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Database: UniProt
Entry: A0A6D2IIY9_9BRAS
LinkDB: A0A6D2IIY9_9BRAS
Original site: A0A6D2IIY9_9BRAS 
ID   A0A6D2IIY9_9BRAS        Unreviewed;       988 AA.
AC   A0A6D2IIY9;
DT   17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   RecName: Full=BED-type domain-containing protein {ECO:0000259|PROSITE:PS50808};
GN   ORFNames=MERR_LOCUS17460 {ECO:0000313|EMBL:CAA7030225.1};
OS   Microthlaspi erraticum.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Coluteocarpeae; Microthlaspi.
OX   NCBI_TaxID=1685480 {ECO:0000313|EMBL:CAA7030225.1, ECO:0000313|Proteomes:UP000467841};
RN   [1] {ECO:0000313|EMBL:CAA7030225.1, ECO:0000313|Proteomes:UP000467841}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mishra B.;
RL   Submitted (JAN-2020) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL27 family.
CC       {ECO:0000256|ARBA:ARBA00009124}.
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DR   EMBL; CACVBM020001092; CAA7030225.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A6D2IIY9; -.
DR   Proteomes; UP000467841; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
DR   CDD; cd06090; KOW_RPL27; 1.
DR   Gene3D; 2.30.30.770; -; 1.
DR   InterPro; IPR007021; DUF659.
DR   InterPro; IPR008906; HATC_C_dom.
DR   InterPro; IPR001141; Ribosomal_eL27.
DR   InterPro; IPR041991; Ribosomal_eL27_KOW.
DR   InterPro; IPR038655; Ribosomal_eL27_sf.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR   InterPro; IPR003656; Znf_BED.
DR   PANTHER; PTHR32166:SF121; HAT TRANSPOSON SUPERFAMILY; 1.
DR   PANTHER; PTHR32166; OSJNBA0013A04.12 PROTEIN; 1.
DR   Pfam; PF05699; Dimer_Tnp_hAT; 1.
DR   Pfam; PF04937; DUF659; 1.
DR   Pfam; PF01777; Ribosomal_L27e; 1.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR   SUPFAM; SSF50104; Translation proteins SH3-like domain; 1.
DR   PROSITE; PS50808; ZF_BED; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000467841};
KW   Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274};
KW   Ribosomal protein {ECO:0000256|ARBA:ARBA00022980};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00027}.
FT   DOMAIN          216..274
FT                   /note="BED-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50808"
FT   REGION          287..308
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          322..361
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          100..127
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        336..361
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   988 AA;  111890 MW;  77C321C4964E071C CRC64;
     MVKFLKQNKA VILLQGRYAG KKAVIIKSFD DGSRDRPYGH CLVAGLKKYP SKVIRKDSAK
     KTAKKSRVKC FIKLVNYQHL MPTRYTLDVD LKDVATIDAL QSKDKKVAAL KEAKAKLEER
     FKTGKNRWFF TKLRKISQTL HFSVALRFLS SVSPTPLLRL IPPSSSPEPN SLYRNFNQVL
     FRTDPTPRNQ PGHNLQTKKA SLRMDSDLEP VALTPQKQDS AWKHCLVYKY GDRVQMRCLY
     CRKMFKGGGI TRVKEHLAGK KGQGTICDQV PEEVRLFLQQ CIDGTVRRQR KRRKSSPEPL
     PIAYFPPGDE LETTTTTQIV PAGPSDADDN GFKSPELVAG QSSGRTKQRT YRSRKNSNNN
     AAFDRSDLAN VEVGDGDLME NLIPVAISSV KNIVHPSSKE REKTVHMAIG RFLFDIGADF
     DAVSSVNFQP LFDAIVSGGF GVSIPNHEDL RGWVLKSCVE EMKNEIDECK LLWKKTGCSV
     LVQELSSNEA TKVLNFFVYS PEKVVFLKSV DASEILASSS DGDVDDDDKL YELLKEVVEE
     VGETSVVQVI TKCEDHYVSA GKKLMDVYRS LYWVPCAAHC LEKMLEEFGK IDWISDIIEQ
     ARTVTRIIYN HSDVLNLMRR FTFGNDIVLP GFTVSATNFA TMARFADLKP HLQSMVTSSE
     WNECPYSKEA GGLAMAETIS DESFWKALTL ANNITVPLLR VLKIVCSEKR PAMGYVYAGL
     YRAKEAIKTH LVHREDYIIY WKIIDKWWLQ QHRLPLHAAG FYLNPKFFYS IDEEMRSEIH
     LAVVDCIEKL VPDVNVQDVI VKDINSYKNA GGIFGRNLAI RARDTMLPAE WWSTYGESCL
     NLSRFAIRIL SQTCSSLVGS GRNLTPVKQV YETKNSIERQ RLSDLVFVQY NMRLRRLGVE
     SGDEIVDPLS YSNMEVLEDW VSRNQVCIEG NGSSDWKSLE PVKRTEEIAV IDETEDLGSG
     FDDAEIFKGE KEVSDEGYYT NISEKLFT
//
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