ID   C5LN26_PERM5            Unreviewed;       434 AA.
AC   C5LN26;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN   ORFNames=Pmar_PMAR028276 {ECO:0000313|EMBL:EER01826.1};
OS   Perkinsus marinus (strain ATCC 50983 / TXsc).
OC   Eukaryota; Sar; Alveolata; Perkinsozoa; Perkinsea; Perkinsida; Perkinsidae;
OC   Perkinsus.
OX   NCBI_TaxID=423536 {ECO:0000313|Proteomes:UP000007800};
RN   [1] {ECO:0000313|EMBL:EER01826.1, ECO:0000313|Proteomes:UP000007800}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 50983 / TXsc {ECO:0000313|Proteomes:UP000007800};
RA   El-Sayed N., Caler E., Inman J., Amedeo P., Hass B., Wortman J.;
RL   Submitted (JUL-2008) 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; GG683700; EER01826.1; -; Genomic_DNA.
DR   RefSeq; XP_002769108.1; XM_002769062.1.
DR   AlphaFoldDB; C5LN26; -.
DR   EnsemblProtists; EER01826; EER01826; Pmar_PMAR028276.
DR   GeneID; 9040434; -.
DR   OrthoDB; 383715at2759; -.
DR   Proteomes; UP000007800; 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   PIRSF; PIRSF036836; RNase_bind_SBP1; 2.
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|PROSITE-ProRule:PRU00175};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007800};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT   DOMAIN          368..412
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          1..86
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          320..359
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..84
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        328..347
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   434 AA;  48010 MW;  84D0C19D472D40F6 CRC64;
     MGNSSSRRGR TQSPQHSQQE AEQQHQQEQQ SRPRRQGTSF SLWPTVSWMG ISRPTMRDTT
     NSTQQQQQSS IVVQSRQRPP AAAYQQQQRP VYVFRGGRYV PDPTADPRPY QAPFSPFSLV
     QTIPEIKQTC VVKNPCNLRK DTIKFIEDGT NTPPKLCFMV DTTTPCTVRL HYFVVGDASS
     HTTDIPEIKG VRTYTYDLPH AGLRQKIITN DEVQRIDRRQ PLPAGWSSTA YTKGSHRYPA
     VVEIMSKSNS NGNSKDIICT GQLTYLSFPP VEGTELMMNV KVLKQRVLFS TQAYDMHDIY
     GIEAPQSAVH EVVEQIGDTV EGKIVKGGGN SPSSSSEEES INGEAAPSPS HPSPGHYDDE
     ADAMASECVI CLSEARTTVV LPCRHMCLCN DCAVRVQEAN PGHVSAKCPI CRQPVTSMLQ
     IAASPSSIIR ESTS
//