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Database: UniProt
Entry: A0A2P4ZAY7_9HYPO
LinkDB: A0A2P4ZAY7_9HYPO
Original site: A0A2P4ZAY7_9HYPO 
ID   A0A2P4ZAY7_9HYPO        Unreviewed;       697 AA.
AC   A0A2P4ZAY7;
DT   23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT   23-MAY-2018, sequence version 1.
DT   02-APR-2025, entry version 19.
DE   RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE            EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN   ORFNames=TGAM01_v209618 {ECO:0000313|EMBL:PON21455.1};
OS   Trichoderma gamsii.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=398673 {ECO:0000313|EMBL:PON21455.1, ECO:0000313|Proteomes:UP000054821};
RN   [1] {ECO:0000313|EMBL:PON21455.1, ECO:0000313|Proteomes:UP000054821}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T6085 {ECO:0000313|EMBL:PON21455.1,
RC   ECO:0000313|Proteomes:UP000054821};
RX   PubMed=26893428;
RA   Baroncelli R., Zapparata A., Piaggeschi G., Sarrocco S., Vannacci G.;
RT   "Draft Whole-Genome Sequence of Trichoderma gamsii T6085, a Promising
RT   Biocontrol Agent of Fusarium Head Blight on Wheat.";
RL   Genome Announc. 4:e01747-15(2016).
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};
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:PON21455.1}.
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DR   EMBL; JPDN02000049; PON21455.1; -; Genomic_DNA.
DR   RefSeq; XP_024404640.1; XM_024550598.1.
DR   AlphaFoldDB; A0A2P4ZAY7; -.
DR   STRING; 398673.A0A2P4ZAY7; -.
DR   GeneID; 29988177; -.
DR   Proteomes; UP000054821; 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   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; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR   Pfam; PF01485; IBR; 1.
DR   SUPFAM; SSF57850; RING/U-box; 2.
DR   PROSITE; PS51873; TRIAD; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054821};
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};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          227..434
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51873"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          111..139
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   697 AA;  79146 MW;  3BFB74F1DB3BE400 CRC64;
     MDPLSVPVSP TAPAPDVPER PSTAERPTTG SVTVIELNDA EYCTRVLQLP LGKSEAEADE
     ELLARASAVG ITATLPSLAS QCPPASSWSD SSFGTPQDRL FSNISNKTNG TGVSTQSSAV
     CPPSPLFDSE GGERRSSTSS LTFAHYERYI STIDSGSNDD KPAKDPLPIY NFSPRRVFIP
     SPKSMASAGS KKSSFQAIKE RLFGRRKKKK KVIQILPPPL PPPVVEVRIV CTTCRDSFEE
     KSSALHKLKC GHIHCVDCVK TMIKQAVEDE TLMPPSCCSS PLTPSLIRAI LNQDDQDTFL
     LAVVKLNTPA DEQLFCPDPD CGHFIPPQDG YDVRHPFDLA CVKCNGRMCG ICKDIGHGLG
     EHCPLDWELT LLKKKQQQQN DKEIWRRCYQ CRNLVSTSET SQITTCLCKA QFCSVCTGIW
     DPITGCPNLC SFEDELQRRR IAATLSSINE LKLRSNPSVQ QLGQEQQQEL HRFMKYKFKT
     KDALQTRHLM QEATLEEKYE LQEEAIQARH KKTLNSMEVR HLKAEMELQD RLNKYEDTIG
     YRIKHMEGYC NGLGRNPSSQ AAARTVTEKD LRELGHHYHI RDTMEQIWAG KINVMRERQD
     RQQEDCRVTQ ENELETFMDK RQEVLDKMEA EFLREETHFN EVFAARQRHI QARWVLVIEV
     LCREFEQQSP KQACRRVSIP KWPEDRVFRT RNSEKQQ
//
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