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Database: UniProt
Entry: A0A444XWD1_ARAHY
LinkDB: A0A444XWD1_ARAHY
Original site: A0A444XWD1_ARAHY 
ID   A0A444XWD1_ARAHY        Unreviewed;       871 AA.
AC   A0A444XWD1;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   RecName: Full=Myb-like domain-containing protein {ECO:0000259|PROSITE:PS50090};
GN   ORFNames=Ahy_B08g088994 {ECO:0000313|EMBL:RYQ94110.1};
OS   Arachis hypogaea (Peanut).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   dalbergioids sensu lato; Dalbergieae; Pterocarpus clade; Arachis.
OX   NCBI_TaxID=3818 {ECO:0000313|EMBL:RYQ94110.1, ECO:0000313|Proteomes:UP000289738};
RN   [1] {ECO:0000313|EMBL:RYQ94110.1, ECO:0000313|Proteomes:UP000289738}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Fuhuasheng {ECO:0000313|Proteomes:UP000289738};
RC   TISSUE=Leaves {ECO:0000313|EMBL:RYQ94110.1};
RA   Chen X.;
RT   "Sequencing of cultivated peanut Arachis hypogaea provides insights into
RT   genome evolution and oil improvement.";
RL   Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RYQ94110.1}.
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DR   EMBL; SDMP01000018; RYQ94110.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A444XWD1; -.
DR   STRING; 3818.A0A444XWD1; -.
DR   Proteomes; UP000289738; Chromosome b08.
DR   GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   CDD; cd12203; GT1; 1.
DR   CDD; cd07714; RNaseJ_MBL-fold; 1.
DR   Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR   Gene3D; 3.40.50.10710; Metallo-hydrolase/oxidoreductase; 1.
DR   Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 1.
DR   InterPro; IPR001279; Metallo-B-lactamas.
DR   InterPro; IPR044822; Myb_DNA-bind_4.
DR   InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR   InterPro; IPR011108; RMMBL.
DR   InterPro; IPR042173; RNase_J_2.
DR   InterPro; IPR001005; SANT/Myb.
DR   PANTHER; PTHR43694; RIBONUCLEASE J; 1.
DR   PANTHER; PTHR43694:SF1; RIBONUCLEASE J; 1.
DR   Pfam; PF12706; Lactamase_B_2; 1.
DR   Pfam; PF13837; Myb_DNA-bind_4; 1.
DR   Pfam; PF07521; RMMBL; 1.
DR   SMART; SM00849; Lactamase_B; 1.
DR   SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
DR   PROSITE; PS50090; MYB_LIKE; 1.
PE   4: Predicted;
KW   Exonuclease {ECO:0000256|ARBA:ARBA00022839};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW   Reference proteome {ECO:0000313|Proteomes:UP000289738};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          771..835
FT                   /note="Myb-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50090"
FT   REGION          38..64
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          655..715
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          733..754
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        46..64
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        661..691
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        735..754
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   871 AA;  96871 MW;  AAE70BCF47E1E366 CRC64;
     MASSTSFASL LLPLYNPAFR PKPTTSLPAF RSIHSSVLPA TDGSQAPHKR TRRMEGPRKS
     MEDSVQRKME QFYEGKDGPP LRVLPIGGLG EIGMNCMLVG NHDRYILIDA GVMFPDYDEL
     GVQKIIPDTT FIRKWSHKIE ALVITHGHED HIGALPWVIP ALDSNTPIFA SSFTMELIKK
     RLKEHGIFLP SRLKIFRTRK KFMAGPFEIE PIRVTHSIPD CCGLVLRCSD GTILHTGDWK
     IDETPLDGKV FDREALEELS KEGVTLMMSD STNVLSPGRT ISESVVKDAL LRHISASKGR
     VITTQFASNL HRLGSVKAAA DLTGRKLVFV GMSLRTYLDA AWKDGKAPID PSTLVKAEDI
     DAYAPKDLLI VTTGSQAEPR AALNLASYGS SHAFKLTKED IVLYSAKVIP GNESRVMKML
     NRISEIGSTI IMGKNEGLHT SGHAYRGELE EVLRIVKPQH FLPIHGELLF LKEHELLGKS
     NGIRHTAVIK NGEMLGVSHL RNRRVLSNGF ISLGRENLQL KYSDGDKAFG TSSDLFIDER
     LKIALDGIIV VSMEVFRPQR ADSLAENTLK GKIRITTRCL WLDKGKLLDA LHKAAHAALS
     SCPVKCPLAH MERTVAEVLR KMVRKYSGKR PEVIAIAIEN PAAVLAEEIN TKLSGKSHVD
     HGTSTLRKIV DGHRKENQPD TTQIRDDVND VEGLLPEEDT GPPTEEAEGD LSDSEEFWKP
     FIASSPVEKS IKANNGYVPR KEHKSNLKKD DSEDISEANF VKASSSELKS SKSGKRNKWK
     PEEIKKLIDM RGKLHDRFQI VKGRMALWEE ISQSLLADGI SRSPGQCKSL WTSLVQKYQE
     IKNEKGSSKS SWQYLEDMEK IMPDSKAMAT K
//
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