ID A0A2V0P6C4_9CHLO Unreviewed; 684 AA.
AC A0A2V0P6C4;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=Rsub_08386 {ECO:0000313|EMBL:GBF95424.1};
OS Raphidocelis subcapitata.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Sphaeropleales; Selenastraceae; Raphidocelis.
OX NCBI_TaxID=307507 {ECO:0000313|EMBL:GBF95424.1, ECO:0000313|Proteomes:UP000247498};
RN [1] {ECO:0000313|EMBL:GBF95424.1, ECO:0000313|Proteomes:UP000247498}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-35 {ECO:0000313|EMBL:GBF95424.1,
RC ECO:0000313|Proteomes:UP000247498};
RX PubMed=29795299; DOI=10.1038/s41598-018-26331-6;
RA Suzuki S., Yamaguchi H., Nakajima N., Kawachi M.;
RT "Raphidocelis subcapitata (=Pseudokirchneriella subcapitata) provides an
RT insight into genome evolution and environmental adaptations in the
RT Sphaeropleales.";
RL Sci. Rep. 8:8058-8058(2018).
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 -!- 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:GBF95424.1}.
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DR EMBL; BDRX01000064; GBF95424.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V0P6C4; -.
DR STRING; 307507.A0A2V0P6C4; -.
DR InParanoid; A0A2V0P6C4; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000247498; Unassembled WGS sequence.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd16655; RING-Ubox_WDSUB1-like; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000225; Armadillo.
DR InterPro; IPR003613; Ubox_domain.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR23315; U BOX DOMAIN-CONTAINING; 1.
DR PANTHER; PTHR23315:SF7; U-BOX DOMAIN-CONTAINING PROTEIN 4; 1.
DR Pfam; PF04564; U-box; 1.
DR SMART; SM00185; ARM; 5.
DR SMART; SM00504; Ubox; 1.
DR SUPFAM; SSF48371; ARM repeat; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51698; U_BOX; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000247498}.
FT DOMAIN 1..73
FT /note="U-box"
FT /evidence="ECO:0000259|PROSITE:PS51698"
FT COILED 56..90
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 684 AA; 70476 MW; F55442EA1464A968 CRC64;
MDDLFLCPIS QEVMEDPVVA ADGHTYERVA IVQWLAAHNT SPLTNLPLES RVLLPNHTLR
AAIKEWKERS QMLQRQQQQQ QQQQQQQQQQ QQPQQQQQQQ RRDAAALAAA AAASAEAARR
AVDRHPAALA DLVCALGSSR EQVAADAAAA LEHLATSSDV LERLYQLLLE KAPAGTPTTT
KLAAFLEQLS GQGAAVQRHM VEAPSGLKAL VAALGVAAAA GHAAGALANI AALDAQARRC
LVAAPGLLPA LAACIRSEDS FGAAQAAKAV CQITAGDASE AELTRHVAAA AGMLAALTAA
LRRPGEGEAA RRAAVAIFNI AFDSAGPELP LRIVEAGALP ALVRLLGSTG VDDAIDAARA
LIQLCRQGGV DVVNKLADVD SVLPALAATV ASGDAEAVTH TACVLGQLAQ QGSPELLQRI
AAPESGVLPA LAAVLADNPA QVSDAAASAL AQICKRNAVQ EVVETDGVLA GLAEMMRRGS
ETEAVKAVCW MAKLGSSVQR MRIAEQPGMV EALAMLAGSR GDAWLQRRGL AVLAISYLAS
EPRAARAIGS TGSVVPDLVA VLQLGGETGA CAAAAICNIA RHADAQLRRK IVAVPDALPA
IIAAAGRRVA AAVEALKWLT AGGESDLVGK VADAPGALQA LLRAQARSGT VCTAIEALQQ
IAACDRGRLH CEIAQAAAQV LRPA
//
