ID V9IAY2_APICE Unreviewed; 1963 AA.
AC V9IAY2;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE SubName: Full=Chromodomain-helicase-DNA-binding protein 4 {ECO:0000313|EMBL:AEY57807.1};
GN ORFNames=ACCB00415.2 {ECO:0000313|EMBL:AEY57807.1};
OS Apis cerana (Indian honeybee).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Apidae; Apis.
OX NCBI_TaxID=7461 {ECO:0000313|EMBL:AEY57807.1};
RN [1] {ECO:0000313|EMBL:AEY57807.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Brain {ECO:0000313|EMBL:AEY57807.1};
RA Sun L., Zheng H., Wang Y., Xie X., Zhu Y., Gu W., Wang S.;
RT "Decoding the brain transcriptome of the Eastern honeybee (Apis cerana)
RT based on pyrosequencing.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; JR037514; AEY57807.1; -; mRNA.
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:UniProtKB-KW.
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; cd00084; HMG-box_SF; 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; IPR000330; SNF2_N.
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:SF17; 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; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS50013; CHROMO_2; 1.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50016; ZF_PHD_2; 2.
PE 2: Evidence at transcript level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW DNA-binding {ECO:0000313|EMBL:AEY57807.1};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:AEY57807.1};
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 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 369..416
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 426..473
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 598..633
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 729..911
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1043..1205
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 202..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 307..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 658..701
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1321..1393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1520..1691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..77
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..136
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..273
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..295
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..353
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 672..701
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1325..1351
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1368..1392
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1527..1570
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1571..1691
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1963 AA; 222783 MW; ADCEED434706D258 CRC64;
MASDEEVDES YAGEDDLDET GGQVSNVNQQ VDGSSDAEES QRLEEDDDYE PEERKKKKGK
KRKARSEDKK GKKKKKKKKS DSGDESDFGG GGETGDIAGD DSDYAGNRKS RKSSSRKSSS
HNASAPPSQE PTTGMPTIEE VCNTFGLTDV QIEYTDADFQ NLTTYKLFQQ HVRPLLAKEN
PKVPMSKLMM LVAAKWRDFS ELNPHTQPDT DVSSANVDED SRNARANRSG AVQEGEDEEE
DDEDSDRKRK SRGSRAKKGK KASKVPTLKI KLGKRKRGSS DEEAEGSGVG TDRDSDMEFE
QMLADAEEPV GADGTNKGNT EESGIEPPAE PPVRRKAKTK IGNKTKKKKK TKTTSKFPDG
EEGLQTDHQD YCEVCQQGGE IILCDTCPRA YHLVCLEPEL EETPEGKWSC PHCEGEGAAE
DDDEHMEFCR ICKDGGELLC CDSCTSAYHT HCLNPPLSEI PDGDWKCPRC SCPPIRGKVA
KILTWRWKDC PETPSEEPST SKATPKQRRM REFFVKWADM SYWHCDWITE LQLDVFHPLM
FRNYSRKYDM DEPPKLEEPL DESDSRVKRL KEQDGATNRD EYNLEERFYR YGVRPEWLVV
HRVINHRLSR DGRATYLVKW RELGYDQATW EDEHEDIPGL KQAIEYYLDL RAANCCDGSS
SRKGKKGKGK KSKTRELIDD EERTPKRYTP PPDKPTTDLK KKYERQPEYL DQTGMQLHPY
QLEGLNWLRY SWGQGIDTIL ADEMGLGKTI QTITFLYSLY KEGHCKGPFL VSVPLSTIIN
WEREFETWAP DFYCVTYVGD KDSRIVIREN ELSFEEGAVR GGRASKIRSN QIKFNVLLTS
YELISIDSAC LGSIDWAVLV VDEAHRLKSN QSKFFRLLAS YNIAYKLLLT GTPLQNNLEE
LFHLLNFLCR DKFNDLAAFQ NEFADISKEE QVKKLHELLG PHMLRRLKAD VLKNMPSKSE
FIVRVELSPM QKKYYKYILT RNFEALNPKG GGQQVSLLNI MMDLKKCCNH PYLFPAASQE
APTAPNGSYE TSALIKAAGK LVLLSKMLKK LRDDGHRVLI FSQMTKMLDI LEDYLEGEGY
KYERIDGNIT GAQRQEAIDR FNAPGAQQFV FLLSTRAGGL GINLATADTV IIYDSDWNPH
NDIQAFSRAH RIGQANKVMI YRFVTRNSVE ERVTQVAKRK MMLTHLVVRP GMGGKGANFS
KQELDDILRF GTEELFKEEE GKEDEAIHYD DKAVAELLDR SKEGIEQKEN WANEYLSSFK
VASYVTKEGE TEEEADTEII KQEAENTDPA YWIKLLRHHY EQQQEDIART LGKGKRIRKQ
VNYNDGGVTG DQSTRDDQPW QENLSDYNSD FSAPSDDDKE DDDFDEKGDG DLLSRRSRRR
LERRDEKDRP LPPLLARVNG NIEVLGFNAR QRKAFLNAIM RYGMPPQDAF NSQWLVRDLR
GKSEKNFKAY VSLFMRHLCE PGADNAETFA DGVPREGLSR QHVLTRIGVM SLIRKKVQEF
EHINGYYSMP EMIRKPVEPV KVDGSGDAAT GTSSTSATPA TSNAASPSPA ATPTPTAISG
ITITDTNKSN SDSSEIKECK EEQKDKEITE TKDVKEESKD SKEEEENNTE KDKDKDDVKK
EEKDAESETI DKEKDKLDIK EEKSLTKHDE KVENTENKTK QDSEEDVVIV KDDEEETEKR
EEKDNKEKDI KDCDSETIKP KRKFMFNIAD GGFTELHTLW LNEEKAAVPG REYEIWHRRH
DYWLLAGIVT HGYGRWQDIQ NDIRFAIINE PFKMDVGKGN FLEIKNKFLA RRFKLLEQAL
VIEEQLRRAA YLNLTQDPNH PAMSLNARFA EVECLAESHQ HLSKESLAGN KPANAVLHKV
LNQLEELLSD MKSDVSRLPA TLARIPPVAQ RLQMSERSIL SRLAATAPGG NNSQSGQAAL
LAQQFPAGFS GGQLPATFAG AANFGNFRPQ YSVPGQPPQG FTA
//