ID B7P7I9_IXOSC Unreviewed; 729 AA.
AC B7P7I9;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 28-JAN-2026, entry version 78.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=IscW_ISCW017552 {ECO:0000313|EMBL:EEC02561.1};
OS Ixodes scapularis (Black-legged tick) (Deer tick).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Parasitiformes; Ixodida; Ixodoidea; Ixodidae; Ixodinae; Ixodes.
OX NCBI_TaxID=6945;
RN [1] {ECO:0000313|EMBL:EEC02561.1, ECO:0000313|Proteomes:UP000001555}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wikel {ECO:0000313|Proteomes:UP000001555}, and Wikel colony
RC {ECO:0000313|EMBL:EEC02561.1};
RG Ixodes scapularis Genome Project Consortium;
RA Caler E., Hannick L.I., Bidwell S., Joardar V., Thiagarajan M., Amedeo P.,
RA Galinsky K.J., Schobel S., Inman J., Hostetler J., Miller J., Hammond M.,
RA Megy K., Lawson D., Kodira C., Sutton G., Meyer J., Hill C.A., Birren B.,
RA Nene V., Collins F., Alarcon-Chaidez F., Wikel S., Strausberg R.;
RT "Annotation of Ixodes scapularis.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:ISCW017552-PA}
RP IDENTIFICATION.
RC STRAIN=wikel {ECO:0000313|EnsemblMetazoa:ISCW017552-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 -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SIMILARITY: Belongs to the ZNF598/HEL2 family.
CC {ECO:0000256|ARBA:ARBA00035113}.
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 EMBL; ABJB010035484; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ABJB010162845; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DS652265; EEC02561.1; -; Genomic_DNA.
DR AlphaFoldDB; B7P7I9; -.
DR STRING; 6945.B7P7I9; -.
DR PaxDb; 6945-B7P7I9; -.
DR EnsemblMetazoa; ISCW017552-RA; ISCW017552-PA; ISCW017552.
DR VEuPathDB; VectorBase:ISCI017552; -.
DR VEuPathDB; VectorBase:ISCP_020401; -.
DR VEuPathDB; VectorBase:ISCW017552; -.
DR HOGENOM; CLU_015828_0_0_1; -.
DR InParanoid; B7P7I9; -.
DR OrthoDB; 3838338at2759; -.
DR Proteomes; UP000001555; Unassembled WGS sequence.
DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0072344; P:rescue of stalled ribosome; IBA:GO_Central.
DR CDD; cd16615; RING-HC_ZNF598; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR041888; RING-HC_ZNF598/HEL2.
DR InterPro; IPR056437; Znf-C2H2_ZNF598/HEL2.
DR InterPro; IPR044288; ZNF598/HEL2.
DR InterPro; IPR013087; Znf_C2H2_type.
DR InterPro; IPR059042; Znf_C2H2_ZNF598.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR22938:SF0; E3 UBIQUITIN-PROTEIN LIGASE ZNF598; 1.
DR PANTHER; PTHR22938; ZINC FINGER PROTEIN 598; 1.
DR Pfam; PF25447; RING_ZNF598; 1.
DR Pfam; PF23230; zf-C2H2_13; 1.
DR Pfam; PF23208; zf_C2H2_ZNF598; 1.
DR SMART; SM00355; ZnF_C2H2; 5.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 1: Evidence at protein level;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175};
KW Proteomics identification {ECO:0007829|PeptideAtlas:B7P7I9};
KW Reference proteome {ECO:0000313|Proteomes:UP000001555};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 10..50
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 279..680
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..421
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..521
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..542
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..591
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 620..631
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 729 AA; 80569 MW; 4D21A1FF65C4A0CC CRC64;
MDVKEDDNVC IVCWREIQVY AIGLCDHPVC HECSTRMRVL CRKSECPICR RNLPKVIFVK
EARPFEELNR RLYPVDAHPQ VCFEDDQVRQ AYRALLENRC KYCPPGAKRP VFASFGMLRT
HVRREHHRTY CDLCVEHLKI FPGERTAYSK KDLSRHLHSG DLEDTSHKGH PLCQFCDVRY
FDHDELYRHL RREHYYCHFC GDDYRLQYYR NYEYLREHFR QEHFLCEEGD CRNETFTAAF
RSEIDLKAHR AQHHNRSMTK AQAKQARTLD LEFSIAPRAG VSGNHEDGSH ARRLPRQGGH
QRPNRSGALP QNNREEQPAR GPPSTAQRPA ERQAQTLDLT WEAPPPVDYQ CDKEFPQLGG
EGAGPGTGPF LPTPYSSRRP EQVNFDSVDE FPSLNPSAPP PRPASAVPRA RPPAARASSS
AKPQSNGQAK GGQEDRNNNA GGDPDSRRNG GANVTVRLVQ PPPAASQPSA AACARDGSKA
HSSARGPPKP AFEEDFPALA SRVVPRMSAA SATSAEAGSS SRQQIKTKKK KADEPKRADP
QARKPAPVVD GHPPATESSA VEPSAPHRAA SAPKPSAATD DATNGTNATD NLLQLISAAR
KGNATHPQPS GGESSDSEEE ERRALSQKDF PHLNGRATAA PPGFRKPKPP PGFARPGADR
SRPADVSLAP GAATVPSVPQ APQYTQPARF QQRNLELIGA AVQLLVCATC QQVLSADDFR
SHRTLHDPA
//
