ID A0A9J7INK6_SPOLT Unreviewed; 2232 AA.
AC A0A9J7INK6;
DT 28-JUN-2023, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2023, sequence version 1.
DT 18-JUN-2025, entry version 12.
DE SubName: Full=Uncharacterized protein LOC111352260 isoform X2 {ECO:0000313|RefSeq:XP_022820439.1};
GN Name=LOC111352260 {ECO:0000313|RefSeq:XP_022820439.1};
OS Spodoptera litura (Asian cotton leafworm).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea;
OC Noctuidae; Amphipyrinae; Spodoptera.
OX NCBI_TaxID=69820 {ECO:0000313|Proteomes:UP000301870, ECO:0000313|RefSeq:XP_022820439.1};
RN [1] {ECO:0000313|RefSeq:XP_022820439.1}
RP IDENTIFICATION.
RC STRAIN=Ishihara {ECO:0000313|RefSeq:XP_022820439.1};
RC TISSUE=Whole body {ECO:0000313|RefSeq:XP_022820439.1};
RG RefSeq;
RL Submitted (MAR-2025) to UniProtKB.
CC -!- SIMILARITY: Belongs to the RBR family. {ECO:0000256|ARBA:ARBA00008278}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_022820439.1; XM_022964671.1.
DR GeneID; 111352260; -.
DR Proteomes; UP000301870; Chromosome 15.
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; 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 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:UP000301870};
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 1865..2101
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 1869..1918
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 65..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 121..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 366..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 507..822
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 948..983
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1160..1183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1213..1250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1270..1344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1491..1514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1692..1794
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..10
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..82
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..130
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..155
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..408
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..421
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..450
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 521..535
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..572
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 573..586
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 598..609
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..637
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 660..673
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 683..717
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 733..743
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1163..1174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1213..1222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1229..1248
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1286..1296
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1302..1317
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1327..1338
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1491..1500
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1501..1513
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1692..1706
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1734..1743
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1744..1759
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1782..1791
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2232 AA; 248626 MW; D0C93F202E8B21A8 CRC64;
MLKGRGRDPR NVTSSPPAHL AKIMRPPALA HGAMPPTTPT SMHRVPQTRP EPDYEVVEFP
SDQYVNAKIQ PPPPPPPRPP TGHPVDAGAS CGLCGGGGAR VRCTECGRRA LCASCDDMYH
RHPKRRHHQR QALSVTQLRE ERPPLPPKAG PPVPPPRKHK ISGDRMSASP KPPPVLDQRR
ATLSSPHHAA MMMGAHIQGS PVPPANLIQA PQHHQQMPLH LQTKMTTTPT PNHLGSMPFL
PTNMHIAGSH HAAMPGQSNT LAHMNTAWNR PRGSLQGFSG HPNMHAPAEQ WDNSDNMAPT
MQNWGRPLRR GASVLELGGG AATSCAGCTH CAPVPWRYGS CASLDHPWAN TSPGWAPTCC
TPGHPTHGVQ PHPHLPPQTP QPYRRAESRT VSRAASRAGS RAASPAMSVR SRTSRRMKHR
TPSPPPLPSS DADSESESES DHGPPSKTQE KEEDSLGPAP PPPSSSWQCE HCTFVNEPGV
RVCAICCRTP VSVPKTITKE LSENVERLRI THKQSPSPAR TTEEPRFDRE VEKPKTKPKK
ERTSTGCGPS PPREGNTAKK QVNRLVTPTR ESSANHDDKL QGRHDMGVGP SPPREVRNGT
NHMDMSTEIS PPRDINKTMR VSPYRDSRQS PRPEVPKRHS ISVGPSPPRD NAYVNAPLKQ
LSTNNQKKST GTSPPRDVIE RQYPSSATNK TNVSNTGTSP PPQSISTQTY EVPNTTAWER
ASSVSRSRPR RRFRDEARRE RSQSRHSMSS DTRESDRSIR TAGPGNRWDW RERDSSPGGE
WGDGYNRLSR RASHLDLRRS RPNQRSTYYG SEAASPERQS SRAISLEALA GTGAKREAER
GIELAQMMAE AERLGFSAAE VQAALTQSPA SPLSWLRERW PSLCAGVRAA AARLAPNAAI
SELEARAALA RHRGAMWPAV TECVERHKRQ TEIMGVGEEG RLRGHVWGSP VGVDDDAAPP
RSSSRHSHRM REDSSDEFEA PTPARFQDDD WMYLPLNVNL NDYEREANYL ENNTVDQANV
ENKDDVAKKL KMLLQEAGVP AIDEKLLLQG LLAGKPLFEP QVNASASPKP QSIDLDQSEN
DFIDAYNALT RSSPLPNINK TTNSTEMFNS NKVVSQNDSI NGEIMNGTAN GRIETVNEIT
NQNTQSITNS KQIKKIDHKQ LSKIKQNNKL PTKSEQNEKN IVDKVNTSSN EIIPLINSST
NHINLNAQNL NKNESSVESN TSHFHKNHKS EENLSDRSNQ RQIDEKSNLN DIVDNTQRLI
QQMKEEINSD INSIDGRTMS HSEGESSSDE TNDEQESSYS DTEERTENMT SDEKELTSSE
DEDPSEKQQA MQYHMTSSEE NENFEEALDH VENQLEDFKH ANIEMLDSIA RTLQEEHTFT
VEVDETPKTD APEPLRKEDV NNNVFVAVNS FEEIYEELST QNNSDKNVSS KSQFNLNVEE
VAIPRNIDLL GKEAVFFSVM QTIAPTKLVI SKNVLPILNA KLGTVQETDN VNSNTVNVSS
PQQTNEKNTS NSVEPLVEQD ISLTEIEIQP VSKQAEFLET TNEPSDDHPV EILNLEEPQP
LLPDADEHTE PEALNISENN SNNENSIKDT PISLEEAGNG QNVESEQIPA YSSNDNSINK
NTISSKSNIP KLVRIIPNNK IKNDKNSPKL IVSKVPVRRT SIKQYPAPAP PKSHFGNIQS
GHVKQLQTRL FNNKTVKPTN PTSSETIEVK PSTSTMSKKK PAPPPPIQMK QEKQPSPSKT
VTTPKEKKPF FRETCRTEDE WTDSDSDDSQ LQIVRPVEEP KQSPPSPPPP ITMRRVSGQI
IDLAKIRLPE GSPERQARML LAEGATETWE QAQLAVELVS RGADPPAALL AALECIDLSS
ALAYLYQDCE LCASRLPEHE MVSMLRCTHR CCRECAHHYF TVQITERSIA DCVCPYCKLP
ELENLPEDAW LEYFAHLDIL LKTLLEVDVH ELFQRKLRDR TLARDPNFRW CMECSSGFFV
HPKQKKIRCP ECRSISCASC RKPWNSNHEG LSCEQYTAWL EDNDPERSMT AIQQHLRDNG
LECPRCHFKY SLSRGGCMHF TCTQCKYEFC YGCGKPFTMG ARCGLSDYCA KLGLHAHHPR
NCLFYLRDKE PHELQTLLQM NNVTYETNAS EGSTGRCPVQ LQRETPTGLV DGTCGSEAPA
NYAGLCKNHY LEYLSRSVRR CNIDPLPILG IDDLETLVRR AAFRLPPRPY GSLDGLYKRA
LVEIVKEKIP LD
//
