ID W9QM01_9ROSA Unreviewed; 1592 AA.
AC W9QM01;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Chromodomain-helicase-DNA-binding protein Mi-2-like protein {ECO:0000313|EMBL:EXB41286.1};
GN ORFNames=L484_004456 {ECO:0000313|EMBL:EXB41286.1};
OS Morus notabilis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Moraceae; Moreae; Morus.
OX NCBI_TaxID=981085 {ECO:0000313|EMBL:EXB41286.1, ECO:0000313|Proteomes:UP000030645};
RN [1] {ECO:0000313|Proteomes:UP000030645}
RP NUCLEOTIDE SEQUENCE.
RA He N., Zhao S.;
RT "Draft Genome Sequence of a Mulberry Tree, Morus notabilis C.K. Schneid.";
RL Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; KE343794; EXB41286.1; -; Genomic_DNA.
DR RefSeq; XP_010090914.1; XM_010092612.1.
DR STRING; 981085.W9QM01; -.
DR eggNOG; ENOG502QV7S; Eukaryota.
DR Proteomes; UP000030645; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd15532; PHD2_CHD_II; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR032308; TDBD.
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; PTHR46309; PHD FINGER PROTEIN 12; 1.
DR PANTHER; PTHR46309:SF1; PHD FINGER PROTEIN 12; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF16135; TDBD; 1.
DR SMART; SM00249; PHD; 2.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000313|EMBL:EXB41286.1};
KW DNA-binding {ECO:0000313|EMBL:EXB41286.1};
KW Helicase {ECO:0000313|EMBL:EXB41286.1};
KW Hydrolase {ECO:0000313|EMBL:EXB41286.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000313|EMBL:EXB41286.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030645};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 785..830
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 376..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 535..652
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1111..1168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1299..1322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1510..1552
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 444..458
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 536..595
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 600..636
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1111..1127
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1510..1526
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1592 AA; 175566 MW; A712AAED26AB187F CRC64;
MDQDISVKRD LEGKSQRRES ALRNAHKSQP NKVFLFLLVL LPLSSSSSLS LSKIFNWLCS
PENLPSRSEQ SERRIAGDGI AEVHGEMEEG VRSGGSSGIV VKNRNSSGCL IVRRKGDALA
GGLVSSSSRK VSEAKKEKKR GRLICSDSGS SDELLIPHRR RVGPETIRVC NDLSSFGKGV
VEENEIGRKR ERLEQNRHNE DGFFGNNGLD ESERKIGKLD VFDFNEYDES GVGFGGIRFS
GSMHMARSGA EREFETGSSR HLVDNRRNLY FERMNSMNRG SHTGKSRFEI NREGAQVSLL
RDKFTGHSDQ AIRLQGKNGV LKVMVNKKKC MSGPPERYNF LKPEECQKVS RMEDTAKKNA
PVPPFYLEEN ILEKPGSVAR SEKKHKSSRK SLPTKTSKNS NCDSEDSDAS LQREAENVAA
NKSSKRISCE AEDPPSCEKL QPNSIKEGKL RRGSGTEKQK LRERIRGMLV DAGWKIDYRP
RRNRDYLDAV YINPSGTAYW SIIKAYDALQ KQVNDEENEV KPSVDGSAAR LIADEDLSQL
TRKTRKKMEK EMKRKQRDRS ESENAREIRG KRSTSAKHDS ESMDSDSHDD KLSTFMKQGG
KSFKGRTNEN GFASVNSNGR NYTQHLHDSG ERSASGSNPR MLHGRKSRKD GRCTLLVRSS
GKGLNSETDG FVPYTGKRTL LSWLIDSGTV QLSQKVQYKN RRRTKVMLEG WITRDGIHCG
CCSKILTISK FEIHAGSKLR QPYQNIFLDS GISLLQCQID AWNRQGDSEH IGYHSVDTDG
DDPNDDTCGI CGDGGDLICC DGCPSTFHQS CLDIQMLPPG DWHCPNCTCK FCGIASQNAA
EEDDTIDSTL LTCSLYHNSC VQDIDVNSVD SSIIDSSFCG QKCKELFEHL QKYIGIKHDL
EAGFSWSLIR RTDEETEISH RGVPQRVECN SKLAVAMTVM DECFLPIVDR RSGINLIRNV
LYNCGSNFNR LNYGGFCTAI LERGDELISA ASLRFHGTKL AEMPFIGTRN IYRRQGMCRR
LFCAIESALC SLKVEKLVIP AISELAHTWT TVFGFTPLEE TLKQEMRSMN MLVFPGIDML
QKILGEQEHE ANMTSSGVCT KQTEGKGKQC IKPEVPLKPD IDSSTRNEAT EEVAQVQSGS
RRADRANERT EEVAAAESSP KSVDHANETM EELAAVESSP KTEDHADETM EEVAQVESGS
KCTDHANETV EEVAAVESSP RGVDHVDTME EGAAIESSPK GVDLGNETME EGAAMESSPK
SVDLANGTTE EVVAIESSTK SVDHANETTE EIAAIESSTK SVDHANETTD EVAAVESESN
PSVELESNDT VMMSVSVNVS LELENPDGTT CSESPSGPII SRIKSLSPSK TSHDAAAIEN
KLVPDPLLED NSKSFIQCRG AFTKETSLLS SSVEASHELK TQVPRDGTMF SETQREGKCV
SGSESLSPPD GGGLHVEHNQ VFNSVKENTD SLKDDVMDNS HKMKFENACS VPASAGKTFA
DQISEEVMET TDVSASSSSG HTGSSLPVKS DLDFGENPHV ASDSMNSVEN DHEDQIRLPH
FNGSNKLILF MVCQVPNSGE FGCVQDSAEL MS
//
