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Database: UniProt
Entry: I2H1D1_TETBL
LinkDB: I2H1D1_TETBL
Original site: I2H1D1_TETBL 
ID   I2H1D1_TETBL            Unreviewed;      1069 AA.
AC   I2H1D1;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 1.
DT   24-JAN-2024, entry version 64.
DE   RecName: Full=ISWI chromatin-remodeling complex ATPase ISW2 {ECO:0008006|Google:ProtNLM};
GN   Name=TBLA0C03810 {ECO:0000313|EMBL:CCH60183.1};
GN   ORFNames=TBLA_0C03810 {ECO:0000313|EMBL:CCH60183.1};
OS   Tetrapisispora blattae (strain ATCC 34711 / CBS 6284 / DSM 70876 / NBRC
OS   10599 / NRRL Y-10934 / UCD 77-7) (Yeast) (Kluyveromyces blattae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Tetrapisispora.
OX   NCBI_TaxID=1071380 {ECO:0000313|EMBL:CCH60183.1, ECO:0000313|Proteomes:UP000002866};
RN   [1] {ECO:0000313|EMBL:CCH60183.1, ECO:0000313|Proteomes:UP000002866}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 34711 / CBS 6284 / DSM 70876 / NBRC 10599 / NRRL Y-10934 /
RC   UCD 77-7 {ECO:0000313|Proteomes:UP000002866};
RX   PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA   Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA   Wolfe K.H.;
RT   "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT   accidents.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
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; HE806318; CCH60183.1; -; Genomic_DNA.
DR   RefSeq; XP_004179702.1; XM_004179654.1.
DR   AlphaFoldDB; I2H1D1; -.
DR   STRING; 1071380.I2H1D1; -.
DR   GeneID; 14495163; -.
DR   KEGG; tbl:TBLA_0C03810; -.
DR   eggNOG; KOG0385; Eukaryota.
DR   HOGENOM; CLU_000315_0_2_1; -.
DR   InParanoid; I2H1D1; -.
DR   OMA; EFQFRES; -.
DR   OrthoDB; 5482994at2759; -.
DR   Proteomes; UP000002866; Chromosome 3.
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   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:UniProt.
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   Coiled coil {ECO:0000256|SAM:Coils};
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:UP000002866}.
FT   DOMAIN          149..314
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          447..598
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   DOMAIN          837..890
FT                   /note="SANT"
FT                   /evidence="ECO:0000259|PROSITE:PS51293"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          84..114
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          627..653
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1026..1069
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          810..837
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        627..652
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1069 AA;  123581 MW;  24E9A635F14C2189 CRC64;
     MSEKSDYELA LEPFKEDMPP LDPESNKKRY LIKDGGKPHF DLDGTVKRFQ HLLGLSGLFR
     HFIEGKAKKD DRFQRVLDIL DDDGNKKGKG RAGHQDKRRR KTETEEDAEL LKGETDGDEE
     NLEFQFRESP GYIDGLLRSY QIQGVNWLIS LHKNGLAGIL ADEMGLGKTL QTITFLGYLR
     YVEKKPGPFL VIAPKSTLNN WLREINKWTP DVNAFILQGD KVERSELIKT KLLECDFEIV
     VASYEIIIRE KAAFRKIDWE YIVIDEAHRI KNEESMLSQV LREFSSRNRL LITGTPLQNN
     LHELWALLNF LLPDIFSSSE DFDSWFSSNE SEEDQDKIVK QLHTVLQPFL LRRIKSDVET
     SLLPKKELNL YVGMSNMQKK WYKQILEKDL DAVNGSNGNK ESKTRLLNIV MQLRKCCNHP
     YLFDGAEPGP PYTTDEHLVY NSAKLNVLDK LLEKVKEEGS RVLIFSQMSR VLDIMEDYCY
     FRGYEYCRID GQTAHEDRIA AIDEYNAPDS SKFIFLLTTR AGGLGINLTT ADIVVLFDSD
     WNPQADLQAM DRAHRIGQKK QVKVYRFVTD NSVEEKILER ATQKLKLDQL VIQQNRTSTQ
     KKKQKEKQNE QKDALLSMIQ HGAADVFKSG NTSTGSSARG TPHPSGTTSG NDDAAEKEAI
     DLESILELSE GKTQSLNQKY ATLGLDDLQK FNQDSAYEWN GTDFKKKTVE KDIISPLWIN
     PTKRERKENY NIDGYYKDVL NTGKTTTPTQ PRMPKPHAFN SHQFQPPQLK VLYEKERMWT
     AKKTGYKPTM EDVKNTYGEI EEEEKKKQLL ELLNLSIHNA QELSEEEKQE KLELEKKGFT
     NWNKIEFRKF ISASGKYGRN SIQAIAMELS GTKTLEEVRE YAKAFWKNIE QIEDYEKYLK
     SIEVEEEKIR RVKFQQEALR RKLSQCKAPL FDLSLKFPPS SSNKRTYSEE EDRFILLMLF
     KYGLDRDDVY ELIRDEIRDS PLFELDFFFQ SRTPTELARR GYTLLQCLEK EFNSSIVMDE
     ETKLRMKNED EEGSKVREEM GEASGANGTS ETSETSGTTD GHIDKKMKV
//
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