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Database: UniProt
Entry: A0A8S4GHS6_9CHLO
LinkDB: A0A8S4GHS6_9CHLO
Original site: A0A8S4GHS6_9CHLO 
ID   A0A8S4GHS6_9CHLO        Unreviewed;       601 AA.
AC   A0A8S4GHS6;
DT   12-OCT-2022, integrated into UniProtKB/TrEMBL.
DT   12-OCT-2022, sequence version 1.
DT   02-APR-2025, entry version 10.
DE   RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE            EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN   ORFNames=YPF701_LOCUS676 {ECO:0000313|EMBL:CAG9460558.1};
OS   Pedinophyceae sp. YPF-701.
OC   Eukaryota; Viridiplantae; Chlorophyta; Pedinophyceae.
OX   NCBI_TaxID=765719 {ECO:0000313|EMBL:CAG9460558.1, ECO:0000313|Proteomes:UP000836011};
RN   [1] {ECO:0000313|EMBL:CAG9460558.1, ECO:0000313|Proteomes:UP000836011}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YPF-701 {ECO:0000313|EMBL:CAG9460558.1,
RC   ECO:0000313|Proteomes:UP000836011};
RA   Iha C., Iha C.;
RL   Submitted (SEP-2021) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.;
CC         EC=2.3.2.31; Evidence={ECO:0000256|ARBA:ARBA00001798};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CAG9460558.1}.
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DR   EMBL; CAJZHL010000002; CAG9460558.1; -; Genomic_DNA.
DR   OrthoDB; 10009520at2759; -.
DR   Proteomes; UP000836011; Unassembled WGS sequence.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
DR   CDD; cd20346; BRcat_RBR_ANKIB1; 1.
DR   CDD; cd22583; Rcat_RBR_ARI7-like; 1.
DR   Gene3D; 1.20.120.1750; -; 1.
DR   Gene3D; 4.10.1060.10; Zinc finger, RanBP2-type; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR045840; Ariadne.
DR   InterPro; IPR031127; E3_UB_ligase_RBR.
DR   InterPro; IPR002867; IBR_dom.
DR   InterPro; IPR044066; TRIAD_supradom.
DR   InterPro; IPR001876; Znf_RanBP2.
DR   InterPro; IPR036443; Znf_RanBP2_sf.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR   Pfam; PF19422; Ariadne; 1.
DR   Pfam; PF01485; IBR; 1.
DR   Pfam; PF22191; IBR_1; 1.
DR   SMART; SM00647; IBR; 2.
DR   SMART; SM00547; ZnF_RBZ; 1.
DR   SUPFAM; SSF90209; Ran binding protein zinc finger-like; 1.
DR   SUPFAM; SSF57850; RING/U-box; 3.
DR   PROSITE; PS51873; TRIAD; 1.
DR   PROSITE; PS01358; ZF_RANBP2_1; 1.
DR   PROSITE; PS50199; ZF_RANBP2_2; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000836011};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00322}.
FT   DOMAIN          117..333
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51873"
FT   DOMAIN          572..601
FT                   /note="RanBP2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50199"
FT   REGION          1..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          537..556
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        18..33
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   601 AA;  67941 MW;  70412CC45040CE6C CRC64;
     MSDEEWSDAS GELHSDVSDS EDASMYADDD ENEVVLTQTK QEPFEVWDVE EVAKRLESIL
     RQVSDITTLG RSDAARLLRK FEWNTERGQE EWFSRQAELQ EELGIAREPV PAPPDQKEAT
     CGICWTDKPA SEMTSGPCGH PFCADCWRHH LAAQLEMKDA KNALLSMRCM QPGCGCAISL
     ETYRHVVDDA FAEKYRRHEL EDFVEASRAV RHCPAADCAA CVHTLRPSQA AQEVTCSCGT
     RFCFDCSEEP HRPSSCHMVQ KWLAKSSAEA ANMQWILANT KPCPKCQRPI EKNAGCMHMN
     CSQCRYEFCW LCLQDWSKHG EGTGGFYNCN MYEERRRQGE FSKEERMKKG AQRALDRWVH
     YFERYDFHTR GSRSWQEELA KRSMRKISEN TATPESQLKF KAEVGAMLAE CKRVLKWTYC
     YGYWTWGVQD PEEGAVPEAL QQRRAFFEFN QGFAELLCEK LYQTLKDGLE RFEGQTAARA
     RREHPDLSDR EIQGKIAEEW SAWRADLMSR CQVTEKSFHN LITELERGFD RAAEDYGGAG
     PSGAAEGAAG AAGGAGAASA VDPEVSRSVE AATGIWACTV CTFMNEPDVQ TCGACNTARP
     R
//
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