UniProt: A0A445BX93

Database: UniProt
Entry: A0A445BX93_ARAHY

LinkDB:  A0A445BX93_ARAHY 
Original site:  A0A445BX93_ARAHY

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Ontology (5)   
   GO (5)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (9)   
   InterPro (5)   
   Pfam (1)   
   PROSITE (2)   
   SMART (1)   
All databases (16)   

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ID   A0A445BX93_ARAHY        Unreviewed;       344 AA.
AC   A0A445BX93;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   RecName: Full=E3 ubiquitin-protein ligase RMA {ECO:0000256|RuleBase:RU369090};
DE            EC=2.3.2.27 {ECO:0000256|RuleBase:RU369090};
DE   AltName: Full=Protein RING membrane-anchor {ECO:0000256|RuleBase:RU369090};
DE   AltName: Full=RING-type E3 ubiquitin transferase RMA {ECO:0000256|RuleBase:RU369090};
GN   ORFNames=Ahy_A08g039783 {ECO:0000313|EMBL:RYR43359.1};
OS   Arachis hypogaea (Peanut).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   dalbergioids sensu lato; Dalbergieae; Pterocarpus clade; Arachis.
OX   NCBI_TaxID=3818 {ECO:0000313|EMBL:RYR43359.1, ECO:0000313|Proteomes:UP000289738};
RN   [1] {ECO:0000313|EMBL:RYR43359.1, ECO:0000313|Proteomes:UP000289738}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Fuhuasheng {ECO:0000313|Proteomes:UP000289738};
RC   TISSUE=Leaves {ECO:0000313|EMBL:RYR43359.1};
RA   Chen X.;
RT   "Sequencing of cultivated peanut Arachis hypogaea provides insights into
RT   genome evolution and oil improvement.";
RL   Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: E3 ubiquitin-protein ligase. {ECO:0000256|RuleBase:RU369090}.
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         ECO:0000256|RuleBase:RU369090};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|RuleBase:RU369090}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|RuleBase:RU369090}; Single-pass type IV membrane protein
CC       {ECO:0000256|RuleBase:RU369090}.
CC   -!- DOMAIN: The RING-type zinc finger domain is responsible for E3 ligase
CC       activity. {ECO:0000256|RuleBase:RU369090}.
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:RYR43359.1}.
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DR   EMBL; SDMP01000008; RYR43359.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A445BX93; -.
DR   STRING; 3818.A0A445BX93; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000289738; Chromosome a08.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd16745; RING-HC_AtRMA-like; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR045103; RNF5/RNF185-like.
DR   InterPro; IPR018957; Znf_C3HC4_RING-type.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR12313:SF59; E3 UBIQUITIN-PROTEIN LIGASE RMA1; 1.
DR   PANTHER; PTHR12313; E3 UBIQUITIN-PROTEIN LIGASE RNF5-RELATED; 1.
DR   Pfam; PF00097; zf-C3HC4; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Endoplasmic reticulum {ECO:0000256|RuleBase:RU369090};
KW   Membrane {ECO:0000256|RuleBase:RU369090};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU369090};
KW   Reference proteome {ECO:0000313|Proteomes:UP000289738};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU369090};
KW   Transmembrane {ECO:0000256|RuleBase:RU369090};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU369090};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|RuleBase:RU369090};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU369090};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   TRANSMEM        305..326
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU369090"
FT   DOMAIN          124..173
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
SQ   SEQUENCE   344 AA;  38153 MW;  0F278C376D2A8A2C CRC64;
     MHNTTYKIEI LAIISYSCGA LGKRSSCASD TQSIYLDLKK FTNYKGGAQV AVIGGILTIE
     YDSGTAIIHC RKAKRMDLHQ YFEGGMPQMD YFEDNSSLEM WKCASDSDAI ADSDGNASGG
     GFECNICLEC VQDPVVTLCG HLYCWPCIYK WLNFRNISSE IGEKRKPQCP VCKSEISQSS
     LVPLYGRGQA SSASEDKAHQ AGVVIPRRPL GPGSSSTANV SQPTSRVYHS HYPDPSQQFN
     SIPGSYSSPL TNSFNTTYGI IGETIYARVF GNQVTNIYTY PNSYHLAGNN NPRIRRYLME
     ADRSLSRICF FLFCCTWSSF VMIITVRHIR SKGRVRSATK AITI
//

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