ID A0A164Z666_9CRUS Unreviewed; 1711 AA.
AC A0A164Z666;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=AT-rich interactive domain-containing 4B-like protein {ECO:0000313|EMBL:KZS15988.1};
GN ORFNames=APZ42_018393 {ECO:0000313|EMBL:KZS15988.1};
OS Daphnia magna.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Branchiopoda;
OC Diplostraca; Cladocera; Anomopoda; Daphniidae; Daphnia.
OX NCBI_TaxID=35525 {ECO:0000313|EMBL:KZS15988.1, ECO:0000313|Proteomes:UP000076858};
RN [1] {ECO:0000313|EMBL:KZS15988.1, ECO:0000313|Proteomes:UP000076858}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Xinb3 {ECO:0000313|EMBL:KZS15988.1,
RC ECO:0000313|Proteomes:UP000076858};
RC TISSUE=Complete organism {ECO:0000313|EMBL:KZS15988.1};
RA Gilbert D.G., Choi J.-H., Mockaitis K., Colbourne J., Pfrender M.;
RT "EvidentialGene: Evidence-directed Construction of Genes on Genomes.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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:KZS15988.1}.
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DR EMBL; LRGB01000781; KZS15988.1; -; Genomic_DNA.
DR STRING; 35525.A0A164Z666; -.
DR Proteomes; UP000076858; Unassembled WGS sequence.
DR GO; GO:0005694; C:chromosome; IEA:UniProt.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR CDD; cd20389; Tudor_ARID4_rpt1; 1.
DR CDD; cd20390; Tudor_ARID4_rpt2; 1.
DR Gene3D; 2.30.30.140; -; 3.
DR Gene3D; 1.10.150.60; ARID DNA-binding domain; 1.
DR InterPro; IPR012603; ARID4A/B_PWWP.
DR InterPro; IPR001606; ARID_dom.
DR InterPro; IPR036431; ARID_dom_sf.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR002999; Tudor.
DR InterPro; IPR025995; Tudor-knot.
DR PANTHER; PTHR13964:SF27; HAT-TRICK, ISOFORM D; 1.
DR PANTHER; PTHR13964; RBP-RELATED; 1.
DR Pfam; PF01388; ARID; 1.
DR Pfam; PF08169; RBB1NT; 1.
DR Pfam; PF11717; Tudor-knot; 1.
DR SMART; SM01014; ARID; 1.
DR SMART; SM00501; BRIGHT; 1.
DR SMART; SM00333; TUDOR; 1.
DR SUPFAM; SSF46774; ARID-like; 1.
DR SUPFAM; SSF54160; Chromo domain-like; 1.
DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 1.
DR PROSITE; PS51011; ARID; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000076858};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT DOMAIN 301..392
FT /note="ARID"
FT /evidence="ECO:0000259|PROSITE:PS51011"
FT REGION 122..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 282..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 398..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 471..499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 512..673
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 745..967
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1019..1209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1254..1388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1401..1633
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1664..1691
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 410..442
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..541
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 542..671
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 745..766
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 780..813
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 843..864
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 875..895
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 941..967
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1019..1036
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1043..1093
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1096..1111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1136..1165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1166..1191
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1271..1286
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1336..1350
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1404..1437
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1488..1511
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1516..1530
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1568..1599
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1711 AA; 188362 MW; 3BBCFA6C8821F63F CRC64;
MGDDPPFLSV GTEVSAKYKG AFCEAKVRKV VKSIKCKVMF KLGLGSAVVS DDQIKGLLRV
GAQVEAKHPE KAQFVEAVIN KIQDCSQYTV VFDDGDITTL RRTSLCLKSG RHFAESETLD
QLPLTHPEHF GTPVLGGRRG GRRRDESSDE DGDEDSELGR PEKSALRKTE DREPNIGKIV
CVEVSDKKKG KEAWFPGLIV APTAQDAVSI RVKDEYLVRS FKDARYYTVP KKEAMEFTRE
IALKTEHNAL KTAIEKAMQY LDKNELPAHW DREALFGLDD ASSINESKGG SDADSSEEET
PEEKDHFVAQ LYKFMDDNGT PINKGPTINS RDLDLYRLFK IVNKMGGFNR VTNQNGWKVV
TKKLILNSAS NSSTHVKQAY KKYLYGFEDF YRKLGCTMNS PRGAKSRARP GRSLIRDRDR
GTSGSSTPKG DLEEEEKIKV EDVPPVSPST QELVPMIETA VVVDEETISV TVEEEEVDES
SSSVSQPPPR KQRERSLPLR LQDTITTKLV VVKKEEESGG DEAIEQEVES NSSQSVRSQR
GTRSRIPREK SDESEQPETN RSARKRGKSR LEDKTTEEDD KTSRVKVKEE TTNGKEDSEK
KSKENTEKKN KTPGREPKNR GRKSEDAGKV EEPKMVEEEP ITVDQEEPTP KRRGRKPRVL
GDSEEDEGGR LPANVDVQIG DKLKVYYGDK PIQDSKVTYE AKVCEIRCEG SSKLYLVHYT
GWNTRYDEWI KRARIAENLT WTPNRKRSKS VHGQGTIRTS TSAPTGKAVP AKRGRTRGQD
SSRSATPSSV TSTSSTGQRN ANLASGEDSG NKIPPTKNSR RRSRRVSEIS GMSAESMNSS
DDEEEEGTVR VRKKPTKKVA SANIESEESE PVDVEESERT PRRRHQRRRI SEAEQMPSEN
KIQDPPVVDI SASVTTLTPV RRGRRRAVTA PESAVADPVP IKEEQVEEEK TSEAAADLIS
VSEEEPKGKD FDLKKIRSEL KMPVDIAATT IALKVSSPVP PSLPPPPIPI AVSTVPTTST
VLSPMQQQQH AVESQASASG RGDDDIYEFR EPEPFEFEVR TRRESPFSED RVHHRFTQRK
TTKEEEEDPS PKKTNAMPVR SGSNERSKSV ITSPPRGGRP CSTAITVPVV PPEESELTQE
TPTASCPSPV ASQPSDDVIS IAPFSNAQSP PPPPSPLPTL PTLPIGPASP KAVDPPVEEE
TLTEEQPQAS AVNCLDLAPP IASPSPVLPM PAIPAIAARP VMAASSAHVV FAHKSTSLEV
KLRKAAEEHE DDNGDADEEE DGVEEDSPAN DTKSNRLPSK RERRKAGARK AISREFIESD
EDSPEDPGAA SDTTANKVVD DEKTSSDSTP SEIAEDDEPA DKDNEPDCLL AVRKHSPNCS
SPLKLKTDED LDENSLLCEE TIPGSPVTHS TAPSLDGPDI SLPTPSTSRS TEMPFASAPS
APNMPRTRGL SGGNNSAPRA NRKRGLRQAL AMQRPGCVRP LGGPSLVLEN TPPTTPDGSI
SSSSSSPQGD HGGMSPDHDS SVKSDREFSE NDNAAPSPQV LHNTVEIPVV RNIGPRASAT
AQPVPTPVLK RREDEVPRQM QQQHPEEESP VKRRRRGVVM SACDPNSARK GRGHGRSPRR
TGSDSEDTTP DYVNSSSIVP GCINLTNYQP RSTRYNFCTD LDPELDATQR IASLQDKLRE
LRQTYSALKA KVMLIDRRRK KLKRKEKEAA S
//
