GenomeNet

Database: UniProt
Entry: A0A195BW50_9HYME
LinkDB: A0A195BW50_9HYME
Original site: A0A195BW50_9HYME 
ID   A0A195BW50_9HYME        Unreviewed;       744 AA.
AC   A0A195BW50;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   28-JAN-2026, entry version 27.
DE   RecName: Full=C2H2-type domain-containing protein {ECO:0000259|PROSITE:PS50157};
GN   ORFNames=ALC53_00350 {ECO:0000313|EMBL:KYM92812.1};
OS   Atta colombica.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Myrmicinae; Atta.
OX   NCBI_TaxID=520822 {ECO:0000313|EMBL:KYM92812.1, ECO:0000313|Proteomes:UP000078540};
RN   [1] {ECO:0000313|EMBL:KYM92812.1, ECO:0000313|Proteomes:UP000078540}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Treedump-2 {ECO:0000313|EMBL:KYM92812.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KYM92812.1};
RA   Nygaard S., Hu H., Boomsma J., Zhang G.;
RT   "Atta colombica WGS genome.";
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KQ976396; KYM92812.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A195BW50; -.
DR   STRING; 520822.A0A195BW50; -.
DR   Proteomes; UP000078540; Unassembled WGS sequence.
DR   GO; GO:0043022; F:ribosome binding; IEA:TreeGrafter.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
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   InterPro; IPR057634; PAH_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   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; PF23230; zf-C2H2_13; 1.
DR   Pfam; PF23208; zf_C2H2_ZNF598; 1.
DR   SMART; SM00355; ZnF_C2H2; 3.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00042};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078540};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00042};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00042}.
FT   DOMAIN          698..725
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   REGION          225..248
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          312..559
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        225..236
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        237..248
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        323..332
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        363..385
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        397..417
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        444..464
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        493..505
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        545..559
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   744 AA;  81200 MW;  1126BC19D85E5998 CRC64;
     MDNDELYRHL RRDHLYCHFC DADGLHQYYS SYDYLRDHFR QEHYLCEEGV CAEEKFTSVF
     RTDIDLKAHK ASVHGKQLSK AAAKQARTLE LEFTLAPRGE NRMNRRSMLG ASTSRNTRDY
     NGRDYGSRDY QQGAISNSSN SFMSNNEPIF TKQPSVDVQS TDEFPTLGGS VIPVVPTLSQ
     PKSRGNVTIR STVRNQPLAV TDENFPALGP DSVGPSISKT VNFSVSSSSN ATGSSGLPQC
     QKGSASSNVS IQVNHEPNGT VTTRVSGPNI RIRPTQLSID SDFPALGNSE PSTSTANSIQ
     WKEVLQWTCS KSASANTPKS KVAPPPSIPS APPIRSGEDF PSLSKSLKSK KQSMITVVPS
     WGQNSQNISN VQTSSTNNTK TTTDQTKSKT KKKKAKQASS GNSSSGNESG SSKSNINTVV
     TKKDIELART GNSDNSRVAK ESSRVTQDTN ASGDNSKNSS VQNSKEPEHV NKKDKRKNKN
     NVDGNTGVTT VINTESESGG NSSNGEKQRK RSELKIDSLN TANNNIHRTE DFPALGSTSS
     RPPGFTNPPP GFSSPTLPPP GFSIKYSLDG LHGGNGLTFT NSSGESYSIL PDNNSKHMTH
     VYVSPPDFQK RNTCLVAKLN AVLVEQNKIE EFRYVSGLFR GGTCDAQEYY THCCEVMGAN
     AFESIFPELL VLLPDIAKQQ ELFKVHKRET GGKAKGLEMC ATCGQVLKNG SDFRMHMSSH
     TLENHFPALG KSNMPPPKNT WVRK
//
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