ID F4WYZ3_ACREC Unreviewed; 925 AA.
AC F4WYZ3;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=G5I_11207 {ECO:0000313|EMBL:EGI60647.1};
OS Acromyrmex echinatior (Panamanian leafcutter ant) (Acromyrmex octospinosus
OS echinatior).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Acromyrmex.
OX NCBI_TaxID=103372 {ECO:0000313|Proteomes:UP000007755};
RN [1] {ECO:0000313|EMBL:EGI60647.1}
RP NUCLEOTIDE SEQUENCE.
RA Nygaard S., Zhang G.;
RT "The genome of the leaf-cutting ant Acromyrmex echinatior suggests key
RT adaptations to social evolution and fungus farming.";
RL Submitted (FEB-2011) 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 -!- SIMILARITY: Belongs to the ZNF598/HEL2 family.
CC {ECO:0000256|ARBA:ARBA00035113}.
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DR EMBL; GL888463; EGI60647.1; -; Genomic_DNA.
DR RefSeq; XP_011062410.1; XM_011064108.1.
DR RefSeq; XP_011062411.1; XM_011064109.1.
DR AlphaFoldDB; F4WYZ3; -.
DR STRING; 103372.F4WYZ3; -.
DR EnsemblMetazoa; XM_011064108.1; XP_011062410.1; LOC105150790.
DR EnsemblMetazoa; XM_011064109.1; XP_011062411.1; LOC105150790.
DR GeneID; 105150790; -.
DR KEGG; aec:105150790; -.
DR eggNOG; KOG2231; Eukaryota.
DR InParanoid; F4WYZ3; -.
DR OrthoDB; 3059402at2759; -.
DR Proteomes; UP000007755; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
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; IPR041888; RING-HC_ZNF598/Hel2.
DR InterPro; IPR044288; ZNF598/Hel2.
DR InterPro; IPR013087; Znf_C2H2_type.
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; PF13920; zf-C3HC4_3; 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.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 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:UP000007755};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00042}.
FT DOMAIN 13..53
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 879..906
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT REGION 283..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 405..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 491..527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 539..740
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 906..925
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 539..563
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 576..600
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 604..618
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 619..645
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 646..661
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 662..686
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 698..723
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 724..738
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 925 AA; 102613 MW; 98C68E5CE56D1644 CRC64;
MSGNNDSFNN NTCVVCYKNV DIYSIGMCEH PVCYECSTRM RVLCLQNECP ICRQDLPKVV
FTREIKPFHN LTNTNLLDTR YDIYFSSLDI QEKFTELLAN TCSICKEKMV FSSFNSLKDH
MRQQHELHYC DLCVENLKIF SNERRCYTRS SLATHRRKGD IDDRSHKGHP LCEFCDQRYM
DNDELYRHLR RDHLYCHFCD ADGLHQYYSS YDYLRDHFRQ EHYLCEEGVC AEEKFTSVFR
TDIDLKAHKA SVHGKQLSKA AAKQARTLEL EFTLAPRGEN RMNRRGMLGA STSRNTRDYN
GRDYGSRDYQ QGAISNSSNS FMSNNEPIFT KQPSVDVQST DEFPTLGGSA IPVVPTLSQP
KSRGNVTIRS TVRNQPLAVT DENFPALGPD SAGPSISKTV NFSVSSSSNA TGSNGLPQCQ
KGSASSNVSI QVNHEPNGTV TTRVSGPNIR IRPTQLSIDS DFPALRNSEP STSTANSIQW
KEVLQWTCSK SASANTPKSK VAPPPSIPSA PPIRSGEDFP SLSKSLKSKK QSMITVVPSW
RQNSQNISNV QTSNSNNTKT TTDQTKSKTK KKKAKQASSG NSSSGNESGS SKSNINTVVT
KKDIELARTG DSDNSRVASK ESSRVTQDTN ASSDNSKNSS VQNSKELEHA NKKDKRKNKN
NVDGNSSVTT VINTESESGG NGSSNGEKQR KRSELKIDSL NTANNNIHRT EDFPALGSTS
SRPPGFTNPP PGFSSPTLPP PGFSIKYSLD GLHGSNGLTF TNSSGESYSI LPDNSSKHMT
HVYVSPPDFQ KRNTCLVAKL NAVLVDQNKI EEFRYVSGLF RGGTCDAQEY YTHCCEVMGA
SAFESIFPEL LVLLPDIAKQ QELFKMHKRE TGGKAKGLEM CATCGQILKN GSDFRMHMSS
HTLENHFPAL GKSNTPPPKN TWVRK
//
