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Database: UniProt
Entry: L8I0M5_9CETA
LinkDB: L8I0M5_9CETA
Original site: L8I0M5_9CETA 
ID   L8I0M5_9CETA            Unreviewed;      1058 AA.
AC   L8I0M5;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   24-JAN-2024, entry version 58.
DE   RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE            EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
DE   Flags: Fragment;
GN   ORFNames=M91_12425 {ECO:0000313|EMBL:ELR49661.1};
OS   Bos mutus (wild yak).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=72004 {ECO:0000313|EMBL:ELR49661.1, ECO:0000313|Proteomes:UP000011080};
RN   [1] {ECO:0000313|EMBL:ELR49661.1, ECO:0000313|Proteomes:UP000011080}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=yakQH1 {ECO:0000313|Proteomes:UP000011080};
RX   PubMed=22751099; DOI=10.1038/ng.2343;
RA   Qiu Q., Zhang G., Ma T., Qian W., Wang J., Ye Z., Cao C., Hu Q., Kim J.,
RA   Larkin D.M., Auvil L., Capitanu B., Ma J., Lewin H.A., Qian X., Lang Y.,
RA   Zhou R., Wang L., Wang K., Xia J., Liao S., Pan S., Lu X., Hou H., Wang Y.,
RA   Zang X., Yin Y., Ma H., Zhang J., Wang Z., Zhang Y., Zhang D., Yonezawa T.,
RA   Hasegawa M., Zhong Y., Liu W., Zhang Y., Huang Z., Zhang S., Long R.,
RA   Yang H., Wang J., Lenstra J.A., Cooper D.N., Wu Y., Wang J., Shi P.,
RA   Wang J., Liu J.;
RT   "The yak genome and adaptation to life at high altitude.";
RL   Nat. Genet. 44:946-949(2012).
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. {ECO:0000256|ARBA:ARBA00008278}.
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DR   EMBL; JH882390; ELR49661.1; -; Genomic_DNA.
DR   AlphaFoldDB; L8I0M5; -.
DR   STRING; 72004.ENSBMUP00000033340; -.
DR   Proteomes; UP000011080; Unassembled WGS sequence.
DR   GO; GO:0071797; C:LUBAC complex; IEA:InterPro.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0019538; P:protein metabolic process; IEA:UniProt.
DR   CDD; cd19815; Bbox1_HOIP; 1.
DR   CDD; cd20337; BRcat_RBR_HOIP; 1.
DR   CDD; cd16631; mRING-HC-C4C4_RBR_HOIP; 1.
DR   CDD; cd10464; PUB_RNF31; 1.
DR   CDD; cd20351; Rcat_RBR_HOIP; 1.
DR   CDD; cd14325; UBA_RNF31; 1.
DR   Gene3D; 1.20.120.1750; -; 1.
DR   Gene3D; 1.20.58.2190; -; 1.
DR   Gene3D; 6.10.140.1100; -; 1.
DR   Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR   Gene3D; 4.10.1060.10; Zinc finger, RanBP2-type; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR047543; Bbox1_RNF31-like.
DR   InterPro; IPR047540; BRcat_RBR_RNF31-like.
DR   InterPro; IPR002867; IBR_dom.
DR   InterPro; IPR036339; PUB-like_dom_sf.
DR   InterPro; IPR018997; PUB_domain.
DR   InterPro; IPR047542; Rcat_RBR_RNF31-like.
DR   InterPro; IPR026254; RNF31-like.
DR   InterPro; IPR032065; RNF31-UBA.
DR   InterPro; IPR041031; RNF31_C.
DR   InterPro; IPR040641; RNF31_PUB.
DR   InterPro; IPR047541; RNF31_RBR_mRING-HC-like.
DR   InterPro; IPR044066; TRIAD_supradom.
DR   InterPro; IPR015940; UBA.
DR   InterPro; IPR047539; UBA_RNF31.
DR   InterPro; IPR000315; Znf_B-box.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   InterPro; IPR001876; Znf_RanBP2.
DR   InterPro; IPR036443; Znf_RanBP2_sf.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR16004:SF2; E3 UBIQUITIN-PROTEIN LIGASE RNF31; 1.
DR   PANTHER; PTHR16004; RING FINGER PROTEIN 31-RELATED; 1.
