ID   A0A316YLI1_9BASI        Unreviewed;       786 AA.
AC   A0A316YLI1;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN   ORFNames=FA10DRAFT_266603 {ECO:0000313|EMBL:PWN90099.1};
OS   Acaromyces ingoldii.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Exobasidiomycetes; Exobasidiales; Cryptobasidiaceae; Acaromyces.
OX   NCBI_TaxID=215250 {ECO:0000313|EMBL:PWN90099.1, ECO:0000313|Proteomes:UP000245768};
RN   [1] {ECO:0000313|EMBL:PWN90099.1, ECO:0000313|Proteomes:UP000245768}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCA 4198 {ECO:0000313|EMBL:PWN90099.1,
RC   ECO:0000313|Proteomes:UP000245768};
RX   PubMed=29771364; DOI=10.1093/molbev/msy072;
RA   Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA   Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA   Spatafora J.W., Aime M.C.;
RT   "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT   clade Ustilaginomycotina.";
RL   Mol. Biol. Evol. 0:0-0(2018).
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|ARBA:ARBA00000900};
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DR   EMBL; KZ819636; PWN90099.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A316YLI1; -.
DR   STRING; 215250.A0A316YLI1; -.
DR   InParanoid; A0A316YLI1; -.
DR   OrthoDB; 383715at2759; -.
DR   Proteomes; UP000245768; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR045194; MGRN1/RNF157-like.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR22996; MAHOGUNIN; 1.
DR   PANTHER; PTHR22996:SF0; RING-TYPE E3 UBIQUITIN TRANSFERASE; 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   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245768};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          706..761
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          1..143
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          174..226
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          476..512
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          609..628
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          658..692
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        67..82
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        176..192
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        611..628
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   786 AA;  82862 MW;  FC88C322795DE75F CRC64;
     MSLAATAHHF VGRLNSRRRT DVETQAAEEG SGTANDYGGG GGGDGGGHHA REASGRSVLS
     NISDRFASMR QRERESDMFR VQNRIERSTA TATARGDIEA GALPATEAQG GASATAPAAG
     ATTVAAAPTT GTKSRREKEE GATLFGPNLA NYFGTGSSSS GAVAGLGLGG AGTSTQPGAG
     PVNGTTSPLA PAVPTSPISP GPNDGTWGLR GRTRLGSRGR ARGASLSGLS NLSLPLEADE
     SVASLPQQVA ADLPNEQLAM AEGIEISTLR RWIERSTVGG AVEIAGPDGA SSVKGELGNP
     PTLCSTLQSY VNLKRNTVRL NLVSAEQQQA VLQNRRLQAA TDASASSPVL ESPLALRSVT
     SFGTFAQSSR ATSIPPPTHS LQFEYDCAAP LATIQVFVRA SRKHGTWLNW IAMREAQGLA
     TDLTLDGADE DKYLAQRGPP PHVLGWPVHS AKIRRGFGKP LVANLPLHID YFAPPKPAVS
     KDTKKDGPAV PETPGLREEA PAAPPLTPVT PGVADPLAAA TIPAEETKEE KAAREKAERE
     TLKMAIVVEA LDEEGKTLKE PNLQMTYLRL SSLPVRSTMQ ETMQHANEEA GPGVRDGDAV
     QDIAPVATEA HPDGKGDEEE QLKQDEQRQQ EVKRVWSIQV EGQEAEIGPH RFQLQELYGL
     SSRPPPVRSP EDDDGEHENE NEEGGATQQT AATPVVDFEG SSGGECLICL SSPPTTLLLP
     CTHGLCLECA VQLSDSVKAT REGERRRGKK PRRKYACPVC RRPYTNMLHL SPADEKAVAQ
     AAAAVV
//