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Database: UniProt
Entry: Q2GSC3_CHAGB
LinkDB: Q2GSC3_CHAGB
Original site: Q2GSC3_CHAGB 
ID   Q2GSC3_CHAGB            Unreviewed;       614 AA.
AC   Q2GSC3;
DT   21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2006, sequence version 1.
DT   24-JAN-2024, entry version 72.
DE   RecName: Full=Enoyl reductase (ER) domain-containing protein {ECO:0000259|SMART:SM00829};
GN   ORFNames=CHGG_09131 {ECO:0000313|EMBL:EAQ85117.1};
OS   Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS   NRRL 1970) (Soil fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX   NCBI_TaxID=306901 {ECO:0000313|EMBL:EAQ85117.1, ECO:0000313|Proteomes:UP000001056};
RN   [1] {ECO:0000313|Proteomes:UP000001056}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970
RC   {ECO:0000313|Proteomes:UP000001056};
RX   PubMed=25720678; DOI=10.1128/genomeA.00021-15;
RA   Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT   "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL   Genome Announc. 3:E0002115-E0002115(2015).
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000256|ARBA:ARBA00008072}.
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DR   EMBL; CH408034; EAQ85117.1; -; Genomic_DNA.
DR   RefSeq; XP_001227058.1; XM_001227057.1.
DR   AlphaFoldDB; Q2GSC3; -.
DR   GeneID; 4395094; -.
DR   VEuPathDB; FungiDB:CHGG_09131; -.
DR   eggNOG; KOG1198; Eukaryota.
DR   HOGENOM; CLU_444801_0_0_1; -.
DR   InParanoid; Q2GSC3; -.
DR   OrthoDB; 2688376at2759; -.
DR   Proteomes; UP000001056; Unassembled WGS sequence.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0016651; F:oxidoreductase activity, acting on NAD(P)H; IEA:InterPro.
DR   CDD; cd08249; enoyl_reductase_like; 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; IPR016477; Fructo-/Ketosamine-3-kinase.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020843; PKS_ER.
DR   InterPro; IPR047122; Trans-enoyl_RdTase-like.
DR   PANTHER; PTHR45348; HYPOTHETICAL OXIDOREDUCTASE (EUROFUNG); 1.
DR   PANTHER; PTHR45348:SF2; ZINC-TYPE ALCOHOL DEHYDROGENASE-LIKE PROTEIN C2E1P3.01; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   Pfam; PF03881; Fructosamin_kin; 1.
DR   SMART; SM00829; PKS_ER; 1.
DR   SUPFAM; SSF50129; GroES-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001056}.
FT   DOMAIN          15..342
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
FT   REGION          370..403
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          592..614
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        370..389
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        598..614
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   614 AA;  65794 MW;  4FF22975485B17D9 CRC64;
     MASNLNRAAW LHKAGTPLEV GEAPMPTAGP NELVIRNAAV AINPLDCHMQ SAGVFVQQWP
     SVFGCDVAGV VHEVGSDVHE RFKVGDRVIG HAINLTSGRP QDGAFALYTT IPASKAAILP
     SSIPFTSGVV VPFALEAAVC ALSVKQPGTA LPNVPTPALG LPYPSLTDPP TTITTTTTTN
     PQKTLIIYGG SSSVGSMATQ LATAAGIRVL AIASARNFSL CRACGAAAVF DYHDTSFVDD
     VVSAATAEGG EFVGIFDAVS TPETYANGLA MLQRLGSGHL ACVHPPPEVP EGVQAGMIFA
     VDEIATPVWR DYVTAALEAG RLKCLPPPLV VGKGLEFVQE ALEKCAQGGF EGELHVDSKR
     RRTSMWVLDA GSRKTPHQRR ADDSSRNNTS THRTEGPSQV TTMSMTRAKA TPLAELVLPN
     TQSQTERAAV DIIHHPHFQS SFEVGGNITK ACRYQVVFNL GAVGKHMCNG EFESLKAIHA
     VSPGFVPEPY AWGEVTDGQG DYFLLVEFCH LRCQPAVPEK LSSRLADMHM RSVSPTGKFG
     FHVPTCHAKI IQAVDAWDDS CVYQDMTTLC KMFCSKDLEQ AMVHLEERKT LEGTLTVASS
     EDEDEEEEEE EEEE
//
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