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Database: UniProt
Entry: A0A0V0YJ39_TRIPS
LinkDB: A0A0V0YJ39_TRIPS
Original site: A0A0V0YJ39_TRIPS 
ID   A0A0V0YJ39_TRIPS        Unreviewed;      1433 AA.
AC   A0A0V0YJ39;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=E3 ubiquitin-protein ligase RBBP6 {ECO:0000313|EMBL:KRY00003.1};
DE   Flags: Fragment;
GN   Name=Rbbp6 {ECO:0000313|EMBL:KRY00003.1};
GN   ORFNames=T4E_1269 {ECO:0000313|EMBL:KRY00003.1};
OS   Trichinella pseudospiralis (Parasitic roundworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=6337 {ECO:0000313|EMBL:KRY00003.1, ECO:0000313|Proteomes:UP000054815};
RN   [1] {ECO:0000313|EMBL:KRY00003.1, ECO:0000313|Proteomes:UP000054815}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS141 {ECO:0000313|EMBL:KRY00003.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRY00003.1}.
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DR   EMBL; JYDU01000011; KRY00003.1; -; Genomic_DNA.
DR   STRING; 6337.A0A0V0YJ39; -.
DR   Proteomes; UP000054815; Unassembled WGS sequence.
DR   GO; GO:0019899; F:enzyme binding; IEA:UniProt.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd16620; vRING-HC-C4C4_RBBP6; 1.
DR   Gene3D; 4.10.60.10; Zinc finger, CCHC-type; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR014891; DWNN_domain.
DR   InterPro; IPR025829; Zn_knuckle_CX2CX3GHX4C.
DR   InterPro; IPR001878; Znf_CCHC.
DR   InterPro; IPR036875; Znf_CCHC_sf.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR15439; RETINOBLASTOMA-BINDING PROTEIN 6; 1.
DR   PANTHER; PTHR15439:SF0; SOMETHING THAT STICKS LIKE GLUE, ISOFORM A; 1.
DR   Pfam; PF08783; DWNN; 1.
DR   Pfam; PF13920; zf-C3HC4_3; 1.
DR   Pfam; PF13696; zf-CCHC_2; 1.
DR   SMART; SM01180; DWNN; 1.
DR   SMART; SM00343; ZnF_C2HC; 1.
DR   SUPFAM; SSF57756; Retrovirus zinc finger-like domains; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS51282; DWNN; 1.
DR   PROSITE; PS50158; ZF_CCHC; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054815};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00047}.
FT   DOMAIN          28..100
FT                   /note="DWNN"
FT                   /evidence="ECO:0000259|PROSITE:PS51282"
FT   DOMAIN          202..216
FT                   /note="CCHC-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50158"
FT   DOMAIN          295..334
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          722..974
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1000..1042
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1055..1433
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        727..741
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        756..810
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        814..877
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        891..908
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        909..923
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        924..944
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        945..969
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1001..1042
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1055..1069
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1092..1143
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1192..1230
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1245..1259
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1270..1301
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1363..1397
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1398..1421
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KRY00003.1"
SQ   SEQUENCE   1433 AA;  159053 MW;  4BC9E9CBDA8B30F4 CRC64;
     LLFCCLRELV VEAAFVLLFC VVPVMSCIHY KFKSSLDYKT VSFEGLSVTL TNLKRLILEK
     EGIRTADFDL KVSNAQTGKE YTEDGGPIMR HTSVVVARVP ADAQRRLPKV WDRSTEGVVV
     SSSSSIDSVG FSSLLVRFAF YEFAIGAFLQ FAFINLQKTG KNMTEEERIK LMEKESTREY
     DPSKYCKKNV TLTGTPPPSY LCNRCGQTGH WIKFCPTLNV KRTTGIPKNE LLETTPDDPQ
     AMMTSIGTFA VPVLHKNAFL IGKKEKPFIS EEDDESLRKP AEASEKEALP TELLCSLCDN
     ILKDAVVIPC CGFSFCDQCI RKHLLGKQEC PNCREPAVAA ASLIPNGQLR MAVLKYRREK
     DCQNKPAAVH IPMAATMKCP QSLASTSNAA VCKNVAKNSI TAVQAGGGGA GAFSSSKQEN
     LLSSKAVKPT VGARGGGVEQ KMNPNVFGSS TKLTNMVPRC ITNHNYNSTN ATAVLVSNNS
     TAKSNPKNTG VPLTTVTSAA MKCSALTATA PAAAFLGVAS SNANNAAGVG GGNGNNVVGG
     NGGAGAGGGT VMTTKAAVLR ANSPNAPVFP PTIPPYMPQP YYAGFQGLAS YPVSIPPPVL
     PVAMPVRPFG TPFPSQPPPP GCTYILLGKL THSRHISHQQ TYDRWWTRSH FAWKKVILYQ
     SINKLNRNYR DRDAWDDYLA LKDRLRPSRR TSSDSSRSPR RRRRRSSNFF CFVFNRSSHR
     HSSYRKSSRD RYREISKSHS SRRSSSTRHR HDSSRGRRVT AVVEEKRTRE RRKYENDHRH
     QKSDQRRDAK DDGSKGSKKK NVDVMKEVVR EASLKPTNMN NQDENESNVN KSQQSVVKTT
     DGERSKSIPA VNRQDTKRST AKVATASTNT STSAAVDGKV EATDKRHYSS SSKRSSKHHH
     HHHHHHQQQQ QQQQQQQQHR VKRKLSSSTA EGKENLDVHS NLKRKPTPSK SGGSKRRSPA
     TTTTTVAGAR NKDDDNDVLV SERLDFCELT EIDVYTLSEC EKSATEPTPG SEKTNNIQQQ
     PEQQQQHQEQ QEQPKNNNQK ATTITTTTVE LKARNSNGCQ QQKQQQQQQQ RQTEKKRNHG
     QPPAVGGDSR GRSVAEKTHD KKLHRDCNNN GKEEKRDEHR PKKGGGDIVM EKRNRDERPK
     VSSLNVVAEE LPAADDDTAS AIVADVNDAD GVGDSGGGGG GGAAAGADAA EVDGNEEGKE
     QPEKQETAKV SHHQQEQPND QEKQNEDQDG GKSLNSDSAE NKKEKKRKKQ KRKKKKKDRK
     EATSAASSSG KSKKKKKHHR RRRRRQHSRH RRHHRRHNHH RADGSRDQSS SSPPPPRPES
     KRHHRKKRSK RADDHTSDTA AGGGGGADNG ELVVDKKKAV KYSKSTYASS SSNNNNNNNN
     NNSKHRYAQY NNSGNNHEDL HSRMERRWDA SEEEGRTSSR HKSDGRHRRH RYH
//
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