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Database: UniProt
Entry: G9NES1_HYPAI
LinkDB: G9NES1_HYPAI
Original site: G9NES1_HYPAI 
ID   G9NES1_HYPAI            Unreviewed;       604 AA.
AC   G9NES1;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=FAD-binding PCMH-type domain-containing protein {ECO:0000259|PROSITE:PS51387};
GN   ORFNames=TRIATDRAFT_83859 {ECO:0000313|EMBL:EHK50802.1};
OS   Hypocrea atroviridis (strain ATCC 20476 / IMI 206040) (Trichoderma
OS   atroviride).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=452589 {ECO:0000313|EMBL:EHK50802.1, ECO:0000313|Proteomes:UP000005426};
RN   [1] {ECO:0000313|EMBL:EHK50802.1, ECO:0000313|Proteomes:UP000005426}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 20476 / IMI 206040 {ECO:0000313|Proteomes:UP000005426};
RX   PubMed=21501500; DOI=10.1186/gb-2011-12-4-r40;
RA   Kubicek C.P., Herrera-Estrella A., Seidl-Seiboth V., Martinez D.A.,
RA   Druzhinina I.S., Thon M., Zeilinger S., Casas-Flores S., Horwitz B.A.,
RA   Mukherjee P.K., Mukherjee M., Kredics L., Alcaraz L.D., Aerts A., Antal Z.,
RA   Atanasova L., Cervantes-Badillo M.G., Challacombe J., Chertkov O.,
RA   McCluskey K., Coulpier F., Deshpande N., von Doehren H., Ebbole D.J.,
RA   Esquivel-Naranjo E.U., Fekete E., Flipphi M., Glaser F.,
RA   Gomez-Rodriguez E.Y., Gruber S., Han C., Henrissat B., Hermosa R.,
RA   Hernandez-Onate M., Karaffa L., Kosti I., Le Crom S., Lindquist E.,
RA   Lucas S., Luebeck M., Luebeck P.S., Margeot A., Metz B., Misra M.,
RA   Nevalainen H., Omann M., Packer N., Perrone G., Uresti-Rivera E.E.,
RA   Salamov A., Schmoll M., Seiboth B., Shapiro H., Sukno S.,
RA   Tamayo-Ramos J.A., Tisch D., Wiest A., Wilkinson H.H., Zhang M.,
RA   Coutinho P.M., Kenerley C.M., Monte E., Baker S.E., Grigoriev I.V.;
RT   "Comparative genome sequence analysis underscores mycoparasitism as the
RT   ancestral life style of Trichoderma.";
RL   Genome Biol. 12:R40.1-R40.15(2011).
CC   -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC       family. {ECO:0000256|ARBA:ARBA00005466}.
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:EHK50802.1}.
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DR   EMBL; ABDG02000012; EHK50802.1; -; Genomic_DNA.
DR   RefSeq; XP_013948961.1; XM_014093486.1.
DR   AlphaFoldDB; G9NES1; -.
DR   STRING; 452589.G9NES1; -.
DR   GeneID; 25785763; -.
DR   eggNOG; KOG0157; Eukaryota.
DR   HOGENOM; CLU_018354_4_4_1; -.
DR   OMA; RCVGNEG; -.
DR   OrthoDB; 1641938at2759; -.
DR   Proteomes; UP000005426; Unassembled WGS sequence.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.465.10; -; 2.
DR   InterPro; IPR012951; BBE.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   PANTHER; PTHR13878; GULONOLACTONE OXIDASE; 1.
DR   PANTHER; PTHR13878:SF91; L-GULONOLACTONE OXIDASE 3; 1.
DR   Pfam; PF08031; BBE; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005426};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..604
FT                   /note="FAD-binding PCMH-type domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003524214"
FT   DOMAIN          107..294
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   604 AA;  65062 MW;  F772D5C96C676987 CRC64;
     MHLTKFMLLL GVPSALAKCK CTPTDDCWPS TFEWKSLNST VQGQLIANEP LAKPCYAGFS
     NNFTQCQEIS KLYQDASFRE ASPIGYMYPV LDTCVPINGS ITGNPVCDLG SASVYSINAS
     GAADVAAGVK FARDNNVRLV VKNTGHDIRA RQGYGSLSIW MKHIKPELQF QETYSPSDSS
     CQSTWNGSAI VVGAGYIWDE VYAFAAEHGH IAVGGADRTV GAVGGYLQGG GHGFASHDFG
     LAADQVLEYQ VVLATGDVVT ASACQNVDLF SALRGGGGGT FGIVLAATLK VYPTQPVLKH
     SLSVTALSTD ISALLNVSVT ILSKYPTLLD AGFSGYGQLE RILGQNPAYS HSFGKLLAID
     GSSSNSSSEI ERAESLVNEE ILDFLSSLNG TGFSVTSTFQ KYDTFQDYFN SGSHDSNASN
     NPSPAMVSRF FDNDSLSNNQ QNLSSMLEAI FPQSASQVQA IASLLEFCLV GGGEVLSPQP
     HTAIHPGWRK TYMLAENFDV PPTDSGLQGV RQVKEYATST KLKAMKDATP VLGTYLNEAD
     PNDPDWKEAF YGNQYSWLNS VKQTYDPDGV FWCYRCVGYE GWEEITGPML YGPLCQTNEV
     GDYS
//
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