ID G9N3L2_HYPVG Unreviewed; 973 AA.
AC G9N3L2;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Thioredoxin domain-containing protein {ECO:0000259|PROSITE:PS51352};
GN ORFNames=TRIVIDRAFT_213844 {ECO:0000313|EMBL:EHK18896.1};
OS Hypocrea virens (strain Gv29-8 / FGSC 10586) (Gliocladium virens)
OS (Trichoderma virens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=413071 {ECO:0000313|EMBL:EHK18896.1, ECO:0000313|Proteomes:UP000007115};
RN [1] {ECO:0000313|EMBL:EHK18896.1, ECO:0000313|Proteomes:UP000007115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Gv29-8 / FGSC 10586 {ECO:0000313|Proteomes:UP000007115};
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 -!- 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:EHK18896.1}.
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; ABDF02000085; EHK18896.1; -; Genomic_DNA.
DR RefSeq; XP_013953093.1; XM_014097618.1.
DR AlphaFoldDB; G9N3L2; -.
DR STRING; 413071.G9N3L2; -.
DR EnsemblFungi; EHK18896; EHK18896; TRIVIDRAFT_213844.
DR GeneID; 25790769; -.
DR VEuPathDB; FungiDB:TRIVIDRAFT_213844; -.
DR eggNOG; KOG0908; Eukaryota.
DR eggNOG; KOG2539; Eukaryota.
DR HOGENOM; CLU_007075_0_1_1; -.
DR InParanoid; G9N3L2; -.
DR OMA; CTNHSTC; -.
DR OrthoDB; 146346at2759; -.
DR Proteomes; UP000007115; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR CDD; cd02947; TRX_family; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR015324; Ribosomal_Rsm22-like.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR13184; 37S RIBOSOMAL PROTEIN S22; 1.
DR PANTHER; PTHR13184:SF5; METHYLTRANSFERASE LIKE; 1.
DR Pfam; PF09243; Rsm22; 1.
DR Pfam; PF00085; Thioredoxin; 1.
DR PRINTS; PR00421; THIOREDOXIN.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Reference proteome {ECO:0000313|Proteomes:UP000007115};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 1..109
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 174..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 460..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 905..932
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 944..973
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 354..388
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 196..217
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 912..932
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 944..961
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 973 AA; 108147 MW; 6687E42F0DA4AA29 CRC64;
MSGPIHIGSD GEWQSLLSGT TVVIADFYAD WCGPCKMIAP HFERLAKEHS RPKKVAFAKV
NVDNQANIAR TNGVTAMPTF VVFHNGTTVE TIRGANPTAL TEAITKAVSL SNGGKAEDVF
KTPGRTLGGD GSVPGQGRHW SVTLLINIIM MFVGLYLASL FSIDSYKAAE QSMFNPKRQQ
PPLKPASAAG PAPAGSARAQ QQSTALQEPT GGSRSQSVED IEKVVREAKQ RFRDTLPKGY
LNEEEYALYE RLYGPPLRET APEDVGIPTH ADMGGQSTRV NDERTLLRQL EEGGFEEVTY
RIPYQESGVA EASSGSEQPL ASDSALEAIE ESPGYVDAVA RNPREHEALQ RLMQDFKAAQ
KKQLEDEIAA AREEAEAEQE AYEMDEEDDF FEESEETTAE LGRDMSLGET RRFHPFTLQG
RFHGSPVEIS LPQSGLVTPI RDLLDRTHLS HVKAAAEAAF GGQGLPTSPS TPEGRKNGQM
GGVGLPPDQR HMTEIEADAF LAGYLPPAYA SVTSVLREVR KRLGSDWIQQ RLKKKENAGL
SVLDAGAGGA GLVAWEQILN TEWDLLREKG EVTGSQPPGR KTVITGSDRL RHRLKSFLHN
TTFLPRLPDY EHSGEMQGEH LDAGNKPQPR KSYDLIIASH LFLKEKQDHY RQAILNNLWT
LLNKDGGVLI VIEKAHPRGF EAVAHVRDTL LKQFLLPQNG EPSIPTEELN PAFHKEREAG
HIIAPCTNHG TCPMYKEAGK SKGRKDYCYF NQRFTRPTFY TKMLGNSSNN QGDVEFSYVA
IQRGCSKTDQ LPGWKATELA FAGYKNSKES PDMQTLPRMV LPPLKRKGHV TLDVCTPEGK
IERWTVPKSF SKLAYHDARK SHWGDLWALG AKTKVSRSVR VGSGVDDGGK RAEGGKKPRK
VEITMDGGRL SANEKNARKE RRTKGKRERQ TDLIKEILEA EDLEEQEIER EMDTEVEEEL
KLEEEEKQRR RRR
//