ID   A0A177DVE6_ALTAL        Unreviewed;       676 AA.
AC   A0A177DVE6;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   02-APR-2025, entry version 33.
DE   RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE            EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN   ORFNames=CC77DRAFT_1029430 {ECO:0000313|EMBL:OAG23486.1};
OS   Alternaria alternata (Alternaria rot fungus) (Torula alternata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Alternaria;
OC   Alternaria sect. Alternaria; Alternaria alternata complex.
OX   NCBI_TaxID=5599 {ECO:0000313|EMBL:OAG23486.1, ECO:0000313|Proteomes:UP000077248};
RN   [1] {ECO:0000313|EMBL:OAG23486.1, ECO:0000313|Proteomes:UP000077248}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRC1lrK2f {ECO:0000313|EMBL:OAG23486.1,
RC   ECO:0000313|Proteomes:UP000077248};
RG   DOE Joint Genome Institute;
RA   Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA   Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT   "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT   ascomycete fungi.";
RL   Submitted (MAY-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; KV441473; OAG23486.1; -; Genomic_DNA.
DR   RefSeq; XP_018388907.1; XM_018526512.1.
DR   AlphaFoldDB; A0A177DVE6; -.
DR   GeneID; 29112106; -.
DR   KEGG; aalt:CC77DRAFT_1029430; -.
DR   VEuPathDB; FungiDB:CC77DRAFT_1029430; -.
DR   OMA; LECVKCW; -.
DR   Proteomes; UP000077248; 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; cd22584; Rcat_RBR_unk; 1.
DR   Gene3D; 1.20.120.1750; -; 1.
DR   InterPro; IPR031127; E3_UB_ligase_RBR.
DR   InterPro; IPR002867; IBR_dom.
DR   InterPro; IPR044066; TRIAD_supradom.
DR   PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR   Pfam; PF01485; IBR; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS51873; TRIAD; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077248};
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          137..366
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51873"
FT   REGION          360..429
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          493..526
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        360..375
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        388..407
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        493..502
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   676 AA;  74146 MW;  2CE6FCD0D18F1EA2 CRC64;
     MGSKLSRAVR PQVKAVASPV ATGQHHDIDH VNAQKGRQEI TPQLPGTFAY DDINIATSIT
     TTAIAPRRNS APALSTTSAA SVAMEQIYRI SAELRLAQAE RDLMSIEYTS TDIDPPPAVA
     TVPPSPAPAP PAPVQETGVQ CIVCCTQLPS SKDPKHAKEV IKPCRECGSA YCGSCIKRMF
     TECCKDTTRM PPRCCVQIQP HQAKPHLTRE EFADFRSKYE EWLTPNPFYC PMPTCSAFIP
     ERLLPEEVTK RKGKRADSGI GTPTSKSVAC PACETGICPD CRQVAHPDSL CNISEFGIDA
     ETTELLKSWG YKKCPKCGHG LKRMFGCNHM ECRCGAHFCY ACMEDYSNCN GGCGEENDYD
     DESFDEDEDE DEDVSPEQHD DTRLLPDTND TPDASNEATQ LQGTTGEAAT ALPQPASQPR
     NLDGGGHRYW QRQDLNFGEE PTEDYQDRSW DCEHGFDSCK ITLAKALNND PSTEMECVKC
     WCAIHPEIKP PNAASNTNTS VRTVPAGARG ANRGITRGMA AGRGRGRGWG RGRGAYVPPR
     GLFEAHGAVG TAPHLRHTLS SLLSQSVPAR EPFPMEDVQY SSERTVDTYG NTIATSEMGL
     RHRASDETFS NKIVPMRDDQ GSTLREFHRT PSTIFSESPA KFSLAYECYS CALLVCKKCR
     DGILDAQNAE RHVDED
//