTION.
RX PubMed=21592964; DOI=10.1074/jbc.m111.233569;
RA Singh R.P., Prasad H.K., Sinha I., Agarwal N., Natarajan K.;
RT "Cap2-HAP complex is a critical transcriptional regulator that has dual but
RT contrasting roles in regulation of iron homeostasis in Candida albicans.";
RL J. Biol. Chem. 286:25154-25170(2011).
CC -!- FUNCTION: Catalytic component of the ISW2 complex, which acts in
CC remodeling the chromatin by catalyzing an ATP-dependent alteration in
CC the structure of nucleosomal DNA. The ISW2 complex is involved in
CC coordinating transcriptional repression and in inheritance of telomeric
CC silencing (By similarity). ISW2 is required for chlamydospore
CC formation, distinctive morphological feature of the fungal pathogen
CC C.albicans that can be induced to form in oxygen-limited environments
CC and has been reported in clinical specimens. {ECO:0000250,
CC ECO:0000269|PubMed:14663094}.
CC -!- SUBUNIT: Component of the ISW2 complex. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00624}.
CC -!- INDUCTION: Expression is induced by the HAP43 transcription factor and
CC repressed in response to high doses of peroxide stress.
CC {ECO:0000269|PubMed:16339080, ECO:0000269|PubMed:21592964}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. ISWI subfamily.
CC {ECO:0000305}.
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DR EMBL; CP017625; AOW28638.1; -; Genomic_DNA.
DR RefSeq; XP_716066.1; XM_710973.1.
DR AlphaFoldDB; Q5A310; -.
DR SMR; Q5A310; -.
DR STRING; 237561.Q5A310; -.
DR GeneID; 3642235; -.
DR KEGG; cal:CAALFM_C306310CA; -.
DR CGD; CAL0000192526; ISW2.
DR VEuPathDB; FungiDB:C3_06310C_A; -.
DR eggNOG; KOG0385; Eukaryota.
DR HOGENOM; CLU_000315_0_2_1; -.
DR InParanoid; Q5A310; -.
DR OMA; IHDWQFF; -.
DR OrthoDB; 61251at2759; -.
DR Proteomes; UP000000559; Chromosome 3.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IBA:GO_Central.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0031491; F:nucleosome binding; IEA:InterPro.
DR GO; GO:0071280; P:cellular response to copper ion; IMP:CGD.
DR GO; GO:0001410; P:chlamydospore formation; IMP:CGD.
DR GO; GO:0030447; P:filamentous growth; IMP:CGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd17997; DEXHc_SMARCA1_SMARCA5; 1.
DR CDD; cd00167; SANT; 1.
DR Gene3D; 1.10.1040.30; -; 1.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 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; IPR000330; SNF2_N.
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; SSF101224; 1.
DR SUPFAM; SSF46689; SSF46689; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51293; SANT; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW Reference proteome.
FT CHAIN 1..1056
FT /note="ISWI chromatin-remodeling complex ATPase ISW2"
FT /id="PRO_0000422104"
FT DOMAIN 151..316
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 457..608
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 833..885
FT /note="SANT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT REGION 85..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1010..1056
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 267..270
FT /note="DEAH box"
FT COMPBIAS 1021..1036
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1041..1056
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 164..171
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 1056 AA; 123094 MW; CCC6AC16C1F2A9E0 CRC64;
MTTTSTTTTN TTNGQFCSDE SLEERRKRFL LEVDAKHERA HDKDDATKRF QYLLGLSALF
RKFINLNASK DPAFKKRIRE IDSKTSFKES SKKAKNSRRR KTEKEEDAEL LQDEEHQDDE
DHQHTVMTES PSYIKEGKLR EYQIQGLNWL ISLYENRLSG ILADEMGLGK TLQTISFLGY
LRYIKHIDGP FIVIVPKSTL DNWRREFAKW TPDVNVVVLQ GDKEQRASII KDQLYTAKFD
VLITSFEMIL REKSALQKFR WEYIVVDEAH RIKNEDSSLS KIIRLFYSRN RLLITGTPLQ
NNLHELWALL NFLLPDVFGD SDQFDEAFDN QNSEELDEEE KQRRQDKAVS ELHQLLSPFL
LRRVKADVEK SLLPKIETNV YIGMTDMQVE WYKRLLEKDI DAVNGVVGKR EGKTRLLNIV
MQLRKCCNHP YLFDGAEPGP PYTTDEHLVY NSGKMIILDK MLKKFKAEGS RVLIFSQMSR
VLDILEDYCY FRDYEYCRID GSTSHEDRIE AIDEYNAPDS EKFIFLLTTR AGGLGINLTS
ADIVILYDSD WNPQADLQAM DRAHRIGQKK QVKVFRFVTE KAIEEKVLER AAQKLRLDQL
VIQQGRQMNS NNNVGNSKDD LIGMIQHGAK EVFENSKGTM LDDDVEEILK RGAEKTAELN
NKFNKLGLDD IQNFTSDASA YEWNGQDFTK KGNNASLGLN WINPSKRVRK ELTYSVDNYY
KDVLKQPAVV KEKVVKQPVV KPKAPKSYNV QDHQFFADEL VTLLEREQLA FKKEISYQYS
VDDFGDSDEE FLEQDDEDDM TRDEKRKIAQ EKINNAVALT EEEIATRDRL LEESFHNWSR
RDFTNFIHAT AKYGRNEYKK IAKALGNKKR SEIERYSKMF WQNYQKIEGY EKYLSQIEAV
EKKREKLINQ QKLLAKKIES LQDPLEDLKI QYPPNNSKRV YSKTEDKFLL YCVHKYGLST
ENLYDKIKDE ILTSDIFKFD WYIRSRTPQE IGRRISTLLL AITREMEGPL HGKKRKAMGE
SNNSSRFGSV EPSSINGEKH SPEVIDNEQT VKKLKL
