ID A0A0S4ITU9_BODSA Unreviewed; 453 AA.
AC A0A0S4ITU9;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=BSAL_56395 {ECO:0000313|EMBL:CUE79115.1};
OS Bodo saltans (Flagellated protozoan).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Eubodonida; Bodonidae; Bodo.
OX NCBI_TaxID=75058 {ECO:0000313|EMBL:CUE79115.1, ECO:0000313|Proteomes:UP000051952};
RN [1] {ECO:0000313|Proteomes:UP000051952}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lake Konstanz {ECO:0000313|Proteomes:UP000051952};
RG Pathogen Informatics;
RL Submitted (SEP-2015) 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};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SIMILARITY: Belongs to the RING-type zinc finger family. LOG2
CC subfamily. {ECO:0000256|ARBA:ARBA00025721}.
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DR EMBL; CYKH01000195; CUE79115.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S4ITU9; -.
DR VEuPathDB; TriTrypDB:BSAL_56395; -.
DR OMA; APHNFYL; -.
DR OrthoDB; 383715at2759; -.
DR Proteomes; UP000051952; 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 CDD; cd16789; mRING-HC-C3HC5_MGRN1-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR045195; LOG2-like_mRING_C3HC5.
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 SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Reference proteome {ECO:0000313|Proteomes:UP000051952};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT DOMAIN 405..444
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 297..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 367..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 453 AA; 48701 MW; DD7AEA97A076B277 CRC64;
MGGLFSTPDD SNGSNGGAPK SFYLVLGGPS IRYNRPGRGP LIFDVEPMST NTEDLVEHAE
VVRPTANVRT KQKFQLVPIT PPNPTGYPQT TQWTFRLRFQ IDYCASTPPQ RVEVFLGTKI
EYRQGEGILL VPRNGTSSIS TAGSAADAFE IQRNDGSAAA SNRNAPTRVM FKSSGFPTVT
GSTDLTTVDM TQYCAEFTLA DLIPALPKDQ LATPCSLKEC PIVIVVQFDV PPAQSRRPPA
ASSVAAAALL NGGTNASTAS RSRTDSLNET VPEVTAVHRL YTFLSFDEKQ VASLYGKTSQ
GVESPAAGGG ARRRAQGDSQ REPNGGTNDE DVTMTELRNV DLTLVKQYLE FSGEVYELDD
IYDLGGDDLG SPANADPPGA TPRAGGEEEI AAADPVEDDD EANTCVICLC NPKDTTVIPC
RHLCLCAECA VQLRHQSNKC PICRRPIERL MTM
//
