ID A0A6P6YML9_DERPT Unreviewed; 1335 AA.
AC A0A6P6YML9;
DT 02-DEC-2020, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 1.
DT 18-JUN-2025, entry version 22.
DE SubName: Full=Uncharacterized protein LOC113799792 {ECO:0000313|RefSeq:XP_027206289.1};
GN Name=LOC113799792 {ECO:0000313|RefSeq:XP_027206289.1};
OS Dermatophagoides pteronyssinus (European house dust mite).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Sarcoptiformes; Astigmata; Psoroptidia; Analgoidea;
OC Pyroglyphidae; Dermatophagoidinae; Dermatophagoides.
OX NCBI_TaxID=6956 {ECO:0000313|Proteomes:UP000515146, ECO:0000313|RefSeq:XP_027206289.1};
RN [1] {ECO:0000313|RefSeq:XP_027206289.1}
RP IDENTIFICATION.
RC STRAIN=Airmid {ECO:0000313|RefSeq:XP_027206289.1};
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_027206289.1; XM_027350488.1.
DR FunCoup; A0A6P6YML9; 10.
DR EnsemblMetazoa; XM_027350488.1; XP_027206289.1; LOC113799792.
DR GeneID; 113799792; -.
DR KEGG; dpte:113799792; -.
DR InParanoid; A0A6P6YML9; -.
DR OMA; ELECELC; -.
DR OrthoDB; 9978677at2759; -.
DR Proteomes; UP000515146; 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; cd20337; BRcat_RBR_HOIP; 1.
DR CDD; cd20351; Rcat_RBR_HOIP; 1.
DR Gene3D; 6.10.140.1100; -; 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; 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; 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; 1.
DR SMART; SM00184; RING; 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; 2.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000515146};
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 958..1195
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 962..1011
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 1064..1107
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 69..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 229..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 291..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 915..939
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..90
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..104
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..260
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..304
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1335 AA; 153421 MW; B36079D5AF727912 CRC64;
MPMMMVNDYR LSSLSRDAKN RLRRARMKRS QSTTTMYNGS VNRKHFVNDE ILVPDNRPIR
REKSIMMTHS PSPATVSIKS SKSLSIDPNR SYSDTVSDSS SSSMQSRNKI IDSVVFVKNL
SKNKVDSEHV QSMIGGWSCH FCTFINNSDR NVCDICCKTR LSPVEQIKST NSNPIPKNEN
LSIKTDEQPI QNEQEIIFDE NFVQEQIEIE KKLQQQKENE LNLMETNKKF ESSHQIDSSS
GIIEKPIDDD SISKKIDQKS TDNGNKGLDH DDEKIVAKII EEKISQQFEK LKLSPQSSSL
TSRSVDNDQS NVSPINKDPI ISPTNPTIQS MNQQQFYPIK SNYSWSNCST PLPLNQINYH
SHRPSSSLSS SNNSMANNIF GLNQSMMMDS PYYQQNLNFQ DDIQSIISNS SNSSLFYPNF
VPNQQQQQKS LINSGKQMIQ IIRDAEKKGY SSDDLEVAIQ FDPVSPLEWL EKNWKNLCEI
VRTISNNQIV EFESTNGNSK IENFSMITEK DAKIALRLCK GNLLQSIEKC VQRYQENKLF
DSNVNKNLPT KSEFFAMKVT GVGSGRANND ANHLINANDN LEFQESNNAK EFNLSKHSKL
PMEEFLQSPD GLMDKDKLLE FYLENIRDSK NLPDFNQLET LIMNWQKEKM INDQEREQSR
IREKERQKMQ KLIDIQKRID NGGGGSGYLS DGTTTEEELD REVARVFQNR PSLSSSELMI
DSSDHTPIFT EQDINRQQQQ SKNRKQRIET KLNELVAKHT AAATAAISSS NDENITPIQQ
TVVDAEEELS PISISAESDD NFTDAVAEIE SSSPLFLSSK QQQQQNKQIK AQIVIDQIYK
FMATTQPVKN VAGKFSIGNP ICLLSTKKIM EKIYRNPLNL QTISSINTDV RQPQTTGNPI
LIQPAETPKL IKSSPVNKLE SAEPESSSLS IVEKSNSPLS SPVEQQQQYS YEFQWARTEL
ECELCTRIVS IDDIIVMITC QHYACHNCMK NYLQIQIREQ QRLVIQCPFC NEPDIGAEQD
EKVFEYLAIF DPFIRHIIDR DVYELFQRKM RDRALMRDPN FLWCIKCSSG FIVPNPKALT
VICPDCRHTF CRSCKKQWKQ QHLNQSCEQF ALWEKDHSLD YAEQLLNKHL EEFGIECPNC
HFRYQLAKGG CMHFRCTQCS FDFCGGCYRP FKLGSRCFRA KVCERLGLHA HHPRNCLFYL
RDKDISDLRK LLDENHIEYK TDDDVNDQNK KTTTATTTSI TTLSRCQVME QKEVNFAMKD
KPCNRFVDVA GLCKLHYKEY LGNLIYRNRI DPISIFNEME LELTLKRENI RIPSKIRGED
YLGKLKELIL EKIPL
//
