ID A0A0N0BI03_9HYME Unreviewed; 1853 AA.
AC A0A0N0BI03;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=AT-rich interactive domain-containing protein 4B {ECO:0000313|EMBL:KOX77031.1};
GN ORFNames=WN51_10425 {ECO:0000313|EMBL:KOX77031.1};
OS Melipona quadrifasciata.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Apidae; Melipona.
OX NCBI_TaxID=166423 {ECO:0000313|EMBL:KOX77031.1, ECO:0000313|Proteomes:UP000053105};
RN [1] {ECO:0000313|EMBL:KOX77031.1, ECO:0000313|Proteomes:UP000053105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0111107301 {ECO:0000313|EMBL:KOX77031.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KOX77031.1};
RA Pan H., Kapheim K.;
RT "The genome of Melipona quadrifasciata.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KQ435736; KOX77031.1; -; Genomic_DNA.
DR STRING; 166423.A0A0N0BI03; -.
DR OrthoDB; 445024at2759; -.
DR Proteomes; UP000053105; 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; IPR000953; Chromo/chromo_shadow_dom.
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; SM00298; CHROMO; 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:UP000053105};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT DOMAIN 377..470
FT /note="ARID"
FT /evidence="ECO:0000259|PROSITE:PS51011"
FT REGION 191..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 353..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 480..638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 702..928
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1007..1031
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1374..1449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1584..1784
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1135..1191
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1802..1843
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 214..233
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..556
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..582
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 583..628
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 702..762
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 763..777
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 778..810
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 811..835
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 846..898
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 905..928
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1374..1430
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1584..1601
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1621..1654
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1746..1784
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1853 AA; 210263 MW; 513BF086AE18CA24 CRC64;
MNVDTPLSYA QCRPSYYFDF YLETDIHLSR EAVEKSCFQK VQRHHPIGVE WLADKLRWGG
NGQGTGACTH SSREGDDPPY LSVGTEVSAK YKGAFCEAKI RKVVRSVKCR VTYKQGLGTA
TVADDQIKGT LRVGASVEAK HGDRKEFVEA TITKIQDCSQ YTVVFDDGDI TTLRRTALCL
KSGRHFAESE TLDQLPLTHP EHFGNPVIGG RRGRRSRQAQ DESSDDEDSP PRGTRDSGSS
GTGKEGMETE PEIGRVVCVE LGDKKKKDYW FPGLVVAPTA QDTVRIRVRD DYLVRSFKDA
RYYTVPKKEA TEFTKELVNK VENSTLKVAV ERALQFLEKN ELPPHWDRDS LFGHSVSSGN
SDSDGELDSD SSDDEPREEK DHFVAQLYKF MDDRGTPINN CPMIGSEDID LYRLFRAVYK
LGGYNRVTNQ NQWKLITRRL SFTMQNSPST HNLVKQAYKK FLHSFEDFYR KLGCTMVNHP
RGTIRKQRPG RSLIRDKDRN TPVPPQISVA KTEKEKKDKK VTEEEKKEKK EIKKEQSVKE
EEIVKIKKKD EFEESGSGQD SDVNVEAEAE SSSSSEKSQK ISTETRTPSR ESERKTLSKQ
RRLIDEDLKK RGRKRKEYET EKSRTDEQST DSAPCYKGPV ELGDRLKVYY GPTHESKVTY
EAKVIDMEKD GTEPMYLVHY TGWNTRYDEW IKSSRIAQNF TQAQGRMKRI KATSRPQTPS
TNLSNNINKS SKIISNTSSN TSQNRRRAQS VAPTTSVVSS SSTKETKKEE KEKEVSQPVR
STTPLSVISS SSRTKSPATP ANNRQTRTRN NDMSSIEHRR RTRRTSGHAD IIPSETEESE
TYDSDTTESE QTRTKSKTVE ERKRKEARYR VEDRMKPDET SEGEEDKDNL EEPRRGRRLR
RTISKSQGIK SEPDSDEEQP KGRDFDLNQI RSELKGFDKA VKLELVRVEP DPEDEIKIEE
KENVSVSPKL EKNLEASKLE TIPESKIIDN TEDIYEFKEP EPFEFEVRNK RDTSGEKDKL
KKRVFEEEPK SPKKKQKIIV APVIKEVKSE TDNDSRKKVK KLFSKRTDDI TDNLHSHKSL
QSTSLTTCEE AFDKLCESPP FNQVKPIPII EETGKINNGI DLLFSDLPGD DDATHDDSED
RLIISEAEVS EAEQENLFTY QQEMFPSNDG NDLMESNKED VNLQIESVRE DITLTVSNKP
DIVVEQKQSI KSPLHSQSPE LKPLDSKLLD ITPVPSPIVT VPAPISARLP ATSTIEEKHA
AAMAFRSKTK DVKKEDEIPE VVWKTSKEIS KKLDTTVVQK SKEDQHGPKI ENENNKREEE
AIVINNENQC EEIMCVVIKQ KEEELQQFKP KKEVEIKKFV ETKIEHTKIQ EKEEEEWKRV
ENEKSKKIED EFKEDDFKEK ENHKKIINQD MVDSADSSDS EQRLIIDNEE SQDVKSSTSN
FDAKLRAELD RLQDTQERYS QLQTQKSMQP LKHQQQECIT EFKTEFKTEI KEIPVTKTDE
EGETINSLLC EEEIPGSPAP ITESVEQINA GPSCSPPKVE TAESNIVLME MPFASAPTSG
QSTTSSTVAT LSMALPKTIE TSVPVSLSMQ QNPTLSMRQQ SHHLPALMPA QRRESNEAAP
VMDNTPPTTP DSSISNISGS PREERTGGSS PTSEDNMKHN RDSSEADNDS GGKGPGFSED
DTLPNVEGNS ADRILKPPAK RTIEETQSPK KRKRNRKHSE CDKNTTKKTG RHSNRHGRHG
GGSDSDDTSE GSNLCGVNST SANHTNIASV PDLSNYSSRS PRPTKYNFYV ELDPELDGSQ
RIAVLQQKLA ELRKTYNAVK VELAAIERRR KKLRRREREA IKAAKAEMQQ ACS
//
