ID I4YCE1_WALMC Unreviewed; 391 AA.
AC I4YCE1;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=WALSEDRAFT_60356 {ECO:0000313|EMBL:EIM21633.1};
OS Wallemia mellicola (strain ATCC MYA-4683 / CBS 633.66) (Wallemia sebi (CBS
OS 633.66)).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Wallemiomycotina;
OC Wallemiomycetes; Wallemiales; Wallemiaceae; Wallemia.
OX NCBI_TaxID=671144 {ECO:0000313|EMBL:EIM21633.1, ECO:0000313|Proteomes:UP000005242};
RN [1] {ECO:0000313|EMBL:EIM21633.1, ECO:0000313|Proteomes:UP000005242}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4683 / CBS 633.66 {ECO:0000313|Proteomes:UP000005242};
RX PubMed=22326418; DOI=10.1016/j.fgb.2012.01.007;
RA Padamsee M., Kumar T.K.A., Riley R., Binder M., Boyd A., Calvo A.M.,
RA Furukawa K., Hesse C., Hohmann S., James T.Y., LaButti K., Lapidus A.,
RA Lindquist E., Lucas S., Miller K., Shantappa S., Grigoriev I.V.,
RA Hibbett D.S., McLaughlin D.J., Spatafora J.W., Aime M.C.;
RT "The genome of the xerotolerant mold Wallemia sebi reveals adaptations to
RT osmotic stress and suggests cryptic sexual reproduction.";
RL Fungal Genet. Biol. 49:217-226(2012).
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; JH668231; EIM21633.1; -; Genomic_DNA.
DR RefSeq; XP_006958328.1; XM_006958266.1.
DR AlphaFoldDB; I4YCE1; -.
DR STRING; 671144.I4YCE1; -.
DR GeneID; 18473908; -.
DR KEGG; wse:WALSEDRAFT_60356; -.
DR eggNOG; KOG4265; Eukaryota.
DR HOGENOM; CLU_706369_0_0_1; -.
DR InParanoid; I4YCE1; -.
DR OMA; WIDNTEN; -.
DR OrthoDB; 383715at2759; -.
DR Proteomes; UP000005242; 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 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.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000005242}.
FT DOMAIN 281..377
FT /note="RING-type"
FT /evidence="ECO:0000259|SMART:SM00184"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 346..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 391 AA; 44053 MW; 8A3A39AA34D2EBF9 CRC64;
MFSSLFRRNT PRQEVPAVSL KSAKPVDKSS KPNQKRLYGP DIQFDDRNSN ASGEIDNELL
NNWINNKSNQ QQTPSSTLKL ECNLKRNSLR ILTNDKATSI KSTESDRPVS PSMSIAPISR
QSQSLRFICD STSPKVRVLL TWTDSEQPFL DQLIDGGWDK MWQSPSKLDL IAHEQKLTKS
EDSETDSTSS NDLKKVELKL RIDLVCSDVN GAPISPLNKQ STYLNIHRCD ECWLLRVDKR
VANIGSNLYD LHEIYGLSSH TKENNDDVNQ VIVDDHVGGE CVICLASARD TLLLPCRHLV
ACKDCATRMT DFGSGAQTER DGGIWGTENN EPTTLNSNEN DRVIAAEAGN NNNNNETHTR
PSRRRKRKPK GWYCPVCRQP YTAMLRVAYK D
//
