ID A0A2H9ZVI2_9ASPA Unreviewed; 1106 AA.
AC A0A2H9ZVI2;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Chromodomain-helicase-DNA-binding protein 4 {ECO:0000313|EMBL:PKA47297.1};
DE EC=3.6.4.12 {ECO:0000313|EMBL:PKA47297.1};
GN ORFNames=AXF42_Ash017242 {ECO:0000313|EMBL:PKA47297.1};
OS Apostasia shenzhenica.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Orchidaceae;
OC Apostasioideae; Apostasia.
OX NCBI_TaxID=1088818 {ECO:0000313|EMBL:PKA47297.1, ECO:0000313|Proteomes:UP000236161};
RN [1] {ECO:0000313|EMBL:PKA47297.1, ECO:0000313|Proteomes:UP000236161}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Shenzhen {ECO:0000313|Proteomes:UP000236161};
RC TISSUE=Stem {ECO:0000313|EMBL:PKA47297.1};
RX PubMed=28902843; DOI=10.1038/nature23897;
RA Zhang G.Q., Liu K.W., Li Z., Lohaus R., Hsiao Y.Y., Niu S.C., Wang J.Y.,
RA Lin Y.C., Xu Q., Chen L.J., Yoshida K., Fujiwara S., Wang Z.W., Zhang Y.Q.,
RA Mitsuda N., Wang M., Liu G.H., Pecoraro L., Huang H.X., Xiao X.J., Lin M.,
RA Wu X.Y., Wu W.L., Chen Y.Y., Chang S.B., Sakamoto S., Ohme-Takagi M.,
RA Yagi M., Zeng S.J., Shen C.Y., Yeh C.M., Luo Y.B., Tsai W.C.,
RA Van de Peer Y., Liu Z.J.;
RT "The Apostasia genome and the evolution of orchids.";
RL Nature 549:379-383(2017).
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DR EMBL; KZ453531; PKA47297.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H9ZVI2; -.
DR STRING; 1088818.A0A2H9ZVI2; -.
DR OrthoDB; 450464at2759; -.
DR Proteomes; UP000236161; Unassembled WGS sequence.
DR GO; GO:0000785; C:chromatin; IEA:UniProt.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
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 Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR018501; DDT_dom.
DR InterPro; IPR047365; Tudor_AtPTM-like.
DR InterPro; IPR028942; WHIM1_dom.
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; PTHR46508; PHD FINGER FAMILY PROTEIN; 1.
DR PANTHER; PTHR46508:SF1; PHD FINGER FAMILY PROTEIN; 1.
DR Pfam; PF02791; DDT; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF21743; PTM_DIR17_Tudor; 1.
DR Pfam; PF15612; WHIM1; 1.
DR SMART; SM00571; DDT; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR PROSITE; PS50827; DDT; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000313|EMBL:PKA47297.1};
KW DNA-binding {ECO:0000313|EMBL:PKA47297.1};
KW Helicase {ECO:0000313|EMBL:PKA47297.1};
KW Hydrolase {ECO:0000313|EMBL:PKA47297.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000313|EMBL:PKA47297.1};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000236161};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT TRANSMEM 1088..1105
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 202..262
FT /note="DDT"
FT /evidence="ECO:0000259|PROSITE:PS50827"
FT DOMAIN 422..469
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 127..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 975..1003
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..31
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 985..1003
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1106 AA; 121042 MW; C80E83BAFC750D64 CRC64;
MEGNGMEGAG AIGCDEELKK SGEEERVDQG TEASGSGRMD DIVGGDTGGR GGGLVGAYVV
RNSSGIGRVF LGKVVSYDNS SKLYRVMYED GHQEDLEVES VNRILMEEGA GGKLTRRKRR
LDQMVPLGGL KRPNTRSRAS ISDIPAPASQ LNAEDASGDG DSSSDSCDHA LVPTAVQDSS
SLEIQILPLE LPPSSGDIFV PKNSVAYLFS TYNFLRSFSL QLFLSPFGFD DYVGSLNSTV
QNSLMDAIHL CLMRALSRQL QVLSSEGFEL ANKCLTCYDW TLLDVLTWPA FLVEYLCVMG
HLKELDLKDC SNGALDGDYY CLPVATKLKV LQVICDDVVN SVELRAELEM RESMKEDGDI
CLDSNLRLEG ELATVQHKSS MTTASMVAGA LQESVAFDNR VVSTTVSEIS ADASTNSQDK
NSDECCLCGM DGSLVCCDGC PSAYHFRCIG LNKAFLPSGL WFCPECNVNR LGPTSSRVGR
GIRGAEVFGI DPNGRIFMGT CNYLLVFDSL NNESICRYYN LDDVPKVLDA ISIEASSFLY
IDICRRISEY FEVPLVEMKA EKMEPVMGNS FSFDLAVSNS SSTSPWRIMN LQNSLGYNSM
CSTILGNSRN DVPKVDGSEA QVATSIIRQA GISDSEMNLL GLDEVCDNKI PEAAEGILVQ
TIEENLTSGV AIFEDQKILS SKHINKREQP CFGSSVTDFS ISNKPLFAEK SNLLNNVSCS
PKNGSDICKE DAVSSIYSTK NFFFVTCESR NISNANVVTH KKTSDKNTHV SFKHIPYINQ
YTQGDIAASA AARLAILSSE DGKYSEAHGS SNPRKAVSAS IALQMKAFSG AVMNFLWPCF
DKKVMDVPRE RCGWCIACKG MSTNKKGCLL NLAASNAIKG PARNINLRAG KRYEGHLPTI
AAHMLIMVES LQGFLIGPFL DVEYSKQWHK QVREAHSFWV LKSLLLELEK NIRGIAFSGG
WNKLMDGFSV ENPTLSSGMH TAQSEKHVHG SRRSKKTPEL LSSEDDGNDV LWWRGGKLSK
VVLQIGILPR SLSKKAARQG GRKLISGVPY PGCSSYPRRS RQFAWRAAVE LSRTTYQLAL
QVSQPPCLVL IFFHSFLLVT LLIFSN
//
