ID Q9Y0W1_DROME Unreviewed; 1476 AA.
AC Q9Y0W1;
DT 01-NOV-1999, integrated into UniProtKB/TrEMBL.
DT 01-NOV-1999, sequence version 1.
DT 24-JAN-2024, entry version 137.
DE SubName: Full=ATP-dependent chromatin assembly factor large subunit {ECO:0000313|EMBL:AAD38952.1};
GN Name=Acf {ECO:0000313|FlyBase:FBgn0027620};
GN Synonyms=Acf1 {ECO:0000313|EMBL:AAD38952.1};
GN ORFNames=CG1966 {ECO:0000313|FlyBase:FBgn0027620};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000313|EMBL:AAD38952.1};
RN [1] {ECO:0000313|EMBL:AAD38952.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=10385622;
RA Ito T., Levenstein M.E., Fyodorov D.V., Kutach A.K., Kobayashi R.,
RA Kadonaga J.T.;
RT "ACF consists of two subunits, Acf1 and ISWI, that function cooperatively
RT in the ATP-dependent catalysis of chromatin assembly.";
RL Genes Dev. 13:1529-1539(1999).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00475}.
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DR EMBL; AF148962; AAD38952.1; -; mRNA.
DR PeptideAtlas; Q9Y0W1; -.
DR AGR; FB:FBgn0027620; -.
DR FlyBase; FBgn0027620; Acf.
DR VEuPathDB; VectorBase:FBgn0027620; -.
DR HOGENOM; CLU_002479_1_0_1; -.
DR PhylomeDB; Q9Y0W1; -.
DR ChiTaRS; Iswi; fly.
DR ExpressionAtlas; Q9Y0W1; baseline and differential.
DR GO; GO:0016590; C:ACF complex; IDA:FlyBase.
DR GO; GO:0008623; C:CHRAC; IBA:GO_Central.
DR GO; GO:0000228; C:nuclear chromosome; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006338; P:chromatin remodeling; IEA:InterPro.
DR GO; GO:0006335; P:DNA replication-dependent chromatin assembly; IDA:FlyBase.
DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IMP:FlyBase.
DR GO; GO:0007399; P:nervous system development; IMP:FlyBase.
DR GO; GO:0045740; P:positive regulation of DNA replication; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IBA:GO_Central.
DR GO; GO:0031445; P:regulation of heterochromatin formation; IMP:FlyBase.
DR CDD; cd05504; Bromo_Acf1_like; 1.
DR CDD; cd15543; PHD_RSF1; 1.
DR Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR037325; Acf1_Bromo.
DR InterPro; IPR047171; BAZ1A.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018501; DDT_dom.
DR InterPro; IPR028942; WHIM1_dom.
DR InterPro; IPR028941; WHIM2_dom.
DR InterPro; IPR013136; WSTF_Acf1_Cbp146.
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; PTHR46510; BROMODOMAIN ADJACENT TO ZINC FINGER DOMAIN PROTEIN 1A; 1.
DR PANTHER; PTHR46510:SF1; BROMODOMAIN ADJACENT TO ZINC FINGER DOMAIN PROTEIN 1A; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF10537; WAC_Acf1_DNA_bd; 1.
DR Pfam; PF15612; WHIM1; 1.
DR Pfam; PF15613; WSD; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00571; DDT; 1.
DR SMART; SM00249; PHD; 2.
DR SUPFAM; SSF47370; Bromodomain; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 2.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS50827; DDT; 1.
