ID A0A2T7P7G1_POMCA Unreviewed; 923 AA.
AC A0A2T7P7G1;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU367105};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU367105};
GN ORFNames=C0Q70_08615 {ECO:0000313|EMBL:PVD29364.1};
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:PVD29364.1, ECO:0000313|Proteomes:UP000245119};
RN [1] {ECO:0000313|EMBL:PVD29364.1, ECO:0000313|Proteomes:UP000245119}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SZHN2017 {ECO:0000313|EMBL:PVD29364.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:PVD29364.1};
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 ECO:0000256|RuleBase:RU367105};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|RuleBase:RU367105}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU367105}.
CC -!- SIMILARITY: Belongs to the Deltex family.
CC {ECO:0000256|ARBA:ARBA00009413, ECO:0000256|RuleBase:RU367105}.
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:PVD29364.1}.
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DR EMBL; PZQS01000005; PVD29364.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T7P7G1; -.
DR STRING; 400727.A0A2T7P7G1; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000245119; Miscellaneous, Linkage group lg5.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniRule.
DR CDD; cd02907; Macro_Af1521_BAL-like; 1.
DR Gene3D; 3.30.390.130; -; 1.
DR Gene3D; 3.40.220.10; Leucine Aminopeptidase, subunit E, domain 1; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR039396; Deltex_C.
DR InterPro; IPR039399; Deltex_C_sf.
DR InterPro; IPR039398; Deltex_fam.
DR InterPro; IPR002589; Macro_dom.
DR InterPro; IPR043472; Macro_dom-like.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR12622; DELTEX-RELATED; 1.
DR PANTHER; PTHR12622:SF36; E3 UBIQUITIN-PROTEIN LIGASE DTX3-RELATED; 1.
DR Pfam; PF18102; DTC; 1.
DR Pfam; PF01661; Macro; 1.
DR Pfam; PF13923; zf-C3HC4_2; 1.
DR SMART; SM00506; A1pp; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF52949; Macro domain-like; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51154; MACRO; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|RuleBase:RU367105};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU367105};
KW Reference proteome {ECO:0000313|Proteomes:UP000245119};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU367105};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU367105};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 402..586
FT /note="Macro"
FT /evidence="ECO:0000259|PROSITE:PS51154"
FT DOMAIN 771..809
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 622..653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 695..741
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 748..767
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 695..736
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 923 AA; 100656 MW; F7669E8C7C7A0ADC CRC64;
MTYLNVLKCV ESCSSIEGML TAAGSSSAVA GSASAVVGSA SAVAGSESAV AGSASTSKGE
NLLAQTVQKL QSQSHEMYTV HPLPPEVFTK VQVWVDSKIA ALLLASGVNT DELTNGGGVQ
IGWDEATQEN TLKGKMYEVE WAQKYLSDKC DNHSRMHGTL VSSLIAGRGG VDVIHGVKSL
QLTNGDRVKD MSATGEQYSQ PTEEEWKWSR SNEKVACCSH DCHSLRLPAS KPSFSALSLE
TDKPTATFEN GSIKQNSSLT KEEINYSMYH NDGESKIHSS EHGDMEKLRQ QNSDDASQYL
KSNIGAEGSH LLHEGSARTH WLKEEEDKNM LGVSQSLLPS TMACEISGPS TDHRSKDISD
KVIGAYGGEL SDDELNGAYG GGTLLGSKST ALFLASPVSA DLISRNFSIN SQLKLKIYCE
DIVRVQTDAV VSPANSHLHN IGGVARALEY AAGPEMQDEC CMIVRKMGRL MTTQVVETKA
CGRLGHLKYV FHAVGPIVST DVEQSIYELS ETFFNCLELA EKLHLRSLAF PFISTGIFGM
STDHCVLALI TAVLAYPEMC SCISLQEVHF VHNDVNVVGE AIILADQQLE NEDKESAKQR
LQQGRQLNRL YDAYPHSLST SSLISKKNES SPTPRPSGSL ASRQSVTRAH SFTSRVEDAT
LMKKTAFTDV RPKEEIKTKK SPLLKQTITT RNIKQSVCEP LNTRTVKKSA PESLTNKSSR
VTQESRNSSY SSSRKKPAEM ASKKGRYCKS CSTSDSDTSE AADGEDSDDI CPVCLQKLQS
PKKLKCGHVF CLECIEQAMK FKPRCPKCQY NYGIQTGSQP QSGRMTHRIS PLQHIPGFPR
VGSIIIDYDF PSGVQEMLKK AFDHRLVFTI GDSRTTGAND VITWNDIHHK TSIYGGPESF
GYPDAGYLIR VKEELAAKGI TSP
//
