ID F0XQQ3_GROCL Unreviewed; 897 AA.
AC F0XQQ3;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=CMQ_315 {ECO:0000313|EMBL:EFW99997.1};
OS Grosmannia clavigera (strain kw1407 / UAMH 11150) (Blue stain fungus)
OS (Graphiocladiella clavigera).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Leptographium.
OX NCBI_TaxID=655863 {ECO:0000313|Proteomes:UP000007796};
RN [1] {ECO:0000313|EMBL:EFW99997.1, ECO:0000313|Proteomes:UP000007796}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=kw1407 / UAMH 11150 {ECO:0000313|Proteomes:UP000007796};
RX PubMed=21262841; DOI=10.1073/pnas.1011289108;
RA DiGuistini S., Wang Y., Liao N.Y., Taylor G., Tanguay P., Feau N.,
RA Henrissat B., Chan S.K., Hesse-Orce U., Alamouti S.M., Tsui C.K.M.,
RA Docking R.T., Levasseur A., Haridas S., Robertson G., Birol I., Holt R.A.,
RA Marra M.A., Hamelin R.C., Hirst M., Jones S.J.M., Bohlmann J., Breuil C.;
RT "Genome and transcriptome analyses of the mountain pine beetle-fungal
RT symbiont Grosmannia clavigera, a lodgepole pine pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:2504-2509(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SIMILARITY: Belongs to the ZNF598/HEL2 family.
CC {ECO:0000256|ARBA:ARBA00035113}.
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; GL629807; EFW99997.1; -; Genomic_DNA.
DR RefSeq; XP_014169412.1; XM_014313937.1.
DR AlphaFoldDB; F0XQQ3; -.
DR STRING; 655863.F0XQQ3; -.
DR GeneID; 25976218; -.
DR eggNOG; KOG2231; Eukaryota.
DR HOGENOM; CLU_008515_1_0_1; -.
DR InParanoid; F0XQQ3; -.
DR OrthoDB; 3059402at2759; -.
DR Proteomes; UP000007796; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0072344; P:rescue of stalled ribosome; IEA:InterPro.
DR CDD; cd16615; RING-HC_ZNF598; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR041888; RING-HC_ZNF598/Hel2.
DR InterPro; IPR044288; ZNF598/Hel2.
DR InterPro; IPR013087; Znf_C2H2_type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR22938:SF0; E3 UBIQUITIN-PROTEIN LIGASE ZNF598; 1.
DR PANTHER; PTHR22938; ZINC FINGER PROTEIN 598; 1.
DR Pfam; PF13920; zf-C3HC4_3; 1.
DR SMART; SM00355; ZnF_C2H2; 4.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000007796};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 135..175
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 407..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 703..826
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 844..897
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..435
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..481
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 724..749
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 759..809
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 897 AA; 95542 MW; 3324B4DDF1DAA2D8 CRC64;
MQSGMVQSQT SVAAQPRAEN CRAVGAVWNC QQRSPGNKAE GRCRMTHMGN STTFDRPKCV
PQTYSVLRLR STNVQIAGRL RENDKLVANE SKETRRICAT SDGFDRRGKR SGRRGKDARL
LAPETETDGE EAEVCFICAN PVIHQSIAPC NHVTCHICAL RMRALYRNKD CPHCRTAAPY
VIFTDDVTKR YEEYGAGDIT TTDETSGIRY SNEDIVGDTV LLLRYNCPDE ACDYAGFGWP
DLHRHVREVH HKKMCDLCTR NKKVFTHEHE LFTDKGLDRH MRNGDDRPGA VDQTGFKGHP
LCGFCGERFY DDDKLYEHCR NKHERCFICD RRDARQPHYY RNYDALEEHF RRDHYLCIDR
ECMDKKFVVF ESEMDLKAHQ LEEHGNTLSK DVRRDVQVVS LSDFDYRPAY QNNGGRGGER
GGGGRNHDGR SGRGRDPNAE LPLAVGPPQS MRRDEIAYQR QRQLEVQSAQ TVTTRTFGSR
LTPSGGGGGG GGGGSGGGSS SSRPSRPKAS TPDPLADPLQ GLSPAEVASL TPQERARRVR
HGAVLERAAN LLANDAGKVQ SFRAELAAFR SGAATAAQLV DGLAGLLADT TSPTALGSLV
REVADLYEEP GRADALRQAW QNRRAVTAAT GASSSSVQPV DDYPSLPGLG GMHGATTSTS
GWAGAAAVSP SIRIPASSGG GQHSTRVLRL KHSTRPGAAA VAAAAATAPS TGPAGRIVPG
ATWTVPSSGR QASAGTTSNS SSRPSASPAP ASSAAFPALP STKKANSTPT LSWLGASGSS
STAAPAASSS TAARIGGSSS SSSSSRPHQR PPGEDAFPAL PAAPKPLTTI FGYGRGAVRR
DVGGRDTGFS WGDGETAGGA GGGDVAAEAD DDVGGGSGNG KGKKKGRQGK KVLVSWG
//
