ID A0A8J6L2W7_TENMO Unreviewed; 2418 AA.
AC A0A8J6L2W7;
DT 25-MAY-2022, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 1.
DT 18-JUN-2025, entry version 14.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0008006|Google:ProtNLM};
GN ORFNames=GEV33_013149 {ECO:0000313|EMBL:KAH0809634.1};
OS Tenebrio molitor (Yellow mealworm beetle).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC Tenebrionidae; Tenebrio.
OX NCBI_TaxID=7067 {ECO:0000313|EMBL:KAH0809634.1, ECO:0000313|Proteomes:UP000719412};
RN [1] {ECO:0000313|EMBL:KAH0809634.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Stoneville {ECO:0000313|EMBL:KAH0809634.1};
RC TISSUE=Whole head {ECO:0000313|EMBL:KAH0809634.1};
RA Eriksson T., Andere A., Kelstrup H., Emery V., Picard C.;
RT "The yellow mealworm (Tenebrio molitor) genome: a resource for the emerging
RT insects as food and feed industry.";
RL J Insects Food Feed 6:445-455(2020).
RN [2] {ECO:0000313|EMBL:KAH0809634.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Stoneville {ECO:0000313|EMBL:KAH0809634.1};
RC TISSUE=Whole head {ECO:0000313|EMBL:KAH0809634.1};
RA Eriksson T.;
RL Submitted (AUG-2021) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the RBR family. {ECO:0000256|ARBA:ARBA00008278}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAH0809634.1}.
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DR EMBL; JABDTM020028008; KAH0809634.1; -; Genomic_DNA.
DR Proteomes; UP000719412; Unassembled WGS sequence.
DR GO; GO:0071797; C:LUBAC complex; IEA:InterPro.
DR GO; GO:0036435; F:K48-linked polyubiquitin modification-dependent protein binding; IEA:TreeGrafter.
DR GO; GO:0070530; F:K63-linked polyubiquitin modification-dependent protein binding; IEA:TreeGrafter.
DR GO; GO:1990450; F:linear polyubiquitin binding; IEA:TreeGrafter.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:TreeGrafter.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0097039; P:protein linear polyubiquitination; IEA:TreeGrafter.
DR CDD; cd19815; Bbox1_HOIP; 1.
DR CDD; cd20337; BRcat_RBR_HOIP; 1.
DR CDD; cd20351; Rcat_RBR_HOIP; 1.
DR Gene3D; 1.20.120.1750; -; 1.
DR Gene3D; 6.10.140.1100; -; 1.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 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; IPR047542; Rcat_RBR_RNF31-like.
DR InterPro; IPR026254; RNF31-like.
DR InterPro; IPR032065; RNF31-UBA.
DR InterPro; IPR041031; RNF31_C.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR000315; Znf_B-box.
DR InterPro; IPR001876; Znf_RanBP2.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR16004:SF2; E3 UBIQUITIN-PROTEIN LIGASE LUBEL; 1.
DR PANTHER; PTHR16004; RING FINGER PROTEIN 31-RELATED; 1.
DR Pfam; PF18091; E3_UbLigase_RBR; 2.
DR Pfam; PF01485; IBR; 1.
DR Pfam; PF22191; IBR_1; 1.
DR Pfam; PF16678; UBA_HOIP; 1.
DR SMART; SM00647; IBR; 2.
DR SMART; SM00547; ZnF_RBZ; 1.
DR SUPFAM; SSF57850; RING/U-box; 3.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS50119; ZF_BBOX; 1.
DR PROSITE; PS01358; ZF_RANBP2_1; 1.
DR PROSITE; PS50199; ZF_RANBP2_2; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000719412};
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 71..117
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT DOMAIN 537..560
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 1960..2198
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 1964..2013
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 14..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 108..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 241..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 398..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 577..789
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1115..1136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1215..1261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1273..1303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1420..1832
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1873..1892
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..179
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..251
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..296
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..426
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..468
