ID A0A2G5DTG2_AQUCA Unreviewed; 636 AA.
AC A0A2G5DTG2;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 28-JAN-2026, entry version 29.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=AQUCO_01500384v1 {ECO:0000313|EMBL:PIA46801.1};
OS Aquilegia coerulea (Rocky mountain columbine).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Ranunculales; Ranunculaceae; Thalictroideae;
OC Aquilegia.
OX NCBI_TaxID=218851 {ECO:0000313|EMBL:PIA46801.1, ECO:0000313|Proteomes:UP000230069};
RN [1] {ECO:0000313|EMBL:PIA46801.1, ECO:0000313|Proteomes:UP000230069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Goldsmith {ECO:0000313|Proteomes:UP000230069};
RA Hodges S., Kramer E., Nordborg M., Tomkins J., Borevitz J., Derieg N.,
RA Yan J., Mihaltcheva S., Hayes R.D., Rokhsar D.;
RT "WGS assembly of Aquilegia coerulea Goldsmith.";
RL Submitted (SEP-2017) 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}.
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DR EMBL; KZ305032; PIA46801.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5DTG2; -.
DR STRING; 218851.A0A2G5DTG2; -.
DR InParanoid; A0A2G5DTG2; -.
DR OrthoDB; 7537227at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000230069; Unassembled WGS sequence.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd21037; MLKL_NTD; 1.
DR CDD; cd16664; RING-Ubox_PUB; 1.
DR FunFam; 1.20.930.20:FF:000002; RING-type E3 ubiquitin transferase; 1.
DR FunFam; 1.25.10.10:FF:000082; RING-type E3 ubiquitin transferase; 1.
DR FunFam; 3.30.40.10:FF:000335; RING-type E3 ubiquitin transferase; 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; IPR058678; ARM_PUB.
DR InterPro; IPR000225; Armadillo.
DR InterPro; IPR059179; MLKL-like_MCAfunc.
DR InterPro; IPR057623; PUB12-19-like_N.
DR InterPro; IPR045210; RING-Ubox_PUB.
DR InterPro; IPR003613; Ubox_domain.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR23315:SF49; RING-TYPE E3 UBIQUITIN TRANSFERASE; 1.
DR PANTHER; PTHR23315; U BOX DOMAIN-CONTAINING; 1.
DR Pfam; PF25598; ARM_PUB; 1.
DR Pfam; PF25368; PUB10_N; 1.
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; 2.
DR PROSITE; PS51698; U_BOX; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000230069};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 250..324
FT /note="U-box"
FT /evidence="ECO:0000259|PROSITE:PS51698"
FT REPEAT 385..427
FT /note="ARM"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00259"
FT REPEAT 467..509
FT /note="ARM"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00259"
SQ SEQUENCE 636 AA; 70967 MW; 0237C8D5D3B0F20A CRC64;
MEESLEKKME VIKGLMEVIE EMGMFNDYRR TQRKECFSLV RRIKLLVPLL EEISDGNKQI
PIEALNCLVN LKKVFVSAKK LLKNCNKGSK IFLAIESEVI MERFHSVYDK LNQALDDMPY
DELGIADEVK EQIELLRTQL RRAKTRTDTQ DIELAVDMMV VFSKKDDRNA DTAILERLAN
KLELRTMTDL KVETMAVRKL IKERNGRSAE SSQHIIDLLS KFKQVAGVSD SKLLSVLAAP
KNLEKCSSLA IPNEFLCPIT LEIMTDPVIV ASGQTYDRES IQKWFQSDHK TCPKTRQTLS
HLSLAPNFAL RNLIMQWCDK NNFKLPKKEF CLDTTGTSNK CKEEISLLIQ DLCSSQLDVQ
IKAVMKIRIL SKENPDNRVM IANCGGIPPL VQLLSFPDSN IQEHTVTALL NLSIDEVNKR
HIASAGAIPA IIAILQNGKI EARENSAACL FSLSVIDENK VTIGCSNGIP PLVDLLQNGT
VRGKKDAATA LFNLALNQAN KTRAIKAGIV KPLIQLLLDR NLGMADEALS ILLLVASHPE
GRTTIGQLSF IETLVEFIKA GTPKNKECAI AVLLELGKHD SSFILAALQF GVYDHLAEVA
RSGTNRAQRK SNSLLQLMTK CEHIPQSCLH SSYAHK
//
