ID D7MTF6_ARALL Unreviewed; 660 AA.
AC D7MTF6;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=ARALYDRAFT_917551 {ECO:0000313|EMBL:EFH40057.1};
OS Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=81972 {ECO:0000313|Proteomes:UP000008694};
RN [1] {ECO:0000313|Proteomes:UP000008694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694};
RX PubMed=21478890; DOI=10.1038/ng.807;
RA Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M.,
RA Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G.,
RA Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K.,
RA Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J.,
RA Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y.,
RA Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.;
RT "The Arabidopsis lyrata genome sequence and the basis of rapid genome size
RT change.";
RL Nat. Genet. 43:476-481(2011).
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}.
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DR EMBL; GL348720; EFH40057.1; -; Genomic_DNA.
DR RefSeq; XP_002863798.1; XM_002863752.1.
DR AlphaFoldDB; D7MTF6; -.
DR STRING; 81972.D7MTF6; -.
DR EnsemblPlants; scaffold_800951.1; scaffold_800951.1; scaffold_800951.1.
DR GeneID; 9301614; -.
DR Gramene; scaffold_800951.1; scaffold_800951.1; scaffold_800951.1.
DR KEGG; aly:9301614; -.
DR eggNOG; KOG0167; Eukaryota.
DR HOGENOM; CLU_006348_5_1_1; -.
DR OrthoDB; 2721872at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000008694; Unassembled WGS sequence.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd16664; RING-Ubox_PUB; 1.
DR Gene3D; 1.20.930.20; Adaptor protein Cbl, N-terminal domain; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR036537; Adaptor_Cbl_N_dom_sf.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000225; Armadillo.
DR InterPro; IPR045210; RING-Ubox_PUB.
DR InterPro; IPR003613; Ubox_domain.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR23315; U BOX DOMAIN-CONTAINING; 1.
DR PANTHER; PTHR23315:SF49; U-BOX DOMAIN-CONTAINING PROTEIN 15; 1.
DR Pfam; PF00514; Arm; 2.
DR Pfam; PF04564; U-box; 1.
DR SMART; SM00185; ARM; 5.
DR SMART; SM00504; Ubox; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50176; ARM_REPEAT; 3.
DR PROSITE; PS51698; U_BOX; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000008694};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 289..363
FT /note="U-box"
FT /evidence="ECO:0000259|PROSITE:PS51698"
FT REPEAT 421..463
FT /note="ARM"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00259"
FT REPEAT 462..504
FT /note="ARM"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00259"
FT REPEAT 503..545
FT /note="ARM"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00259"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 660 AA; 73927 MW; 224D619571A5A0EF CRC64;
MVIVMDADEE STGDAENLEE EVTAEEPIHD EAVDAVEIHD EEVKNGDDDC DGLVSDIVSV
IEFLDQINGY RKTQQKECFN LVRRLKILIP FLEEIRGFDS PSCRHFVNRL RKVILVAKKL
LETCSNGSKI YMALDSETMM TRFHSIYEKL NRVLVKTPFD ELTISEDVKE EIDALCKQLK
KAKRRTDTQD IELAVDMMVV FSKTDPRNAD SAIIERLAKK LELQTTEDLK TETIAIKSLI
QEKGGLNIET KQHIIELLNK FKKLQGLEAT DILYQPVINK AFTKSTSLIL PHEFLCPITL
EIMLDPVIIA TGQTYEKESI QKWFDAGHKT CPKTRQELDH LSLAPNYALK NLIMQWCEKN
NFKIPEKEAS PHSENEQKDE VSLLVEALSS SHLEEQRRSV KQMRLLAREN PENRVLIANA
GAIPLLVQLL SYPDSGIQEN AVTTLLNLSI DEVNKKLISN EGAIPNIIEI LQNGNREARE
NSAAALFSLS MLDENKVTIG LSNGIPPLVD LLQHGTLRGK KDALTALFNL SLNSANKGRA
IDAGIVQPLL NLLKDRNLGM IDEALSILLL LASHPEGRQA IGQLSFIETL VEFIRQGTPK
NKECATSVLL ELGSNNSSFI LAALQFGVYE YLVEITTSGT NRAQRKANAL IQLISKSEQI
//