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Database: UniProt
Entry: A0A7E6FUP9_OCTVU
LinkDB: A0A7E6FUP9_OCTVU
Original site: A0A7E6FUP9_OCTVU 
ID   A0A7E6FUP9_OCTVU        Unreviewed;      1262 AA.
AC   A0A7E6FUP9;
DT   10-FEB-2021, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2021, sequence version 1.
DT   18-JUN-2025, entry version 22.
DE   RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE            EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN   Name=LOC115223791 {ECO:0000313|RefSeq:XP_036371365.1,
GN   ECO:0000313|RefSeq:XP_036371369.1, ECO:0000313|RefSeq:XP_036371371.1,
GN   ECO:0000313|RefSeq:XP_036371374.1};
OS   Octopus vulgaris (Common octopus).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Cephalopoda;
OC   Coleoidea; Octopodiformes; Octopoda; Incirrata; Octopodidae; Octopus.
OX   NCBI_TaxID=6645 {ECO:0000313|Proteomes:UP000515154, ECO:0000313|RefSeq:XP_036371365.1};
RN   [1] {ECO:0000313|RefSeq:XP_036371365.1, ECO:0000313|RefSeq:XP_036371369.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (MAR-2025) to UniProtKB.
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};
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DR   RefSeq; XP_036371365.1; XM_036515472.1.
DR   RefSeq; XP_036371369.1; XM_036515476.1.
DR   RefSeq; XP_036371371.1; XM_036515478.1.
DR   RefSeq; XP_036371374.1; XM_036515481.1.
DR   Proteomes; UP000515154; Linkage group LG2.
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   CDD; cd16774; RING-HC_RBR_ANKIB1; 1.
DR   FunFam; 1.25.40.20:FF:000040; RBR-type E3 ubiquitin transferase; 1.
DR   FunFam; 3.30.40.10:FF:000129; 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; IPR047563; RING-HC_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; PF12796; Ank_2; 1.
DR   Pfam; PF19422; Ariadne; 1.
DR   Pfam; PF01485; IBR; 1.
DR   Pfam; PF22191; IBR_1; 1.
DR   SMART; SM00248; ANK; 2.
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; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000515154};
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          133..165
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   DOMAIN          303..575
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51873"
FT   DOMAIN          307..353
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          909..943
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1179..1199
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1238..1262
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        930..943
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1182..1199
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1238..1247
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1262 AA;  142491 MW;  1FD767389FB28118 CRC64;
     MGSSSSKFRK YLQNGDEIAA LNVYNGNNEF RKSLDPNSSY GDSCNHETPV HYASRHGMRT
     LLRIFLHNHH GNPNKTNSRK ETALHYVCQE RNSQYYTVRQ RRCDCLNLIL QWRGATLKDG
     QTEKVDLAAQ DEKLNTALHY ASSSGLKNCV ELLVQNGSPL FIENVDQLTP CDIAEKNGHG
     DIALFLESKM VFSNEGSQED HEEVVIPVSD TEEYSGLRTQ DLQEVKDQLL VETADMLSVP
     LFTAEALLRN HEWSRETLLE AWMTDPFACC EKCGVTPPPS LYSDQPILPE TLNSPTTSEP
     PEQDAICDIC TCTFMMSEEP VHMPCEHRFC RSCWEQYLNL KIQEGDAHHI TCPGYDCSRL
     VPVDVIENVV SRPMARRYLQ FDIKAFVDSN PSMKWCPYPG CARAVHLPEI ENNTGSNSLL
     STVKIPEDTS RAVDCGNGHY FCWNCLGEAH EPCCCDNWKQ WHQKIAEIKP EQFIPSHYHL
     TGYLVDQQKR SIEYVPNFKQ KINGTEVETE AAANCLWLVT NSKPCPNCKS PIQKNEGCNH
     MKCSKCKYDF CWVCLEQWKR HNSSTGGYFK CNRYEAVKKV EQQTQLLLSE AQARNTQMQE
     LNRFVHFYTR FKNHENSYKL EVPLLNTAKE KMMKLAEAVT DHVSAKLETK FVEDAVHQLL
     KARCVLKCSY VYAYYLDGPG YKKIVFECMQ TELEECTEIL SQIVNRLYLR TPRRRIIEQA
     HIVQRKRHEF IAAIVKGLVP PETPPAMRKR KRKKYSIDLE DEELRKAILA SIQEVDPANP
     WIKDASGRHT NVMAVLDWPD SDSDSSEADT TGTSLKSIGK CSRSGCNRLQ ALNPRTGILH
     DHCSLHCLHL DHQKNNSKQQ DGLPEVFLDE QMELLRALEM SRLQYMRETG LLNIPQANSE
     IDINSLDAQD NGFSTAAPNP GLNESHDTNM SEPLTTNQTD QNSSNEFSHQ LQTMLSNILN
     EAVEQMQSNS SDVWVKRDLS KTENVDPATP VKSPSSNENI LSRSCNSKMS LQSEIATEEL
     EQLGAYAGAQ TKPLPVSPPS TNSCFGIIKD LSVTNILATD EDKTNSFLNK DFSFGIKKNE
     ISTQFQDASI SQSRSKSFDS STELNQSLDI SANNCLKKVE MTADCSDGEN EKPTGKSNFV
     EKAQNTVKHF DTDCVSLLEI SQNLLHMTES LFENSEQDIA VDSSTEGPNE TNTLKSPEAS
     TRDLTVNDLN TVRNGNEDQV EEGYGNQCTA SCDPAVSQEV TTRPNNTTKD HNEESNGQYF
     SV
//
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