ID A0A401KM03_ASPAW Unreviewed; 223 AA.
AC A0A401KM03;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=AAWM_03196 {ECO:0000313|EMBL:GCB20311.1};
OS Aspergillus awamori (Black koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=105351 {ECO:0000313|EMBL:GCB20311.1, ECO:0000313|Proteomes:UP000286921};
RN [1] {ECO:0000313|EMBL:GCB20311.1, ECO:0000313|Proteomes:UP000286921}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IFM 58123 {ECO:0000313|EMBL:GCB20311.1,
RC ECO:0000313|Proteomes:UP000286921};
RA Kusuya Y., Shimizu M., Takahashi H., Yaguchi T.;
RT "Aspergillus awamori IFM 58123T.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
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};
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:GCB20311.1}.
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DR EMBL; BDHI01000007; GCB20311.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401KM03; -.
DR STRING; 105351.A0A401KM03; -.
DR Proteomes; UP000286921; Unassembled WGS sequence.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR15710:SF4; E3 UBIQUITIN-PROTEIN LIGASE IRUKA; 1.
DR PANTHER; PTHR15710; E3 UBIQUITIN-PROTEIN LIGASE PRAJA; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000286921};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 147..192
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 81..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 199..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..213
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 223 AA; 25052 MW; 20646ABD2594D23F CRC64;
MSTYEVEHNT TDPSTTTPNN STTPDQHHRR RRPDLSTFFS ALSEITPDEA RHRPHAVPVP
RDVSAAFYSL AEALDLMRRE GGGGAALPSE TQGTAGGDGD NDLLTTMIQS LLSTAEMPPR
EVEGASEEFC DQLDRIPRTA LNSSQVCPIC NNPFLEDQYP LVVRLPCHPT HLFDLECVRP
WLRLRGTCPL DRTDFAKQER EKAEARRKLA EEDEEEEWDG MYA
//
