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Database: UniProt
Entry: K5WZ79_AGABU
LinkDB: K5WZ79_AGABU
Original site: K5WZ79_AGABU 
ID   K5WZ79_AGABU            Unreviewed;       402 AA.
AC   K5WZ79;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
DE   Flags: Fragment;
GN   ORFNames=AGABI1DRAFT_37502 {ECO:0000313|EMBL:EKM80841.1};
OS   Agaricus bisporus var. burnettii (strain JB137-S8 / ATCC MYA-4627 / FGSC
OS   10392) (White button mushroom).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Agaricineae; Agaricaceae; Agaricus.
OX   NCBI_TaxID=597362 {ECO:0000313|EMBL:EKM80841.1, ECO:0000313|Proteomes:UP000008493};
RN   [1] {ECO:0000313|Proteomes:UP000008493}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JB137-S8 / ATCC MYA-4627 / FGSC 10392
RC   {ECO:0000313|Proteomes:UP000008493};
RX   PubMed=23045686; DOI=10.1073/pnas.1206847109;
RA   Morin E., Kohler A., Baker A.R., Foulongne-Oriol M., Lombard V., Nagy L.G.,
RA   Ohm R.A., Patyshakuliyeva A., Brun A., Aerts A.L., Bailey A.M.,
RA   Billette C., Coutinho P.M., Deakin G., Doddapaneni H., Floudas D.,
RA   Grimwood J., Hilden K., Kuees U., LaButti K.M., Lapidus A., Lindquist E.A.,
RA   Lucas S.M., Murat C., Riley R.W., Salamov A.A., Schmutz J., Subramanian V.,
RA   Woesten H.A.B., Xu J., Eastwood D.C., Foster G.D., Sonnenberg A.S.,
RA   Cullen D., de Vries R.P., Lundell T., Hibbett D.S., Henrissat B.,
RA   Burton K.S., Kerrigan R.W., Challen M.P., Grigoriev I.V., Martin F.;
RT   "Genome sequence of the button mushroom Agaricus bisporus reveals
RT   mechanisms governing adaptation to a humic-rich ecological niche.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:17501-17506(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};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004477}.
CC   -!- SIMILARITY: Belongs to the HRD1 family.
CC       {ECO:0000256|ARBA:ARBA00010089}.
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DR   EMBL; JH971388; EKM80841.1; -; Genomic_DNA.
DR   RefSeq; XP_007328020.1; XM_007327958.1.
DR   AlphaFoldDB; K5WZ79; -.
DR   STRING; 597362.K5WZ79; -.
DR   GeneID; 18829242; -.
DR   KEGG; abp:AGABI1DRAFT37502; -.
DR   eggNOG; KOG0802; Eukaryota.
DR   HOGENOM; CLU_009169_0_0_1; -.
DR   InParanoid; K5WZ79; -.
DR   OMA; SPKGHAT; -.
DR   OrthoDB; 2912447at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000008493; Unassembled WGS sequence.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   CDD; cd16479; RING-H2_synoviolin; 1.
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   InterPro; IPR024766; Znf_RING_H2.
DR   PANTHER; PTHR22763:SF184; E3 UBIQUITIN-PROTEIN LIGASE HRD1; 1.
DR   PANTHER; PTHR22763; RING ZINC FINGER PROTEIN; 1.
DR   Pfam; PF12678; zf-rbx1; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008493};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT   TRANSMEM        24..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        63..85
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        97..115
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        121..139
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        159..180
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        251..270
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          322..375
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          379..402
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EKM80841.1"
SQ   SEQUENCE   402 AA;  46190 MW;  BE9EC942B766FA0A CRC64;
     MPPLQQLLRH GSNRVLRSAL SHRVQLYFLV SLVALSAVVF NALRNYSNFY SVAISLSKSS
     RSVLVLANFA VLLALLGAHI VQRIFFGALR ANEVERLYDR LWFFITESLL AFTIFRDEFD
     IGFVLMFGFL LFVKSFHWLS SDRVEWMDQQ QYPGPPVLFH IRMISLFSIL WLVDFMMFVI
     AMDHTIAYGV GGMVLFASEY GILMASLMNT VFKYLLFAYD LRRAGRRGGE NAPPWENKSM
     WVFYIELTTD FLKLTTYLIF FIIIITFYGL PLNIVRDVYI TARSFITRLR ALHRYQTATR
     NMDQRYPNAT ETELAATSDR TCIICREDMV PAVQGQPPVS DGPNVTPKKL PCGHIFHFYC
     LRSWLERQQS CPTCRQTVLE PNTPRRPANG PAVAPQQQGN AP
//
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