ID A0A0M4F0G9_DROBS Unreviewed; 2001 AA.
AC A0A0M4F0G9;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Mi-2 {ECO:0000313|EMBL:ALC44637.1};
DE Flags: Fragment;
GN ORFNames=Dbus_chr3Lg1803 {ECO:0000313|EMBL:ALC44637.1};
OS Drosophila busckii (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=30019 {ECO:0000313|EMBL:ALC44637.1, ECO:0000313|Proteomes:UP000494163};
RN [1] {ECO:0000313|EMBL:ALC44637.1, ECO:0000313|Proteomes:UP000494163}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Whole larvae {ECO:0000313|EMBL:ALC44637.1};
RA Zhou Q., Bachtrog D.;
RT "Ancestral chromatin configuration constrains chromatin evolution on
RT differentiating sex chromosomes in Drosophila.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP012525; ALC44637.1; -; Genomic_DNA.
DR SMR; A0A0M4F0G9; -.
DR STRING; 30019.A0A0M4F0G9; -.
DR OMA; TWRWAVR; -.
DR Proteomes; UP000494163; Chromosome 3l sequence.
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:UP000494163};
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 362..409
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 422..469
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 473..556
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 603..664
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 734..916
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1048..1210
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 181..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 662..705
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1331..1387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1535..1733
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..44
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..66
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..107
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..227
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..253
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..308
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..347
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 678..705
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1335..1353
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1366..1387
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1539..1559
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1565..1664
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1665..1683
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1708..1733
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ALC44637.1"
SQ SEQUENCE 2001 AA; 225977 MW; A16D38A59DA3702A CRC64;
NFIEEEEAVE DTAQVAELSN DSDAPLKPNQ NDEDDDYEPD DNRKKKKGKK RKTKKGEEKG
RKKKKRKKNE SEEDSDFVQH DEEVEYPSTS SKRGRKRKEE KQAQREKESS SSGMPSVEDV
CSAFSVCDVE IEYSEDDLQS LTTYKSFTQH VRPILQKENP KIAAPKLMML VAAKWREFCE
SNPHIQQEQP PAAAPEADEP RSSRSSRNEK PDDIYEEEED EEEKLEEEEE EKKPRRKRSG
RSSNKKGRRP SGKVPTLKIK FGKRKRDSSD EEPEASGASE RDSDLEFERM LQKSDESADE
KETEKSKPVA EATAAGAGAQ EDGAPVVRKK AKTKIGNKFK KKSKLKKTKN FPEGEDGEHE
HQDYCEVCQQ GGEIILCDTC PRAYHLVCLE PELDEPPEGK WSCPHCEADG GAAEEEDDDE
HQEFCRVCKD GGELLCCDSC PSAYHTFCLN PPLDTIPDGD WRCPRCSCPP LVGKAEKIIT
WRWVVQRRAS SSEASTSKGA KQSQSGGNRI REYFIKWHNM SYWHCDWVSE VQLDVHHPLM
IRSFQRKYDM EEPPKFEESL DEADTRFKRI QRHKDKVGMK HTDDDDEALE ERFYKNGVKP
EWLIVQRVIN HRTARDGSTM YLVKWRELPY DKSTWEEEGD DIPGLRQAID YYQDLRAVCT
SETTRGSSSK KNKKGRKNKK LELDDEDRPV KHYTPPPEKP TTDLKKKYEG QPAFLDDTGM
QLHPYQIEGI NWLRYSWGQG IDTILADEMG LGKTIQTVTF LYSLYKEGHC RGPFLVAVPL
STLVNWEREF ELWAPDFYCI TYIGDKDSRA VIRENELTFD ESAIRGTKVS RLRTTQYKFN
VLLTSYELIS MDAPCLGSID WAVLVVDEAH RLKSNQSKFF RILNSYSIAY KLLLTGTPLQ
NNLEELFHLL NFLSRDKFND LNAFQGEFAD VSKEEQVKRL HEMLGPHMLR RLKTDVLKNM
PSKSEFIVRV ELSAMQKKFY KFILTKNYEA LNSKSGGGSC SLINIMMDLK KCCNHPYLFP
SAAEEAPTSA GGIYEINSLT KAAGKLVLLS KMLKQLKSQN HRVLIFSQMT KMLDILEDFL
EGEQYKYERI DGGITGTVRQ EAIDRFNAPG AQQFVFLLST RAGGLGINLA TADTVIIYDS
DWNPHNDIQA FSRAHRIGQA NKVMIYRFVT RNSVEERVTQ VAKRKMMLTH LVVRPGMGGK
GANFTKQELD DILRFGTEDL FKEDDKEEAI HYDDKAVAEL LDRSNRGIEE KESWANEYLS
SFKVASYATK EEEEEEETEI IKQDAENSDP AYWVKLLRHH YEQHQEDVGR SLGKGKRVRK
VVNYTDGGVV AADTTRDDSN WQDNGSEYNS EYSAGSDEDG GDDDFDEQNG ERKAKRRLDR
RDDRPLPPLL ARVGGNIEVL GFNARQRKSF LNAIMRYGMP PQDAFNSQWL VRDLRGKSER
NFKAYVSLFM RHLCEPGADN AETFADGVPR EGLSRQHVLT RIGVMSLIRK KVQEFEHING
YYSMPELILK PCEPVRAGVA GVVAKVEPAD GGVAAKAPAE SATTSNSATP ATSAAPSPAP
ASEKSEDKAT LEKSTPEKQE VKSEPEAEGE SKAAEAPVKE ELSEESGDAK TTDATVKTEP
TKVEPKEEAG KEKEDKPSPV KEQLKEEPKS SSEGEEKDKA SEEKPSTSSS STTTTTTATT
TTNIIDDDDD DVMIVKEDGE LEKPTAGVNA NASANANSPK DQKNATTATA TTKGVEDSLE
VLKRKFMFNI ADGGFTELHT LWLNEEKAAV PGREYEIWHR RHDYWLLAGI VTHGYGRWQD
IQNDIRFAII NEPFKMDVGK GNFLEIKNKF LARRFKLLEQ ALVIEEQLRR AAFLNLAQDP
SHPAMSLNAR FAEVECLAES HQHLSKESLA GNKPANAVLH KVLNQLEELL SDMKSDVSRL
PATLARIPPV AQRLQMSERS ILSRLAATAG NASNAAQLMA QFPDGFQGTS LPAFTAGPAG
NFANFRPQFS VPGQLSNNAG S
//
