ID A0A067QV85_ZOONE Unreviewed; 946 AA.
AC A0A067QV85;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 28-JAN-2026, entry version 42.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=L798_13186 {ECO:0000313|EMBL:KDR12980.1};
OS Zootermopsis nevadensis (Dampwood termite).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Polyneoptera; Dictyoptera; Blattodea; Blattoidea; Termitoidae;
OC Termopsidae; Zootermopsis.
OX NCBI_TaxID=136037 {ECO:0000313|EMBL:KDR12980.1, ECO:0000313|Proteomes:UP000027135};
RN [1] {ECO:0000313|EMBL:KDR12980.1, ECO:0000313|Proteomes:UP000027135}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Whole organism {ECO:0000313|EMBL:KDR12980.1};
RX PubMed=24845553; DOI=10.1038/ncomms4636;
RA Terrapon N., Li C., Robertson H.M., Ji L., Meng X., Booth W., Chen Z.,
RA Childers C.P., Glastad K.M., Gokhale K., Gowin J., Gronenberg W.,
RA Hermansen R.A., Hu H., Hunt B.G., Huylmans A.K., Khalil S.M.,
RA Mitchell R.D., Munoz-Torres M.C., Mustard J.A., Pan H., Reese J.T.,
RA Scharf M.E., Sun F., Vogel H., Xiao J., Yang W., Yang Z., Yang Z., Zhou J.,
RA Zhu J., Brent C.S., Elsik C.G., Goodisman M.A., Liberles D.A., Roe R.M.,
RA Vargo E.L., Vilcinskas A., Wang J., Bornberg-Bauer E., Korb J., Zhang G.,
RA Liebig J.;
RT "Molecular traces of alternative social organization in a termite genome.";
RL Nat. Commun. 5:3636-3636(2014).
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}.
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DR EMBL; KK852980; KDR12980.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A067QV85; -.
DR FunCoup; A0A067QV85; 257.
DR STRING; 136037.A0A067QV85; -.
DR eggNOG; KOG2231; Eukaryota.
DR InParanoid; A0A067QV85; -.
DR OMA; FYCDICT; -.
DR OrthoDB; 3838338at2759; -.
DR Proteomes; UP000027135; 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; 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:UP000027135};
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 14..54
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 280..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 402..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 552..579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 593..673
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..299
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..459
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 602..626
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 651..662
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 946 AA; 105234 MW; 02E5EF3E567DD265 CRC64;
MTSNVITENS ENACVVCFKN VVIYSVGECD HPVCYECSTR MRVLCRQNEC PICRQDMPKV
IFTKEVQLFR NIKNYSYLMD KKFKICFDTA DIQAAYSRLL EHVCSVCTGR PAFRTFQNLK
DHMRKEHELQ YCDLCVENLK IFTGERRCYT RQELALHRRK GDPDDRSHRG HPLCEFCDQR
YMDSDELFRH LRRDHLFCHF CDADGFHQYY SSYDYLREHF RSEHFLCEEG NCMEEKFTSV
FRTEIDLKAH RASVHGRSIG KAATKQARML ELEFTLAPRP RDRLDGMRGG RRGSGRQRMR
HDEEEPQGAV GGDCDNQHFD PAPMFRNAPN INTSCIEEFP TLGGEAPPVL GPPLRQNSRK
VPANNSGLTI RTVHQSQPLA ITDENFPALG LEGSTGGCKT VRLSVNSGSQ DRPNSAAASS
IRGSNQKAPT NVSIHVNHRP SGSSQNIHIR PTSVPSQFHS DFPSLSGSKV STASSSVQWL
GNHGSMGAKT KVQPQTQAPR AFKTEEDFPS LSSKFSTGCN VANTTSSSDA GSDDRFKKAS
SVMIPVTSSW TMTQGSSDVS RIHESSGEPS GIPGRSNYDI LANTTSSLGN IKVKSRKKKT
KNAVSHNANM YSNDSVLTKP AQSAVSESGK RKKKQGNREA EVQQNTQTNK NDCENRENEK
PAEFGNGTDN SSTFERKRSE LLIQSLTPQD ATEDNNNELS TSFNDRVYED MYPPFSSEIL
DDFHAIGSPG CWPPGLDVPV NRGKLSSAPP PGFGGTTNSC STTAPPPGFS VTLNSVARPQ
SNGLTFTSSS GQSYSILPGR SGNSYKFVPP QDFSHRNQAL VTRVKKMLGD AQSVDEFCQL
SKMFRQGDIS ASDFYTHCQE KMGMKEFTEI FAELLVLLPD IEKQQELWSV HADTGKWSAK
DLEVCATCQQ VLSAADLRHH VGSHTLENHF PALGSSEPVS QTWGKK
//
