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Database: UniProt
Entry: A0A2Y9DIX9_TRIMA
LinkDB: A0A2Y9DIX9_TRIMA
Original site: A0A2Y9DIX9_TRIMA 
ID   A0A2Y9DIX9_TRIMA        Unreviewed;      2172 AA.
AC   A0A2Y9DIX9;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Bromodomain adjacent to zinc finger domain protein 2B isoform X8 {ECO:0000313|RefSeq:XP_004375469.1};
GN   Name=LOC101359017 {ECO:0000313|RefSeq:XP_004375469.1};
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_004375469.1};
RN   [1] {ECO:0000313|RefSeq:XP_004375469.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the WAL family. {ECO:0000256|ARBA:ARBA00007444}.
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DR   RefSeq; XP_004375469.1; XM_004375412.3.
DR   GeneID; 101359017; -.
DR   KEGG; tmu:101359017; -.
DR   OrthoDB; 2912910at2759; -.
DR   Proteomes; UP000248480; Unplaced.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd05503; Bromo_BAZ2A_B_like; 1.
DR   CDD; cd01397; HAT_MBD; 1.
DR   CDD; cd15630; PHD_BAZ2B; 1.
DR   Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR037374; BAZ2A/B_Bromo.
DR   InterPro; IPR001487; Bromodomain.
DR   InterPro; IPR036427; Bromodomain-like_sf.
DR   InterPro; IPR018359; Bromodomain_CS.
DR   InterPro; IPR018501; DDT_dom.
DR   InterPro; IPR016177; DNA-bd_dom_sf.
DR   InterPro; IPR001739; Methyl_CpG_DNA-bd.
DR   InterPro; IPR028942; WHIM1_dom.
DR   InterPro; IPR028941; WHIM2_dom.
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; PTHR45915:SF1; BROMODOMAIN ADJACENT TO ZINC FINGER DOMAIN PROTEIN 2B; 1.
DR   PANTHER; PTHR45915; TRANSCRIPTION INTERMEDIARY FACTOR; 1.
DR   Pfam; PF00439; Bromodomain; 1.
DR   Pfam; PF02791; DDT; 1.
DR   Pfam; PF01429; MBD; 1.
DR   Pfam; PF00628; PHD; 1.
DR   Pfam; PF15612; WHIM1; 1.
DR   Pfam; PF15613; WSD; 1.
DR   PRINTS; PR00503; BROMODOMAIN.
DR   SMART; SM00297; BROMO; 1.
DR   SMART; SM00571; DDT; 1.
DR   SMART; SM00391; MBD; 1.
DR   SMART; SM00249; PHD; 1.
DR   SUPFAM; SSF47370; Bromodomain; 1.
DR   SUPFAM; SSF54171; DNA-binding domain; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   PROSITE; PS00633; BROMODOMAIN_1; 1.
DR   PROSITE; PS50014; BROMODOMAIN_2; 1.
DR   PROSITE; PS50827; DDT; 1.
DR   PROSITE; PS50982; MBD; 1.
DR   PROSITE; PS50016; ZF_PHD_2; 1.
PE   3: Inferred from homology;
KW   Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW   ProRule:PRU00035}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248480};
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:PRU00146}.
FT   DOMAIN          740..811
FT                   /note="MBD"
FT                   /evidence="ECO:0000259|PROSITE:PS50982"
FT   DOMAIN          1088..1153
FT                   /note="DDT"
FT                   /evidence="ECO:0000259|PROSITE:PS50827"
FT   DOMAIN          1935..1985
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   DOMAIN          2081..2151
FT                   /note="Bromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50014"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          140..350
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          409..433
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          457..483
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          527..692
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          714..742
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          842..875
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1022..1044
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1263..1342
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1480..1543
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1585..1609
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1669..1695
