ID A0A8B8HSK7_VANTA Unreviewed; 2173 AA.
AC A0A8B8HSK7;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 18-JUN-2025, entry version 18.
DE SubName: Full=Uncharacterized protein LOC113394376 isoform X2 {ECO:0000313|RefSeq:XP_026487462.1};
GN Name=LOC113394376 {ECO:0000313|RefSeq:XP_026487462.1};
OS Vanessa tameamea (Kamehameha butterfly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC Nymphalidae; Nymphalinae; Vanessa.
OX NCBI_TaxID=334116 {ECO:0000313|RefSeq:XP_026487462.1};
RN [1] {ECO:0000313|RefSeq:XP_026487462.1}
RP IDENTIFICATION.
RC TISSUE=Thorax {ECO:0000313|RefSeq:XP_026487462.1};
RG RefSeq;
RL Submitted (MAR-2025) to UniProtKB.
CC -!- SIMILARITY: Belongs to the RBR family. {ECO:0000256|ARBA:ARBA00008278}.
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DR RefSeq; XP_026487462.1; XM_026631677.1.
DR Proteomes; UP000694848; Unplaced.
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; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR Gene3D; 2.30.30.380; Zn-finger domain of Sec23/24; 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; IPR001876; Znf_RanBP2.
DR InterPro; IPR036443; Znf_RanBP2_sf.
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; 2.
DR SMART; SM00547; ZnF_RBZ; 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; PS01358; ZF_RANBP2_1; 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:UP000694848};
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 1806..2042
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 1810..1859
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 107..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 337..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 483..792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 916..950
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1089..1141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1196..1275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1349..1368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1532..1557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1653..1678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..137
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..385
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..395
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..518
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 534..547
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..562
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 581..596
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 597..614
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 629..648
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 660..684
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1095..1104
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1113..1123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1132..1141
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1229..1238
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1246..1257
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1543..1557
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1656..1665
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2173 AA; 242677 MW; C3D76711EED890BC CRC64;
MLKNRGRDPR SAIPSTPLLV RSIAPRAPMA KPEPDYEVVE FPADQYVNAK IQPPPPPPPR
PATGHPIDAG ASCGLCGGGG ARVRCTECGR RALCASCDDM YHRHPKRRNH QRQALSHSQL
LDERPPLPPK AAPPVPPPRR HKISGERSSA SPRPSVMDQR RATLNPTVAA HSPMSTITNP
NHFSTQRAHI QQPQGAVPNM SHMGSMPYLP NAVHHANTTV PSQEQTIALG QFSSWGRPRG
SLQGFNIAPN MMQPPPLEPW ELQENLSTQS WGRPLRRGAS VMELGGGPTG CTGCAHCATN
PWRYGSCANL DHQWIGPSPA PSAGPWPQTC CSPHSVTHNS RIMPHTHPHA PQTPQPYRRM
DIRGVSRAAS RAGSRAASPA LSLRSRTSRR SKHRTPSPPI PSSDADSESE VESDHPETID
KDDENSLGPA PPPPAATWQC EHCTFVNEPG VRVCAVCCRT PTIKPKIVTD VINNGVERLK
VAEKTSRSPS IHSSHAVDKT IIKTDDKGKK NRSTKERTST GCGPSPPRED KSMAKSTNVL
KTTPTREQSN ERIEQTRIRH DIAVGPSPPK EILDGQRTSL SKNSTVNQSS NVTSNNFRSS
SRIGSPVNGS SKLHNISVGP SPPRDSPKRT MSSYQSNSIN FQKKSVGNSP PRENVESRPL
SRSSRTNAGT SPPPQSISTQ TYEVPNNWER AQSVARSRPR RRLREENRRE RSHSRLSLSS
DTRESERSVH TSGGRWEWRE PRDSSPSADW SESERRRASQ LTRRASHLDV RRRPGQRSSV
FGSEAPSPEP MSSNRAISLE ALVGAGSRGD AERGLELARL MTDAEKLGFS AAEVHAALAQ
NPVAPLAWLS ERWPSLCAGV RAAAARLAPG VNVTELEARA SLAKHRGAMW PAVNDCVERS
RRQVVVIGEE GRLRGHVWGP PTGADDEGAP PSPFSSRLHR TREDSSDEFE VTTNKFQDDD
WMYLPLEINT KTNHEFESPV IKEDTTMTNE DSSLDIAEKL KSLLIKAGIP LADEKLLLKS
LLGNHSMYSE NSDINHSKTI EQNKPNVTDF IQSENDFIDA YNALTRLSPL PSLKKKDITG
TNDVLEQIET QSPQENNDNI SENISNDHDL TKNPKTFESQ TKLNPIEKNT SETELSNVRE
NNYSHETVTK IEDIIQDTPV INTKDVKEDK SINLNEIVDN TQKIIQQMKN EINSDINSIN
DKSDTQSEAD DSANDSHSSS EKESSYSETD ADGTEDLTSD EKDTSTSDDE NPNDQLEDQA
SIHRTSSEDN EQFEEAMDHV ENELEDFKQT NIEILNSIAR SLQEEHTITI EINESNDKDY
RQRNQDMNNN LFAAVNSFEE IYAELNNDRQ KKENTTTDTY SNQLKSSSNN SSIASEIKTK
FNPAYIQQEI NISYFRPDSP IKVVITDRVP QFFTASLEIF DNLLEKDNSS LERNLNDQVY
ETVEEPSKEV IKNNITNEYL EVREKNNDPV NNSLEISKDN ISTIDTLTIN TNINNSNEKD
LNQMNSIAYE KHGHTNNIAG VEIINNSLDV NKHQENISPP EPSNTQTQVY RENSEKNSLI
DSSKMKTTTN KSNIPKLVKT IQSNKQKIEN KNLPKLIASK VPIRRASLKQ YPAPNPPKGH
FGDIKSGHVK QLQTRLFNSK VAKTNIETTA MPEIRASTST MSKKSPAPPP PTQPAIQGQD
ATLSKNKNVY FRETCRTEDE WTESDPEDQD FQINLNNVEE SVPTPVSQIQ PVTLRHISGQ
LIDLANVRVP EGSPERQARM LLAEGATETW EQAQLAVDLI SQGTDPPAAL LAALECTDLS
SALAYLHQDC ELCASKFPEH EMVSMLRCTH RCCQECARHY FTVQITERSI VDCVCPYCKE
PELENLSEDD WLDYFAHMDI LLKTLLEIEV HELFQRKLRD RTLAKDPNFK WCVECSSGFF
VHPKQKKLRC PECKSITCSS CRKQWSVNHD GITCEQYAAW LEDNDPEKSI AAVQQHLREN
GLECPRCHFK YSLSRGGCMH FTCTQCKYEF CYGCGKPFTM GARCGLSEYC ARLGLHAHHP
RNCLFYLRDK EPHELQTLLQ MNNVSYETEA AEGSNNRCPI QLQRETPTGL VDTTCGSEVQ
PKQAGLCKNH YLEYLSRLVR GRRVDPLPIL GVDDLETLVR RAALRPPPRP YGSLDGLYKR
GLAEIVREKI PLD
//
