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}.
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; 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
//