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Database: UniProt
Entry: G9N9U9_HYPVG
LinkDB: G9N9U9_HYPVG
Original site: G9N9U9_HYPVG 
ID   G9N9U9_HYPVG            Unreviewed;       935 AA.
AC   G9N9U9;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   RecName: Full=RING-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=TRIVIDRAFT_195607 {ECO:0000313|EMBL:EHK16717.1};
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:EHK16717.1, ECO:0000313|Proteomes:UP000007115};
RN   [1] {ECO:0000313|EMBL:EHK16717.1, 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   -!- SIMILARITY: Belongs to the SH3RF family.
CC       {ECO:0000256|ARBA:ARBA00008649}.
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:EHK16717.1}.
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DR   EMBL; ABDF02000090; EHK16717.1; -; Genomic_DNA.
DR   RefSeq; XP_013950915.1; XM_014095440.1.
DR   AlphaFoldDB; G9N9U9; -.
DR   STRING; 413071.G9N9U9; -.
DR   EnsemblFungi; EHK16717; EHK16717; TRIVIDRAFT_195607.
DR   GeneID; 25789902; -.
DR   VEuPathDB; FungiDB:TRIVIDRAFT_195607; -.
DR   eggNOG; KOG0802; Eukaryota.
DR   HOGENOM; CLU_005224_1_0_1; -.
DR   InParanoid; G9N9U9; -.
DR   OMA; NNCVNQG; -.
DR   OrthoDB; 1462937at2759; -.
DR   Proteomes; UP000007115; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.60.90; -; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR018957; Znf_C3HC4_RING-type.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   InterPro; IPR043145; Znf_ZZ_sf.
DR   PANTHER; PTHR16079:SF4; E3 UBIQUITIN-PROTEIN LIGASE CHFR; 1.
DR   PANTHER; PTHR16079; UBIQUITIN LIGASE PROTEIN CHFR; 1.
DR   Pfam; PF00097; zf-C3HC4; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF57850; RING/U-box; 2.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   PROSITE; PS50002; SH3; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007115};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}; Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Ubl conjugation {ECO:0000256|ARBA:ARBA00022843};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          48..102
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          873..934
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   REGION          1..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          126..167
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          184..276
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          319..476
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          507..547
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        22..38
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        128..167
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        195..226
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        228..243
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        244..261
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        319..338
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        352..374
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        404..424
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        448..476
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        526..547
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   935 AA;  104449 MW;  8B96FEFB9038AE2A CRC64;
     MNRNSPRTNH LRPYALSKQS GHLPIRQKNQ NMNGVSQTEL RPGQGVDICT ELLYQPLTLL
     DCLHTYCGAC LKEWFRFQAE KVGRAPTPPP PDAIIFTCPS CRSAVRDTRH NATVATLLDM
     YTAANPAKER SEADKQEMEE KYKPGDQVLP KVKTRERTAE EKRAEEEDRR LIDEVREMSL
     REAVAAAIPE TPQARSARRH AEGRSSDGRA RSGSDYRSDG RSQRARDGRG GNGQSNTEHL
     SVEGDSQSRS RRSESRQRQV EHQSSLRSLI GSEMSERDIE REIEEFARQI QEEGLLDGLD
     LDNIDLSRDD ELSQRITEAY RRRQRGRSRQ ESERRADART NNNATSTSRD SRLRPDNARP
     QSRHRAHSRS TSEVGDRNRP PISASANLGV REPERRARRR TTSGGHHSTP PIVSSLSAMD
     TRPAAHSQND LALRRDPNDF DPTASVPALR ISRNSSSVTI PAAAQSSDTP ASGNGKIASF
     ASRAQSYPSA SSTPHSITPE LMEITAARNS KSNRPTEVVV SPPDSLVASP VQSPTATTSR
     HQHTRSQLFE EPSISCSRCR KPDIQYDLHY NCKTCNDGHW NMCLDCYRSG KGCLYWFGFG
     YGAWKKWEKR KQADESIPMP HMLNAGRYLR PASTTVSSDG KKKFTADDPK SRLETGTFCS
     RCFAWTNDCF WRCDACNEGD WGFCNNCVNQ GKSCSHRLLP LAHEGTFKST YEPRSPRSGG
     RPSTATAITG AQVSGIGPFK PLTFNPKCNI CKDVIPPSQT RYHCFSCTNT ALQDATPGDY
     DICTSCYSNL ESKGDVSEEN GSSGWRRCPS GHRMVVIGFM EGKLGQWRYV ERDKVGGRAL
     RAEPLENIAH PDFQKWSCLG EISYTRSFPP DGGSGLVAHA MWSWYPKSGA EDELMFPRGA
     DIQEIRDING DWFFGTYMGA KGLFPAPYVK MPQQS
//
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