ID E0W1M0_PEDHC Unreviewed; 1999 AA.
AC E0W1M0;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE SubName: Full=Chromodomain helicase-DNA-binding protein, putative {ECO:0000313|EMBL:EEB19526.1};
DE EC=2.7.11.1 {ECO:0000313|EMBL:EEB19526.1};
GN Name=8232196 {ECO:0000313|EnsemblMetazoa:PHUM578860-PA};
GN ORFNames=Phum_PHUM578860 {ECO:0000313|EMBL:EEB19526.1};
OS Pediculus humanus subsp. corporis (Body louse).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Paraneoptera; Psocodea; Phthiraptera; Anoplura; Pediculidae;
OC Pediculus.
OX NCBI_TaxID=121224;
RN [1] {ECO:0000313|EMBL:EEB19526.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=USDA {ECO:0000313|EMBL:EEB19526.1};
RA Kirkness E., Hannick L., Hass B., Bruggner R., Lawson D., Bidwell S.,
RA Joardar V., Caler E., Walenz B., Inman J., Schobel S., Galinsky K.,
RA Amedeo P., Strausberg R.;
RT "Annotation of Pediculus humanus corporis strain USDA.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EEB19526.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=USDA {ECO:0000313|EMBL:EEB19526.1};
RG The Human Body Louse Genome Consortium;
RA Kirkness E., Walenz B., Hass B., Bruggner R., Strausberg R.;
RT "The genome of the human body louse.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblMetazoa:PHUM578860-PA}
RP IDENTIFICATION.
RC STRAIN=USDA {ECO:0000313|EnsemblMetazoa:PHUM578860-PA};
RG EnsemblMetazoa;
RL Submitted (FEB-2021) to UniProtKB.
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DR EMBL; AAZO01007049; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DS235872; EEB19526.1; -; Genomic_DNA.
DR RefSeq; XP_002432264.1; XM_002432219.1.
DR STRING; 121224.E0W1M0; -.
DR EnsemblMetazoa; PHUM578860-RA; PHUM578860-PA; PHUM578860.
DR GeneID; 8232196; -.
DR KEGG; phu:Phum_PHUM578860; -.
DR CTD; 8232196; -.
DR VEuPathDB; VectorBase:PHUM578860; -.
DR eggNOG; KOG0383; Eukaryota.
DR HOGENOM; CLU_000315_22_1_1; -.
DR InParanoid; E0W1M0; -.
DR OMA; TWRWAVR; -.
DR OrthoDB; 2910821at2759; -.
DR Proteomes; UP000009046; Unassembled WGS 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: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 GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
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; IPR049730; SNF2/RAD54-like_C.
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: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; 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 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW DNA-binding {ECO:0000313|EMBL:EEB19526.1};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:EEB19526.1};
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 Reference proteome {ECO:0000313|Proteomes:UP000009046};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000313|EMBL:EEB19526.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 351..398
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 409..456
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 586..647
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 715..897
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1029..1191
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 193..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 645..686
