ID   A0A081CN12_PSEA2        Unreviewed;       883 AA.
AC   A0A081CN12;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN   ORFNames=PAN0_035c6290 {ECO:0000313|EMBL:GAK68058.1};
OS   Pseudozyma antarctica (Yeast) (Candida antarctica).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Moesziomyces.
OX   NCBI_TaxID=84753 {ECO:0000313|EMBL:GAK68058.1};
RN   [1] {ECO:0000313|EMBL:GAK68058.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=JCM 10317 {ECO:0000313|EMBL:GAK68058.1};
RA   Morita T., Saika A., Koike H.;
RT   "Draft genome sequence of the yeast Pseudozyma antarctica JCM 10317 known
RT   as a producer of lipase B which used in a wide range of industrial
RT   applications.";
RL   Submitted (JUL-2014) 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};
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DR   EMBL; DF830102; GAK68058.1; -; Genomic_DNA.
DR   RefSeq; XP_014653743.1; XM_014798257.1.
DR   AlphaFoldDB; A0A081CN12; -.
DR   GeneID; 26307102; -.
DR   HOGENOM; CLU_015503_0_0_1; -.
DR   OrthoDB; 383715at2759; -.
DR   Proteomes; UP000053758; 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:UP000053758};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          804..859
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          1..48
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          111..144
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          160..219
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          237..299
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          628..659
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        162..178
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        179..204
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        258..292
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   883 AA;  92532 MW;  73BCD8F4B750DFC1 CRC64;
     MAAPSGLGPS DTAAVPDFTE KRGEGAAAAI DPTPSPRQGF SLSISTPLHH PIPTVDPLGT
     MSTLLSFARA GPAHRAPPRD EEANVAVAVD GAPSTSSSSR WSRPFARASN WGSNVEMRPH
     PAPEPARNSD LEQATPAAGG RHERTASALS FLSAVHVPSL STLRQRDRDN ERRRQNQRAN
     NPDQPVVSAL ATVTTAPPAS RAANKKSRSS RREREEAATL FGPNLANYFG SGISSSGAVS
     SHGAGVPQPP PVTSPVSPTA APDSAVDPTT NNTAAAATAD ATYPQASSSR RVRLGSRGRA
     RGASLSGLSM MSLGAESVTS LGDLNVDRSN DAPAQAHGMI QGSTADLIDQ LNRDAGPNTT
     DGHIAMSEGV DITTLQRWIH RSTGNSDAAI PTAAAAAATY GPPVCTTLQS FVNLKRNTLK
     LSPKTNVDAA KPAEADANFL RTRPSLSLLP TLSYASTGAA STATSLLPEP THSLYFEYDC
     AAPYASVQIF IRASRKHGSW LNYQPASSNT GDPLAQPTNP DGSPAWLAQC APPPHVLGWP
     VHVAKLAKGF GVGHTATIPL DLAYYAPPRR AKLDANTAGA SGGAAAGETG EPIAAHPRIA
     STVEPVTPAA IPETPGFEFQ RRLELDADDA DDDPPARHAR AGSSRVPGAV VDSGAGAGEA
     SSGAVALSAE VAAQPAVEEE TKEQRLAREK AERETLKLAI VVEALDEHAR PLREPNLQTS
     YLRLTSLPVK KSVSERLASL STEVRTWSSQ VEGQEAEIGP HRFQLQELYG LSSKPPAVAP
     APPEGEEEEA PQMAMVDASS GSECLICLSS PPTTLLLPCT HGLCLECAVQ LRDSVVGIRQ
     SERRRGRTPR RKYACPVCRR AYTSMLHLSK ADEKSAVHST APS
//