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Database: UniProt
Entry: V9IAY2_APICE
LinkDB: V9IAY2_APICE
Original site: V9IAY2_APICE 
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
//
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