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Database: UniProt
Entry: A0A4S4EM30_CAMSI
LinkDB: A0A4S4EM30_CAMSI
Original site: A0A4S4EM30_CAMSI 
ID   A0A4S4EM30_CAMSI        Unreviewed;       247 AA.
AC   A0A4S4EM30;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=PHD finger protein ALFIN-LIKE {ECO:0000256|RuleBase:RU369089};
GN   ORFNames=TEA_030115 {ECO:0000313|EMBL:THG17699.1};
OS   Camellia sinensis var. sinensis.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; Ericales; Theaceae; Camellia.
OX   NCBI_TaxID=542762 {ECO:0000313|EMBL:THG17699.1, ECO:0000313|Proteomes:UP000306102};
RN   [1] {ECO:0000313|EMBL:THG17699.1, ECO:0000313|Proteomes:UP000306102}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Shuchazao {ECO:0000313|Proteomes:UP000306102};
RC   TISSUE=Leaf {ECO:0000313|EMBL:THG17699.1};
RX   PubMed=29678829; DOI=.1073/pnas.1719622115;
RA   Wei C., Yang H., Wang S., Zhao J., Liu C., Gao L., Xia E., Lu Y., Tai Y.,
RA   She G., Sun J., Cao H., Tong W., Gao Q., Li Y., Deng W., Jiang X., Wang W.,
RA   Chen Q., Zhang S., Li H., Wu J., Wang P., Li P., Shi C., Zheng F., Jian J.,
RA   Huang B., Shan D., Shi M., Fang C., Yue Y., Li F., Li D., Wei S., Han B.,
RA   Jiang C., Yin Y., Xia T., Zhang Z., Bennetzen J.L., Zhao S., Wan X.;
RT   "Draft genome sequence of Camellia sinensis var. sinensis provides insights
RT   into the evolution of the tea genome and tea quality.";
RL   Proc. Natl. Acad. Sci. U.S.A. 115:E4151-E4158(2018).
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.
CC       {ECO:0000256|RuleBase:RU369089}.
CC   -!- SUBUNIT: Interacts with H3K4me3 and to a lesser extent with H3K4me2.
CC       {ECO:0000256|RuleBase:RU369089}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|RuleBase:RU369089}.
CC   -!- DOMAIN: The PHD-type zinc finger mediates the binding to H3K4me3.
CC       {ECO:0000256|RuleBase:RU369089}.
CC   -!- SIMILARITY: Belongs to the Alfin family.
CC       {ECO:0000256|ARBA:ARBA00010445, ECO:0000256|RuleBase:RU369089}.
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:THG17699.1}.
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DR   EMBL; SDRB02003456; THG17699.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4S4EM30; -.
DR   STRING; 542762.A0A4S4EM30; -.
DR   Proteomes; UP000306102; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0042393; F:histone binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-UniRule.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:UniProtKB-UniRule.
DR   CDD; cd15613; PHD_AL_plant; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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; CPG BINDING PROTEIN; 1.
DR   PANTHER; PTHR12321:SF180; PHD FINGER PROTEIN ALFIN-LIKE 9; 1.
DR   Pfam; PF12165; Alfin; 1.
DR   Pfam; PF00628; PHD; 1.
DR   SMART; SM00249; PHD; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 1.
DR   PROSITE; PS50016; ZF_PHD_2; 1.
PE   3: Inferred from homology;
KW   Chromatin regulator {ECO:0000256|RuleBase:RU369089};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU369089}; Nucleus {ECO:0000256|RuleBase:RU369089};
KW   Reference proteome {ECO:0000313|Proteomes:UP000306102};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163,
KW   ECO:0000256|RuleBase:RU369089};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW   ECO:0000256|RuleBase:RU369089}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU369089};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00146}.
FT   TRANSMEM        79..100
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          191..243
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   REGION          134..191
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        134..158
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        171..190
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   247 AA;  28122 MW;  B13EE8DDFF3BB6C4 CRC64;
     MDGGQPYNPR TVEEVFRDFK GRRAGMIKAL TTEKENLCLY GFPSEQWKVN LPAEEVPPEL
     PEPALGINFA RDGMQEKDWL SLVAVHSDAW LLAVAFYFGA RFGFDKADRK RLFNMINDLP
     TIFEVVTGTA KKQVKEKSSV SNHSNSKSKS NPKPQDSESQ GKYLKEPELK DEDEEGLEEE
     EEEEEEEEHG DTLCGACGEN YASDEFWICC DICEKWFHGK CVKITPARAE HIKQYKCPSC
     SNKRARP
//
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