ID A0AAE1GV73_9NEOP Unreviewed; 926 AA.
AC A0AAE1GV73;
DT 29-MAY-2024, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2024, sequence version 1.
DT 28-JAN-2026, entry version 9.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=KUF71_019846 {ECO:0000313|EMBL:KAK3909837.1};
OS Frankliniella fusca.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Paraneoptera; Thysanoptera; Terebrantia; Thripoidea; Thripidae;
OC Frankliniella.
OX NCBI_TaxID=407009 {ECO:0000313|EMBL:KAK3909837.1, ECO:0000313|Proteomes:UP001219518};
RN [1] {ECO:0000313|EMBL:KAK3909837.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PL_HMW_Pooled {ECO:0000313|EMBL:KAK3909837.1};
RC TISSUE=Head {ECO:0000313|EMBL:KAK3909837.1};
RA Catto M.A., Jacobson A., Kennedy G., Labadie P., Hunt B.G., Srinivasan R.;
RL Submitted (JUL-2021) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KAK3909837.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PL_HMW_Pooled {ECO:0000313|EMBL:KAK3909837.1};
RX PubMed=37344773;
RA Catto M.A., Labadie P.E., Jacobson A.L., Kennedy G.G., Srinivasan R.,
RA Hunt B.G.;
RT "Pest status, molecular evolution, and epigenetic factors derived from the
RT genome assembly of Frankliniella fusca, a thysanopteran phytovirus
RT vector.";
RL BMC Genomics 24:0-0(2023).
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:KAK3909837.1}.
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DR EMBL; JAHWGI010000122; KAK3909837.1; -; Genomic_DNA.
DR AlphaFoldDB; A0AAE1GV73; -.
DR Proteomes; UP001219518; Unassembled WGS sequence.
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 Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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 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; 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; 4.
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:UP001219518};
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 8..48
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 320..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 372..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 399..461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 528..684
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..356
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 399..420
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..568
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 569..579
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 588..597
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 645..663
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 926 AA; 103185 MW; F88F70AC51833FD5 CRC64;
MSTTDNTCVV CFKTVEIYSI GVCDHPVCYE CSTRMRVLCR QNECPICRQD LPKVIFSKNV
RPYKEVATKS YPSDKEFKIL FDGGPAKSAF EKLLQHECSI CGSSKTFNTF QLLKDHMRKS
HELFYCDLCV DNLKIFSHER RVYTRQDLAH HRRKGDVDDR SHKGHPLCQF CDQRYMDNDE
LFRHLRKDHL FCHFCDADGL HQYYSTYDVL REHFKKEHFL CEEGTCYEEQ FTSAFRSEID
LKAHRASSHS RSMGKQAAKQ ARTLEVEFTL APRRERIDRN FRGGDRPMRR PMSPSFVCNH
AGACNCNRED TVAQLDSAVR STPDLRPSDE PRLNPNDFPS LGGNSSSTVP TLVSSGGSKG
RGSAVMIRAG RPPLKTDENF PALSEAAPAP SHKVWLSVNS RGQQDRPTSA PTNFSIQVNR
RQPPSNPAQP QSSMQTLSSR NVRMRGPAPV STGSSDLGDA NFPALKPLDS YRGISAEQWI
SSQPADGPNP VRSKVSTLSS AEAAQLLNNK PSNQQQSSKK PQFVIEEDFP SLGPSSSGAP
ISAKKPNVKK ASSVTIPMSN SWSQQARDNS PEKSSDSDVH SSAASNTKSK KKKKKSKNVN
VSESADKKVL SEQTFSNASS ESSKKKKKQK QQPSQDQEVS KERPNCQNGK LESNDIGNQS
KANQENRDPI PDGSQGSNSR KRSELQIESL HINETQSSME DTTNRLLSIL RGDNALQKSS
ASSSINPPPG FELPVEPVPS LKSVPPPGFS VKVNSVPRSP SNQLTFTSSS GESYPILPTV
RLHQFVQPPD FQRRNAALMA RVIDTLKDPS LQEEFRQMSI LFRQGQLSAA SYYKHCVELM
GEKAFNNCFP EMLVLLPEID RQQDLLAVYS QFNSGKAPLP KFEVCASCRQ VLAPSDLRVH
ASTHSLENNF PALSSSESLP SAWNRK
//
