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Database: UniProt
Entry: A0A196SJJ3_BLAHN
LinkDB: A0A196SJJ3_BLAHN
Original site: A0A196SJJ3_BLAHN 
ID   A0A196SJJ3_BLAHN        Unreviewed;       778 AA.
AC   A0A196SJJ3;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=AT-rich interactive domain-containing protein 3C {ECO:0000313|EMBL:OAO16099.1};
GN   ORFNames=AV274_2180 {ECO:0000313|EMBL:OAO16099.1};
OS   Blastocystis sp. subtype 1 (strain ATCC 50177 / NandII).
OC   Eukaryota; Sar; Stramenopiles; Bigyra; Opalozoa; Opalinata; Blastocystidae;
OC   Blastocystis.
OX   NCBI_TaxID=478820 {ECO:0000313|EMBL:OAO16099.1, ECO:0000313|Proteomes:UP000078348};
RN   [1] {ECO:0000313|EMBL:OAO16099.1, ECO:0000313|Proteomes:UP000078348}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 50177 / NandII {ECO:0000313|Proteomes:UP000078348};
RA   Gentekaki E., Curtis B., Stairs C., Eme L., Herman E., Klimes V.,
RA   Arias M.C., Elias M., Hilliou F., Klute M., Malik S.-B., Pightling A.,
RA   Rachubinski R., Salas D., Schlacht A., Suga H., Archibald J., Ball S.G.,
RA   Clark G., Dacks J., Van Der Giezen M., Tsaousis A., Roger A.;
RT   "Nuclear genome of Blastocystis sp. subtype 1 NandII.";
RL   Submitted (MAY-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:OAO16099.1}.
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DR   EMBL; LXWW01000099; OAO16099.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A196SJJ3; -.
DR   STRING; 478820.A0A196SJJ3; -.
DR   OrthoDB; 5001776at2759; -.
DR   Proteomes; UP000078348; Unassembled WGS sequence.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:InterPro.
DR   CDD; cd16100; ARID; 1.
DR   Gene3D; 3.30.40.100; -; 1.
DR   Gene3D; 1.10.150.60; ARID DNA-binding domain; 1.
DR   Gene3D; 1.20.1020.10; TAZ domain; 1.
DR   InterPro; IPR045147; ARI3A/B/C.
DR   InterPro; IPR001606; ARID_dom.
DR   InterPro; IPR036431; ARID_dom_sf.
DR   InterPro; IPR035898; TAZ_dom_sf.
DR   InterPro; IPR011124; Znf_CW.
DR   InterPro; IPR000197; Znf_TAZ.
DR   PANTHER; PTHR15348; AT-RICH INTERACTIVE DOMAIN-CONTAINING PROTEIN ARID DOMAIN- CONTAINING PROTEIN DEAD RINGER PROTEIN B-CELL REGULATOR OF IGH TRANSCRIPTION BRIGHT; 1.
DR   PANTHER; PTHR15348:SF0; PROTEIN DEAD RINGER; 1.
DR   Pfam; PF01388; ARID; 1.
DR   Pfam; PF07496; zf-CW; 1.
DR   Pfam; PF02135; zf-TAZ; 1.
DR   SMART; SM01014; ARID; 1.
DR   SMART; SM00501; BRIGHT; 1.
DR   SMART; SM00551; ZnF_TAZ; 1.
DR   SUPFAM; SSF46774; ARID-like; 1.
DR   SUPFAM; SSF57933; TAZ domain; 1.
DR   PROSITE; PS51011; ARID; 1.
DR   PROSITE; PS50134; ZF_TAZ; 1.
PE   4: Predicted;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078348};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          131..211
FT                   /note="TAZ-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50134"
FT   DOMAIN          408..502
FT                   /note="ARID"
FT                   /evidence="ECO:0000259|PROSITE:PS51011"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          243..292
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          312..336
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          516..562
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          614..724
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        253..267
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        519..551
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        646..660
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        661..680
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        681..699
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   778 AA;  83291 MW;  3B395CC77EBC0A14 CRC64;
     MDSKPLEGAK GIDKQMVDPN PRDGLISPRQ FYSPTLGEQM QSRGSFDFTE NDLGSSIIAG
     GGSTVYSPFL MQLSYSDKTA GDAMKNYAGS FEMGKTSESA ASTKNGPPVI MLPDSATQSS
     NHIFSKLLAL VSENSPLLSQ CLEQLNHVSH CHKLEGECTF PLCLTIKRDV YHTSNCTDEN
     CPTCLLMRPL ILLHSMNCKE EGCQIILCSR YHSAWTVFQH SLTGLPLPRM DVLFSLSAKP
     KQSVPLVKTE PPPTKKGHSR GSRSSAYAEE ARSDLAKSPQ MPTLPKSAAT PTLDEVKSIP
     ITPIPAYSMP SQALSAPESP FMQGGSSSTS KGSADSKQFS SSLSAQYIAC CKCGKHRAVP
     STLDVSLLPH FECSMNIWDD NKYNSCLIEE NVDINYSINL ARKGPNYEQD CAHFVNKLKS
     FLASNQIMSY RPPTLGRKEV DLYRLFREVT AYGGCESVVS KEGTWAKIYR GLDNFSPTET
     SASFRLKKMY TKYLLAYEKH VFNFLPMPAK KHRYSHAQAA QAAQASQAAQ TSQAGQTGQT
     TQASQGAHGI QNSAIFPPGG SYAEHGKAQA KASYANALYT DTTLQSSLLS SMHYTPGAGI
     GLIGGNVNGS AGGTGSAGGT GSAGGTCSAG GWEKEGSGKT RGASMKRSFE ASNLNAGGRE
     ESSSRGEEIG GHRLRSATKE SYRTGRSASA RTSPQPQGVG ARVTRRREQL DISKSPLLTG
     EDPEGAAGLQ ALMSLRTSLS PMLHAADEAK WDALLTAATD GKKGELESLP TAAMSAAK
//
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