ID A0A2T7PWC1_POMCA Unreviewed; 1401 AA.
AC A0A2T7PWC1;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 18-JUN-2025, entry version 30.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN ORFNames=C0Q70_00314 {ECO:0000313|EMBL:PVD37713.1};
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:PVD37713.1, ECO:0000313|Proteomes:UP000245119};
RN [1] {ECO:0000313|EMBL:PVD37713.1, ECO:0000313|Proteomes:UP000245119}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SZHN2017 {ECO:0000313|EMBL:PVD37713.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:PVD37713.1};
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=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.;
CC EC=2.3.2.31; Evidence={ECO:0000256|ARBA:ARBA00001798};
CC -!- SIMILARITY: Belongs to the RBR family. Ariadne subfamily.
CC {ECO:0000256|ARBA:ARBA00005884}.
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:PVD37713.1}.
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DR EMBL; PZQS01000001; PVD37713.1; -; Genomic_DNA.
DR STRING; 400727.A0A2T7PWC1; -.
DR OrthoDB; 69641at2759; -.
DR Proteomes; UP000245119; Linkage Group LG1.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
DR CDD; cd20346; BRcat_RBR_ANKIB1; 1.
DR CDD; cd20361; Rcat_RBR_ANKIB1; 1.
DR FunFam; 1.20.120.1750:FF:000003; RBR-type E3 ubiquitin transferase; 1.
DR FunFam; 3.30.40.10:FF:000019; RBR-type E3 ubiquitin transferase; 1.
DR Gene3D; 1.20.120.1750; -; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR045840; Ariadne.
DR InterPro; IPR031127; E3_UB_ligase_RBR.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR047564; Rcat_RBR_ANKIB1.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR Pfam; PF00023; Ank; 1.
DR Pfam; PF19422; Ariadne; 1.
DR Pfam; PF01485; IBR; 1.
DR Pfam; PF22191; IBR_1; 1.
DR SMART; SM00647; IBR; 2.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF57850; RING/U-box; 2.
DR PROSITE; PS50088; ANK_REPEAT; 1.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000245119};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT REPEAT 45..78
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 281..523
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 285..334
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 687..708
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 845..894
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 962..1030
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1165..1190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1274..1304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1334..1356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1381..1401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 845..856
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 857..870
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 871..882
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 964..978
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 979..1009
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1165..1184
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1280..1295
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1401 AA; 155955 MW; 5DC53E0638FF05A5 CRC64;
MGSASSKFRK HLQNGDEVQA LQLYTTHSDL QKGLDPNCSY GDSHQHETPL HYASRHGMKT
LLRLFLYDKG GNPNKSNAKK ETALHCVCME KNSQFYNVQR RRAECLNMVL SWRGATLQEG
QVEKVDLGAQ DEILVHHGAP LSIENEDNWT PCESAEKSGF DKIARYLESK IVFSTDVDAE
IIPPIEEYCG LRAQDLQEAK DQLLVETADM LSVPLFTAEA LLRNHEWSRE TLLEAWMDNP
VVCCEKCGVT PPSTLFSDKP QVQESLASPL PSPSHASVHS GDVECNICTT VFQAADEPVH
MTCAHQFCRD CWEKYLTMKI QEGDAHHITC PAFNCPMLVP VEIIENIVSR DMALRYLQFD
IKAFVDSNPD MKWCPYPGCG RAVKLPELSG LASSTPRTRN TLPSDTSRSV DCGAAHYFCW
ECQGEAHEPC SCENWVKWQQ KIADIKPEKL SGTEEETEMA ANCLWLVTNS KPCPNCKSPI
QKNEGCNHMK CSKCKHDFCW VCLEQWKRHN SSTGGYFKCN RYEVVKKVEE QAQQVLTDAE
ERNARMQELN RFVHYYTRFK NHENSYKLEE PLLQTAKDKM MKLAEAVTDI ATANAETQFV
EDAVRQLLKA RRVLKCSYIY GYYLDGPGYK KIVFEFMQTE LEECTEILSQ MVNRLYLRTP
RARIIEQARN VQRRRLEFTG AIAKGLVPPE TPPSMKKGKR RRKYSMETED EDLRKAIMAS
IQEVDPGNPW IKDASGRHTN VMALLEWPME DSDDSDSEVS VSALREYGKC HRIGCNRPKA
VNPRTQQIHD YCSRRCKHHH EMLVMQDLEQ QQEEIPEVIL DEHMDLLRAL EMSRLQFLRD
KGLLHEPEDQ GGERNDQQSQ QQQQQQPQIQ ASGSRPRSNS SAGEVKKRSR GMTPLEELDF
ELQRVLELTS SIAQTSGGET AADMMDQSSR GIYLKRKFSQ SRFEENASTI VTRVPNKSVE
DLYQSDSCSK TKASPGQNEG SSLSGHLESS QGGEHPSTSS YYSPASASPE GACSMWSDDQ
RGKPAGGEGV SVEGGMFGLI KDLSVSNIHA DESDKTSEFL AKDFQALFRM CKGSGDMNTS
NEDPVGEKGS CSFQKVSPGY LHQSTFSFNP TLSLDTSAGS SSSTMSFLPP DQECDASTNA
ALLDPHLQNC ASLYQDGSWG SKSFDGSSAS SGGRYKPKSS NIKNKSNHDL DASLATAESG
RLKQERKSGT LSAPVIGASL KKNPTRSSVP VLLSHKRRDG AGEVKEQHIS LLEMAEHLLQ
MTAEMRSHMQ LLHHDKDGAS PSSSSADMSP ESSPSCHPSG SMCLESDIPD QVHLHSSETG
LVRGICDDIG LASEETEGPS AAPQGEGDND DGIVEAAASA SFAQLVMGDE EDSVQLNVVD
SLDFNDDDDD GEGSHRASFF V
//
