ID A0A1J1IH40_9DIPT Unreviewed; 2734 AA.
AC A0A1J1IH40;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 18-JUN-2025, entry version 35.
DE SubName: Full=CLUMA_CG011133, isoform A {ECO:0000313|EMBL:CRK97753.1};
GN ORFNames=CLUMA_CG011133 {ECO:0000313|EMBL:CRK97753.1};
OS Clunio marinus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Chironomoidea; Chironomidae;
OC Clunio.
OX NCBI_TaxID=568069 {ECO:0000313|EMBL:CRK97753.1, ECO:0000313|Proteomes:UP000183832};
RN [1] {ECO:0000313|EMBL:CRK97753.1, ECO:0000313|Proteomes:UP000183832}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Syromyatnikov M.Y., Popov V.N.;
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CVRI01000047; CRK97753.1; -; Genomic_DNA.
DR STRING; 568069.A0A1J1IH40; -.
DR OrthoDB; 9978677at2759; -.
DR Proteomes; UP000183832; 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; cd16631; mRING-HC-C4C4_RBR_HOIP; 1.
DR CDD; cd20351; Rcat_RBR_HOIP; 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; IPR047541; RNF31_RBR_mRING-HC-like.
DR InterPro; IPR044066; TRIAD_supradom.
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; 1.
DR Pfam; PF01485; IBR; 1.
DR Pfam; PF22191; IBR_1; 1.
DR Pfam; PF16678; UBA_HOIP; 1.
DR SMART; SM00647; IBR; 1.
DR SMART; SM00184; RING; 2.
DR SUPFAM; SSF57850; RING/U-box; 3.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000183832};
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 DOMAIN 2362..2598
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 2366..2415
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 119..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 243..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 455..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 536..666
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 833..854
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1334..1362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1662..1692
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2051..2173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2191..2262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..258
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..270
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..316
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..473
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 484..496
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 578..595
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 596..614
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 615..624
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 657..666
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1666..1679
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2086..2098
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2110..2121
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2122..2139
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2191..2205
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2217..2244
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2245..2262
