ID A0A2T4CFA8_TRILO Unreviewed; 804 AA.
AC A0A2T4CFA8;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 02-APR-2025, entry version 29.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN ORFNames=M440DRAFT_1324606 {ECO:0000313|EMBL:PTB80249.1};
OS Trichoderma longibrachiatum ATCC 18648.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=983965 {ECO:0000313|EMBL:PTB80249.1, ECO:0000313|Proteomes:UP000240760};
RN [1] {ECO:0000313|EMBL:PTB80249.1, ECO:0000313|Proteomes:UP000240760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18648 {ECO:0000313|EMBL:PTB80249.1,
RC ECO:0000313|Proteomes:UP000240760};
RG DOE Joint Genome Institute;
RA Aerts A., Atanasova L., Chenthamara K., Zhang J., Grujic M., Henrissat B.,
RA Kuo A., Salamov A., Lipzen A., Labutti K., Barry K., Miao Y., Rahimi M.J.,
RA Shen Q., Grigoriev I.V., Kubicek C.P., Druzhinina I.S.;
RT "Multiple horizontal gene transfer events from other fungi enriched the
RT ability of initially mycotrophic Trichoderma (Ascomycota) to feed on dead
RT plant biomass.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.;
CC EC=2.3.2.31; Evidence={ECO:0000256|ARBA:ARBA00001798};
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DR EMBL; KZ679127; PTB80249.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T4CFA8; -.
DR STRING; 983965.A0A2T4CFA8; -.
DR OrthoDB; 1431934at2759; -.
DR Proteomes; UP000240760; Unassembled WGS sequence.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
DR CDD; cd20335; BRcat_RBR; 1.
DR CDD; cd22585; Rcat_RBR_DEAH12-like; 1.
DR Gene3D; 1.20.120.1750; -; 1.
DR Gene3D; 4.10.1000.10; Zinc finger, CCCH-type; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR031127; E3_UB_ligase_RBR.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR013087; Znf_C2H2_type.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR Pfam; PF01485; IBR; 1.
DR Pfam; PF22191; IBR_1; 1.
DR SMART; SM00647; IBR; 2.
DR SMART; SM00356; ZnF_C3H1; 1.
DR SUPFAM; SSF90229; CCCH zinc finger; 1.
DR SUPFAM; SSF57850; RING/U-box; 2.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS50103; ZF_C3H1; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00723}; Reference proteome {ECO:0000313|Proteomes:UP000240760};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00723};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00723}.
FT DOMAIN 19..46
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 589..801
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT ZN_FING 19..46
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 804 AA; 89097 MW; 5605A23807CCC5EE CRC64;
MQFGAATTNH PSTATAPPQS AKPACRFYKS GTCIKGEKCL FRHAEEDLVS RDVAPATPVA
TEAIEDDPKK DDFSRSIGGA FVQFETGAKV SKIRLPSDFS AVRINGLPQG TSEQSVRTML
AKEGLDISVD NVYMLHMDGS CGASVRSDDP SFSKRLCTLF QSGCAWEGVR VYATPIAAPM
PSGHNARRVD CKKVHVSWHK AVRNAWLNFG NGETAKRVSE LFSKGTYRIL DQKVTTGPAT
EAQPAFHSYA RPRPRNCLNW TVMLTEVPAA AETKDILQAI PLERNRPRHV EVGPPTYSTD
AEEASVMVRS LLTKVGPLEY FEVTLETNAR RVKATARFLD ESDARRAAAE LDKRELPFHR
KARLTVQMVY SAKFKVGTNI YDAVYPRILA QQKTWKDKNV FFKAYNSTDS LKRFRLLKIE
GESADDVAIA KADLESILAG VVAKGDGATL WDSSLKANGQ LFQAIKKLEE ELSVTVLRDR
GRSELRLFGS LPHCEEAERR LAELIRVESL SMSARVIELE PHKFFWACHG GYRKIAARLG
PEKASFDIIS TPKRIVISGS LEDYDVALAI MEGREQVAEP VVQHEVDEAV QECSVCWTEA
DMPVKISCGH VYCQDCFERS CTVGDGTAAD FALLCHGNQG TCKALIAVGD LQEHLSSSTL
EDVLERSFAS YIKRNPNEFR YCPTPDCGYI YRVSSEARTQ NCSNCLRPTC SACHEPHVGM
SCADHRDIKS GGYQAFTKLK KELGIKDCPR CRTPLEKISG CNHMTCIACE AHICWVCLMT
FPEGKGIYEH MRKLHGGHID LPGL
//
