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Database: UniProt
Entry: S4RY73_PETMA
LinkDB: S4RY73_PETMA
Original site: S4RY73_PETMA 
ID   S4RY73_PETMA            Unreviewed;       788 AA.
AC   S4RY73;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   18-JUN-2025, entry version 69.
DE   RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE            EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
OS   Petromyzon marinus (Sea lamprey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Cyclostomata;
OC   Hyperoartia; Petromyzontiformes; Petromyzontidae; Petromyzon.
OX   NCBI_TaxID=7757 {ECO:0000313|Ensembl:ENSPMAP00000010164.1};
RN   [1] {ECO:0000313|Ensembl:ENSPMAP00000010164.1}
RP   IDENTIFICATION.
RG   Ensembl;
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};
CC   -!- SIMILARITY: Belongs to the RBR family. Ariadne subfamily.
CC       {ECO:0000256|ARBA:ARBA00005884}.
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DR   AlphaFoldDB; S4RY73; -.
DR   STRING; 7757.ENSPMAP00000010164; -.
DR   Ensembl; ENSPMAT00000010209.1; ENSPMAP00000010164.1; ENSPMAG00000009240.1.
DR   GeneTree; ENSGT00940000165758; -.
DR   HOGENOM; CLU_009823_1_0_1; -.
DR   OMA; GPMEDPW; -.
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; 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; -; 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; IPR048962; ARIH1-like_UBL.
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; IPR027370; Znf-RING_euk.
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; PF12796; Ank_2; 1.
DR   Pfam; PF19422; Ariadne; 1.
DR   Pfam; PF01485; IBR; 1.
DR   Pfam; PF22191; IBR_1; 1.
DR   Pfam; PF21235; UBA_ARI1; 1.
DR   Pfam; PF13445; zf-RING_UBOX; 1.
DR   SMART; SM00248; ANK; 2.
DR   SMART; SM00647; IBR; 2.
DR   SMART; SM00184; RING; 3.
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; 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   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          137..169
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   DOMAIN          324..559
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51873"
FT   DOMAIN          328..373
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          276..312
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          750..788
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        300..310
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        778..788
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   788 AA;  89293 MW;  B81B9C2ACC97F6CD CRC64;
     MGSASTKFRK ALQAGDEGLA LQLYYTNVPL AQQLDPNASY GEAYDNNTAM HYATRHAMPR
     LLSVFLREKE GNPNKRNGLE ETALHCACTP LAVLIVPPSG QQEERRLLCL RMLLDWQGPL
     LGPQQRERAK VDARDHHGNT PLHYAACSGM KRCVELLVVR GASLFVENED GATPCDRAEI
     NRHYEVALHL ESRMVLAQDY PDGDGDEPQE PLASGCREPF EGLRAQELRE LKDLLIVETA
     DMLQVPLFTA EALLRSHGWD RERLLEAWML NSDECCQRSG VQPPPPPPTG QNSWGTIPDS
     RPPLRSPITP PGDLRHGLST VGARESLCEI CLGRMPESDP VDVPCGHLFC KKCWEEYLNM
     KIQEGKAHSI LCPAYDCYSL VPIETIEVLV CREMARRYLQ FDIKAFVDTN PSIRWCPVPR
     CEQAVRLALP GAAGGSAARA HTPTAVDCGS GHTFCWECLG EAHEPCDCGT WKQWLQKIVD
     MKPEELSGVS VAAEDAANCL WLISNSKPCP SCKSPIQKND GCNHMQCTKC KHDFCWICLE
     EWKKHSSSTG GYYRCTRYEV IQAVEDSSRD VANEAEKKHK KFQELDRFMH YYSRFKNHEH
     SYKLELPLLQ TARAKMEILR SALENMEGVD TSFIEHAVQE LLKTRRVLRG SYGYGYFLEP
     HSTQKDIFEL MQMDLEMLTE DLAQKVNRPY LRTPRQKIVR AARLAQQKRQ EFLASVARGV
     APPDSPPSSR RQLVGRPWEW EFLGFSSPEE YEEVLERRRR RSRRGDPRSS HSHLTDPGLR
     EESSTGRP
//
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