ID   A0A3B4UC82_SERDU        Unreviewed;      1245 AA.
AC   A0A3B4UC82;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Jumonji and AT-rich interaction domain containing 2 {ECO:0000313|Ensembl:ENSSDUP00000015768.1};
OS   Seriola dumerili (Greater amberjack) (Caranx dumerili).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Carangiformes; Carangidae; Seriola.
OX   NCBI_TaxID=41447 {ECO:0000313|Ensembl:ENSSDUP00000015768.1, ECO:0000313|Proteomes:UP000261420};
RN   [1] {ECO:0000313|Ensembl:ENSSDUP00000015768.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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   AlphaFoldDB; A0A3B4UC82; -.
DR   Ensembl; ENSSDUT00000016056.1; ENSSDUP00000015768.1; ENSSDUG00000011434.1.
DR   GeneTree; ENSGT00940000159220; -.
DR   Proteomes; UP000261420; Unplaced.
DR   GO; GO:0005634; C:nucleus; IEA:UniProt.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   CDD; cd16870; ARID_JARD2; 1.
DR   Gene3D; 1.10.150.60; ARID DNA-binding domain; 1.
DR   Gene3D; 2.60.120.650; Cupin; 1.
DR   InterPro; IPR001606; ARID_dom.
DR   InterPro; IPR036431; ARID_dom_sf.
DR   InterPro; IPR003347; JmjC_dom.
DR   InterPro; IPR003349; JmjN.
DR   InterPro; IPR004198; Znf_C5HC2.
DR   PANTHER; PTHR10694; LYSINE-SPECIFIC DEMETHYLASE; 1.
DR   PANTHER; PTHR10694:SF113; PROTEIN JUMONJI; 1.
DR   Pfam; PF01388; ARID; 1.
DR   Pfam; PF02373; JmjC; 1.
DR   Pfam; PF02375; JmjN; 1.
DR   Pfam; PF02928; zf-C5HC2; 1.
DR   SMART; SM01014; ARID; 1.
DR   SMART; SM00501; BRIGHT; 1.
DR   SMART; SM00558; JmjC; 1.
DR   SMART; SM00545; JmjN; 1.
DR   SUPFAM; SSF46774; ARID-like; 1.
DR   SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR   PROSITE; PS51011; ARID; 1.
DR   PROSITE; PS51184; JMJC; 1.
DR   PROSITE; PS51183; JMJN; 1.
PE   4: Predicted;
KW   Chromatin regulator {ECO:0000256|ARBA:ARBA00022853}.
FT   DOMAIN          527..568
FT                   /note="JmjN"
FT                   /evidence="ECO:0000259|PROSITE:PS51183"
FT   DOMAIN          591..682
FT                   /note="ARID"
FT                   /evidence="ECO:0000259|PROSITE:PS51011"
FT   DOMAIN          867..1030
FT                   /note="JmjC"
FT                   /evidence="ECO:0000259|PROSITE:PS51184"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          44..80
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          180..239
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          271..293
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          314..516
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          768..790
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1207..1245
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        54..80
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        193..223
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        331..371
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        372..391
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        415..479
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        484..516
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1245 AA;  137522 MW;  2E2C883F2DA650BB CRC64;
     MSKERPKRNI IQKKYDDSDG IPWSEERVMR KVLYLSLKEF RSAQKRQLDP RLQAQRKFAQ
     SQPNSPSTTP VKVADPGSLN TGLATVPSSS LSLLSSSSLS SSIQDLSRRK PKTEDFLTFL
     CLRRAAEELR KQVSKVNGLT RAGSAQAVGG AKKSRDFRLP SKTVKKYTAT VSKGHVTYTK
     AKQKELGKKT KLSSSNKHNS AASAPSSANN HNQHSQPAAS NGLANSGKAA APAHHSNAKT
     RKQVLLSNGL HNVAAGARLN GRLNGQRHNT LAKEDGQRQC QQGQGECPGR EGLRNSKRRL
     EVVLNSVGTG VVEQKAKTTG TEAKKAKLQP TPLETRSSSK KVANQEKAAT QITTPTTPVS
     NGHESETPLS PKQTPPVTPP PTPPPQQTPT PSTPAANTEP VNQRPKRASA GKLMLIRQAQ
     QQQSRSHGRN SSSSSPSSGQ NHPQNPSRAS TTSDPQQTSV SSSSTTSSLL TSTNSPGQLK
     PAALRPAERD KEWEREKEMT RQKEREQEKE WERQRSRPEG WAALGEVPVF RPAPREFQDP
     LVYLDAVREQ AEAAGMCRVV PPPDWRPECK LSEEMRFVTQ VQRVHMLGRR WGPNVQRLAC
     IRKHLKSQGI TMDEPPVIGC EVDLSRFFQL INDMGGMQQV MDLKKWTKLA DLLRIPKSAQ
     DRLAKLQEAY LQYILSYDSL SAEERLRLQA EVLQEKKNLE LRRGPLEGLL DSSTPSALVL
     PRYEPKNGLV GGIVGGGTGH QRTNGVYHHL KELEAQVKAG RRRLFAQEKQ GKEDRQHGEE
     QEEEEDRGVL SDQHKCIYKQ GKSVSLTNFF RIARNTMTMC FNKEPGAAEV EQEYWRIVEQ
     RDSHVAVHCG KVDTSTHGSG FPTGKSEPFS HGWNLTVLPN NSGSILRHLG AVPVTIPWLN
     IGMVFSTSCW SRDQNRLPYI DYLHTGADCI YSVPAEEKAK LDKVVHTLLQ ANGTPGLEML
     EKNIMQISPE VLCREGIKVY RTVQRSGQFV VCFPGAFVSK VCCGYSVSET VHFATPHWMN
     LGYQASKDLK CRRIAKPFSM EKLLYQIATA ESKRDNGLLL TTISALLKDL NIEMGQRQEL
     YKAGLLSSAR YGTHDGGLGP GEGRKKPRGK WLALESSERR CQICQHLCYL SMVVQETDNV
     VFCLECALRY VEKHKSCRGL KMMYRYDEEQ INSLVNQVCG RAMLKNSSGG GGGGVVVSGG
     GGEPCLGLSP AKASPAKRGP RKRDTVEVSL PRLSSSHMPK AAAVS
//