ID A0A1I8H820_9PLAT Unreviewed; 2624 AA.
AC A0A1I8H820;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE SubName: Full=RING-type domain-containing protein {ECO:0000313|WBParaSite:maker-uti_cns_0004911-snap-gene-0.9-mRNA-1};
OS Macrostomum lignano.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX NCBI_TaxID=282301 {ECO:0000313|Proteomes:UP000095280, ECO:0000313|WBParaSite:maker-uti_cns_0004911-snap-gene-0.9-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:maker-uti_cns_0004911-snap-gene-0.9-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) 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 WBParaSite; maker-uti_cns_0004911-snap-gene-0.9-mRNA-1; maker-uti_cns_0004911-snap-gene-0.9-mRNA-1; maker-uti_cns_0004911-snap-gene-0.9.
DR Proteomes; UP000095280; Unplaced.
DR GO; GO:0071797; C:LUBAC complex; IEA:InterPro.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd20337; BRcat_RBR_HOIP; 1.
DR Gene3D; 1.20.120.1750; -; 4.
DR InterPro; IPR047540; BRcat_RBR_RNF31-like.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR026254; RNF31-like.
DR InterPro; IPR041031; RNF31_C.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR013087; Znf_C2H2_type.
DR InterPro; IPR001876; Znf_RanBP2.
DR InterPro; IPR001841; Znf_RING.
DR PANTHER; PTHR16004:SF2; E3 UBIQUITIN-PROTEIN LIGASE RNF31; 1.
DR PANTHER; PTHR16004; RING FINGER PROTEIN 31-RELATED; 1.
DR Pfam; PF18091; E3_UbLigase_RBR; 3.
DR Pfam; PF01485; IBR; 4.
DR SMART; SM00647; IBR; 8.
DR SMART; SM00184; RING; 7.
DR SMART; SM00355; ZnF_C2H2; 4.
DR SMART; SM00547; ZnF_RBZ; 3.
DR SUPFAM; SSF57850; RING/U-box; 9.
DR PROSITE; PS51873; TRIAD; 4.
DR PROSITE; PS50089; ZF_RING_2; 2.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
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:PRU00042}.
FT DOMAIN 44..271
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 48..95
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 1185..1411
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 1452..1700
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 1863..1894
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 2014..2241
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 2438..2483
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 331..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 720..752
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 806..884
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1051..1089
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1103..1125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1885..1945
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 723..751
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 809..872
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1051..1087
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1103..1117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1885..1918
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1929..1945
