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ALFL2_ORYSI
ID   ALFL2_ORYSI             Reviewed;         244 AA.
AC   B8B8I3;
DT   21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=PHD finger protein ALFIN-LIKE 2;
GN   ORFNames=OsI_25444;
OS   Oryza sativa subsp. indica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39946;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. 93-11;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
CC   -!- FUNCTION: Histone-binding component that specifically recognizes H3
CC       tails trimethylated on 'Lys-4' (H3K4me3), which mark transcription
CC       start sites of virtually all active genes. {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with H3K4me3 and to a lesser extent with H3K4me2.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- DOMAIN: The PHD-type zinc finger mediates the binding to H3K4me3.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the Alfin family. {ECO:0000305}.
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DR   EMBL; CM000132; EEC81763.1; -; Genomic_DNA.
DR   AlphaFoldDB; B8B8I3; -.
DR   SMR; B8B8I3; -.
DR   STRING; 39946.B8B8I3; -.
DR   iPTMnet; B8B8I3; -.
DR   PRIDE; B8B8I3; -.
DR   EnsemblPlants; BGIOSGA024567-TA; BGIOSGA024567-PA; BGIOSGA024567.
DR   Gramene; BGIOSGA024567-TA; BGIOSGA024567-PA; BGIOSGA024567.
DR   HOGENOM; CLU_058315_1_0_1; -.
DR   OMA; GMNRIDW; -.
DR   Proteomes; UP000007015; Chromosome 7.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0042393; F:histone binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   CDD; cd15613; PHD_AL_plant; 1.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR045104; Alfin.
DR   InterPro; IPR021998; Alfin_N.
DR   InterPro; IPR044104; PHD_AL_plant.
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; PTHR12321; PTHR12321; 1.
DR   Pfam; PF12165; Alfin; 1.
DR   Pfam; PF00628; PHD; 1.
DR   SMART; SM00249; PHD; 1.
DR   SUPFAM; SSF57903; SSF57903; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 1.
DR   PROSITE; PS50016; ZF_PHD_2; 1.
PE   3: Inferred from homology;
KW   Chromatin regulator; Metal-binding; Nucleus; Reference proteome;
KW   Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..244
FT                   /note="PHD finger protein ALFIN-LIKE 2"
FT                   /id="PRO_0000412938"
FT   ZN_FING         187..239
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT   REGION          137..178
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        137..165
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            197
FT                   /note="Histone H3K4me3 binding"
FT                   /evidence="ECO:0000250"
FT   SITE            203
FT                   /note="Histone H3K4me3 binding"
FT                   /evidence="ECO:0000250"
FT   SITE            207
FT                   /note="Histone H3K4me3 binding"
FT                   /evidence="ECO:0000250"
FT   SITE            212
FT                   /note="Histone H3K4me3 binding"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   244 AA;  27405 MW;  DA9D14887A53F2E0 CRC64;
     MEMAAPVSPA PRTVEDIFKD FSGRRAGLVR ALTVDVDEFY GFCDPEKENL CLYGHPNGRW
     EVALPAEEVP PELPEPALGI NFARDGMHRR DWLSLVAVHS DSWLLSVAFF FGARLNGNER
     KRLFSLINDH PTVLEALSDR KHGRDNKSGA DNGSKSRHSG KRANDVQTKT SRPAVVDDGY
     DEEEHSETLC GTCGGRYNAN EFWIGCDICE RWFHGKCVRI TPAKAEHIKH YKCPDCSSSK
     KSRQ
 
 
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