DR PROSITE; PS51136; WAC; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 2: Evidence at transcript level;
KW Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW ProRule:PRU00035};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW ProRule:PRU00475}; Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 25..131
FT /note="WAC"
FT /evidence="ECO:0000259|PROSITE:PS51136"
FT DOMAIN 346..411
FT /note="DDT"
FT /evidence="ECO:0000259|PROSITE:PS50827"
FT DOMAIN 1062..1112
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1373..1443
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 712..743
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 915..941
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1116..1227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1279..1357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 269..329
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 712..734
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 920..941
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1117..1138
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1139..1177
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1201..1216
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1294..1320
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1322..1348
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1476 AA; 170459 MW; C18A6CEBF57E66B3 CRC64;
MPICKREGFD LNQKEGKNET FHDNDQVFCC YITKRIFRDY EHYFRHVMVI NSTVWQCEAT
GKENLTYEEA VKSERAARKK MEQFKQSLRA PVLLVVEHAQ QSAVNTLNMI VAKFLRKRYF
IGEEVSVQAK KNATYTVLGV KLDKNMPEPL NGIYEDTDNL VYRLRPNKGD PSAELDLPFR
QLRRSRMEFN LENLSMFIKS NVSRVDGLLR PKPEAYKQYV TNPGVNFSTI FIGKMPRYSP
AKIKKPDGKK QSTLNKYIVA GEATAAKSKA KAKSDAKSLA EELERVKREK EAKLIELEKQ
KAEKKAQLIE RVENECNLLL QKTDDLERTD QKVLPRYRQI VTLLPEHLLG DAFMMREFMH
TYTGLLSGIE VFRQNLSFYE MTRALTAREI AGPLSDILLV LLGTVFDLQK EEEEECAVTY
LDRAAQTQEP YWSMAQAAKS HLYAKRHFSF KVNELPLDAL TLSEVLRLHL LGSGAFVNEK
AERWRVMYRN GYSSKEDPGL ELRLEHSHIL RILKNHSVYQ LKFKDIMLLI RCLMSQIMTY
SGTINLIEER MEQTAKARQD LRALVVGENK RLAAVEINRK KLTQMHHLEV NGVEPEKREA
LVEKLKKSIA ELHAQSDQQH RKHELQMLKL HSQLFNFLVY LGMDRCYRKY YVLESMPGIF
VEHSPDSLDT CLEQPITNKS QIEIRQQSAL PKNRKDLRVY LLKLYGDDEK KTKKKAKHSL
ENKENQEHRL NGSAEPMDVE SNSPEAPTHF ELLMCSGDKR SCIVHDSRNG QRQRWAYIYK
AEEIDELIKA LNPNGLREYE LLQELSVLRS LIEQHAKTCP VDLLSLENET MRKKFMAAME
SETNRKYGEA NFGLPNGTDL NEVMRLHLVD RIIQFENDIY TGDLGRLKVK DMEKWRSDLL
GGNYDAQCKL QWGPGGKLED EAGSDNESHE THEEDDGALL GKYARKPYRD PGMYLAASAD
TKPLPDSDDE EDQHTNAVLI PIAVHNMASA LLQVEQAIGK RFLKEPYGMK KWDPKQEALK
LACDSRLHQW EVSLMESTSF AQVFLHLNIL HDCIQWRRST NKSLCKVCRR GSDPEKMLLC
DECNAGTHMF CLKPKLRSVP PGNWYCNDCV KSLGLSHGQN EKDKKQATKK KRKFIVEEED
DEATDEEEEE KKDDDMTDED AEHENEKHDE DVEDDESVTS TPSSSRVNGR ILRRPRTRPT
SRRLTSKEIE EHAQEDVDSG DVSDDASLTA GEDTIEDESD EEKVCQKCFY DGGEIKCVQC
RLFFHLECVH LKRPPRTDFV CKTCKPMPQR PRRRHSNMNG DHDRDEEEPK AKRPRNSLRL
SIDKTARPSN GNNNNNNNNS SVNNNNHRRS GRRTNEHMPL NSAALYDLLE QIMKHKAAWP
FLRPVLTSEV PDYHQIIKTP MDLAKIKSKL NMGAYQLNEE LLSDIQLVFR NCDLYNVEGN
EIYDAGCQLE RFVIDRCRDM QLPFRPSDMN GEVKAC
//