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2624 AA; 292180 MW; 6A3D8D9450D3F95A CRC64;
MPRRSQWQCP HCTFINDGAQ GRQLHRRLIC SVCGKSTDLS ELQTSAECPV CTDEKKLVEV
PLCGCEVCSD CLCQQIEVRL MNDSSVSVLT CPVCDKLDDR ALTDTSCEYF PLLRRLLAGQ
LKPAVMKKLD ERLRDWRLKL TDNFCWCSGC SNGFEVSEHH DRQVRCPHCG KETCRKCGKA
WHERHRGVSC QQFGEWRQQT DLSERGLAQF LESRGSSCPK CGFQFELSRG GCLHLTCRQC
KAEFCSDCGS LFVRQECCGG NKGLHCHHGS ECVETFRDWP LEKVRQTALE RGVQLELVGV
AGAGGRCSVQ EQKETSGGGL EDGKCGRPVV EGATGAGSSQ KTNPGSRRKP RNHLSIGGKD
WTVATVGKEA KFILTDTKGV DRREPFFRLV PEGVESDGAQ VPVRFRIEAS EGKVKYLCSF
TPKMPGVHLL TFGFGNVTMG RSYRVEVRDL AATDGAVDAA NLVVQRMAHR VFAERCLICS
RPGASIRCLE AGCGFQLICE SCHTNWHSVE NHRVEVLPPP PQAQRRCDTW LTERLQEVKQ
LREFKDFSDT DLIDSIQSCE KACDDVVALL AHLRSQCCKC SKQMPRHKLF HMATCECELC
CGCFCSFLSG MPGQLECPVC GVAWSGDHVA RNTTMILVYE LESQLGNDEA ARLLQIGSAT
KGGTVVHSEA AAAASMLTSA ATAAASAAVG AAGSDFLQRA AAEEQARAAL EIGITAWTDG
SANEGERKQR ERKQREQQQR EQKHREQRGA VVHSEAAAAA SMLTSAATAA ASAAVGAAGS
DFLQRAAAEE QARAALEIGI TAWTDGSANE GERKQREQQQ REQKHREQRE RERKQREQQQ
KEQKQREKQL QREQQQREKQ QKEQKQRETA ERATGGTTKG GAVARSEAAA AASMLTSAAT
AAAVLQSERQ EAILSNACEC QMCPECFEKF LVDLKSSRIQ CPVCQVACDD EDSLDFMRMQ
LMEMEDVLGS DTVEYAVARL EVLVLGAKAC RLAAPTRMAS ASQNIEWQCQ HCTFINSAMC
DTSNPKSRII CSVCSKSVSC QELLDLNQRQ QRAQHLERAP KPKLRKDQHH EQSSHDAVRD
SWSLRDPETD AAAEPFSIGM FQRLSRTRMS ETSSSSGLRR RIGEEHDPDA VEADDIFTRS
LKPFYPTQSA TRGMLHHKQN RPVKKSSLTT ISVRNSKAAP TKTTVSKECP VCTDDKKLVE
VPLCGCEVCS DCLCQQIEVR LMHDSSVSVL TCPVCDKLDD RALTDTSCEF PLLQRLLAGQ
LKPAVMKKLD ERLRDWRLKL TDNFCWCSGC SNGFEVSEHH DRQVRCPHCG KETCRKCGKA
WHERHRGVSC QQFGEWRQQT DLSERGLAQF LESRGSSCPK CGFQFELSRG GCLHLTCRQC
KAEFCSDCGS LFVRQECCGG NKGLHCHHGS ECVETFRDWP LEKVRQTALD RGVELELVGV
AGAGGRCSVQ EQKETSGGGL EDSECGRPVM EAGLCESHLK EALASAMRGK KKKLREQQQN
QQENFFLDLM QNSEFKGRDL YDLAEAAKGS NNRCDYVDFI QGFKQSEYKF DENVVDLVEK
KITEWNLFRD PNFRWCSSCG FGMVLGDIMI GLKFQCPNCE AFTCKECKKP WKDQHEGIDC
DQFEKWLMDN DPEYQEKGVG FFLQANGIEC PNCRFQYALA KGGSLHFTCR MCRFKFCADC
DGEHTIIHGR GLSCKHPRDC LFYLRDFGVD RLQRLLNLHK VEFESEAENP VDKCEVMEQK
EVANGLKDEP CGVDVKPGQA NLCEKHYIEY LVSLVNKQKL DPVSVMDEGE LRGACLREGI
DFSGVGENNV AALRALIAQQ KPLVKLAAPT RMASASENIE WQCQHCTFIN SSVCDTSNPK
SRIICSVCSK SVSCEELLDL HQRQQRAQHL ERAPKPKPRK NQQHRQSFDD ESRASWSLRD
AETDAAAEPL SISMSQRFSR TRMSETSSTL GLRRCIGEER DPGAVEANDI FTRSSKPFYP
THRATEGVLQ WDQIRPLRAI SIRNSKAAPM ETTASKECPV CIDDKKLVEV PLCDCEVCSD
CLCQQIEVRL MHDSSVSVLT CPVCDKLDDR ALTDTSCEYF PLLQRLLAGQ LKPAVMKKLD
ERLRDWRLKL TDNFCWCSGC SNGFEVSEHH DRQVRCPHCG KETCRKCGKA WHERHRGVSC
QQFGEWRQQT DLSERGLAQF LESRGSSCPK CGFQFELSRG GCLHLTCRQC KAEFCSDCGS
LFVRQECCGG NKGLHCHHGS ECVETFRDWP LEKVRQAALE RGVQLELVGV AGAVGRCSVQ
EQKETSGGGL EDGECGRPVV ESGLCESHLK EALASAMHGN KKTLREQQNL FLLLTQRGGA
VARSEAAAAA SMLTSAATSA ASAAVGAAGS DSIEWSDRAQ NLALQLRVED WVAERVLAVK
SMPKFNEFSE SDLAVAIESC GVLAFEDDAL LSQLRRKCSR CSNDLPRHKL VAMAACECQM
CPECFRKFLL ELKSSRIQCP VCKDVCDDED SRDFMRMQLM EMADLLGSDT VEYAVVHLEE
NSSKNSDEGW EVVEAAGKKG TKSKASKDAS TVPLNTSNGY CPHRNGGLPK MDTRTVRKLL
QSLQTECLQE MLRASGLITN GWAAAVIGIM QQVFNKKEII TKCT
//
