ID A0A218WY98_PUNGR Unreviewed; 228 AA.
AC A0A218WY98;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=PHD finger protein ALFIN-LIKE {ECO:0000256|RuleBase:RU369089};
GN ORFNames=CDL15_Pgr016946 {ECO:0000313|EMBL:OWM77548.1}, CRG98_021071
GN {ECO:0000313|EMBL:PKI58510.1};
OS Punica granatum (Pomegranate).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Myrtales; Lythraceae; Punica.
OX NCBI_TaxID=22663 {ECO:0000313|EMBL:OWM77548.1, ECO:0000313|Proteomes:UP000197138};
RN [1] {ECO:0000313|Proteomes:UP000197138}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Dabenzi {ECO:0000313|Proteomes:UP000197138};
RX PubMed=28654223; DOI=10.1111/tpj.13625;
RA Qin G., Xu C., Ming R., Tang H., Guyot R., Kramer E.M., Hu Y., Yi X.,
RA Qi Y., Xu X., Gao Z., Pan H., Jian J., Tian Y., Yue Z., Xu Y.;
RT "The pomegranate (Punica granatum L.) genome and the genomics of
RT punicalagin biosynthesis.";
RL Plant J. 91:1108-1128(2017).
RN [2] {ECO:0000313|EMBL:OWM77548.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Fresh leaf {ECO:0000313|EMBL:OWM77548.1};
RA Xu C.;
RT "The pomegranate genome and the genomics of punicalagin biosynthesis.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:PKI58510.1, ECO:0000313|Proteomes:UP000233551}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AG2017 {ECO:0000313|EMBL:PKI58510.1}, and cv. AG2017
RC {ECO:0000313|Proteomes:UP000233551};
RC TISSUE=Leaf {ECO:0000313|EMBL:PKI58510.1};
RA Akparov Z., Amiraslanov A., Hajiyeva S., Abbasov M., Kaur K., Hamwieh A.,
RA Solovyev V., Salamov A., Braich B., Kosarev P., Mahmoud A., Hajiyev E.,
RA Babayeva S., Izzatullayeva V., Mammadov A., Mammadov A., Sharifova S.,
RA Ojaghi J., Eynullazada K., Bayramov B., Abdulazimova A., Shahmuradov I.;
RT "De-novo sequencing of pomegranate (Punica granatum L.) genome.";
RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
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|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|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:OWM77548.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MTKT01002534; OWM77548.1; -; Genomic_DNA.
DR EMBL; PGOL01001367; PKI58510.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A218WY98; -.
DR STRING; 22663.A0A218WY98; -.
DR Proteomes; UP000197138; Unassembled WGS sequence.
DR Proteomes; UP000233551; 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 InterPro; IPR045104; Alfin.
DR InterPro; IPR021998; Alfin_N.
DR PANTHER; PTHR12321; CPG BINDING PROTEIN; 1.
DR PANTHER; PTHR12321:SF98; PHD FINGER PROTEIN ALFIN-LIKE 4; 1.
DR Pfam; PF12165; Alfin; 1.
PE 3: Inferred from homology;
KW Chromatin regulator {ECO:0000256|RuleBase:RU369089};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|RuleBase:RU369089};
KW Nucleus {ECO:0000256|RuleBase:RU369089};
KW Reference proteome {ECO:0000313|Proteomes:UP000233551};
KW Transcription {ECO:0000256|RuleBase:RU369089};
KW Transcription regulation {ECO:0000256|RuleBase:RU369089};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|RuleBase:RU369089};
KW Zinc-finger {ECO:0000256|RuleBase:RU369089}.
FT TRANSMEM 7..28
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 31..138
FT /note="Alfin N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12165"
FT REGION 147..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 228 AA; 26062 MW; 1B57DC180FF0F36E CRC64;
MDARATVYLS YQTCVEIILI SVVNILLFPV VDSVEFYMQC DPDREGDQAL YGFLDGHWEV
KVPEEEMPPK FPEPTIIINV PKDDKPFEEW LFNVVAFSDA WLLSMMTHYA KSLKFSKADR
GWLFSTIRKL PTVLEVVKEV KPAPAVLNNS SCHTGPNSEN QRDSELHSES HLVAVHPKPE
DQDKLALQEE HKDEPGGDRC AIPSGIYIWS VSWIICKVCK KWVQMQKN
//
