ID A0A1I8MJF7_MUSDO Unreviewed; 2001 AA.
AC A0A1I8MJF7;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Chromodomain-helicase-DNA-binding protein Mi-2 homolog isoform X1 {ECO:0000313|RefSeq:XP_005180660.1};
GN Name=101901187 {ECO:0000313|EnsemblMetazoa:MDOA005536-PA};
GN Synonyms=LOC101901187 {ECO:0000313|RefSeq:XP_005180660.1};
OS Musca domestica (House fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Muscoidea;
OC Muscidae; Musca.
OX NCBI_TaxID=7370 {ECO:0000313|EnsemblMetazoa:MDOA005536-PA};
RN [1] {ECO:0000313|EnsemblMetazoa:MDOA005536-PA}
RP IDENTIFICATION.
RC STRAIN=Aabys {ECO:0000313|EnsemblMetazoa:MDOA005536-PA};
RG EnsemblMetazoa;
RL Submitted (JAN-2021) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_005180660.1}
RP IDENTIFICATION.
RC STRAIN=Aabys {ECO:0000313|RefSeq:XP_005180660.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_005180660.1; XM_005180603.3.
DR EnsemblMetazoa; MDOA005536-RA; MDOA005536-PA; MDOA005536.
DR GeneID; 101901187; -.
DR KEGG; mde:101901187; -.
DR VEuPathDB; VectorBase:MDOA005536; -.
DR OrthoDB; 2910821at2759; -.
DR Proteomes; UP000095301; Unassembled WGS sequence.
DR Proteomes; UP000694905; Unplaced.
DR GO; GO:0005694; C:chromosome; IEA:UniProt.
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:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd18667; CD1_tandem_CHD3-4_like; 1.
DR CDD; cd18662; CD2_tandem_CHD3-4_like; 1.
DR CDD; cd17994; DEXHc_CHD3_4_5; 1.
DR CDD; cd15531; PHD1_CHD_II; 1.
DR CDD; cd15532; PHD2_CHD_II; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 2.40.50.40; -; 2.
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 Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR012957; CHD_C2.
DR InterPro; IPR009462; CHD_II_SANT-like.
DR InterPro; IPR012958; CHD_N.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR009463; DUF1087.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
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 InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45623:SF13; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED; 1.
DR PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR Pfam; PF08074; CHDCT2; 1.
DR Pfam; PF06461; CHDII_SANT-like; 1.
DR Pfam; PF08073; CHDNT; 1.
DR Pfam; PF00385; Chromo; 1.
DR Pfam; PF06465; DUF1087; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00628; PHD; 2.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00298; CHROMO; 2.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01146; DUF1086; 1.
DR SMART; SM01147; DUF1087; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00249; PHD; 2.
DR SUPFAM; SSF54160; Chromo domain-like; 2.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS50013; CHROMO_2; 2.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000694905};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 373..420
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 433..480
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 484..556
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 606..667
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 733..915
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1047..1209
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 194..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 667..707
