ID A0A4S2L2F0_9HYME Unreviewed; 955 AA.
AC A0A4S2L2F0;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 28-JAN-2026, entry version 20.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=DBV15_09673 {ECO:0000313|EMBL:TGZ57022.1};
OS Temnothorax longispinosus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Temnothorax.
OX NCBI_TaxID=300112 {ECO:0000313|EMBL:TGZ57022.1, ECO:0000313|Proteomes:UP000310200};
RN [1] {ECO:0000313|EMBL:TGZ57022.1, ECO:0000313|Proteomes:UP000310200}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Whole body {ECO:0000313|EMBL:TGZ57022.1};
RX PubMed=30967075;
RA Kaur R., Stoldt M., Jongepier E., Feldmeyer B., Menzel F.,
RA Bornberg-Bauer E., Foitzik S.;
RT "Ant behaviour and brain gene expression of defending hosts depend on the
RT ecological success of the intruding social parasite.";
RL Philos. Trans. R. Soc. Lond., B, Biol. Sci. 374:20180192-20180192(2019).
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:TGZ57022.1}.
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DR EMBL; QBLH01000237; TGZ57022.1; -; Genomic_DNA.
DR STRING; 300112.A0A4S2L2F0; -.
DR Proteomes; UP000310200; 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 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 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:UP000310200};
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 281..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 409..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 490..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 521..768
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 935..955
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..336
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..355
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..447
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..475
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 497..508
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 533..542
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 573..588
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 607..624
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 631..645
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 655..671
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 693..704
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 755..768
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 955 AA; 105803 MW; 003E3FF2C362221B CRC64;
MSGNNDSFNN NTCVVXYKNV DIYSIGMCEH PVCYECSTRM RVLCRQNECP ICRQDLPKVV
FTREIKSFHS LTGTNLLDTR YDIYFNSLDI QEKFTELLAN TCSICKEKMV FSSFNSLKEH
MRQRHELHYC DLCVDNLKIF SNERRCYTRA SLATHRRKGD VDDRSHKGHP LCEFCDQRYM
DNDELYRHLR RDHLYCHFCD ADGLHQYYSS YDYLRDHFRQ EHYLCEEGVC AEEKFTSVFR
TDIDLKAHKA SVHGKQLSKA AAKQARTLEL EFTLAPRGEN RMNRRGMLGA STSRSARDYN
GRDYSSRDYN SRDYNSRDYS SRDYSSRDYS SRDYSSRDYQ QSSVPSGSNS FVSNNEPTFM
RQPSVDVQST DEFPTLGGSA APIVPTLAQP KSRGNVTIRS TVRNQPLAVT DENFPALGPD
SSGPSISKTV NFSVSSSSNS TGSSGLSQCQ KGSTSSNVSI QVNHEPNGTV TTRVSGPNIR
IRPAQLSIDS DFPALGSSEP STSTASSTQW KEVLQWTCSK SASANTPKSK KVAPPPSIPS
APPIRSGEDF PSLSKSSKSK KQSVITVVPS WGQNSQQNNV QSSSISNNTK TTMDQTKGKT
KKKKAKQASS GNSSSGNESS GSKSNINTVI TKKDIELSHT GDSDNSRVAS KANLRATQDT
NNASADNSTS KNSREWEHAS KKDKRKNKNN ANGSSGIATV INTESGSGGN GSSNGEKQRK
RSELKIDSLN TTNNNIHRTE DFPALGSTSS RPPGFTNPPP GFASPTLPPP GFSIKYNSLD
GLHGGNGLTF TNSSGESYSI LPDNSNKHEA HDYVSPPDFQ KRNTCLVAKL NAVLVDQDKI
EEFRYVSGLF RGGTCDAQEY YTHCREVMGA SAFESVFPEL LVLLPDIVKQ QELFKVHKRE
AGGKAKGLEM CATCGQVLKN GLDFRTHMSS HTLENHFPAL GKSNTPPPRN TWVRK
//
