ID A0A9D3XAK5_9SAUR Unreviewed; 909 AA.
AC A0A9D3XAK5;
DT 03-MAY-2023, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2023, sequence version 1.
DT 18-JUN-2025, entry version 11.
DE RecName: Full=Polyhomeotic-like protein 2 {ECO:0008006|Google:ProtNLM};
GN ORFNames=KIL84_022230 {ECO:0000313|EMBL:KAH1175705.1};
OS Mauremys mutica (yellowpond turtle).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Testudinoidea; Geoemydidae; Geoemydinae; Mauremys.
OX NCBI_TaxID=74926 {ECO:0000313|EMBL:KAH1175705.1, ECO:0000313|Proteomes:UP000827986};
RN [1] {ECO:0000313|EMBL:KAH1175705.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MM-2020 {ECO:0000313|EMBL:KAH1175705.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:KAH1175705.1};
RA Gong S., Gao Y.;
RT "The genome of Mauremys mutica provides insights into the evolution of
RT semi-aquatic lifestyle.";
RL Submitted (SEP-2021) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:KAH1175705.1}.
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DR EMBL; JAHDVG010000476; KAH1175705.1; -; Genomic_DNA.
DR Proteomes; UP000827986; Unassembled WGS sequence.
DR GO; GO:0035102; C:PRC1 complex; IEA:TreeGrafter.
DR GO; GO:0003682; F:chromatin binding; IEA:TreeGrafter.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0042393; F:histone binding; IEA:TreeGrafter.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IEA:TreeGrafter.
DR CDD; cd09577; SAM_Ph1_2_3; 1.
DR FunFam; 1.10.150.50:FF:000011; Polyhomeotic-like protein 2 isoform 1; 1.
DR FunFam; 3.30.60.160:FF:000002; Polyhomeotic-like protein 2 isoform 1; 1.
DR Gene3D; 3.30.60.160; -; 1.
DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR InterPro; IPR050548; PcG_chromatin_remod_factors.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR012313; Znf_FCS.
DR InterPro; IPR038603; Znf_FCS_sf.
DR PANTHER; PTHR12247; POLYCOMB GROUP PROTEIN; 1.
DR PANTHER; PTHR12247:SF86; POLYHOMEOTIC-LIKE PROTEIN 2; 1.
DR Pfam; PF16616; PHC2_SAM_assoc; 1.
DR Pfam; PF00536; SAM_1; 1.
DR Pfam; PF21319; zf-FCS_1; 1.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
DR PROSITE; PS51024; ZF_FCS; 1.
PE 4: Predicted;
KW Developmental protein {ECO:0000256|ARBA:ARBA00022473};
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:UP000827986};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00367}.
FT DOMAIN 679..713
FT /note="FCS-type"
FT /evidence="ECO:0000259|PROSITE:PS51024"
FT DOMAIN 845..909
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 105..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 189..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 281..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 378..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 524..607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 657..680
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 779..822
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..27
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..199
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..299
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..402
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..427
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..455
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 562..573
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..592
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 795..810
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 909 AA; 96869 MW; A45C3BF47222BBBA CRC64;
MENEQLQVPP PSSSTSSTST ASSSSSSNGR QPGPQISVYS GIPDRQTVQV IQQALHRQPS
TAAQYLQQMY AAQQQHLMLQ TAALQQQHLS SAQLQSLAAV QQASLAANRQ GGSSGSNAPP
PTPSQQPTIN LATSPAAAQL INRAQSVNSA AASGITQQAV LLGNATSPAL TASQAQMYLR
AQMLEVSGGR MQRGRGPQRW LQSPSRASPI PQQELLLPRG TPARLIFTPT ATVTAVQPEG
SAAPTSQPST TTAQVQNLAI RAQQTVAQGV ASSQAQQLPT LAMKPAPSSS QPASNTSQGK
AVGPAPSMGI KGSQAEQAAE HLKKGDGGVP TSMDSRGHPM SRTVTPVTTH PLIAPAYAQL
QPHQLIQQQK QIQHQFVIQQ QQLQPRPQPQ LIQGGANTSP QLQPLPTPTP SLAVQPSPQV
QGQSHPTPQG PALLSHPPQC QASSQHKPSA NQPYQPTLHA PGLQAVGPAP PAPEGGPQNG
HPGCLNHATQ RKFQHASAVI LQLQPAIGTP QLSIQENARK DVLPADKNPE SLPAQQPQPP
QAALMPPAAP PDPEVSEGNR PPTHEPGQDR VHVQNDPSSP GMTSGNGNSA STVAGAAPQN
GENKPPQAIV KPQVLTHVIE GFVIQEGAEP FPVGRSSLLV GNLKKKYAQG LLAEKLPQQD
NTTTTDSEME EPYLQESKEE GNPPKLKCEL CGRVDFAYKF KRSKRFCSMA CAKRYNVGCT
KRVGLFHPDR SKLQKPGAAT HGRRRTCKGA LPVLSKDTKK QTPVSLSTGS VPLSVTASLQ
LNRSQEDSSR CSDNSSYEEP LSPLSASSST SRRRQGERDL ELPDMHMRDL VGIGHHFLPS
EPTKWNVEDV YEFIRSLPGC QEIAEEFRAQ EIDGQALLLL KEDHLMSAMN IKLGPALKIY
ARISMLKDS
//