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1322..1382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1538..1726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..52
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..74
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..117
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..233
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..266
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..300
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..324
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 677..707
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1334..1352
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1367..1382
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1547..1562
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1577..1681
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1708..1723
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2001 AA; 225724 MW; 9CB03D4A00ADEA4D CRC64;
MASEEENEET IHEEEEAADE TAQQAELSND SDAPLKPNND EDDDYDPEDT RKKKKGKKRK
TRKGEEKGRK KKKRKKNESE DDSDFMQHDD DADYANTSSS KRGRKRKEVD KSSKEKETSS
SGMPSVEDVC LAFDVTDVDI QYTEEELQQL TTYKAFTQHV RPILQKENTK VPAPKLMMLV
TAKWREFCDA HPNLVQNEQN ETANEPRSSR SSRNEKPDDL YEEEEDEEEE EEKESSSSAR
RKRGGRGRGK KGRRSGKVPT LKIKFGKRKR GSSDEDQDAS GASERDSDIE FEKMLQKSDD
SADDIPNTSS AAATASTSAA AAASGEAGAT NDDGTPVVKK KAKVKIGNKF KKKKKLKTTS
RFPDGEDGEH EHQDYCEVCQ QGGEIILCDT CPRAYHLVCL EPELEEPPEG KWSCPHCEAD
GGAAEEDDDD EHQEFCRICK DGGELLCCDS CPSAYHTFCL NPPLDTIPDG DWRCPRCSCP
ALTGKPEKII TWRWAETKDA KGKGKNGSRT REYFVKWHNM SYWHCEWVPE IQMEVHHPLM
IRSFSRKYDM EEPPKFEETL DEADSRYVRI QRHKAKGGIQ ADEEDEQYKK DLEDRFYKNG
VKPEWLIVQR VINHRTARDG TTMYLVKWRD LPYDKSTWED ESDDIPGLKQ AIDYYLDLRA
MCTSEQRLNK KKKGRKSKNK DLEEEERPQR RFTPPPEKPT TDLKKKYEGQ PPFLEATGMQ
LHPYQIEGIN WLRYSWSNGV DTILADEMGL GKTIQTVTFL YSLYKEGHCK GPFLVAVPLS
TIINWEREFE LWAPDFYCIT YVGDKDSRAV IRENELSFEE GAIRGGKASR LRTNQYKFNV
LLTSYELITM DAACLGSIDW AVLVVDEAHR LKSNQSKFFR ILNSYTITYK LLLTGTPLQN
NLEELFHLLN FLSGDKFNDL NAFQNEFADV SKEEQVKRLH EMLGPHMLRR LKADVLKNMP
SKSEFIVRVE LSALQKKFYK FILTKNYEAL NSKSGGNSCS LVNVMMDLKK CCNHPYLFPS
AAEEAATTAG GLYEITSLTK AAGKLVLLSK MLKQLKEQGH RVLIFSQMTK MLDILEDFLE
GEGYKYERID GGITGNLRQE AIDRFNAPGA QQFVFLLSTR AGGLGINLAT ADTVIIYDSD
WNPHNDIQAF SRAHRIGQAN KVMIYRFVTR NSVEERVTQV AKRKMMLTHL VVRPGMGGKG
ANFTKQELDD ILRFGTEELF KEDDKEEAIH YDDKAVAELL DRSNKGIEEK ESWANEYLSS
FKVASYATKE EEEEEETEII KQEAENSDPA YWVKLLRHHY EQHQEDVSRT LGKGKRVRKQ
VNYTDGGVVA AESTRDDSNW QDNNSEYNSD YSAGSEEDGG DDDFDEQNGA EGGRKARRRV
ERRDDRPLAP LLARVGGNIE VFGFNSRQRK SFLNAIMRYG MPPQDAFNSQ WLVRDLRGKS
ERNFKAYVSL FMRHLCEPGA DNAETFADGV PREGLSRQHV LTRIGVMSLI RKKVQEFEHI
NGYYSMPELI LKPCEPVKSL QKEEGSIVEG GGVGVAAAVG GGAKPEDKSA TTSTSATPAT
SAAPSPAPVD KVEDSKPSTT AGNDDVKKES GETEDKKSTE VDSDKKEEKP EVSADDVKKE
AGEKDKELAP DSKDGIKDEK PDTRDLKKES SDGGGGEVKS EKDGASDAAK EEKAKEEANK
TEIIDDDDDD VLIIKDDGEV EKPSQSIHKS VAAASSSSAD NKEGLTKPKI EESLEVLKRK
FMFNIADGGF TELHTLWLNE EKAAVPGREY EIWHRRHDYW LLAGIVTHGY GRWQDIQNDI
RFAIINEPFK MDVGKGNFLE IKNKFLARRF KLLEQSLVIE EQLRRAAFLN LAQDPTHPAM
SLNARFAEVE CLAESHQHLS KESLAGNKPA NAVLHKVLNQ LEELLSDMKS DVSRLPATLA
RIPPVAQRLQ MSERSILSRL AATAGNVNNA AQLMPQFPAG FQGTNLPAFA GGPAANFGNF
RPQFSVPGQL SANNTSNVGG N
//
