ID E2BQ19_HARSA Unreviewed; 931 AA.
AC E2BQ19;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 28-JAN-2026, entry version 55.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=EAI_05154 {ECO:0000313|EMBL:EFN82207.1};
OS Harpegnathos saltator (Jerdon's jumping ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Ponerinae; Ponerini; Harpegnathos.
OX NCBI_TaxID=610380 {ECO:0000313|Proteomes:UP000008237};
RN [1] {ECO:0000313|EMBL:EFN82207.1, ECO:0000313|Proteomes:UP000008237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R22 G/1 {ECO:0000313|EMBL:EFN82207.1,
RC ECO:0000313|Proteomes:UP000008237};
RX PubMed=20798317; DOI=10.1126/science.1192428;
RA Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G.,
RA Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D.,
RA Wang J., Liebig J.;
RT "Genomic comparison of the ants Camponotus floridanus and Harpegnathos
RT saltator.";
RL Science 329:1068-1071(2010).
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; GL449694; EFN82207.1; -; Genomic_DNA.
DR AlphaFoldDB; E2BQ19; -.
DR FunCoup; E2BQ19; 264.
DR STRING; 610380.E2BQ19; -.
DR KEGG; hst:105185317; -.
DR InParanoid; E2BQ19; -.
DR OMA; FYCDICT; -.
DR OrthoDB; 3838338at2759; -.
DR PhylomeDB; E2BQ19; -.
DR Proteomes; UP000008237; 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; 2.
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:UP000008237};
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 13..53
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 279..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 494..697
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 911..931
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..305
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 505..516
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 546..575
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 587..610
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 612..630
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 631..646
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 647..658
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 682..693
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 931 AA; 102922 MW; 6B4E07D0CE332C67 CRC64;
MSGTNDSFNS NTCVVCYKNV EIYSIGMCEH PVCYECSTRM RVLCRQNECP ICRQDLPKVV
FTREIKPFRY LCRGNLLDNQ YAIYFGSSDI QDKFNDLLAN TCSICKEKQV FGSFHSLKDH
MRQRHELHYC DLCVENLKIF SQERRCYTRA SLAQHRRKGD LDDKSHKGHP LCEFCDQRYM
DNDELYRHLR RDHLYCHFCD ADGLHQYYSS YDYLRDHFRQ EHYLCEEGVC AEEKFTSVFR
TDIDLKAHKA SVHGKQLSKA AAKQARTLEL EFTLAPRGEN RMNRRGMLSA STSRNTREHY
NNGRDYHHHQ QQQQQQQQGA AASGASTSFE SFFVRQPSVD VQSTDEFPTL GNAAPVVPTL
TQTKGRGNVT IRSTVRNQPL AVTDENFPAL GPDSAGPSIS KTVNFSVSSG SNAAGSSMPQ
CQKASTSSNV SIQVNHEANG TVTTRVSGPN IRIRPAQLSI DSDFPALGNS EPSTSTANST
QWKEVLQWTC SKSAPTNAAK SKKVAPPPLA SSPPPIRSGE DFPSLSKSSK SKKQSVITVV
PTWGQNSSSH ASASNNNNNN NNTNNNNNAK TTTDLTKGKT KKKKVKQQTS NGNSSSGNES
NSSRSNANTS VVKKDVEHSS ARAGESRVSK ENSQAAHGTS NENAPKSSRE TSQTEHASKK
DKKKNKSNAD NGSSGVSLVH TEASSDGNAS ANGMQKKRSE LKIDSLNTTN NNIHKMEDFP
ALGSSSSRQL ANFANPPPGF GSPVPPPPPG FSVKYNSLDR LHGSNGLTFT SSSGESYSIL
PPDDTGHVYV PPPDFQKRNT CLVARLNEVL LHQDKIDKFR YVSGLFRGGT CDAEEYYTHC
REVMGSDAFE NVFPELLVLL PDIAKQQELF KVHKRELGGK AKGLDVCATC SQVVKNGGDL
RTHMSSHTLE NHFPALGKNS TPPLKNTWVR K
//
