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Database: UniProt
Entry: A0A2K6AA99_MANLE
LinkDB: A0A2K6AA99_MANLE
Original site: A0A2K6AA99_MANLE 
ID   A0A2K6AA99_MANLE        Unreviewed;      1072 AA.
AC   A0A2K6AA99;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE            EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN   Name=RNF31 {ECO:0000313|Ensembl:ENSMLEP00000037006.1};
OS   Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Mandrillus.
OX   NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000037006.1, ECO:0000313|Proteomes:UP000233140};
RN   [1] {ECO:0000313|Ensembl:ENSMLEP00000037006.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) 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. {ECO:0000256|ARBA:ARBA00008278}.
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DR   RefSeq; XP_011826342.1; XM_011970952.1.
DR   RefSeq; XP_011826343.1; XM_011970953.1.
DR   AlphaFoldDB; A0A2K6AA99; -.
DR   STRING; 9568.ENSMLEP00000037006; -.
DR   Ensembl; ENSMLET00000060612.1; ENSMLEP00000037006.1; ENSMLEG00000042615.1.
DR   GeneID; 105532715; -.
DR   KEGG; mleu:105532715; -.
DR   CTD; 55072; -.
DR   GeneTree; ENSGT00530000064112; -.
DR   OMA; YNTFYAK; -.
DR   OrthoDB; 2909614at2759; -.
DR   Proteomes; UP000233140; Unplaced.
DR   GO; GO:0035631; C:CD40 receptor complex; IEA:Ensembl.
DR   GO; GO:0009898; C:cytoplasmic side of plasma membrane; IEA:Ensembl.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0071797; C:LUBAC complex; IEA:Ensembl.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0043130; F:ubiquitin binding; IEA:Ensembl.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:Ensembl.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0023035; P:CD40 signaling pathway; IEA:Ensembl.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:Ensembl.
DR   GO; GO:0060546; P:negative regulation of necroptotic process; IEA:Ensembl.
DR   GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; IEA:Ensembl.
DR   GO; GO:1904417; P:positive regulation of xenophagy; IEA:Ensembl.
DR   GO; GO:0097039; P:protein linear polyubiquitination; IEA:Ensembl.
DR   GO; GO:0050852; P:T cell receptor signaling pathway; IEA:Ensembl.
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; 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; PS01358; ZF_RANBP2_1; 3.
DR   PROSITE; PS50199; ZF_RANBP2_2; 2.
DR   PROSITE; PS00518; ZF_RING_1; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233140};
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          299..329
FT                   /note="RanBP2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50199"
FT   DOMAIN          350..379
FT                   /note="RanBP2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50199"
FT   DOMAIN          564..615
FT                   /note="UBA"
FT                   /evidence="ECO:0000259|PROSITE:PS50030"
FT   DOMAIN          695..929
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51873"
FT   REGION          443..484
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1072 AA;  119523 MW;  48C529B9ED8E79C9 CRC64;
     MPGEEEERAF LAAREELASA LRRDSGQAFS LEQLRPLLAS SLPPTARYLQ LDAARLVRCN
     AHGEPRNYLS TLSTALNILE KYGRNLLSPQ RPRYWRGVKF NNPVFRSTVD AVQGGRDVLR
     LYGYTEEQPD GLSFPEGQEE PNEHQVATVT LEVLLLRTEL SLLLQNTHPR QQALEQLLED
     KVEDDMLQLS EFDPLLREIA PGPLTTPSAP GSTPGPCFLC GSAPGTLHCP SCKQALCPAC
     DHLFHGHPSR AHHLRQTLPG VLQGTHLSPS LPASAQPRPQ STSLLALGNS SLSSPNPASA
     RLPWHCAACA MLNEPWAVLC VACDRPRGCK GLGLGTEGAQ GTGGLEPDLA RGRWACQSCT
     FENEAAAVLC SICERPRLAQ PPSLVVDSRD AGICLQPLQQ GDTLLASAQS HVWYCIHCTF
     CNSSPGWVCV MCNRTSSPIP VQRAPRPYAS SLEKGPPKLG PPQRLSASLP SSCGDPGKQR
     QDKMREEGLQ LVSMIREGEA AGACPEEIFS ALQYSGTEVP LQWLRSELPY VLEMVAELAG
     QQDPGLGAFS CQEARKAWLD RHGNLDEAVE ECVRTRRRKV QELQSLGFGP EEGSLQALFQ
     HGGDVSRALT ELQRQRLEPF HQRLWDSGPE PTPSWDGPDK QSLVRRLLAV YALPSWGRAE
     LALSLLQETP RNYELGDVVE AVRHSQDRAF LRRLLAQECA VCGWALPHNR MQALTSCECT
     ICPDCFRQHF TIALKEKHIT DMVCPACGRP DLTDDTQLLS YFSTLDIQLR ESLEPDAYAL
     FHKKLTEGVL MRDPKFLWCA QCSFGFIYER EQLEATCPQC HQTFCVRCKR QWEEQHRGRS
     CEDFQNWKRM NDPEYQAQGL AMYLQENGID CPKCKFSYAL ARGGCMHFHC TQCRHQFCSG
     CYNAFYAKNK CPDPNCRVKK SLHGHHPRDC LFYLRDWTAL RLQKLLQDNN VMFNTEPPAG
     ARAVPGGGCR VMEQKEVPNG LRDEACGKET PAGYAGLCQA HYKEYLVSLI NAHSLDPATL
     YEVEELETAT ERYLHVRPQP LAGEDPPAYQ ARLLQKLTEE VPLGQSIPRR RK
//
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