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Database: UniProt
Entry: A0A091WB63_OPIHO
LinkDB: A0A091WB63_OPIHO
Original site: A0A091WB63_OPIHO 
ID   A0A091WB63_OPIHO        Unreviewed;      1192 AA.
AC   A0A091WB63;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   22-FEB-2023, entry version 37.
DE   SubName: Full=Stonin-1 {ECO:0000313|EMBL:KFR12897.1};
GN   ORFNames=N306_05712 {ECO:0000313|EMBL:KFR12897.1};
OS   Opisthocomus hoazin (Hoatzin) (Phasianus hoazin).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Opisthocomiformes; Opisthocomidae;
OC   Opisthocomus.
OX   NCBI_TaxID=30419 {ECO:0000313|EMBL:KFR12897.1, ECO:0000313|Proteomes:UP000053605};
RN   [1] {ECO:0000313|EMBL:KFR12897.1, ECO:0000313|Proteomes:UP000053605}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N306 {ECO:0000313|EMBL:KFR12897.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC       Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the Stoned B family.
CC       {ECO:0000256|ARBA:ARBA00005579}.
CC   -!- SIMILARITY: Belongs to the TFIIA subunit 1 family.
CC       {ECO:0000256|ARBA:ARBA00010059}.
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DR   EMBL; KK735175; KFR12897.1; -; Genomic_DNA.
DR   STRING; 30419.A0A091WB63; -.
DR   Proteomes; UP000053605; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005672; C:transcription factor TFIIA complex; IEA:InterPro.
DR   GO; GO:0006897; P:endocytosis; IEA:InterPro.
DR   GO; GO:0006367; P:transcription initiation at RNA polymerase II promoter; IEA:InterPro.
DR   CDD; cd07976; TFIIA_alpha_beta_like; 2.
DR   Gene3D; 1.10.287.100; -; 1.
DR   Gene3D; 2.60.40.1170; Mu homology domain, subdomain B; 2.
DR   Gene3D; 2.30.18.10; Transcription factor IIA (TFIIA), beta-barrel domain; 1.
DR   InterPro; IPR036168; AP2_Mu_C_sf.
DR   InterPro; IPR028565; MHD.
DR   InterPro; IPR012320; SHD_dom.
DR   InterPro; IPR004855; TFIIA_asu/bsu.
DR   InterPro; IPR009088; TFIIA_b-brl.
DR   PANTHER; PTHR10529; AP COMPLEX SUBUNIT MU; 1.
DR   PANTHER; PTHR10529:SF339; STONIN-1; 1.
DR   Pfam; PF00928; Adap_comp_sub; 1.
DR   Pfam; PF03153; TFIIA; 1.
DR   SMART; SM01371; TFIIA; 1.
DR   SUPFAM; SSF49447; Second domain of Mu2 adaptin subunit (ap50) of ap2 adaptor; 1.
DR   SUPFAM; SSF47396; Transcription factor IIA (TFIIA), alpha-helical domain; 1.
DR   SUPFAM; SSF50784; Transcription factor IIA (TFIIA), beta-barrel domain; 1.
DR   PROSITE; PS51072; MHD; 1.
DR   PROSITE; PS51070; SHD; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053605};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163}.
FT   DOMAIN          279..412
FT                   /note="SHD"
FT                   /evidence="ECO:0000259|PROSITE:PS51070"
FT   DOMAIN          416..720
FT                   /note="MHD"
FT                   /evidence="ECO:0000259|PROSITE:PS51072"
FT   REGION          42..86
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          110..161
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1056..1142
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        42..62
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        110..151
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1062..1086
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1087..1105
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1112..1142
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1192 AA;  133711 MW;  283CD0F1B561CF61 CRC64;
     MCSTNPANWV TFDDEPLFQS PQKLIDNQSS CKANGLKLNL SSMHESSSRA SSTGSTPLSS
     PVVDFYVSPG PPSNSPLTTP TRDYPASPCI PKPGIHILYP IPEWPSNANP LPSPGTCSSL
     TSQKLGGLPL STSPNDHPVK TSVSKPTDEG SPNPPGSCEE LGELSSALGR FPYFQNNCAF
     SSPFWKEGCS LSTSPANVGM HRKDKALDRS VCHPKDKETC HDQKSLNQGS FSYICERLEH
     LQADSCDATG SPPVSSTHAW HQLSPAIPRS LFRSRKADGW PFMLRIPEKK NMMSSRQWGP
     IYLSVLPGGV LQMYYEKGLE KPFKEFQLQA HCKLSEPKLE SYNVSGKIHT VKIECVSYTE
     KRRYHPKAEV IHEPEIEQML KLGTTDYNDF TDFLVTVEEE LMKLPTISRQ KRNYEEQEMT
     LEIVDNFWGK VTKAEGKLVE SAVITHIYCL CFVNGSADCF LTLNDVELQK RDERYFEKED
     EKKWIDILDC HFHNCVKAWE FEQSRIIKFT PPDACRLELM RFRTRYNGQD LPFSVKAVVV
     VQGAYVELQA FINMSSIPTR LPSVKYCENI MILFPVPTQW VKALWTMNLQ RQKSLKAKMN
     RRACLGSLHE IESDPVIQVS VGTAKYESAY RAVVWKIDRL PDKNSSSDHP HSLSYKLELG
     SDQEIPSDWY PFATVQFVVH DTCASGTEVR SLGIENDVQP QKHVVQKAFY NCQLKLYKSV
     IEDVIEGVRE LFAEEGVEEQ VLKDLKQLWE TKVMQSKATE GFFRHSHHTP QFTLQLPHNF
     HRVLHASAAS VVIPAGKGFQ NFWAGDMVWS CATLTLPSGI VYPIHVPAGV TLQTASGHLY
     KVNMPLMVTQ ATGDGSILHH PVQQILKPLG QPSVLQASIA GVARVSASSV QAAAETLQPQ
     EPVVQQTMVF QPNVMEKAHL ENSANTALVQ QPSVSQQQLG TNAEWNQCAD STEKTQHGDL
     RTTVFTXXXX XAESLANNSS RVLLDVEEQL DIDPQELVQQ QVSDDIIDLL ITGKSLDDNT
     VLKDQDSIAS SHEQMESNLR SEKDICSDIE DIIQLDGTGD VFPKEETPHT KDREENEFIG
     IIESEDLKVL EDEDEEDDDE DHDSISDMES SSSSEDNEEP QIDIVEEDPL NSGDDVSEQD
     TADLFDTDNV IVCQYDKIHR SKNKWKFYLK DGVMSFEGKD YVFAKAIGDA EW
//
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