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Database: UniProt
Entry: U1I0Q1_ENDPU
LinkDB: U1I0Q1_ENDPU
Original site: U1I0Q1_ENDPU 
ID   U1I0Q1_ENDPU            Unreviewed;       829 AA.
AC   U1I0Q1;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   RecName: Full=BZIP domain-containing protein {ECO:0000259|PROSITE:PS50217};
GN   ORFNames=EPUS_06986 {ECO:0000313|EMBL:ERF75454.1};
OS   Endocarpon pusillum (strain Z07020 / HMAS-L-300199) (Lichen-forming
OS   fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Verrucariales; Verrucariaceae; Endocarpon.
OX   NCBI_TaxID=1263415 {ECO:0000313|EMBL:ERF75454.1, ECO:0000313|Proteomes:UP000019373};
RN   [1] {ECO:0000313|Proteomes:UP000019373}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Z07020 / HMAS-L-300199 {ECO:0000313|Proteomes:UP000019373};
RX   PubMed=24438332; DOI=10.1186/1471-2164-15-34;
RA   Wang Y.-Y., Liu B., Zhang X.-Y., Zhou Q.-M., Zhang T., Li H., Yu Y.-F.,
RA   Zhang X.-L., Hao X.-Y., Wang M., Wang L., Wei J.-C.;
RT   "Genome characteristics reveal the impact of lichenization on lichen-
RT   forming fungus Endocarpon pusillum Hedwig (Verrucariales, Ascomycota).";
RL   BMC Genomics 15:34-34(2014).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU361277};
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000256|RuleBase:RU361277}.
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DR   EMBL; KE720812; ERF75454.1; -; Genomic_DNA.
DR   RefSeq; XP_007787185.1; XM_007788995.1.
DR   AlphaFoldDB; U1I0Q1; -.
DR   GeneID; 19241874; -.
DR   eggNOG; KOG0023; Eukaryota.
DR   HOGENOM; CLU_341956_0_0_1; -.
DR   OrthoDB; 820313at2759; -.
DR   Proteomes; UP000019373; Unassembled WGS sequence.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd12193; bZIP_GCN4; 1.
DR   CDD; cd05283; CAD1; 1.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR   Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR013149; ADH-like_C.
DR   InterPro; IPR013154; ADH-like_N.
DR   InterPro; IPR002328; ADH_Zn_CS.
DR   InterPro; IPR004827; bZIP.
DR   InterPro; IPR046347; bZIP_sf.
DR   InterPro; IPR047109; CAD-like.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR42683; ALDEHYDE REDUCTASE; 1.
DR   PANTHER; PTHR42683:SF18; NADP-DEPENDENT ALCOHOL DEHYDROGENASE (AFU_ORTHOLOGUE AFUA_6G00510); 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   Pfam; PF07716; bZIP_2; 1.
DR   SUPFAM; SSF50129; GroES-like; 1.
DR   SUPFAM; SSF57959; Leucine zipper domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00059; ADH_ZINC; 1.
DR   PROSITE; PS50217; BZIP; 1.
DR   PROSITE; PS00036; BZIP_BASIC; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|RuleBase:RU361277};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019373};
KW   Zinc {ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          774..823
FT                   /note="BZIP"
FT                   /evidence="ECO:0000259|PROSITE:PS50217"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          445..474
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          514..590
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          720..806
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        448..474
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        535..576
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        720..759
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        769..806
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   829 AA;  88689 MW;  45CB5DF93041525B CRC64;
     MPSFTVFKGQ QSGVPKKSTT TKPDQLTGDN VFIRVTASGV CGTDLHYKGA DMVLGHEGIG
     IVETVGPACH FLKRGDRVGW GYEVDSCGHC IECLEGAETF CPDRAIYGVS NLDQGSFATH
     AIWRESFLYP IPQGLSDIDA APLQCGGATT FAALQGIKPS DTVGIMGVGG LGHLAIQFAA
     KMGCRVVVLS GSDRKKAEAL QLGAHEFIAT KDAKKLEVSA PINRLLVTAA VPPNWELILP
     IMAPRSAIYP LSVSSGNLEI PYMGLILQGI SVQGSLVAPR NQHRKMLEFA ALHQVKPVVE
     TFPMTEEGIK QSMDRLERGE VNYRAVLIPK STPPGYGGLL VSFPPPPSIS SSPGKIEPTA
     LSKFQNSTQT NTTSQSLFGE IVNFSPVSKR RSSSASPATI SLFDFTSFIT DYQASWHHQS
     PPQLASATPL SQNSFQQDFE LFGPAPATQL TPQHSRAQAT SSTAPNPQTA FPNHRHLSLN
     SQYQSAGPIS TSFINRSNSN SSAQKPHLYA SNAASTPTLH QQKRTRPPVP PFHSHSTGSL
     HSQTNQIGSQ RRIQATSIPP QGESFLTHSI SDPPLNGPSP DMNLFDDISL PAPGDSLDSS
     NTMFSDSNID FASSWTAINA SGTAQATTNT GTVSPKDIMS ESIAMSAPSS TAFPNLSTPG
     SGYLESPYLG NSSLDTSPMN ADGALDAELD FSSGYTSLFP DANDHLNKLN LQANTSFTSA
     SSGYNASSPM VRQKSSPGRP PSSTHGRQHS VTSGVRPSKQ NKPLPDIVLD PNRDSKEDLK
     RKKNTAAARK SRQRKLESAE ALQTENERLH EEVARLKQIV YSLGGSPDL
//
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