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Database: UniProt
Entry: A0A0J6XYC9_COCIT
LinkDB: A0A0J6XYC9_COCIT
Original site: A0A0J6XYC9_COCIT 
ID   A0A0J6XYC9_COCIT        Unreviewed;      1123 AA.
AC   A0A0J6XYC9;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   22-FEB-2023, entry version 38.
DE   SubName: Full=ISWI chromatin remodeling complex ATPase ISW1 {ECO:0000313|EMBL:KMP00420.1};
GN   ORFNames=CIRG_00562 {ECO:0000313|EMBL:KMP00420.1};
OS   Coccidioides immitis RMSCC 2394.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX   NCBI_TaxID=404692 {ECO:0000313|EMBL:KMP00420.1, ECO:0000313|Proteomes:UP000054565};
RN   [1] {ECO:0000313|Proteomes:UP000054565}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RMSCC 2394 {ECO:0000313|Proteomes:UP000054565};
RX   PubMed=20516208; DOI=10.1101/gr.103911.109;
RA   Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA   Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA   Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA   FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA   Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA   Taylor J.W., Rounsley S.D.;
RT   "Population genomic sequencing of Coccidioides fungi reveals recent
RT   hybridization and transposon control.";
RL   Genome Res. 20:938-946(2010).
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; DS028093; KMP00420.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0J6XYC9; -.
DR   STRING; 404692.A0A0J6XYC9; -.
DR   Proteomes; UP000054565; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0031491; F:nucleosome binding; IEA:InterPro.
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; IPR000330; SNF2_N.
DR   PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR   PANTHER; PTHR45623:SF49; ISW-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}.
FT   DOMAIN          206..371
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          502..653
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   DOMAIN          868..920
FT                   /note="SANT"
FT                   /evidence="ECO:0000259|PROSITE:PS51293"
FT   REGION          1..69
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          133..180
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          827..859
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1044..1123
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        39..61
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        133..178
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1054..1073
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1094..1116
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1123 AA;  128577 MW;  7E42976BAF330EED CRC64;
     MAPSPNVEIP SEVDAPMVDV NGEPATDAAE DRADQTMTDY QDTPDYTDSD THPNTTASSV
     AGDLAPIDGR KRRSEAFQLR KSVLGKKHGR LDESKEDDSI RRFRYLLGLT DLFRHFIDTN
     PNPRIKEIMA EIDRQNEQET EKKKSSTRKG GASGERRRRT EQEEDAELLK DEKQGGPAET
     VFRESPSFIK GGEMRDYQIA GLNWLISLHE NGISGILADE MGLGKTLQTI SFLGYLRHIC
     GITGPHLITV PKSTLDNWNR EFSKWTPEVN VLVLQGAKEE RHQLINDRLI DEKFDVCITS
     YEMVLREKSH LKKFAWEYII VDEAHRIKNE ESSLAQIIRL FNSRNRLLIT GTPLQNNLHE
     LWALLNFLLP DVFGDSEAFD QWFSNQEADQ DTVVQQLHRV LRPFLLRRVK SDVEKSLLPK
     KEVNLYIGMS EMQVKWYQKI LEKDIDAVNG AQGKRESKTR LLNIVMQLRK CCNHPYLFEG
     AEPGPPYTTD EHLVDNAGKM VILDKLLKRL KNQGSRVLIF SQMSRVLDIL EDYCVFREHA
     YCRIDGSTAH EDRIAAIDDY NRPESDKFIF LLTTRAGGLG INLTSADIVI LYDSDWNPQA
     DLQAMDRAHR IGQTKQVVVF RFVTENAIEE KVLERAAQKL RLDQLVIQQG RAQQQTKNAA
     SKDELLSMIQ HGAASVFNSS GGTGTLAGGK DISEDDIDRI LKKGEERTAE LNKKYEKLGI
     DDLQKFTSDN AYEWNGEDFT NRKKDIGLNW INPAKRERKE QSYSIDNYYR QTIPTGGRTA
     DPKPKVPKAP KQIAVHDWQF FPPKLRELQD KETAYFHKEI GYKAVLPEGT EEDLSDREAE
     RELEQQEIDN ANPLTEEEKA EKERLSEQGF ATWNRRDFQQ FVNGSAKFGR TDYEGIATEV
     DSKIPEEIKE YAKVFWKRYT ELQDYPKYLR SIEQGEEKLR KMNHQRKLLR KKMERYRVPL
     QQLKINYNVS TTNKKVYTEE EDRFLLVMLD KHGVDGEGLH EKIREEIRES PLFRFDWFFL
     SRTPVEISRR CTTLLNTVAK EFEADGNVPN GHAGKGRGRD RDDDMENGEV NGPAKKRSKN
     GAVNKKLKAV KSAGGSKATS TATSRAASVS STVVTTKSKG RKK
//
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