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2734 AA; 309737 MW; 53CCAFB868C5A857 CRC64;
MSNQMFNRSM PNWVSEQTGR IGPNPPPLPT KRNNPDPDYE VIDFSSQQYS NSVPSKVIKD
IMQKSPSEVG LKCELCGTIG PVIKCEQCVK NLFCFTCDDM FHRHPKRQNH LRKRVEFVNV
RPPLPPKNTS QPQAPVPPPR RNRKSCLSSP MPERKDQAFS TKQQQKNASV FNASLREKLE
NLNRVTRTMP DVPLPGSRRM QNRPKNNIFD AIKKPPSVAM EKIQSTTAAT LDRMAILQQR
YRQHKEAMNS DNSSDKSRRT STTSTIDSTS FPLINRPPLP PHSVIHNPNH LENGVPRTDS
FSSMSNPPLS PQSYSNHQKP FIDQVQASSA RRPVPIPGSG TLPNHAGRNM SSSVFNLNQG
GYPQPGFVPQ QPNPWGMNPM NQAHSMAQLN MMGNQWNLPS QGWPGSNFNG SNMSLNIPNS
FVQNDQTMWH SWMQQQQFGF PVMPNVMPMR SMTLSRAASP SLSVRSRRSL TTSRSRHKYV
PQDLTDDEDS DIENFTDDSR SRKRLERRPR RNPEQIELDY RDNEVINRIQ KMKEKSKFIR
ERRSGSLTNW PTTKDRDSGS LTPSDEEIKK TAVKQRKSSL TSPSIPQSQK FLSDSTSEKE
KEEEVVNPKK KESTSKFTQP LRSDSASEKE LIKENSPPIK ETNKTKKKTQ PDSDNETVYK
KSPETKLVSE SRPLKIVTHS VVKAKTSNIV NNNNKEGENI SQPEKLIRSV CFVPHVVLSS
PSPTLHRIKF LYPNEFYVVV ASSDESVHDE PDDIVFRREV NDLKIADDEP LSQYQPEKVV
VTEEVKEESF EEKVENKVKV STGCGPSPDR EIQEIFANEE KLETFTPLRE IPSRSSKVSI
GTSPPPQSIS TQTYDVSPFD INSEAESSQY PVEGRFSNRL RRSQSFANTS RLVEPPTTLQ
RSLSRMSFSS ELQDFEALKF ENFMNQRRFE ESSNASAGVH LANLLREAEH FKFNAEELQA
ALNHCEGSNP ILWLRENWQK LIETVQHLAT KYGHELKVNT VGTISAIEAR EALRLHKGNI
WHAVTKCIEQ RQKKYNAIAA RGNFTREDIV TSLTAHHGNI ELALIELNKT QLKPFLMKIW
GPPSGVDNES GNYMMERDTY SLDPNIQEYL NNIIIQNDNN FQHHQNEFKE YFSPSSPQSM
SFQSSSLDDQ IFDENINNED LFTTVDYNSV NNANLLKDIE NLIQNMERKQ TQDNDCTMLK
NIDNILSNIK LNDSRSHSPQ SNLSIEPIRM KSPIMIPNRN DDKIKSDVYS IIDDIRNFVS
NNIQDIVPDL VSQVEQEITT DLSSDIAMEN LEEFQRNRLE EEFEERNFSA IESKEDFHFS
QELEDFLRSR HDEEFNERNS VVDQSRRRRT SSGNSDKEEF DDFFRSRHNE EYMERNNDFH
NVHDDASHES IMVVSQTNAN DDFDTIVAAA VDDAVNENEL NTQENIIMDQ LTKNLTNEAE
SIVENIFNES LRTVLPNDVD DLNSQSNTQQ LEPLKYKSSF NLKINKKPSK RPKCERDFKK
RNSLILENIL MGKMPSISST KSKLKSSTMN ADSSAQDNNS VSVSILNDFV SNINHPAGLI
SENIEQQSVL NPNEINVSGS EKNVESFENV GNEANIINGS TRDEVENESL MLLENSSTQN
DVIEARTETV SVTMNDESAS STAVINDDDT QHIEEVLIKN SHENEIQSLP QTSSNTLSSN
EDDPSLKAPQ NLSELVEDTQ RLIKQMKDEI NAIYVSDDEY ESSEGSEYSD EWGIEYEGEE
IEDEYSYEES EYEDWSGDYI ESEQTEITTD ERELHADEQV AVDLTNINGL NLEISNIGDL
ANPNAMNDVE NAENSNDFHG ESLPLTLMSS ADHFQQDSPG SMETSSEALK DNDVNLNNSQ
IQAAEEVNDE ELTPTANQEE EKVKAAAINN EINGTTSSIK EIVNEAINEV INAISLDESD
INVHNGATQI GGVSFQHDEN DNENDENDEH DTSIIDSIAM NNSEEIQSSE VMPKVSDTTN
ESITSGNQLN YDEIVEETMI LSIEEASNDG VEQFAVLDDG ENDGQKIDES QEPLIIELNV
VVDNQVEMAS AGRSSVETDE TVKLEENANQ DSSEQKLKGA ISKSKIPAKI KSEKKKNSTV
KDTNERASKE SGQNESTSSS SEKIKAPLKK EDNTKEDILH ATNSKPPQAI IKTAPDSTRK
GSFDANSKKK PSFGLLVTSN VKNLQKEFLN KSNIATSSKP QQAQPSKLKP TKLVPQKSFS
NNPTQSFANR LTKLITPSSS TKISDNSDQK ESQKEFRDHS KDVVPEKKYM EHCFSDEYPT
TDDDEEESAK AVSTFLTKKP PTQDFEDETS DQKVNRFLLE GLVPNHLAAE LAVSLIEMKY
PQESALWVSA QVSTIEDAIE LLQQECELCT DKYPLNQMIT MLKCEHQCCK ECASNYFTIQ
ITDRSINDCV CPFCKLPELH DSDEDSILEY FSNLDILLKN ILQSDVHDLF QRKIRDRALL
RDPNFKWCVQ CSSGFFARPK QRRLICPDCG SVTCAKCRKL WEKQHEGLSC EKFAEWKEAN
DPDVQAEGVA KHLKLNGIDC PKCKFRYDLA RGGCMHFTCT QCKYEFCYGC NKDFLMGAKC
KVSSYCAKLG LHAHHPRNCL FYLRDKEPQE LQSLLKINNI EFDEDFQSSS DGAKAFVRCP
VQLQKETPSG LVDTVCSNEV PDGHAGLCRS HYVEYLVSVV YQANIDPLPI LDLTDCVQEL
RRRGIPLPER GPWDTDPIYR EMCQKIVKEN IPLE
//
