ID A0A1Q9C9B7_SYMMI Unreviewed; 1132 AA.
AC A0A1Q9C9B7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN Name=Syvn1 {ECO:0000313|EMBL:OLP79526.1};
GN ORFNames=AK812_SmicGene40174 {ECO:0000313|EMBL:OLP79526.1};
OS Symbiodinium microadriaticum (Dinoflagellate) (Zooxanthella
OS microadriatica).
OC Eukaryota; Sar; Alveolata; Dinophyceae; Suessiales; Symbiodiniaceae;
OC Symbiodinium.
OX NCBI_TaxID=2951 {ECO:0000313|EMBL:OLP79526.1, ECO:0000313|Proteomes:UP000186817};
RN [1] {ECO:0000313|EMBL:OLP79526.1, ECO:0000313|Proteomes:UP000186817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP2467 {ECO:0000313|EMBL:OLP79526.1,
RC ECO:0000313|Proteomes:UP000186817};
RA Aranda M., Li Y., Liew Y.J., Baumgarten S., Simakov O., Wilson M., Piel J.,
RA Ashoor H., Bougouffa S., Bajic V.B., Ryu T., Ravasi T., Bayer T.,
RA Micklem G., Kim H., Bhak J., Lajeunesse T.C., Voolstra C.R.;
RT "Genome analysis of coral dinoflagellate symbionts highlights evolutionary
RT adaptations to a symbiotic lifestyle.";
RL Submitted (FEB-2016) 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 -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004477}.
CC -!- SIMILARITY: Belongs to the HRD1 family.
CC {ECO:0000256|ARBA:ARBA00010089}.
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:OLP79526.1}.
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DR EMBL; LSRX01001473; OLP79526.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q9C9B7; -.
DR OrthoDB; 2912447at2759; -.
DR Proteomes; UP000186817; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR CDD; cd16479; RING-H2_synoviolin; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR22763:SF184; E3 UBIQUITIN-PROTEIN LIGASE HRD1; 1.
DR PANTHER; PTHR22763; RING ZINC FINGER PROTEIN; 1.
DR Pfam; PF13639; zf-RING_2; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Reference proteome {ECO:0000313|Proteomes:UP000186817};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT TRANSMEM 50..73
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 85..102
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 108..127
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 139..158
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 239..280
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 311..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 522..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1063..1098
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 486..513
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1014..1055
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1132 AA; 123431 MW; 72EAB32AA9FA87BE CRC64;
MVLLAMNFSS YIVLSTLVVA GVVAHAFVVH EQFYPAVIYL STDKMCLAVM YNFAFALFLL
LGKIILRVFI GTLRDVEVEQ LVDSGRGFLA DTILFLVFYA PTIDNREVGT VFLIQYICCV
IFMKVGVPRL IVNIKLVGLM ALLLGCDLLA LSYFYSVASK SSTFFTWILF EALTMSSVVL
VSMCKYSIHM IDLRISYLQV ARKLAQRLRS FRRYRRISMN MELCFPDATD AEIEENEFCV
ICRDSLFEGS KPKKLSCGHI FHIDCLKSWL VMQQVCPTCS PKRILHYVDP FDGGDPSREL
FAQRRYVSQA AENCDPEPPL AEPEGNAEEW IDPGEPEEAE ETGLAAAQAA AAAAQAQIAA
PRRPPAPAQP GSASSAAAPE NAGLSVLGLA ASSSHEPAPS EFEDLFEPPV EDKAEAREIV
DDEAPIFERP AMALPAVSTG AASSHANGQG FAASEPVQAT AAATAYPLAA SRQAAPSSAP
SSLPPLEEIT NALDRAEEMA KFLREQQDFW MEQVRQIQAG RCHGQATPGS ENGRLGKSSG
SESDPRRRAE ILRTSDLFVE LRGKASWHGA AALMSNIVID FEVLPEDGPA DRSAPQVCNE
LLRQLQDPSS ELRRGEFGRY AANASISIDG GPLTGAESPG EIPPLVPTTS LAEPPPVGPG
GGKPGVTLVT VTGQYHSRPL SGLDPTGREG LSNAELLERI AQLERQITRS AVGGPGTSFG
GPQVVNYMER LQQVRDEMSQ GYTKLSSSVS WEEDLPPPSL PNTGRGLVDF EVVNYMERLQ
QVRDEMSQGY TKLSSSVSWE EDLPPPSLPN TGRGLVDFEA AEQELRTEQE AGRGNKLKVE
QMEQKLKALE EGERKGPPPA EYPHPLVEEA EEERRQKVIK SPTAYTLANL ASAFWLLQKG
RENEKPSFQS CNHLDYFRKE RGRTTKPRVF DDGNFNLESP ASVKAVTEVT GFDRKAMELG
MQCCSAPLAV PPLKLTGTSV EPYEALVAQG VTLMDREQLL SHAKEMWMKE NVRASKLADA
LTAAEDKLAD QERRLADVTA KYTEAQQEVR QLQHLLGSST SGLTGAVPGD MSSSGFLDIP
PSDGRNGYAK ERVPGSHLTQ VNRSSHFLGK QKVAASSESL RCGGLDLPEN LG
//