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1997..2044
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        144..220
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        221..242
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        243..262
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        263..288
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        311..325
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        330..350
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        527..557
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        564..584
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        605..661
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        671..692
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        714..734
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        842..871
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1300..1321
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1486..1533
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2172 AA;  240920 MW;  96F720D2E9EC3266 CRC64;
     MESGERLSSS TASSTTPTSS STPPVASAVS KGGLSTGVAS LSSTINPCGH LFRAAGDQPF
     NLSTVSSAFP MVSPPVFGLH SASSGHSEFG GLGTLGTPTA LAAHPQLASF PGAEWWRTAD
     VPTRTGATFF PPLLGIPPLF APPAQNHDSS SFHSRTSGKS NRNGPEKGVN GSINGNSTSS
     VSGISTSVLS TTASGSTGQT KTISSGGGNR KCNQEQSKNQ PLDPRADKIK DKKPRKKTME
     SSSNSDSDSG TSSDTSSEGI SSSDSDDLEE DEEEEDQSLE ESEDDDSDSE SEAQHKSNNQ
     VLLHGISDPK ADGQKATEKA QEKRIHQPLP LVSESQTHSS FQSQQKQPQV LSQQLPFIFQ
     SSQAKEESVN KHTSVIQSTG LVSNVKPLSL VNQAKKETYM KLIVPSPDVL KAGNKNTSEE
     SSPLTSELRS KREQYKQTFP AQLKKQESSR SLKKVISALS NPKATSSSPA HPKQTLENNH
     PNPFLTNALL GNHQPNGVIQ SVIQEAPLAL TTKTKIQSRI NENIATASST PFSSPVNLST
     SGRRTPGNQT PVMPSASPIL HSQGKEKAVS NNVNTLQTQH HPHPAKSLVE QFRGTDSDIP
     SSKDSEDSNE DEEEDEEEDE EDDEDDESDD SQSESDSNSE SDTEGSEEED DDDDKDQDES
     DSDTEGEKTS MKLNKTASSV KSPSMSLSAH STPRNLHIAK APGSAPAALC SESQSPAFLG
     TPSSTLTSSP HSGTSKRRRV TDERELRIPL EYGWQRETRI RNFGGRLQGE VAYYAPCGKK
     LRQYPEVIKY LSRNGIMDIS RDNFSFSAKI RVGDFYEARD GPQGMQWCLL KEEDVIPRIR
     AMEGRRGRPP NPDRQRAREE SRMRRRKGRP PNVGNAEFVD NTDAKLLRKL QAQEIARQAA
     QIKLLRKLQK QEQARVAKEA KKQQAIMAAE EKRKQKEQIK IMKQQEKIKR IQQIRMEKEL
     RAQQILEAKK KKKEEAANAK LLEAEKRIKE KEMRRQQAVL LKHQERERRR QHMMLMKAME
     ARKKAEEKER LKQEKRDEKR LNKERKLEQR RLELEMAKEL KKPNEDMCLA DQKPLPELPR
     IPGLVLSGST FSDCLMVVQF LRNFGKVLGF DVNIDVPNLS VLQEGLLNIG DSMGEVQDLL
     VRLLSAAVCD PGLITGYKAK TALGEHLLNV GVNRDNVSEI LQIFMEAHCG QTELTESLKT
     KAFQAHTPEQ KASVLAFLIN ELACSKSVVS EIDKNIDYMS NLRRDKWVVE GKLRKLRIIH
     AKKTGKRDTS GGTDLGEEQH PLGTPTPGRK RRRKGGDSDY DDDDDDDSDE QADEDDEDEE
     DKEDKKGKKA DVCEDEDEGD QAASVEELEK QIEKLSKQQS QYRRKLFDAS HSLRSMMFGQ
     DRYRRRYWIL PQCGGIFVEG MESGEGLEEI AKEREKLKKA ESIQIKEEMF ETSGDILNCL
     NTDHCEQKED LKEKDNTNLF LQKPGSFSKL SKLLEVAKMP PESDSMTPKP NGSANGCTMS
     YQNSGKHSLG SLQSTATQSN VEKTDSNNLF SPGSGGPGKF YSPLPSDQLL KTLTEKNRQW
     FSLLPRTPCD DTSLTHADVS AASLVAPQSQ PPPKSPSPAP APLLGSSSSQ NPIGLNPFAL
     SPLQIKSGVS MMGLQFCGWP TGVLTSNIPF TSSPLPNLGS GLGLSEGNGN SFLTPNAASS
     KSESPVPQNE KVSSTQPAAI EVVKPVDFLS PKPIPEEMQF GWWRIIDPED LKALLKVLHL
     RGIREKALQK QIQKHLDYIT QACIKNKDVA IIELNENEEN QVTRDIVENW SVEEQAMEMD
     LSILQQVEDL ERRVASASLQ VKGWMCPEPA SEREDLVYFE HKSFTKLCKE HDGEFTGKEE
     SSAHALERQS DNPLDIAVTR LADLERNIER RIEEDIAPGL RVWRRALSEA RSAAQVALCI
     QQLQKSIAWE KSIMKVYCQI CRKGDNEELL LLCDGCDKGC HTYCHRPKIT TIPDGDWFCP
     ACIAKASGQT LKIKKLHVKG KKANEPKKGK KVPLAGDTED EDSASTSSSL KRGNKDLKKR
     KMEENTSINL SKQDSFTSVK KPKRDDSKDL ALCSMILTEM ETHEDAWPFL LPVNLKLVPG
     YKKVIKKPMD FSTIREKLSS GQYPNLETFA VDVRLVFDNC ETFNEDDSDI GRAGHSMRKY
     FEKKWTDTFK VS
//
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