ID M7AMX0_CHEMY Unreviewed; 377 AA.
AC M7AMX0;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=PHD finger protein 1 {ECO:0000313|EMBL:EMP26576.1};
GN ORFNames=UY3_16333 {ECO:0000313|EMBL:EMP26576.1};
OS Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Americhelydia; Chelonioidea; Cheloniidae; Chelonia.
OX NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP26576.1, ECO:0000313|Proteomes:UP000031443};
RN [1] {ECO:0000313|Proteomes:UP000031443}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the Polycomblike family.
CC {ECO:0000256|ARBA:ARBA00008084}.
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DR EMBL; KB577777; EMP26576.1; -; Genomic_DNA.
DR AlphaFoldDB; M7AMX0; -.
DR STRING; 8469.M7AMX0; -.
DR eggNOG; KOG4323; Eukaryota.
DR Proteomes; UP000031443; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035064; F:methylated histone binding; IEA:UniProt.
DR CDD; cd15500; PHD1_PHF1; 1.
DR CDD; cd15582; PHD2_PHF1; 1.
DR CDD; cd20449; Tudor_PHF1; 1.
DR Gene3D; 2.30.30.140; -; 1.
DR Gene3D; 3.90.980.20; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR040477; KDM4-like_Tudor.
DR InterPro; IPR031202; PHF1_PDH-finger1.
DR InterPro; IPR047010; PHF1_PHD-finger2.
DR InterPro; IPR002999; Tudor.
DR InterPro; IPR047399; Tudor_PHF1.
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; PTHR12628:SF11; PHD FINGER PROTEIN 1; 1.
DR PANTHER; PTHR12628; POLYCOMB-LIKE TRANSCRIPTION FACTOR; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF18104; Tudor_2; 1.
DR SMART; SM00249; PHD; 2.
DR SMART; SM00333; TUDOR; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 2.
DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000031443};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 97..155
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 349..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..377
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 377 AA; 42242 MW; 0CAC4B8273E6EDC5 CRC64;
MASELPAQTS RVTRTSSRLT SGPWKRPAAP APAVAPSRPR FWEGQDVLAR WTDGLLYLGT
IKKVDASRQV CLVQFEDNSQ FLVLWKDINP AAVPGEEQIC CVCYSESVSP ENQLVRCEKC
GHTYHQECHL PRVLDASSDG AGVLGAWMCR QCVFAVATKR GGALKKGPYA KAMLSMKLVL
PYQLKTLEWD PAHLTNRQQC YCYCGGPGEW NLKMLQCCSC AQWFHEACTQ CLSKPLLYGD
RFYVFECCVC TGGPESVRRL PLRWVDVAHL ILYHLSICCK KKYFDFEREI LPFASENWDN
LLLGELSDTP KRDRYSQLLS ALSSHKDRFI SGKEIKKRKG LFGLHIRVPP PAPQCPGGHG
GSTAQQPQGQ PPLTDSR
//
