ID A0A9J6ER01_RHIMP Unreviewed; 846 AA.
AC A0A9J6ER01;
DT 28-JUN-2023, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2023, sequence version 1.
DT 28-JAN-2026, entry version 12.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=HPB51_001360 {ECO:0000313|EMBL:KAH8036541.1};
OS Rhipicephalus microplus (Cattle tick) (Boophilus microplus).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Parasitiformes; Ixodida; Ixodoidea; Ixodidae; Rhipicephalinae;
OC Rhipicephalus; Boophilus.
OX NCBI_TaxID=6941 {ECO:0000313|EMBL:KAH8036541.1, ECO:0000313|Proteomes:UP000821866};
RN [1] {ECO:0000313|EMBL:KAH8036541.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Rmic-2018 {ECO:0000313|EMBL:KAH8036541.1};
RX PubMed=32814014;
RG Tick Genome and Microbiome Consortium (TIGMIC);
RA Jia N., Wang J., Shi W., Du L., Sun Y., Zhan W., Jiang J.F., Wang Q.,
RA Zhang B., Ji P., Bell-Sakyi L., Cui X.M., Yuan T.T., Jiang B.G., Yang W.F.,
RA Lam T.T., Chang Q.C., Ding S.J., Wang X.J., Zhu J.G., Ruan X.D., Zhao L.,
RA Wei J.T., Ye R.Z., Que T.C., Du C.H., Zhou Y.H., Cheng J.X., Dai P.F.,
RA Guo W.B., Han X.H., Huang E.J., Li L.F., Wei W., Gao Y.C., Liu J.Z.,
RA Shao H.Z., Wang X., Wang C.C., Yang T.C., Huo Q.B., Li W., Chen H.Y.,
RA Chen S.E., Zhou L.G., Ni X.B., Tian J.H., Sheng Y., Liu T., Pan Y.S.,
RA Xia L.Y., Li J., Zhao F., Cao W.C.;
RT "Large-Scale Comparative Analyses of Tick Genomes Elucidate Their Genetic
RT Diversity and Vector Capacities.";
RL Cell 182:1328-1340(2020).
RN [2] {ECO:0000313|EMBL:KAH8036541.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Rmic-2018 {ECO:0000313|EMBL:KAH8036541.1};
RC TISSUE=Larvae {ECO:0000313|EMBL:KAH8036541.1};
RA Jia N., Wang J., Shi W., Du L., Sun Y., Zhan W., Jiang J., Wang Q.,
RA Zhang B., Ji P., Sakyi L.B., Cui X., Yuan T., Jiang B., Yang W.,
RA Lam T.T.-Y., Chang Q., Ding S., Wang X., Zhu J., Ruan X., Zhao L., Wei J.,
RA Que T., Du C., Cheng J., Dai P., Han X., Huang E., Gao Y., Liu J., Shao H.,
RA Ye R., Li L., Wei W., Wang X., Wang C., Huo Q., Li W., Guo W., Chen H.,
RA Chen S., Zhou L., Zhou L., Ni X., Tian J., Zhou Y., Sheng Y., Liu T.,
RA Pan Y., Xia L., Li J., Zhao F., Cao W.;
RL Submitted (SEP-2021) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the ZNF598/HEL2 family.
CC {ECO:0000256|ARBA:ARBA00035113}.
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:KAH8036541.1}.
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DR EMBL; JABSTU010000002; KAH8036541.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A9J6ER01; -.
DR VEuPathDB; VectorBase:LOC119179463; -.
DR OMA; CEKKYDI; -.
DR OrthoDB; 3838338at2759; -.
DR Proteomes; UP000821866; Chromosome 10.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0043022; F:ribosome binding; IEA:TreeGrafter.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:TreeGrafter.
DR GO; GO:0072344; P:rescue of stalled ribosome; IEA:InterPro.
DR CDD; cd16615; RING-HC_ZNF598; 1.
DR InterPro; IPR057634; PAH_ZNF598/HEL2.
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 PANTHER; PTHR22938:SF0; E3 UBIQUITIN-PROTEIN LIGASE ZNF598; 1.
DR PANTHER; PTHR22938; ZINC FINGER PROTEIN 598; 1.
DR Pfam; PF23202; PAH_ZNF598; 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 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000821866};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
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 286..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 349..606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 619..678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..314
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..414
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..456
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 551..562
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 585..606
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 846 AA; 94231 MW; 833926AF997C4259 CRC64;
MDVNENDSVC IVCWRDIHVY AIGLCDHPVC HECSTRMRVL CRKSECPICR RTLPKVIFVK
ECRPFEELNK RLYQVDARPQ ICFEDESVRQ AYRELLDNRC KYCPPSSTKA PTVFSSFAQL
RNHVRKEHSR TYCDLCIEHL KIFPGERTAY TRRDMVRHQN YGDVDDTSHK GHPLCKFCDV
RYFDNDELYR HLRRDHYYCH FCGDDYRLQY YRNYEYLRAH FREEHFLCEE GDCRNETFTA
AFRTEIDLKA HRAQHHNRSL TKAQAKQART LDLEFAVTPR SSANSYNSSG YYDDSGGHGR
RQSRQPRSGR APPSDASREN LLARSQASED LHMTWELQPP VDYRCEKEFP QLGSDKGTPA
PSTSSGSKAP VDPFPVAASS YPPRRPNKVN VNSVDEFPSL NPSSSTATQQ GSAAPLPATM
VPLRKSTKAQ GKGHANGIPP GQRSVGKQQQ DANNNGPREK TTLDWFAQPS GDRSLVKPQL
STVSAVVSAR PAPELGRPKQ ALPKMGLDED FPTLATRSVA RISISSSPTP SPQSEPPWNT
AKSAKIKKKK KTEETKQMES SKHPPGIEIN NNTTTKASAA VASKEQASTQ PLETSSESKP
SFVPPTNNLL QLIAAARKGT TMPAPPEPAS EVVCDVDSSD SDEPPRLTVS DFPSLNGRPP
GTAAPPPGFG KPKKPPPGFA RANMCDMPMG TLSSLVKATT PTTSPAVPPQ YMPPAGFQER
NLALIQDVQQ TLAKRSEDGL FATFKTLSGS FRQSVLSADE YFARCIELFG SEKEFMTIFP
ELLFLLPDIR KQQELMATYN AHRKAQAATS GALPKGPPVQ LLVCATCQQV LSAEDFRSHR
TVHDPS
//
