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Database: UniProt
Entry: I4YEM1_WALMC
LinkDB: I4YEM1_WALMC
Original site: I4YEM1_WALMC 
ID   I4YEM1_WALMC            Unreviewed;       552 AA.
AC   I4YEM1;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 42.
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_28159 {ECO:0000313|EMBL:EIM22413.1};
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:EIM22413.1, ECO:0000313|Proteomes:UP000005242};
RN   [1] {ECO:0000313|EMBL:EIM22413.1, 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; JH668228; EIM22413.1; -; Genomic_DNA.
DR   RefSeq; XP_006957659.1; XM_006957597.1.
DR   AlphaFoldDB; I4YEM1; -.
DR   STRING; 671144.I4YEM1; -.
DR   GeneID; 18471028; -.
DR   KEGG; wse:WALSEDRAFT_28159; -.
DR   eggNOG; ENOG502SA0Q; Eukaryota.
DR   HOGENOM; CLU_493646_0_0_1; -.
DR   InParanoid; I4YEM1; -.
DR   OMA; LANGNCR; -.
DR   OrthoDB; 3682876at2759; -.
DR   Proteomes; UP000005242; 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   SMART; SM00184; RING; 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:UP000005242};
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          250..318
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          48..72
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          146..172
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          263..285
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          325..345
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          357..453
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        15..30
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        365..380
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        392..413
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   552 AA;  61423 MW;  1B4D4EC31EDCD45D CRC64;
     MADRERREAN DERAQTPQNE QNEQNEQNEH FAGFNRTFIV QLDDFVDGNQ SANAGTDRDS
     GAEQPPEGPG RFHIHFLTLS HSRSLERPAR PVLPFQILLS SFMAALRARN GAGNGDNNTG
     DFAGMGGHIQ IERGPLLPEF YPMHQHHHSE GHAHAHPPTP TNNPANGNGE MGERSSLLER
     IEELRSRNPY GEQGAFPPPF TITINFPIAG GLHHEKKPDP ARAERILSAL PKLHKGVTRR
     MSRVGIETTC GVCLDSLNAR AELQKPETEE GEASTSAVPP EEEARREEEI VALPCSHVFH
     SNCLRPWFAL HTLCPMCRFD LDPESMTMST PPPEENRSEG DGNPFVSIIE RLVRGNRERA
     GRTQQQEAEQ SNNGGRAESA FSARQNRHHP YARTRSATDP RGERSERALR GVRADENANN
     ATANTHPDTR SAEEEMPRPA PPPKKFEIPK ASRSLEDILV KRERESGFRC DMKDCKLGPT
     DESDALTTAN MLSIGGSEKP ACAHFLHSHC YHLANSGCRY YNLEHTHDDG RVDSKCPVCK
     AAGRVHKHEL AY
//
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