ID A0A2G5ELC9_AQUCA Unreviewed; 788 AA.
AC A0A2G5ELC9;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
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_00700713v1 {ECO:0000313|EMBL:PIA56553.1};
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:PIA56553.1, ECO:0000313|Proteomes:UP000230069};
RN [1] {ECO:0000313|EMBL:PIA56553.1, 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}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; KZ305024; PIA56553.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5ELC9; -.
DR STRING; 218851.A0A2G5ELC9; -.
DR InParanoid; A0A2G5ELC9; -.
DR OrthoDB; 1342875at2759; -.
DR Proteomes; UP000230069; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd16702; RING_CH-C4HC3_MARCH6; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR011016; Znf_RING-CH.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR13145:SF0; E3 UBIQUITIN-PROTEIN LIGASE MARCHF6; 1.
DR PANTHER; PTHR13145; SSM4 PROTEIN; 1.
DR Pfam; PF12906; RINGv; 1.
DR SMART; SM00744; RINGv; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
DR PROSITE; PS51292; ZF_RING_CH; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Reference proteome {ECO:0000313|Proteomes:UP000230069};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT TRANSMEM 135..158
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 178..201
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 332..355
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 436..456
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 477..501
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 535..554
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 686..713
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 733..754
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 44..105
FT /note="RING-CH-type"
FT /evidence="ECO:0000259|PROSITE:PS51292"
FT DOMAIN 52..99
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 220..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 788 AA; 87648 MW; 56D036A6F35BFBE5 CRC64;
MEIAVETSNS NSTDEERINS NSIESVGTSS SSNKKIEISG KYEEEDDEED VCRICRNTGD
VENPLRYPCA CSGSIKFVHQ DCLLQWLNHS NARKCEVCKH PFSFSPVYAE NAPARLPFQE
FLVGMAMKAC HVLQFVLRLA FVLSVWLLII PFITFWIWRL SFVRSFREAH RLFLTHVSTT
VILTDCLHGF LLSASIVFIF LGATSLRDYF RHLRELGGQD EREDEGDRNG ARAARRPPAP
PNRINDGDGN GEDVGGGQGM AGAGQLIRRN AENVAARLEM QAARLEAHVE QMFDGLDDAD
GAEDVPFDEL VGMQGPVFHL VENAFTVLAS NLIFLGVVIF IPFSFGRIVV HYLSWLFSVT
TNPLLSAAVP LTESALSLAN TTLKSALIDN HVVEAVAETL KANITELDRV SNSIGNPLSA
DILNGAVVGT SRLSDVTTLA VGYMFQISLV VLYLEMLGKT IPQRVEFFSS SPLASSLLHW
IVGIVYMLQI SIFVSLLRGV LRSGVLYFLR DPADPNYNPF RDLIDDPVHK HARRVLLSVA
VYGSLIVVLV FLPVKFAMRL APTVFPLDIS VSDPFTEIPA DMLLFQICIP FAIEHFKLRT
TIKAFLRQWF TAVGWALGLN DFLLPRPEDS RQEAGNEEGN DRLRDAALMA PEVQNRVMLT
SGNDDDTEEY DAEEHTNSEY GFILRIVLLL ILAWMTLLLC NAALIVVPIS LGRALFSTIP
ILPITHGIKC NDLYSFIIGS YAIWAILAGA RYCIEHVKTR RAGILLNRVW KWSAIVLKSS
GLLAIWVK
//