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..490
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 491..503
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 589..610
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..640
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 683..700
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 747..771
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 779..789
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1115..1124
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1230..1240
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1241..1250
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1429..1438
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1443..1465
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1470..1479
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1480..1489
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1499..1520
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1521..1534
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1543..1570
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1571..1587
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1597..1609
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1620..1629
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1707..1737
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1764..1783
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1797..1829
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1873..1889
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2418 AA; 270055 MW; 872E3EA6880E1D45 CRC64;
MRFLSYFRQT RQKFGRYKSG SGAPPPPVPA EEKPRQSFSK NSQEPDYEVI EFGQQYSNAP
PLPVKNETQR SDGRHCQLCG TSNPSIRCDQ CFQIFCLSCD DMYHRHPKRQ THYRRPLDAS
VRPPLPPKGE SHSAPVPPPR RHRRAGSIGP SPCPSPTPSR HNQGLPRKES SFSFKDKMNS
LKRMVGTRPL PPTPSSPTHS SPRQFTSSPP NFDRYNRGFE VPSPSPSLQQ RYRQHQLAMR
GTTPNLSSTG SDFDKPPSRD SGYPDWETEQ WNSRFRSGSI SGSDSGNRMR KLSNTSCPPP
RTLPHSASVF DLNNTMPPHH HHHGFMPMQQ AQSMAQLNCP TCYQGSWMDC AMCDQRTGSN
LSLNVAPPPY PMNPMWMGTW HGPPPSAMYP YPVPMGHVHH HSRPPSPTHS VKSRKSSMSK
KGRKKYREVE ETDDEDDMED RRSIFSHNDR NERKSLGGRF PERQRPSRDT SSVPREVARR
NTIDRVERIS NVRSRPSVRQ SSSESDDEHS ESQKEESEIV EEGSEQDTGP KPLPELPNAN
WECEHCTFVN EAGTKVCLVC CKTASVNVKL VQNEESQNLA PKNLPKSKQN KEQNKLQRSR
SSDDYSKDYS ETESLLNKLG KLKTSEPPKE VPAEPKKGKD GCVSPSASEL EDKAPIVSLE
NGVPGSAVNS SVGTDDSARD KVTMSTGTSP PPQNMSTQTY EDVAQPGEVP KSPRGRPTSR
NNRRRDLRRS NSLHMGTQRR GSEWSLHRSS SRQSFTTDSQ SLPGSREQSP SPYDYGDDSV
ERLLSRDRRP TTNRSYYSIM DLRKPELYRN DPPFYRNDYP SHRPRADSFD FAENGFHSFK
MQGMELVKLL REAEQYKYTA DEVQAALAHC KDANPIDWLR QNWDATIASV QTLATQMGRE
GPMNIVGTVS EEEARAALRL HKGNLWPAVT DCVEQRQRKY AELAARGEFS REDILTVLTA
NHGDLEAAFN ELSKTQLKPF LMRIWGPPVG TENEAGNQGA TLEKIRGEDV ENQRADKEMA
KAVSPIDNGK DRAPPTTEQT PIVKEVPPDE LKKTQNFELL DNIESEVLKN LQDINKLSDS
LETNNEPKST KPKVYVEKSS TVIQVVDHDY EVPEAERDEK RIESDFSDTE SSDEGNRVEE
FVDAVSEVHP VGLAPLKRKS VSTLNITLAS TGEPGESATG VPISVVKNST EVKMIQPSES
TREDVVVEST AAIQLQSAPP KNGDVGASEV KAEQKRDLEA STKQNNTATS LEVPPVLADS
DKERALVMPS VEQDGGLLAS GVEKNVESRP STSTAGGVEE NKNVELADGT NLLENERQSV
ETGLKEKLGE KMTEGGVGGG EIAADVTSVD LESCTMSEDV SVVKNENNDE IVANLIVAQQ
DVRSSVADVK EELNEDVGAG LGTCEVESDL KRNVLVEENA TKAEKNGDSE QQIGQRKSAS
PRLENDRCRK VRPKEVVSSE KKDLSRSGQE VEVVSQSVVE VKEEKEESTG KPVENKPPLT
KKQKKSMKRA KRRSQRRAAR RGSTSTTESS SCEKPLTETD SEPNQKEPLK EVHEEVKNSE
DQEAKPRDVT SSEQPKTDVQ ATTSTDLPEN VEIHPKISTT VQIAQNKQSL LPVPPKRPSR
IPISRQRSIS KSEPKSPDVH TASKIPIKTG SQIPVKNKQH NNIDHTGEGG SVNNSQTGES
PGEVVQTSED KPSGSAEEIV GRSGSAAKDE GVEVEEVERP QRPCVQRDKS EEIEQEMKQS
VQAIKELNRQ LNTNSKSKKG SLGSFRNSSV ESTTSSKQLS YTKSLDNDSD SSVSDSNVEE
LLDPSTDEDS YEDFEEYDEV EESDTEDYNE FDRKNARIVD ELDINLSQIS AKVEKLTTDL
TDNKNDYLDE VCESEEYSSE EEEEAEDESD NKFDVSIEVK QPSEIEVMER QARRFLAEGQ
VKNYQQAELA VSLMALKFSA EEALEAVHDC QTLDAAIAYL QQDCELCAGK YPVNQIVSML
KCTHRCCQEC AKNYFTVQVT DRTIMDCSCP FCKQPELTSS EISEDEVSDY FGNLDILLKG
ILDATVHELF QRKLRDRTLM QDPNFKWCVK CSSGFIANPR QRRLICPDCK TMTCANCRRT
WEKQHEGISC EKFAEWKDAN DPENQATAVA KHLAENGIDC PKCKFRYSLA RGGCMHFTCT
QCKHEFCYGC GKPFMMGAKC GVSQYCGKLG LHAHHPRNCL FYLRDKEPAE LQRLLKEHKI
PFDTEKKEEN AAAAAKCPVP LQRETPNGLI DTVCNNEVTP GQGGLCRMHY LEYLCMSIRR
HKIDTIDILS ADDLETVVRR AAKKLPPNAY GTPRDMLHYV EYLVGLIGRH KLDPVTILDL
VEVGQELRRR GKELPERSAS CNDQEYRLIC VKVGLVGGGL VHVATRVTGA LVPNHLRGLL
AELVCQCAQL HVCLSLLY
//
