ID L1IAI9_GUITC Unreviewed; 311 AA.
AC L1IAI9;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=GUITHDRAFT_98480 {ECO:0000313|EMBL:EKX32919.1};
OS Guillardia theta (strain CCMP2712) (Cryptophyte).
OC Eukaryota; Cryptophyceae; Pyrenomonadales; Geminigeraceae; Guillardia.
OX NCBI_TaxID=905079 {ECO:0000313|EMBL:EKX32919.1};
RN [1] {ECO:0000313|EMBL:EKX32919.1, ECO:0000313|Proteomes:UP000011087}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCMP2712 {ECO:0000313|EMBL:EKX32919.1,
RC ECO:0000313|Proteomes:UP000011087};
RX PubMed=23201678; DOI=10.1038/nature11681;
RG DOE Joint Genome Institute;
RA Curtis B.A., Tanifuji G., Burki F., Gruber A., Irimia M., Maruyama S.,
RA Arias M.C., Ball S.G., Gile G.H., Hirakawa Y., Hopkins J.F., Kuo A.,
RA Rensing S.A., Schmutz J., Symeonidi A., Elias M., Eveleigh R.J.,
RA Herman E.K., Klute M.J., Nakayama T., Obornik M., Reyes-Prieto A.,
RA Armbrust E.V., Aves S.J., Beiko R.G., Coutinho P., Dacks J.B.,
RA Durnford D.G., Fast N.M., Green B.R., Grisdale C.J., Hempel F.,
RA Henrissat B., Hoppner M.P., Ishida K., Kim E., Koreny L., Kroth P.G.,
RA Liu Y., Malik S.B., Maier U.G., McRose D., Mock T., Neilson J.A.,
RA Onodera N.T., Poole A.M., Pritham E.J., Richards T.A., Rocap G., Roy S.W.,
RA Sarai C., Schaack S., Shirato S., Slamovits C.H., Spencer D.F., Suzuki S.,
RA Worden A.Z., Zauner S., Barry K., Bell C., Bharti A.K., Crow J.A.,
RA Grimwood J., Kramer R., Lindquist E., Lucas S., Salamov A., McFadden G.I.,
RA Lane C.E., Keeling P.J., Gray M.W., Grigoriev I.V., Archibald J.M.;
RT "Algal genomes reveal evolutionary mosaicism and the fate of
RT nucleomorphs.";
RL Nature 492:59-65(2012).
RN [2] {ECO:0000313|Proteomes:UP000011087}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCMP2712 {ECO:0000313|Proteomes:UP000011087};
RA Kuo A., Curtis B.A., Tanifuji G., Burki F., Gruber A., Irimia M.,
RA Maruyama S., Arias M.C., Ball S.G., Gile G.H., Hirakawa Y., Hopkins J.F.,
RA Rensing S.A., Schmutz J., Symeonidi A., Elias M., Eveleigh R.J.,
RA Herman E.K., Klute M.J., Nakayama T., Obornik M., Reyes-Prieto A.,
RA Armbrust E.V., Aves S.J., Beiko R.G., Coutinho P., Dacks J.B.,
RA Durnford D.G., Fast N.M., Green B.R., Grisdale C., Hempe F., Henrissat B.,
RA Hoppner M.P., Ishida K.-I., Kim E., Koreny L., Kroth P.G., Liu Y.,
RA Malik S.-B., Maier U.G., McRose D., Mock T., Neilson J.A., Onodera N.T.,
RA Poole A.M., Pritham E.J., Richards T.A., Rocap G., Roy S.W., Sarai C.,
RA Schaack S., Shirato S., Slamovits C.H., Spencer D.F., Suzuki S.,
RA Worden A.Z., Zauner S., Barry K., Bell C., Bharti A.K., Crow J.A.,
RA Grimwood J., Kramer R., Lindquist E., Lucas S., Salamov A., McFadden G.I.,
RA Lane C.E., Keeling P.J., Gray M.W., Grigoriev I.V., Archibald J.M.;
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblProtists:EKX32919}
RP IDENTIFICATION.
RG EnsemblProtists;
RL Submitted (MAR-2016) to UniProtKB.
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; JH993165; EKX32919.1; -; Genomic_DNA.
DR RefSeq; XP_005819899.1; XM_005819842.1.
DR AlphaFoldDB; L1IAI9; -.
DR STRING; 905079.L1IAI9; -.
DR PaxDb; 55529-EKX32919; -.
DR EnsemblProtists; EKX32919; EKX32919; GUITHDRAFT_98480.
DR GeneID; 17289651; -.
DR KEGG; gtt:GUITHDRAFT_98480; -.
DR eggNOG; KOG4265; Eukaryota.
DR HOGENOM; CLU_016631_3_1_1; -.
DR OMA; CRQDVRG; -.
DR OrthoDB; 383715at2759; -.
DR Proteomes; UP000011087; 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 SMART; SM00184; RING; 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:UP000011087};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT DOMAIN 249..288
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 311 AA; 33785 MW; D58718A0946E1459 CRC64;
MGTNSSRPGE GGGNQGGQGA GDTGMAGNPS QMGYGGTRFA GGSTGLFAPR PDGSLFVPNS
QRQVPPAPQL QLTETIRNDV NLKKQTLKLN KCANSPNTYC LEFLFDAAAD CTVSIWFLAE
EQVDSANNTI KFETSYEIQP KTVKFKAALG QHFTQPENEG FNVSLVQNRG QMYYHHGSQH
FPIVIMLQTC DENAHRVQSQ STFATFKSNA DGSLSVAVIK QKIQVKGNAY ELQEIYGIEQ
NDAENSKECV ICMSAPKDTT VLPCRHMCMC SDCAKVLRYQ TNKCPICRCS VESLLQIKVN
SSGETAPVGN S
//
