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
//