ID F0XHF4_GROCL Unreviewed; 647 AA.
AC F0XHF4;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 45.
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_2584 {ECO:0000313|EMBL:EFX02655.1};
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:EFX02655.1, 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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004170};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}.
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DR EMBL; GL629769; EFX02655.1; -; Genomic_DNA.
DR RefSeq; XP_014172137.1; XM_014316662.1.
DR AlphaFoldDB; F0XHF4; -.
DR STRING; 655863.F0XHF4; -.
DR GeneID; 25975589; -.
DR eggNOG; KOG1729; Eukaryota.
DR HOGENOM; CLU_022550_3_0_1; -.
DR InParanoid; F0XHF4; -.
DR OrthoDB; 38671at2759; -.
DR Proteomes; UP000007796; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR CDD; cd16489; mRING-CH-C4HC2H_ZNRF; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR000306; Znf_FYVE.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR46661; E3 UBIQUITIN-PROTEIN LIGASE ZNRF1-LIKE PROTEIN; 1.
DR PANTHER; PTHR46661:SF4; RING-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF01363; FYVE; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00064; FYVE; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Lysosome {ECO:0000256|ARBA:ARBA00023228};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Myristate {ECO:0000256|ARBA:ARBA00022707};
KW Reference proteome {ECO:0000313|Proteomes:UP000007796};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT DOMAIN 599..641
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 107..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 181..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 395..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 518..574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..140
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..160
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..225
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..450
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 459..476
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 527..562
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 647 AA; 69187 MW; FD8AF0C921828E11 CRC64;
MHPIVQYQQD LHACIGMASY HTDGGQSGSA VLDEEVDDDA VPDEVLAAEG HATSQAKGKG
ILLPMSEEGR ASGSQESLTI LVTDGSAANE GGSRQTSENA IVVSSTLSRP NSAASTTPSA
PTAIASSALS SHTELHTNQA SPAPPIVPDA LPPPLPTMLA AEPQPQSQLL LPSLLLPLVP
SPPPAYASRR DPERPTTSTL TETRRRLQSP SPPLPPPPPS PRPRAVSEWV PSTRQEQTSV
VLPSLRDALQ DVSLPRWQPD AEVTYCPICR TQFSIFVRKH HCSCSPHRIT IPYQYIVHPP
GWYSFRTQAA AAASVGDGGV GGFGNSPIDV STLGGGERVR LCNPCVPDPN IAPPHTAWSS
DLASLFPSTG PQTRGQYRTV RTVWGPSRGP MFATFHPLPP GAVRQPSSVG PDSLLTVSPA
SPSSQRHHRL SLPPPSSAPG TSSEPQMHFV VHQRRTQRPG LADPTTRQQI RQPQYQARAQ
PLAEEDECPV CHLELPSRQL SSFEEQREQH IMDCLEAHGG SHQGRRRTAS GDGNSPRGGG
SSGNGGSSNS SSSSSGGGSS TDGISGDGGV FRQPQPHVWR TGMFPYLATE KDCVDAAECT
ICLEEFEVGV PMARLECLCR FHRECIQAWF VKHPGRCPVH NHDSSDY
//