DR   Pfam; PF18091; E3_UbLigase_RBR; 1.
DR   Pfam; PF16678; HOIP-UBA; 1.
DR   Pfam; PF01485; IBR; 1.
DR   Pfam; PF09409; PUB; 1.
DR   Pfam; PF18486; PUB_1; 1.
DR   SMART; SM00647; IBR; 2.
DR   SMART; SM00547; ZnF_RBZ; 3.
DR   SUPFAM; SSF143503; PUG domain-like; 1.
DR   SUPFAM; SSF90209; Ran binding protein zinc finger-like; 1.
DR   SUPFAM; SSF57850; RING/U-box; 3.
DR   PROSITE; PS51873; TRIAD; 1.
DR   PROSITE; PS50030; UBA; 1.
DR   PROSITE; PS50119; ZF_BBOX; 1.
DR   PROSITE; PS01358; ZF_RANBP2_1; 3.
DR   PROSITE; PS50199; ZF_RANBP2_2; 2.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011080};
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:PRU00322}.
FT   DOMAIN          200..246
FT                   /note="B box-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50119"
FT   DOMAIN          290..315
FT                   /note="RanBP2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50199"
FT   DOMAIN          336..365
FT                   /note="RanBP2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50199"
FT   DOMAIN          550..601
FT                   /note="UBA"
FT                   /evidence="ECO:0000259|PROSITE:PS50030"
FT   DOMAIN          681..915
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51873"
FT   REGION          239..280
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          426..466
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ELR49661.1"
SQ   SEQUENCE   1058 AA;  118150 MW;  1ED6DDB15E86C35A CRC64;
     ARGELAGALR RDSGQAFTQE QLWPLLGTSL PPEARYLQLD AARLVRCNAH GEPRNYLNTL
     STALNILEKY GRNLLSPQRP RYWRGVKFNN PVFRSTVDAV QGGRDVLRLY GYTEEQPDGL
     SFPERQEEPD QRQVATVTLE VLLLRTELNL LLQNAHPKPQ ALEQLLKDKV EDDLLQLSEF
     APLLREIAPS PLTIPSAAGS TPAPCFLCGS APGTLHCSAC KQALCLTCDR LFHGHPERAH
     HHRQTLHGAP QAVHPSLPAS APPRPQPASG PTLGDSSFSP PDPASARLLW PCSACALLNE
     PWAVLCVACD RPRGCKGLGP GIEGPQGTGG LEPELSRGHW ACQSCTFENE AAAVLCAICE
     RPRLAQPPSL VVDSQDSGIC LKPLQQGDTV LSPVQTPAWY CIHCTFCNSG PGWVCAMCNR
     TSSPVPVQQT PQPHASSLEE RHPEPGPPRP LHAPVTSSCG DLEKQRQDKM REEGLQLVLK
     IREGEAGGAC PEEVFSALQY SGTEVPLQWL RSELPYVLEM VAELAGQQDP GLGAFSCQEA
     RKAWLDRHGN LDEAVEECVR TRRRKVQELR SLGFEPEEGS LQALFQHGGD VARALTELQR
     QRLEPFHQRL WDSGPEPTPS WDGPDKQSLV RRLLAVHSLP SWGRAELALA LLQETPRNYE
     LGDVVEAVRQ SQDRAFLRRL LAQECAVCSW ALPRNRMQSL TSCECTICPD CFRQHFTIAL
     KEKHITDMAC PGCGRPDLTD DTQLLGYFST LDIQLRESLE PDAYALFHKK LTEGVLMRDP
     KFLWCAQCSF GFIYEREQLE ATCPQCQQTF CVRCKRQWEE QHRGRSCEDF QNWKRTNDPE
     YQAQGLAMYL QENGIDCPKC KFSYALARGG CMHFHCTQCR HQFCSGCYSA FYAKNKCPDP
     NCRVKKSLHG HHPRDCLFYL RDWSAVRLQK LLQDNNVMFN TEPPVGARAV PGGGCRVMEQ
     KEVPNGFRDE ACGKETPAGY AGLCQAHYKE YLVSLINAHS LDPATLYELE ELETAAERYL
     HVRPQALPGE DAPTYHARLL QKLIEEVPLG QSIPRRRK
//
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