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Database: UniProt
Entry: A0A0D9V5Z4_9ORYZ
LinkDB: A0A0D9V5Z4_9ORYZ
Original site: A0A0D9V5Z4_9ORYZ 
ID   A0A0D9V5Z4_9ORYZ        Unreviewed;      1041 AA.
AC   A0A0D9V5Z4;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
OS   Leersia perrieri.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Leersia.
OX   NCBI_TaxID=77586 {ECO:0000313|EnsemblPlants:LPERR01G27300.1, ECO:0000313|Proteomes:UP000032180};
RN   [1] {ECO:0000313|EnsemblPlants:LPERR01G27300.1, ECO:0000313|Proteomes:UP000032180}
RP   NUCLEOTIDE SEQUENCE.
RA   Wing R.A.;
RT   "Oryza genome evolution.";
RL   Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:LPERR01G27300.1, ECO:0000313|Proteomes:UP000032180}
RP   NUCLEOTIDE SEQUENCE.
RA   Yu Y., Lee S., de Baynast K., Wissotski M., Liu L., Talag J.,
RA   Goicoechea J., Angelova A., Jetty R., Kudrna D., Golser W., Rivera L.,
RA   Zhang J., Wing R.;
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EnsemblPlants:LPERR01G27300.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
CC   -!- FUNCTION: Seed storage protein. {ECO:0000256|ARBA:ARBA00003839,
CC       ECO:0000256|RuleBase:RU003681}.
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   -!- SUBUNIT: Hexamer; each subunit is composed of an acidic and a basic
CC       chain derived from a single precursor and linked by a disulfide bond.
CC       {ECO:0000256|ARBA:ARBA00011818, ECO:0000256|RuleBase:RU003681}.
CC   -!- SIMILARITY: Belongs to the 11S seed storage protein (globulins) family.
CC       {ECO:0000256|ARBA:ARBA00007178, ECO:0000256|RuleBase:RU003681}.
CC   -!- SIMILARITY: Belongs to the SINA (Seven in absentia) family.
CC       {ECO:0000256|ARBA:ARBA00009119}.
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DR   AlphaFoldDB; A0A0D9V5Z4; -.
DR   STRING; 77586.A0A0D9V5Z4; -.
DR   EnsemblPlants; LPERR01G27300.1; LPERR01G27300.1; LPERR01G27300.
DR   Gramene; LPERR01G27300.1; LPERR01G27300.1; LPERR01G27300.
DR   eggNOG; KOG3002; Eukaryota.
DR   HOGENOM; CLU_292624_0_0_1; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000032180; Chromosome 1.
DR   GO; GO:0045735; F:nutrient reservoir 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:0048316; P:seed development; IEA:UniProt.
DR   CDD; cd02243; cupin_11S_legumin_C; 2.
DR   CDD; cd02242; cupin_11S_legumin_N; 2.
DR   CDD; cd16571; RING-HC_SIAHs; 1.
DR   Gene3D; 2.60.120.10; Jelly Rolls; 4.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR022379; 11S_seedstore_CS.
DR   InterPro; IPR006044; 11S_seedstore_pln.
DR   InterPro; IPR006045; Cupin_1.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR011051; RmlC_Cupin_sf.
DR   InterPro; IPR049548; Sina-like_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR013010; Znf_SIAH.
DR   PANTHER; PTHR31189:SF84; GLUTELIN TYPE-B 2; 1.
DR   PANTHER; PTHR31189; OS03G0336100 PROTEIN-RELATED; 1.
DR   Pfam; PF00190; Cupin_1; 4.
DR   Pfam; PF21362; Sina_RING; 1.
DR   Pfam; PF21361; Sina_ZnF; 1.
DR   PRINTS; PR00439; 11SGLOBULIN.
DR   SMART; SM00835; Cupin_1; 4.
DR   SUPFAM; SSF51182; RmlC-like cupins; 2.
DR   PROSITE; PS00305; 11S_SEED_STORAGE; 2.
DR   PROSITE; PS51081; ZF_SIAH; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW   ECO:0000256|RuleBase:RU003681};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00455};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032180};
KW   Seed storage protein {ECO:0000256|ARBA:ARBA00023129,
KW   ECO:0000256|RuleBase:RU003681}; Signal {ECO:0000256|RuleBase:RU003681};
KW   Storage protein {ECO:0000256|ARBA:ARBA00022761,
KW   ECO:0000256|RuleBase:RU003681};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00455};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00455}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|RuleBase:RU003681"
FT   CHAIN           25..1041
FT                   /note="RING-type E3 ubiquitin transferase"
FT                   /evidence="ECO:0000256|RuleBase:RU003681"
FT                   /id="PRO_5007746256"
FT   DOMAIN          570..628
FT                   /note="SIAH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51081"
SQ   SEQUENCE   1041 AA;  117115 MW;  51422D25C6B11DC6 CRC64;
     MSAMKLPVVF SVICLFLLCH GSLAQFQSQS TSQWQSSRRG SPRECRFDQL QALEPVRTVR
     SQAGCFNVPE YLLCVELLNL EVLLPHYSNG ATLVYIIQGR GITGPTFPGC PETYQQQFQQ
     SEQVQSFEAQ SQSHKFRDEH QKIHRFRQGD VVALPAGVAH WCYNDGEVPI VAIYVTDIHN
     SANQLDPRHR DFFLAGNNKI GQQFYRSETR ESSKNIFGGF SVELLSEAIG ISSGVARQLQ
     CQNDQRGEIV RVERGLELLQ PYASLQEQEQ EQQQQQQVQL SEYGQTQYEQ KQLRGGCSNG
     LDETFCTMRV RQNIDNPNLA DTYNPRAGRI TYLNAKKFPI LNLLQMSAVK VNLYQNALLS
     PFWNINAHSI VYITQGRARV QVVNNNGKTV FDGELRHGQL LIVPQHHVVL KKAQREGCSY
     IAFKTNPNSI VSHIAGKNSI FRALPNDVVA NAYRISREEA QRIKHNRGDE SGVFTPSHAY
     KSFQDIMTQE ETQPMEQSAG HRSSVVGIDL ELLDCTICSH PLKRPVFQCR VGHVLCSSCH
     GKLPDKKNCH TCSRDTGYDR CYAVEKILES IRVPCRNAAY GCDTKTACHE RESHEDACPH
     APCFCPEPRC GFAGATPALL AHLTGVHGCP PSRGITGPTF PGCPETYQQQ FQQSEQVQSF
     EAQSQSHKFR DEHQKIHRFR QGDVVALPAG VAHWCYNDGE VPIVAIYVTD IHNSANQLDP
     RHRDFFLAGN NKIGQQFYRS ETRESSKNIF GGFSVELLSE AFGISSGVAR QLQCQNDQRG
     EIVRVERGLE LLQPYASLQE QEQQQQQQVQ PSEYGQTQYE QKQLRGGCSN GLDETFCTMR
     VRQNIDNPNL ADTYNPRAGR ITYLNAQKFP ILNLLQMSAV KVNLYQNALL SPFWNINAHS
     IVYITQGRAR VQVVNNNGKT VFDGELRHGQ LLIIPQHHVV LKKAQREGCS YIAFKTNPNS
     IVSHIAGKNS IFRALPNDVV ANAYHISREE AKRIKHNRGD ESGVFTPSHA YRSFQDIMTA
     SSPAPAVETG ALQRCIKVRR G
//
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