ID A0A0F9XHK3_TRIHA Unreviewed; 722 AA.
AC A0A0F9XHK3;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=E3 ubiquitin protein ligase {ECO:0000256|RuleBase:RU365038};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU365038};
GN ORFNames=THAR02_03386 {ECO:0000313|EMBL:KKP04501.1};
OS Trichoderma harzianum (Hypocrea lixii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=5544 {ECO:0000313|EMBL:KKP04501.1, ECO:0000313|Proteomes:UP000034112};
RN [1] {ECO:0000313|Proteomes:UP000034112}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T6776 {ECO:0000313|Proteomes:UP000034112};
RX PubMed=26067977; DOI=10.1128/genomeA.00647-15;
RA Baroncelli R., Piaggeschi G., Fiorini L., Bertolini E., Zapparata A.,
RA Pe M.E., Sarrocco S., Vannacci G.;
RT "Draft whole-genome sequence of the biocontrol agent Trichoderma harzianum
RT T6776.";
RL Genome Announc. 3:E0064715-E0064715(2015).
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|RuleBase:RU365038};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|RuleBase:RU365038}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|RuleBase:RU365038}.
CC -!- SIMILARITY: Belongs to the BRE1 family. {ECO:0000256|ARBA:ARBA00005555,
CC ECO:0000256|RuleBase:RU365038}.
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:KKP04501.1}.
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DR EMBL; JOKZ01000075; KKP04501.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F9XHK3; -.
DR OMA; YRQMQEY; -.
DR OrthoDB; 53681at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000034112; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniRule.
DR CDD; cd16499; RING-HC_Bre1-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR013956; E3_ubiquit_lig_Bre1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR23163:SF0; E3 UBIQUITIN-PROTEIN LIGASE BRE1; 1.
DR PANTHER; PTHR23163; RING FINGER PROTEIN-RELATED; 1.
DR Pfam; PF08647; BRE1; 1.
DR Pfam; PF13920; zf-C3HC4_3; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853,
KW ECO:0000256|RuleBase:RU365038};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|RuleBase:RU365038};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU365038}; Nucleus {ECO:0000256|RuleBase:RU365038};
KW Reference proteome {ECO:0000313|Proteomes:UP000034112};
KW Transferase {ECO:0000256|RuleBase:RU365038};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU365038};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU365038};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 670..709
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 241..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 191..225
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 266..370
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 414..477
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 625..652
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 241..264
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 722 AA; 82181 MW; 04175C9C44C6D4A4 CRC64;
MPVATTPSAS PRPSTLVKME DRKRPAISGA EDLAPPSKRV AINGSKAKDE NTDMKEDTWI
EAYTKGAIYR QMQEYSRKAS TAESRLEELH KRSVHHDDHL RIIDAWWRQC LEELELLVTS
KVPTAEPRDT PYLTAVSFKN LHDFQAHLQE RGKTIKAKAE SLLTQLAAQR ENISPKTTEL
ESQIASLLAA QKEYLLKLDR LSAEKEQMSE QLNAATLRYF KAEKKLDRAK SAQVQRLEQQ
AFANATRPAT TPTEGGSEPS EPNGSANELL VKYEEATAAA TKQKEQLESL LAELKTLQEE
NTSLKSRRET LSDEDYIRTD VFKQFKSQNE DLIKRINTLE ATNKQLREEA EKLQAERTAF
RTQLEADMNQ VAQDYEADIA ARDQDLTRVR SARDEILAEN MQRRANAEQE RIAMEHIKEL
VTAKEDRISA LELELARLKP EGDEETGDAV DVDGISEEDL RQRYKKLSRD FDSINQELPA
MEKAYKKMKD LAQKKVLDFT ALEEKVAILI AEKSKADQKY FAARKDADTR NSEIRTLRHQ
SGKSAELIAQ LKDFESQTRT LLSNLEKQSA DLRQANAALV AESKKMESNS LEAVRKSESV
TKQVGDLTNL VKSKDASTAV IRERNAMQEV EVEKLKVRIE HMQKDRDSWK NKALSNSSEE
EDMLRTMALC TVCRTNFKNT ALKTCGHLFC NKCVDDRISN RMRKCPSCSR AFDKMDVMQV
HF
//
