ID G9P2X6_HYPAI Unreviewed; 812 AA.
AC G9P2X6;
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=Fe2OG dioxygenase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=TRIATDRAFT_266994 {ECO:0000313|EMBL:EHK43589.1};
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:EHK43589.1, ECO:0000313|Proteomes:UP000005426};
RN [1] {ECO:0000313|EMBL:EHK43589.1, 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 isochorismatase family.
CC {ECO:0000256|ARBA:ARBA00006336}.
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:EHK43589.1}.
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DR EMBL; ABDG02000026; EHK43589.1; -; Genomic_DNA.
DR RefSeq; XP_013941757.1; XM_014086282.1.
DR AlphaFoldDB; G9P2X6; -.
DR STRING; 452589.G9P2X6; -.
DR GeneID; 25779205; -.
DR eggNOG; ENOG502QRZN; Eukaryota.
DR HOGENOM; CLU_005335_0_0_1; -.
DR OMA; KMYHLSG; -.
DR OrthoDB; 1644896at2759; -.
DR Proteomes; UP000005426; Unassembled WGS sequence.
DR GO; GO:0051213; F:dioxygenase activity; IEA:InterPro.
DR GO; GO:0006307; P:DNA dealkylation involved in DNA repair; IEA:InterPro.
DR GO; GO:0035552; P:oxidative single-stranded DNA demethylation; IEA:InterPro.
DR CDD; cd00431; cysteine_hydrolases; 1.
DR Gene3D; 1.20.1050.10; -; 1.
DR Gene3D; 2.60.120.590; Alpha-ketoglutarate-dependent dioxygenase AlkB-like; 1.
DR Gene3D; 3.40.50.850; Isochorismatase-like; 1.
DR InterPro; IPR027450; AlkB-like.
DR InterPro; IPR037151; AlkB-like_sf.
DR InterPro; IPR032854; ALKBH3.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR000868; Isochorismatase-like.
DR InterPro; IPR036380; Isochorismatase-like_sf.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR PANTHER; PTHR31212; ALPHA-KETOGLUTARATE-DEPENDENT DIOXYGENASE ALKB HOMOLOG 3; 1.
DR PANTHER; PTHR31212:SF5; ISOCHORISMATASE FAMILY PROTEIN FAMILY (AFU_ORTHOLOGUE AFUA_3G14500); 1.
DR Pfam; PF13532; 2OG-FeII_Oxy_2; 1.
DR Pfam; PF00857; Isochorismatase; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR SUPFAM; SSF52499; Isochorismatase-like hydrolases; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
DR PROSITE; PS50405; GST_CTER; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000005426}.
FT DOMAIN 406..532
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT DOMAIN 674..812
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
FT REGION 78..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 211..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..98
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..234
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..260
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..291
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..317
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 812 AA; 89212 MW; EBC5062CBF62A869 CRC64;
MFAFDQAALP QITTRKALIV VDFQNEFIGD ADPGLPVNRP EGFVKRTAEI ATAFRSAGDV
IWIQSRLDKA RSIDGDQIIL SENSPASQPT SSRNKDRPIA TEASSDESLD PEAFLSHEEP
LHGKASSDPG SNVPLAIEEA IHSKDLKLTK SYYSAFHGTQ LLRALRGRMV TEVFICGSLA
NIGVYATAME AAGHGMAITV IEDCCGYRHN KSETKTPSEP RDATSAKRAK AVASTDEDII
QSLSGLKLDS SPSGPSTAVD KVNQAPEVKA ETQEPQEAAT EVEKENEKDQ PVVEGGSAGR
VADSENESDS SSQSKLCEGD TDVICDALPK PLANEAFDKL EKEVLWQRMS HQGGEVPRLV
AVQGRVDEDG TMPVYRHPAD ESPPLLPFSP TVQAIKAEIE KHLGHPLNHV LIQFYRDGND
YISEHSDKTL DIVKGSYIAN VSLGAERTMI LRTKRLEKDL SGTAAAEAAG KEEKRKIQRA
RLPHNSLCRM GLQTNMKWLH AIRRDKRADR DKSAAELAYS GRRISLTFRH IGTFLDRDET
IIWGQGATGK TRDTAHPISN GQSSEAVKMI QAFGTENHAS DFDWSAHYGR GFDVLHISNS
PRFFASADPL VNMRITLMLA EYGIKYAKGS MASGSESHNE NQNNPPALWS LPIKFIDNDA
AKSVVHGDMA IMLYLYSRYG PGRVTGSGAT TRNPSDLARL FSQFQQGMNL FNIWRQLRCD
GSTGTRAGAL PVTLKQELAV WDSYVVDDLK NERVPFLCED SLTLPDFVVW PTLYSIVEKY
GSEVAFKGLD GLQKYYEAVR QLDNVVTAVG NR
//