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Database: UniProt
Entry: A0A8J5D515_CHIOP
LinkDB: A0A8J5D515_CHIOP
Original site: A0A8J5D515_CHIOP 
ID   A0A8J5D515_CHIOP        Unreviewed;      1596 AA.
AC   A0A8J5D515;
DT   25-MAY-2022, integrated into UniProtKB/TrEMBL.
DT   25-MAY-2022, sequence version 1.
DT   18-JUN-2025, entry version 17.
DE   RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE            EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN   Name=ankib1 {ECO:0000313|EMBL:KAG0729195.1};
GN   ORFNames=GWK47_030836 {ECO:0000313|EMBL:KAG0729195.1};
OS   Chionoecetes opilio (Atlantic snow crab) (Cancer opilio).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC   Malacostraca; Eumalacostraca; Eucarida; Decapoda; Pleocyemata; Brachyura;
OC   Eubrachyura; Majoidea; Majidae; Chionoecetes.
OX   NCBI_TaxID=41210 {ECO:0000313|EMBL:KAG0729195.1, ECO:0000313|Proteomes:UP000770661};
RN   [1] {ECO:0000313|EMBL:KAG0729195.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=MADBK_172401_WGS {ECO:0000313|EMBL:KAG0729195.1};
RC   TISSUE=Digestive gland {ECO:0000313|EMBL:KAG0729195.1};
RA   Jeong J.-H., Ryu S.;
RT   "The High-quality genome of the commercially important snow crab,
RT   Chionoecetes opilio.";
RL   Submitted (JUL-2020) 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:KAG0729195.1}.
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DR   EMBL; JACEEZ010001461; KAG0729195.1; -; Genomic_DNA.
DR   OrthoDB; 69641at2759; -.
DR   Proteomes; UP000770661; Unassembled WGS sequence.
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; 1.25.40.20:FF:000040; 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; -; 2.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2.
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; 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   PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR   Pfam; PF00023; Ank; 1.
DR   Pfam; PF12796; Ank_2; 1.
DR   Pfam; PF01485; IBR; 1.
DR   Pfam; PF22191; IBR_1; 1.
DR   SMART; SM00248; ANK; 3.
DR   SMART; SM00647; IBR; 2.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF57850; RING/U-box; 3.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 2.
DR   PROSITE; PS51873; TRIAD; 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:UP000770661};
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   REPEAT          133..165
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   DOMAIN          327..571
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51873"
FT   DOMAIN          331..382
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          1238..1267
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1314..1334
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1520..1596
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1525..1540
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1541..1567
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1568..1581
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1596 AA;  176777 MW;  83FF52418CE3FFC9 CRC64;
     MGSASSKFKK YLQHGDEFAA MQVFQSSPEL RSNLDPSASY GESHSHNTPL HYAARHGMKH
     LLRTFLSDLG GNPNKKNADD ETAVHCVCRV GQAKSPSAED RRAACIVMIL QWRGPLLQDG
     EKERVQLNAQ DKKGNTALHY SSASGLQKCV ELLVAQGAGL FVENRDRLTP CDLAVRLAHH
     DVATYLESCM VFADSCDGIN ESELIGHDGE ADGDNEVYSG LRAQDLQEAK DQLLVETADM
     LHIPLFTAEA LLRDNEWSKA LLLEKWMTNA VQCCEEAGIA PPASALQLVA SSPPLLSPSP
     PCSVISPPLP PHIPAGLGEQ DEGGREGKNL CEICYGEMRC WELQEHGGAS CQHQFCATCW
     ESYLSLKIQE GGAHHILCPA VRCNILVDVD FIEKMVSPEI ARKYLQFDIQ AFVDRNKTIK
     WCPLPGCGRA VKFPEAELET QPFYFPNTKP PPKTSHAVDC GNGHFFCWEC LGEAHSPSGC
     EQWVEWQGKV AEVKPEELRI SSGETEDAAN FLWLVTNSKP CPNCKSPIQK NEGCNHMKCS
     KCKFDFCWVC LESWKKHSSA TGGYFRCNRF DAQGKADEKL GVMLSEVSVV LVLVLLVVLV
     LLLPPPLLCY GHSCCCCCCC CRCLAANLNA MLSCNTYFKY TFRTTLVAII RTFVLLCDGV
     EQATMRNHQM QELNRFIHYY TRFKNHQNSL KMEEPLLKSA RDKMEVLATS LPSQEQQGQG
     RSWEVKVKGG RMGGREATER EREYDRDISF NVSCVLTASV EKGTRFVEEG VKELLKARRV
     LCGSYVYGYY LEDNGYNKTI FEYMQNELEE VTEKLSEMVA RQYLVTPRRQ IIATTLLARR
     RRHKFVRAVS RGLLPPETPP ALRRARKRRL PGLVGMDPPD DQMENVEAMG RTLDPSQPWV
     KDSRGCHTNL AALLDWPDLD SDEEESSLNQ ALTLTLLGKC NRKSCPRPRA RNPRTGTIHD
     YCSLHCAQRA KYLPEQVVPP LSTSLPLTTS SLPYPSPGDG EPSSSSSWEV CDSSMELLIA
     LEMSRLQMIE DEARRRLSWL QEHSREQGWD GAGDARPHQG CIEVPVVPGT SVAGSSIFTY
     EVACGSRGQG GGGGGHSEAS AWIRPELGEG AISFQPSSAE IAVDYFLKKL ANKEISQRNL
     NVEKHWAENK KVEKDLLCFP NASTPGEMED GLFLYGDLHE NSRLLPPIDL RRDLRRSQSL
     GDLKSCEESL CLFDADHAHL DHPEETLRRQ FAAAAAAARA SMEDEGTESG GDVENTDPGG
     ASEIIGDMDS PLMDLEVRGI LSHLEECSGN VAGGEGSGGV AGQEPSFQLV VDEGTDKDES
     NSTEQSSSAP AANIKGLRIH ISHSNKLEGQ SSNEYESETG IPNSPTLYIS GVSICRSPEP
     RSPKVHHREA RSPSLTLPLC CTPEPRLRLE GRLDTSPLPI YSRSRSSSLV VPSSSNFSPR
     VCARASGTSL HLSSISLQAT RATSPFLTGE LRVTRSASET EKGRLVFQFP KSPTDGALSS
     VLHVEESNLS SDDFHEALFL GKSPKPVKKK RSKNDRKKGA KERSKGERRE KKEARGRTKA
     RTMEKRGKKE KIARKREKVK RSPPLYDAEN TEALKW
//
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