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Database: UniProt
Entry: A0A0K9P548_ZOSMR
LinkDB: A0A0K9P548_ZOSMR
Original site: A0A0K9P548_ZOSMR 
ID   A0A0K9P548_ZOSMR        Unreviewed;       366 AA.
AC   A0A0K9P548;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN   ORFNames=ZOSMA_417G00010 {ECO:0000313|EMBL:KMZ63325.1};
OS   Zostera marina (Eelgrass).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Zosteraceae; Zostera.
OX   NCBI_TaxID=29655 {ECO:0000313|EMBL:KMZ63325.1, ECO:0000313|Proteomes:UP000036987};
RN   [1] {ECO:0000313|Proteomes:UP000036987}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Finnish {ECO:0000313|Proteomes:UP000036987};
RX   PubMed=26814964; DOI=10.1038/nature16548;
RA   Olsen J.L., Rouze P., Verhelst B., Lin Y.-C., Bayer T., Collen J.,
RA   Dattolo E., De Paoli E., Dittami S., Maumus F., Michel G., Kersting A.,
RA   Lauritano C., Lohaus R., Toepel M., Tonon T., Vanneste K., Amirebrahimi M.,
RA   Brakel J., Bostroem C., Chovatia M., Grimwood J., Jenkins J.W.,
RA   Jueterbock A., Mraz A., Stam W.T., Tice H., Bornberg-Bauer E., Green P.J.,
RA   Pearson G.A., Procaccini G., Duarte C.M., Schmutz J., Reusch T.B.H.,
RA   Van de Peer Y.;
RT   "The genome of the seagrass Zostera marina reveals angiosperm adaptation to
RT   the sea.";
RL   Nature 530:331-335(2016).
CC   -!- FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination and
CC       subsequent proteasomal degradation of target proteins. E3 ubiquitin
CC       ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the
CC       form of a thioester and then directly transfers the ubiquitin to
CC       targeted substrates. It probably triggers the ubiquitin-mediated
CC       degradation of different substrates. {ECO:0000256|ARBA:ARBA00024004}.
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   -!- SIMILARITY: Belongs to the SINA (Seven in absentia) family.
CC       {ECO:0000256|ARBA:ARBA00009119}.
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:KMZ63325.1}.
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DR   EMBL; LFYR01001250; KMZ63325.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0K9P548; -.
DR   STRING; 29655.A0A0K9P548; -.
DR   OrthoDB; 395309at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000036987; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR044286; SINL_plant.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR013010; Znf_SIAH.
DR   PANTHER; PTHR46632:SF16; E3 UBIQUITIN-PROTEIN LIGASE SINA-LIKE 10; 1.
DR   PANTHER; PTHR46632; E3 UBIQUITIN-PROTEIN LIGASE SINA-LIKE 4; 1.
DR   Pfam; PF21361; Sina_ZnF; 1.
DR   SUPFAM; SSF49599; TRAF domain-like; 1.
DR   PROSITE; PS51081; ZF_SIAH; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00455};
KW   Reference proteome {ECO:0000313|Proteomes:UP000036987};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00455};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00455}.
FT   DOMAIN          196..254
FT                   /note="SIAH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51081"
FT   REGION          62..83
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   366 AA;  40761 MW;  9766EB3852FB3037 CRC64;
     MCLFLIKFSK IISYIDLRVS FESFWVYRAV FRDEVKIGSS LSGTSKPEKE IASPCKRKCQ
     ELEGGDKGKK ARPSIGTSKP EKEIASLGKR NCQEFEGAEK GKIGHSSPRT SKSEKKIVSL
     AIEGADKQPK EVLDCIIDSD LLDCMVCYEP LIGSIFQCKN GYIVCQTSCK KINRRCPTCK
     CTIGVRNLVL EHIINSIQVR CPYAMNGCAE VFSFCDRQSH AKNCHHAPLS CPFESCSFDG
     CNAELFNHIK DAHAYTEACT GEYVNLAIKI GKQNCLLGDD CSIYLIVVKK QSSAFCILVL
     CISSLTDYKI KLYGNGNSKL SFSGNVPTIK EIVDDHALSS LDNNMLVTYT MYDVDTHHID
     LQIRFI
//
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