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1312..1377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1503..1741
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1975..1999
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..70
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..224
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..261
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..291
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..319
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 657..674
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1314..1336
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1353..1376
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1513..1531
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1534..1660
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1676..1741
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1978..1999
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1999 AA; 229104 MW; 23D1D903F7D036C3 CRC64;
MASDDDIDDS FAGDDNEEAA AGPSNVNSES DENQRGEDDD YEPEDGRRRK KGKKRKARSE
GKKDKKRKKK KKNDSGDDSD INLEDSAGGN DSDYGSSKKT GRKRGSSKHS VPATPTTPSE
ESSKMPSVED VCSSFGLTDV QIKYTEQDFQ DLSSYKLFQQ HIRPLLAKDN PKVPVSKLMM
LVAAKWREFS CMNPHNEEHE NDDNPEPDYI PKPKRSRSSA IKSDNIEDDD DEEEKGRKKR
GRSKKGTKKN SKVPTLKIKL GKRKRGSSDE EENETDKKSE ASDRDSDAEF EQMLQEAEEA
SPDNSKEKED HENTDAPVAP RKAKTKFGVK NKRKPKRKMN DSKSGEQQEH QDYCEVCQQG
GEIILCDTCP RAYHLVCLDP ELEETPEGKW SCPHCEAEGT QEQDDDEHNE FCRLCKDGGE
LLCCDSCTSA YHIFCLNPPL SEIPDGDWKC PRCSAEPLPG KVSKILTWRW ADTPSAEKPP
EESTTTSKRA PRQPRRLREY FVKWAEKSYW HCAWVSELQA SIYTLDVAHP LMLRNYTRKF
DMDEPPKMDE AIDDSDYRMK KIKEFGANDN LLEEKYYKFG IRPEWMIVHR ILNHRTMRDG
RTLYLVKWRD LCYDQATWEE ETEEIPGLKQ AIEYYLDLRA TFNTDGKKGK KGRGKKPKTK
ELQDEDDSRM PRRYTPPPEK PLTNLSKKLD KQPDYIDATG MQLHEYQMEG LNWLRYSWGQ
GIDTILADEM GLGKTIQTIT FLYSLYKEGH CKGPFLVSAP LSTIINWERE FETWAPDFYC
VTYVGDKDSR AVIRENELSF EEGAVRGSRA TKIKASSIKF NVLLTSYELV SIDAACLGSI
DWAVLVVDEA HRLKSNQSKF FRVLAGYNIS YKLLLTGTPL QNNLEELFHL LNFMCRDKFS
DLAAFQNEFA DISKEEQVTK LHDLLGPHML RRLKTDVLKN MPAKSEFIVR VELSPMQKKY
YKWILTRNFE ALNPKGGGQQ VSLLNIMMDL KKCCNHPYLF SAAAEEAPLS ANGTYELQGL
IKASGKLILL SKMLKLLREQ GHRVLIFSQM TKMLDLLEDY LEGEGYKYER IDGSITGNLR
QEAIDRFNAP GAPQFAFLLS TRAGGLGINL ATADTVIIYD SDWNPHNDIQ AFSRAHRIGQ
SNKVMIYRFV TRNSVEERVT QVAKRKMMLT HLVVRPGMGG KNTNFTKQEL DDILRFGTEE
LFKEEEGKEE EAIHYDDKAV ADLLDRSKEG LEQKESWANE YLSSFKVASY ATKEGEDVRE
EEVNTEIIKQ EAENTDPAYW VKLLRHHYEQ QQEDIARTLG KGKRVRKQVN YNDGGVIDTP
QDSTWQENLS DYNSDFSTPS DDDKEDDDFD EKNDDLNSRR SRRKPERREE RDRPLPPLLA
RVGGNIEVLG FNARQRKAFL NAIMRYGMPP QDAFNSQWLV RDLRGKSEKN FKAYVSLFMR
HLCEPGADNA EAFADGVPRE GLSRQHVLTR IGVMSLIRKK VQEFEHINGF YSMPEAIKKT
LIEPKKSEEE KSTTATPNST TPATSAAPSP APETTVKEEK KEEEKEKKDE DNKNKDAEKP
APGEKKSEGT KTDEQETPEV IEIDKSEKVS EKEIKKEIEE ENVKKSEEED KKGDVTADES
TTVKQEKEEK KEVNEDVKVE KADEKGKVVE KKEDGDNKNN VKTEVTNSGD NPSEVVQEPE
ADKEKKDEKD KEKDKKEEKD KDKEKEKDKD KEKEKEKEKE KEKEKEKEKE KEKEEEDKEK
EKAKAKQRFM FNIADGGFTE LHTLWLNEEK AAVPGREYEI WHRRHDYWLL AGIVTHGYGR
WQDIQNDIRF AIINEPFKMD MGKGNFLEIK NKFLARRFKL LEQALVIEEQ LRRAAYLNLT
QDPNHPAMSL NARFAEVECL AESHQHLSKE SLAGNKPANA VLHKVLNQLE ELLSDMKSDV
SRLPATLARI PPVAQRLQMS ERSILSRLAA TTSTNTTLTR SMSSPFPHGF QGGQLPGAYG
NPNFTNFRPQ YSVPGQQTK
//
