ID A0A2T3AU82_AMORE Unreviewed; 668 AA.
AC A0A2T3AU82;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 02-APR-2025, entry version 26.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN ORFNames=M430DRAFT_106760 {ECO:0000313|EMBL:PSS12226.1};
OS Amorphotheca resinae ATCC 22711.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Amorphothecaceae; Amorphotheca.
OX NCBI_TaxID=857342 {ECO:0000313|EMBL:PSS12226.1, ECO:0000313|Proteomes:UP000241818};
RN [1] {ECO:0000313|EMBL:PSS12226.1, ECO:0000313|Proteomes:UP000241818}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22711 {ECO:0000313|EMBL:PSS12226.1,
RC ECO:0000313|Proteomes:UP000241818};
RX PubMed=29315638; DOI=10.1111/nph.14974;
RA Martino E., Morin E., Grelet G.A., Kuo A., Kohler A., Daghino S.,
RA Barry K.W., Cichocki N., Clum A., Dockter R.B., Hainaut M., Kuo R.C.,
RA LaButti K., Lindahl B.D., Lindquist E.A., Lipzen A., Khouja H.R.,
RA Magnuson J., Murat C., Ohm R.A., Singer S.W., Spatafora J.W., Wang M.,
RA Veneault-Fourrey C., Henrissat B., Grigoriev I.V., Martin F.M., Perotto S.;
RT "Comparative genomics and transcriptomics depict ericoid mycorrhizal fungi
RT as versatile saprotrophs and plant mutualists.";
RL New Phytol. 217:1213-1229(2018).
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; KZ679015; PSS12226.1; -; Genomic_DNA.
DR RefSeq; XP_024718224.1; XM_024861100.1.
DR AlphaFoldDB; A0A2T3AU82; -.
DR STRING; 857342.A0A2T3AU82; -.
DR GeneID; 36569181; -.
DR InParanoid; A0A2T3AU82; -.
DR OrthoDB; 9977870at2759; -.
DR Proteomes; UP000241818; 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; cd22584; Rcat_RBR_unk; 1.
DR Gene3D; 1.20.120.1750; -; 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 InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR Pfam; PF01485; IBR; 2.
DR SUPFAM; SSF57850; RING/U-box; 2.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000241818};
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 179..381
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT REGION 71..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 378..429
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 569..596
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 83..93
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 668 AA; 76461 MW; 79EDA3AEB4FA923A CRC64;
MRRSEGPAPT THSDADYLRE VLLLEDGRTE ELCDADLTKE AEALGIAIPR PPSPRNTAHD
SLCESAITVA SHHARTTSSA SRGSDSTGMT SRSSLDHAAP PQMRKRSNPR RSLSFSEYEK
FVMQTEARDA ANLDFSPPPV PAEPAPSLFS VSTRRSYASI RKGIKSRLRL RRTKTSEEAT
PSCICCREDS EKTRPVHTLP CQHSYCDACL RALISQASTD ESKMPPRCCS RAIPASVIKS
LLSREDQHNF MKSVLQFSTP WSQRIFCTNP ACGEFIPKRD KIDPKHPFEV VCRKCRTRVC
STCKSAAHAL GQACPADWEL DAVLQMGGNT GWRRCYKCRD LVELTQGSSY ITCRCKAQFC
YVCGAVWDSV IGCPNFCNGE EELERRRLEE EARIAELEAE RLAKEEEEQQ EAAEKLAAEK
RTLESEQLNT LRTRHINERD RFCAFERKVK RDMWTRQAQV RLDTLGRHSE LQTKMKERHL
GTAAHLEDRQ VGAEMELRAT LKQSERSVHI RLRHMEAYCD GLGRSANGSN PARVVTERDL
RELGQQYNLR DDMERLHQSK INVMRDKQAK QMEHLLSRQE EELKRLTAKH AEELRILELS
FATEDEDFVK LFSERRRRLT SRWYLAEEIE RKKLEIRTKL RFAPMAAIEW PPPAPEMEEQ
LHVVSEDD
//
