ID G9NRI7_HYPAI Unreviewed; 608 AA.
AC G9NRI7;
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_299189 {ECO:0000313|EMBL:EHK46620.1};
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:EHK46620.1, ECO:0000313|Proteomes:UP000005426};
RN [1] {ECO:0000313|EMBL:EHK46620.1, 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:EHK46620.1}.
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DR EMBL; ABDG02000022; EHK46620.1; -; Genomic_DNA.
DR RefSeq; XP_013944816.1; XM_014089341.1.
DR AlphaFoldDB; G9NRI7; -.
DR STRING; 452589.G9NRI7; -.
DR GeneID; 25781305; -.
DR eggNOG; ENOG502QQWK; Eukaryota.
DR HOGENOM; CLU_018354_4_2_1; -.
DR OMA; GLFNCWK; -.
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:SF171; FAD-BINDING PCMH-TYPE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR13878; GULONOLACTONE OXIDASE; 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..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..608
FT /note="FAD-binding PCMH-type domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003524514"
FT DOMAIN 119..303
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 608 AA; 65463 MW; F85AE5D9E2705D93 CRC64;
MHIKESTGLF ALANLAAPAV GLSFTCQPGQ SCWPSLQQWD AFNKTVSGRL KAPVMLGSPC
FPSSKDYNKD VCAEVLGQYG NGTFRETTFG STQFTQWESC GAENCYPGLV QPQASTCSLG
RISPLYVDAL EPSDISATIA FAKQHNIRIV LKNTGHDYLG RSAAANTLGL RTHSMKNMTF
ASSFSAKNCS AASNKKNIGI IGAGVTAEDA IAFFNNHGMM ITMGACHTVG IAGGYGQSAG
HGPLGPSKGL MVDQAVEFDV ITADGVFRTI NECNDPDLFW AMRGGGGQSY AVLVNYKFQV
YPQTKWATWL FNATITPPSS NVTENTVLRD VLTGMSTDQE SWSKAGVAGY NNILPESLTF
LEILPADGDP LTTLKNLTAK FNTLLTTHPG INVISSTYQQ FDSETDFFIG QNTFYTPNTA
VGLSSSVPSR LITVDNFESS EKIDTLVTSI LNGLEAARVQ LGEALASGAN VFLLKTAPFN
TPDAANATST HPAWRKTLWH LVYGVSYEPG TPDSTANLMM SGARAAIDKI QAPLSVQAAY
MNEADPAEPD WQNLFFGENY GTLLAIKKKW DPDTVLNCYK CVGYLGDQDP MYSCYGSNPK
ASVEYPFN
//
