ID A0A2G5DY88_AQUCA Unreviewed; 359 AA.
AC A0A2G5DY88;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 23.
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_01400814v1 {ECO:0000313|EMBL:PIA48482.1};
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:PIA48482.1, ECO:0000313|Proteomes:UP000230069};
RN [1] {ECO:0000313|EMBL:PIA48482.1, 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; KZ305031; PIA48482.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5DY88; -.
DR Proteomes; UP000230069; Unassembled WGS sequence.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0000209; P:protein polyubiquitination; IEA:InterPro.
DR CDD; cd16521; RING-HC_MKRN; 1.
DR Gene3D; 3.30.1370.210; -; 1.
DR Gene3D; 1.20.120.1350; Pneumovirus matrix protein 2 (M2), zinc-binding domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR045072; MKRN-like.
DR InterPro; IPR041367; Znf-CCCH_4.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR11224; MAKORIN-RELATED; 1.
DR PANTHER; PTHR11224:SF10; RING-TYPE E3 UBIQUITIN TRANSFERASE; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR Pfam; PF00642; zf-CCCH; 1.
DR Pfam; PF14608; zf-CCCH_2; 1.
DR Pfam; PF18044; zf-CCCH_4; 2.
DR SMART; SM00184; RING; 1.
DR SMART; SM00356; ZnF_C3H1; 4.
DR SUPFAM; SSF90229; CCCH zinc finger; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50103; ZF_C3H1; 4.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00723}; Reference proteome {ECO:0000313|Proteomes:UP000230069};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00723};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00723}.
FT DOMAIN 1..28
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 29..56
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 137..164
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 206..264
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 293..322
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT ZN_FING 1..28
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 29..56
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 137..164
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 293..322
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
SQ SEQUENCE 359 AA; 40395 MW; BCE97CF964390BCA CRC64;
MSNRVLCKFF VHGACLKGDN CEFSHDWKDQ TNNICTFYQR GVCSYGSRCR YEHVKASRPQ
TTISSSSTIS VRPKASNPVE VTSPRAFVAG EANSISSLPA ELSALSRPFF PPAWKQDSID
HNLQDDDIVG EVTNVDPADR PICSFAAAGE CPRGERCPHI HGDLCPTCGK HCLHPYRPDE
RDEHIITCER KKKQLDALKY SQEIECSVCL DRVLSKPTAA ERKFGLLSEC DHPFCISCIR
NWRSNSPTSG MDINSALRAC PICRKLSYFV IPSVIWYANQ EEKQEIVNNY KAKLSSIDCR
YFDFGNGSCP FGTSCFYKHA YRDGRLEEVA LRHLGAEDGN TVIAKDIRLS DFLSNLRLR
//
