ID A0A2T7PXR0_POMCA Unreviewed; 602 AA.
AC A0A2T7PXR0;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=C0Q70_00824 {ECO:0000313|EMBL:PVD38213.1};
OS Pomacea canaliculata (Golden apple snail).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Caenogastropoda; Architaenioglossa; Ampullarioidea; Ampullariidae; Pomacea.
OX NCBI_TaxID=400727 {ECO:0000313|EMBL:PVD38213.1, ECO:0000313|Proteomes:UP000245119};
RN [1] {ECO:0000313|EMBL:PVD38213.1, ECO:0000313|Proteomes:UP000245119}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SZHN2017 {ECO:0000313|EMBL:PVD38213.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:PVD38213.1};
RA Liu C., Liu B., Ren Y., Zhang Y., Wang H., Li S., Jiang F., Yin L.,
RA Zhang G., Qian W., Fan W.;
RT "The genome of golden apple snail Pomacea canaliculata provides insight
RT into stress tolerance and invasive adaptation.";
RL Submitted (APR-2018) 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 -!- 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:PVD38213.1}.
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DR EMBL; PZQS01000001; PVD38213.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T7PXR0; -.
DR STRING; 400727.A0A2T7PXR0; -.
DR Proteomes; UP000245119; Miscellaneous, Linkage group lg1.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR045194; MGRN1/RNF157-like.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR22996; MAHOGUNIN; 1.
DR PANTHER; PTHR22996:SF0; RING-TYPE E3 UBIQUITIN TRANSFERASE; 1.
DR Pfam; PF13920; zf-C3HC4_3; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}; Reference proteome {ECO:0000313|Proteomes:UP000245119};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 238..277
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 498..602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..525
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..591
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 602 AA; 67301 MW; F12C68AAF5CCFB0D CRC64;
MGGERFESPQ PGEYLFGENE DLNFLGNKPV PFPYPVPTGN EPTKTLKSLV YIRKDTLRLV
KAIATEKVPL DHEESNTLYN IEFVFDSDVR CTIRIHYFAI EEVIGGQIVY HPKSAAMSSE
GFHYKRGAAQ LFSQPTHTIN PSKFSDEEWQ YSFEKEIFPI VIHCLVEEEE HAGHSHIMYA
VIEKSPEGSY LIKPLKQKQF VDGLCYLLQE IYGIENKNME RMKHIDPDED VEDSGAECVI
CMSDMRDTLI LPCRHLCLCS MCAESLRYQA SMCPICRVKF RALLQIRAMR KKIPVTGQQQ
VNVSCMKHWQ DDCKNETDEN PVSQEGVPPG FEAISLVEAL NGQVVPQNGQ MEGVTHPIGV
PTPLFTMDKK GHKETKISLS TSIEYQKEMD PAAVIEKKNN EKDEGKEEQG DDVAITTPLS
DVDLTQIVPD VVDRRRSPEK RVLEEDCAVV GQDLPPDIQV THCRANNKKS VEELPSPGWK
AGCQGCKGEI SCQLTAGDMA DDEREDSSET EPEPDYDEDE AEDESYTLSD PRGMMSSELS
VVSGTLSEQT NPEEMEVLQS SEHLILSDTP GSGTESSSFG SNCSSHALLT QGEGEDQRKM
AV
//
