GenomeNet

Database: UniProt
Entry: E0VIV1_PEDHC
LinkDB: E0VIV1_PEDHC
Original site: E0VIV1_PEDHC 
ID   E0VIV1_PEDHC            Unreviewed;       624 AA.
AC   E0VIV1;
DT   02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2010, sequence version 1.
DT   24-JAN-2024, entry version 67.
DE   RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU367105};
DE            EC=2.3.2.27 {ECO:0000256|RuleBase:RU367105};
GN   Name=8230174 {ECO:0000313|EnsemblMetazoa:PHUM233590-PA};
GN   ORFNames=Phum_PHUM233590 {ECO:0000313|EMBL:EEB13307.1};
OS   Pediculus humanus subsp. corporis (Body louse).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Paraneoptera; Psocodea; Phthiraptera; Anoplura; Pediculidae;
OC   Pediculus.
OX   NCBI_TaxID=121224;
RN   [1] {ECO:0000313|EMBL:EEB13307.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=USDA {ECO:0000313|EMBL:EEB13307.1};
RA   Kirkness E., Hannick L., Hass B., Bruggner R., Lawson D., Bidwell S.,
RA   Joardar V., Caler E., Walenz B., Inman J., Schobel S., Galinsky K.,
RA   Amedeo P., Strausberg R.;
RT   "Annotation of Pediculus humanus corporis strain USDA.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EEB13307.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=USDA {ECO:0000313|EMBL:EEB13307.1};
RG   The Human Body Louse Genome Consortium;
RA   Kirkness E., Walenz B., Hass B., Bruggner R., Strausberg R.;
RT   "The genome of the human body louse.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EnsemblMetazoa:PHUM233590-PA}
RP   IDENTIFICATION.
RC   STRAIN=USDA {ECO:0000313|EnsemblMetazoa:PHUM233590-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC         EC=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900,
CC         ECO:0000256|RuleBase:RU367105};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|RuleBase:RU367105}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU367105}.
CC   -!- SIMILARITY: Belongs to the Deltex family.
CC       {ECO:0000256|ARBA:ARBA00009413, ECO:0000256|RuleBase:RU367105}.
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DR   EMBL; AAZO01002709; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; DS235206; EEB13307.1; -; Genomic_DNA.
DR   RefSeq; XP_002426045.1; XM_002426000.1.
DR   AlphaFoldDB; E0VIV1; -.
DR   STRING; 121224.E0VIV1; -.
DR   EnsemblMetazoa; PHUM233590-RA; PHUM233590-PA; PHUM233590.
DR   GeneID; 8230174; -.
DR   KEGG; phu:Phum_PHUM233590; -.
DR   CTD; 8230174; -.
DR   VEuPathDB; VectorBase:PHUM233590; -.
DR   eggNOG; ENOG502QQ9M; Eukaryota.
DR   HOGENOM; CLU_030422_4_0_1; -.
DR   InParanoid; E0VIV1; -.
DR   OMA; MFYAPSS; -.
DR   OrthoDB; 5487971at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000009046; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniRule.
DR   CDD; cd09633; Deltex_C; 1.
DR   Gene3D; 3.30.390.130; -; 1.
DR   Gene3D; 3.30.720.50; -; 2.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR039396; Deltex_C.
DR   InterPro; IPR039399; Deltex_C_sf.
DR   InterPro; IPR039398; Deltex_fam.
DR   InterPro; IPR004170; WWE-dom.
DR   InterPro; IPR018123; WWE-dom_subgr.
DR   InterPro; IPR037197; WWE_dom_sf.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR12622; DELTEX-RELATED; 1.
DR   PANTHER; PTHR12622:SF4; PROTEIN DELTEX; 1.
DR   Pfam; PF18102; DTC; 1.
DR   Pfam; PF02825; WWE; 2.
DR   Pfam; PF13639; zf-RING_2; 1.
DR   SMART; SM00184; RING; 1.
DR   SMART; SM00678; WWE; 2.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   SUPFAM; SSF117839; WWE domain; 2.
DR   PROSITE; PS50918; WWE; 2.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|RuleBase:RU367105};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU367105};
KW   Notch signaling pathway {ECO:0000256|ARBA:ARBA00022976};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009046};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU367105};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU367105};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          1..74
FT                   /note="WWE"
FT                   /evidence="ECO:0000259|PROSITE:PS50918"
FT   DOMAIN          75..154
FT                   /note="WWE"
FT                   /evidence="ECO:0000259|PROSITE:PS50918"
FT   DOMAIN          423..472
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          217..254
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        217..232
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        238..254
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   624 AA;  70929 MW;  B418D5E975EB9187 CRC64;
     MSNHVVVVWE WENRQGRWRP YTPEVSQHLE RAHAKKLTRV FLSDADPTLD KYFINLTTKK
     QYLDEAGVPY NVRRNFYQPS SPAGKGSKWE WEGDSLGEWH TYDMDVQCLI EAAWAKGEQT
     IDISKTYLGF PYVINFLNLT QVKASTGYVR NVRRVQQAPY PLVKLSQEEM TAFLVNTQIT
     QNSYKQQLER NTENISKPKK NNIARTILNI FGSHYPNSSK ESQSSVRTRE FWDTDSSSTK
     SGRRPSVDTV STYLSHDTAS RGTVADSLDS SEDDIFEGKS YLAKFSKDCN KKKFLQSSKH
     QKIMIKKEIP NMVNKFKNIQ QNCHKLSSAK KSRSEENFLS ESTLKNDGVY VGSYNEDVIP
     YFSKLRASKR NVKTDQSFNG RDWLQTRDYC STDGAIIGVD SASQMVSQFV TVVKSSRWGE
     TTCPICLTDL IDPNDIIVAL VSCEHSLHLS CLNKMLTAQK SQNMYIQCPV CQRIYGEKRG
     NQPPCTMDCC ILHWSLPGHP NARTIQITYN TTSGIQGPEH PNPGKPYYAV GFPRVCYLPD
     TDKGRLVLDL LKVAFERRLI FTVGSSATTG KEDVVTWNEI HHKTEPGISR TGYGYPDPNY
     LDNCLAELAR QGVTPDHSAY QHLP
//
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