ID A0A068YD80_ECHMU Unreviewed; 1136 AA.
AC A0A068YD80;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=E3 ubiquitin protein ligase {ECO:0000256|RuleBase:RU365038};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU365038};
GN ORFNames=EmuJ_001044900 {ECO:0000313|EMBL:CDS42733.1};
OS Echinococcus multilocularis (Fox tapeworm).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC Eucestoda; Cyclophyllidea; Taeniidae; Echinococcus.
OX NCBI_TaxID=6211 {ECO:0000313|EMBL:CDS42733.1};
RN [1] {ECO:0000313|EMBL:CDS42733.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23485966; DOI=10.1038/nature12031;
RA Tsai I.J., Zarowiecki M., Holroyd N., Garciarrubio A., Sanchez-Flores A.,
RA Brooks K.L., Tracey A., Bobes R.J., Fragoso G., Sciutto E., Aslett M.,
RA Beasley H., Bennett H.M., Cai J., Camicia F., Clark R., Cucher M.,
RA De Silva N., Day T.A., Deplazes P., Estrada K., Fernandez C., Holland P.W.,
RA Hou J., Hu S., Huckvale T., Hung S.S., Kamenetzky L., Keane J.A., Kiss F.,
RA Koziol U., Lambert O., Liu K., Luo X., Luo Y., Macchiaroli N., Nichol S.,
RA Paps J., Parkinson J., Pouchkina-Stantcheva N., Riddiford N., Rosenzvit M.,
RA Salinas G., Wasmuth J.D., Zamanian M., Zheng Y., Cai X., Soberon X.,
RA Olson P.D., Laclette J.P., Brehm K., Berriman M., Garciarrubio A.,
RA Bobes R.J., Fragoso G., Sanchez-Flores A., Estrada K., Cevallos M.A.,
RA Morett E., Gonzalez V., Portillo T., Ochoa-Leyva A., Jose M.V., Sciutto E.,
RA Landa A., Jimenez L., Valdes V., Carrero J.C., Larralde C.,
RA Morales-Montor J., Limon-Lason J., Soberon X., Laclette J.P.;
RT "The genomes of four tapeworm species reveal adaptations to parasitism.";
RL Nature 496:57-63(2013).
RN [2] {ECO:0000313|EMBL:CDS42733.1}
RP NUCLEOTIDE SEQUENCE.
RA Zhang Y., Guo Z.;
RL Submitted (NOV-2015) 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|RuleBase:RU365038};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|RuleBase:RU365038}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|RuleBase:RU365038}.
CC -!- SIMILARITY: Belongs to the BRE1 family. {ECO:0000256|ARBA:ARBA00005555,
CC ECO:0000256|RuleBase:RU365038}.
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DR EMBL; LN902842; CDS42733.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A068YD80; -.
DR STRING; 6211.A0A068YD80; -.
DR eggNOG; KOG0978; Eukaryota.
DR OMA; THIEIMT; -.
DR UniPathway; UPA00143; -.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR013956; E3_ubiquit_lig_Bre1.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR23163:SF0; E3 UBIQUITIN-PROTEIN LIGASE BRE1; 1.
DR PANTHER; PTHR23163; RING FINGER PROTEIN-RELATED; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853,
KW ECO:0000256|RuleBase:RU365038};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|RuleBase:RU365038};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU365038}; Nucleus {ECO:0000256|RuleBase:RU365038};
KW Transferase {ECO:0000256|RuleBase:RU365038};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU365038};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU365038};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 1083..1122
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 187..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 333..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 577..650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 740..833
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 364..398
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 427..574
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 692..733
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 851..885
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 935..997
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1033..1060
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..354
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..594
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 595..615
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 616..630
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 777..807
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 814..833
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1136 AA; 128715 MW; 3766B750707AC127 CRC64;
MSKRSHSDQQ PSSGGGESIP GVSAPKRPFL SGSELVLFSR VRSLEELDKR TLQLQNKKLY
EALTEKRSAI SDLRHRIEQL ENRQAKDDAL LCVVNRYWNQ LDEDCLLLLQ RCEVDVDEKV
SNSAESFLKQ LASWEKEEVP EKLQQRVHFS KRIIARLLNS LEKLFVHQSR LRSLLVDELQ
PDRIVKASTA TTSSKTSSRP GGTIEEESME KFSTNATTAD DGGKTDGVSP LSSTEKMIAA
LREEIAALST ENDRLQCLCT SIHANHRQQS LRVRELQDQC QANSDAADEW KAKYEDLEYK
LQQSTAQLAI LDHRLYDAQQ SKKLLEEELA ALKGTSGSPG EGTEEASGTQ GVTKSKYNDM
LCELEEQREL AANRLTELER LQRQHEEKVA ECAKLSMQVN DPPEQLIQES PSYKSLKVQF
NILYGEVKSL RSQLEESRSM IQTIRNAHLK QIEEMEANET AILNQMRGEM LAQEELYSKL
RREFEIIEAD FKQTVAHNEQ AGPINSEMRS LITTLQLQNK QLKNEVVRYR RKSKEAAHDC
QMANNELKAT EEELSRARAS LAEATAAVIQ LTDELAASNP MPSTIAPSEP SQTSDSPPRK
RERENDTERK GADEGVSSSR SSGTEPATSH SEASSKDRKG SSSSQSPEEI IRDLRNQLKI
SQEAEKEMSV LLSMYKVIPK DQRDKATLLQ VEAKLRAELS EARSELATLQ SVNADLQARC
AQLQREYRIA TSSTFPLKRE LEEQADLPEK KVAGESNSTA HYEEPSPREG SVATGSGAVG
PSATNPSHQM SPLSVSTCMN VVSPESGEKS ASAAPILPPP PPPPPPTPHP LMPPVPRKTS
NLDEDKKAWQ VAELQQELQH TQRRCHTLEQ RVSTLQQHLV TAKQQEDVML KEMEVTGQAF
EDVQEQNSRL LKSLREKDDA NLNQMTEWMK TSQLARLLKE EKKLLDEQVR LMQAKIEALT
RAIQKQEDKE RLLLTNLETL EKEAASRQQS QEAYKRKSVE CQQREEDLRV TVQKYLAQLN
EAQTSVQEKA SAYEQVSFRH QRLQEEYTTL KRKYERLRKI EQSHNADEVL LAEIQDYKEQ
LACPTCKTHK KDAILTKCFH VFCLNCLKTR YETRNRKCPK CNATFGANDY HRIYLT
//
