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Database: UniProt
Entry: A0A2Y9R267_TRIMA
LinkDB: A0A2Y9R267_TRIMA
Original site: A0A2Y9R267_TRIMA 
ID   A0A2Y9R267_TRIMA        Unreviewed;       651 AA.
AC   A0A2Y9R267;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=MBT domain-containing protein 1 isoform X4 {ECO:0000313|RefSeq:XP_023588512.1};
GN   Name=LOC101348095 {ECO:0000313|RefSeq:XP_023588512.1};
OS   Trichechus manatus latirostris (Florida manatee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Afrotheria; Sirenia; Trichechidae; Trichechus.
OX   NCBI_TaxID=127582 {ECO:0000313|Proteomes:UP000248480, ECO:0000313|RefSeq:XP_023588512.1};
RN   [1] {ECO:0000313|RefSeq:XP_023588512.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   RefSeq; XP_023588512.1; XM_023732744.1.
DR   AlphaFoldDB; A0A2Y9R267; -.
DR   Proteomes; UP000248480; Unplaced.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd20120; MBT_MBTD1_rpt1; 1.
DR   CDD; cd20123; MBT_MBTD1_rpt2; 1.
DR   CDD; cd20126; MBT_MBTD1_rpt3; 1.
DR   CDD; cd20129; MBT_MBTD1_rpt4; 1.
DR   Gene3D; 2.30.30.140; -; 4.
DR   Gene3D; 3.30.60.160; -; 1.
DR   InterPro; IPR004092; Mbt.
DR   InterPro; IPR012313; Znf_FCS.
DR   InterPro; IPR038603; Znf_FCS_sf.
DR   PANTHER; PTHR12247:SF79; MBT DOMAIN-CONTAINING PROTEIN 1; 1.
DR   PANTHER; PTHR12247; POLYCOMB GROUP PROTEIN; 1.
DR   Pfam; PF02820; MBT; 4.
DR   Pfam; PF21319; zf-FCS_1; 1.
DR   SMART; SM00561; MBT; 4.
DR   SUPFAM; SSF63748; Tudor/PWWP/MBT; 4.
DR   PROSITE; PS51079; MBT; 4.
DR   PROSITE; PS51024; ZF_FCS; 1.
PE   4: Predicted;
KW   Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248480};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00367}.
FT   DOMAIN          68..103
FT                   /note="FCS-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51024"
FT   REPEAT          164..268
FT                   /note="MBT"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00459"
FT   REPEAT          276..372
FT                   /note="MBT"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00459"
FT   REPEAT          374..479
FT                   /note="MBT"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00459"
FT   REPEAT          487..583
FT                   /note="MBT"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00459"
FT   REGION          1..55
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          583..614
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          629..651
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..24
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        30..47
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        632..651
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   651 AA;  73283 MW;  EE3630E017D86653 CRC64;
     MENTKDLTEH SSRPERKRRD SFGMFDGYDS CSEDTSSSSS SEESEEEVAP LPSNLPIIKN
     NGQVYTYPDG KSGMATCEMC GMVGVRDAFY SKTKRFCSVS CSRSYSSNSK KASILARLQG
     KPPTKKAKVL QKQPLVAKLA AYAQYQATLQ NQAKTKAAVS MEGFSWGNYI NSNSFIAAPV
     TCFKHAPMGT CWGDISENVR IEVPNTDCSL PTKVFWIAGI VKLAGYNALL RYEGFENDSG
     LDFWCNICGS DIHPVGWCAA SGKPLVPPRT IQHKYTNWKA FLVKRLTGAK TLPPDFSQKV
     SESMQYPFKT CMRVEVVDKR HLCRTRVAVV ESVIGGRLRL VYEESEDRTD DFWCHMHSPL
     IHHIGWSRSI GHRFKRSDIT KKQDGHFDTP PHLFAKVKEV DQSGEWFKEG MKLEAIDPLN
     LSTICVATIR KVLADGFLMI GIDGSEAADG SDWFCYHATS PSIFPVGFCE INMIELTPPR
     GYTKLPFKWF DYLRETGSIA APVKLFNKDV PNHGFRVGMK LEAVDLMEPR LICVATVTRI
     IHRLLRIHFD GWEEEYDQWV DCESPDLYPV GWCQLTGYQL QPPASQSSRE SQSGSSKQKK
     KAKSQQYKGH KKMTTLQLKE ELLDGEDYNF LQGASDQESN GSANFYIKQE P
//
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