GenomeNet

Database: UniProt
Entry: A0A2B7WSG3_9EURO
LinkDB: A0A2B7WSG3_9EURO
Original site: A0A2B7WSG3_9EURO 
ID   A0A2B7WSG3_9EURO        Unreviewed;       815 AA.
AC   A0A2B7WSG3;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   08-NOV-2023, entry version 21.
DE   RecName: Full=BZIP domain-containing protein {ECO:0000259|PROSITE:PS50217};
GN   ORFNames=GX51_06276 {ECO:0000313|EMBL:PGG99536.1};
OS   Blastomyces parvus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX   NCBI_TaxID=2060905 {ECO:0000313|EMBL:PGG99536.1, ECO:0000313|Proteomes:UP000224080};
RN   [1] {ECO:0000313|EMBL:PGG99536.1, ECO:0000313|Proteomes:UP000224080}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH130 {ECO:0000313|EMBL:PGG99536.1,
RC   ECO:0000313|Proteomes:UP000224080};
RA   Munoz J.F., Mcewen J.G., Clay O.K., Cuomo C.A.;
RT   "Comparative genomics in systemic dimorphic fungi from Ajellomycetaceae.";
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uS7 family.
CC       {ECO:0000256|ARBA:ARBA00007151}.
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:PGG99536.1}.
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   EMBL; PDNC01000100; PGG99536.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2B7WSG3; -.
DR   STRING; 2060905.A0A2B7WSG3; -.
DR   OrthoDB; 2722165at2759; -.
DR   Proteomes; UP000224080; Unassembled WGS sequence.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
DR   CDD; cd12193; bZIP_GCN4; 1.
DR   CDD; cd14868; uS7_Mitochondria_Fungi; 1.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR   Gene3D; 1.10.455.10; Ribosomal protein S7 domain; 1.
DR   InterPro; IPR004827; bZIP.
DR   InterPro; IPR046347; bZIP_sf.
DR   InterPro; IPR000235; Ribosomal_uS7.
DR   InterPro; IPR023798; Ribosomal_uS7_dom.
DR   InterPro; IPR036823; Ribosomal_uS7_dom_sf.
DR   InterPro; IPR047988; Ribosomal_uS7m_fungi.
DR   PANTHER; PTHR11205:SF19; 28S RIBOSOMAL PROTEIN S7, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11205; RIBOSOMAL PROTEIN S7; 1.
DR   Pfam; PF00177; Ribosomal_S7; 1.
DR   SMART; SM00338; BRLZ; 1.
DR   SUPFAM; SSF57959; Leucine zipper domain; 1.
DR   SUPFAM; SSF47973; Ribosomal protein S7; 1.
DR   PROSITE; PS50217; BZIP; 1.
DR   PROSITE; PS00036; BZIP_BASIC; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000224080};
KW   Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274};
KW   Ribosomal protein {ECO:0000256|ARBA:ARBA00022980}.
FT   DOMAIN          751..814
FT                   /note="BZIP"
FT                   /evidence="ECO:0000259|PROSITE:PS50217"
FT   REGION          10..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          61..109
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          157..182
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          388..451
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          687..754
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          769..803
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        66..80
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        81..99
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        391..407
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        416..451
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        689..704
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        718..744
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   815 AA;  88425 MW;  89D528AB5CF3E1DD CRC64;
     MPPRLNLLPT SLLRQSPGPQ QCTAARFASP LSSGRDNAIR TLSTRRDLLL RRPGAVVLAY
     RPRVSSSQHR MGSSSSKSGD GLSEGKEERV ADEKGAESTA AKEGLGSVSE EAADMARIME
     RRTECGEVGG PELLQGSMVG DILKRDKDAL KNAPKVLRDQ LSSSSSSSSS SGSRSFSTSA
     RSRQFDMKQM SAGENDASVA TVEDMLATAT KQKQEQLMQA GLKYEVPETL PRSEHLRHRY
     DPLLDQFTKM LMRHGKLSVA QKQMEKILHN LRSAPAPNPD PSRPLLPGPP APQLPLNPIL
     YLTQVVDSVA PILRIKQQPG AAGGGRSLPI PLPLALRQRR RTAIKWIIDA SEKRKDAALA
     NRVSQEIIAV AEGKSSAWEK RAMVHKQGTA ARANIKSQAV ASSSSDRHDP SLHLERRNTG
     NSQHNNISTA PSGFRVRNGD ESRSLQTQYQ SLPSSTAASS VYTAAPAASN LSSSSSASSS
     SSSSFSSSSL ESIHSSASLQ QPPSLASPNY QQNNDISTQL REDDTPFVNC HLSSDSLAFP
     LYSGELGSHA QNINAATTAP TSPWLDLLEF DHNRSQDGQS LSSSLLLPAG TGLQTEAAST
     LLNPRSDAPV SAAIPEYDLP YPYSKGYELD FDESFLLTAQ DSFATSTQPD TQYSLPDFNH
     QPSNVQQYFM SDLQNIHNQD ITHLQCGVAI PPPSQSQLPT HQIQPKPYSP QPPILVTGTS
     PAPSIANTQH STPSSTQTPR SPTAVAKATP ADRVADKRRR NTLAARRFRQ KQHDRVAELE
     RALESVCRER DELKMQAARW EGEVVALRGM LQKKS
//
DBGET integrated database retrieval system