GenomeNet

Database: UniProt
Entry: A0A195FL50_9HYME
LinkDB: A0A195FL50_9HYME
Original site: A0A195FL50_9HYME 
ID   A0A195FL50_9HYME        Unreviewed;       617 AA.
AC   A0A195FL50;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN   ORFNames=ALC56_05025 {ECO:0000313|EMBL:KYN40714.1};
OS   Trachymyrmex septentrionalis.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Myrmicinae; Trachymyrmex.
OX   NCBI_TaxID=34720 {ECO:0000313|EMBL:KYN40714.1, ECO:0000313|Proteomes:UP000078541};
RN   [1] {ECO:0000313|EMBL:KYN40714.1, ECO:0000313|Proteomes:UP000078541}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tsep2-gDNA-1 {ECO:0000313|EMBL:KYN40714.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KYN40714.1};
RA   Nygaard S., Hu H., Boomsma J., Zhang G.;
RT   "Trachymyrmex septentrionalis WGS genome.";
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
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DR   EMBL; KQ981522; KYN40714.1; -; Genomic_DNA.
DR   RefSeq; XP_018340504.1; XM_018485002.1.
DR   RefSeq; XP_018340505.1; XM_018485003.1.
DR   RefSeq; XP_018340506.1; XM_018485004.1.
DR   AlphaFoldDB; A0A195FL50; -.
DR   STRING; 34720.A0A195FL50; -.
DR   GeneID; 108747491; -.
DR   OrthoDB; 460116at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000078541; Unassembled WGS sequence.
DR   GO; GO:0000151; C:ubiquitin ligase complex; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   GO; GO:0060255; P:regulation of macromolecule metabolic process; IEA:UniProt.
DR   CDD; cd17086; RAWUL_RING1_like; 1.
DR   CDD; cd16739; RING-HC_RING1; 1.
DR   Gene3D; 6.20.210.20; THAP domain; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR032443; RAWUL.
DR   InterPro; IPR043540; RING1/RING2.
DR   InterPro; IPR042741; RING1_RING-HC.
DR   InterPro; IPR006612; THAP_Znf.
DR   InterPro; IPR038441; THAP_Znf_sf.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR46076:SF3; E3 UBIQUITIN-PROTEIN LIGASE RING1; 1.
DR   PANTHER; PTHR46076; E3 UBIQUITIN-PROTEIN LIGASE RING1 / RING 2 FAMILY MEMBER; 1.
DR   Pfam; PF16207; RAWUL; 1.
DR   Pfam; PF05485; THAP; 1.
DR   Pfam; PF13923; zf-C3HC4_2; 1.
DR   SMART; SM00692; DM3; 1.
DR   SMART; SM00184; RING; 1.
DR   SMART; SM00980; THAP; 1.
DR   SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
DR   PROSITE; PS50950; ZF_THAP; 1.
PE   4: Predicted;
KW   DNA-binding {ECO:0000256|PROSITE-ProRule:PRU00309};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078541};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          1..84
FT                   /note="THAP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50950"
FT   DOMAIN          285..325
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          83..123
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          381..502
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        83..98
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        99..123
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        381..486
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   617 AA;  69709 MW;  DA0155CEBC49ECA3 CRC64;
     MVKITSGTWK CVIPHCKSRA RAPGHYFPKD TELRKKWIKA ISMSHVPDEK IKKCRICHLH
     FDESSYIINL QRRRLKIDAI PNRNLSTGNE TDDSQSSAST VPEEEEEEEK EEKEEDEEMD
     DVTETVATQS FLDVYKSYIR TVNFLEKEKA ILKNNVDIEE ETQQETQPEI LRIVEEEKTI
     LENNVDIEEG TQREIQPEIV RTVEEEKAIL ENNVDIEEGT QQETQSCNNV NIEEGTQQET
     QPEIVGLNKT WELSLYELHR TPQDAITDNT EIAVSPRSLH SELMCPICLD MLKKTMTTKE
     CLHRFCSDCI ITALRSGNKE CPTCRKKLVS KRSLRPDPNF DLLISKIYPS RDEYEAHQER
     VLAKLNKSHS QAALVNSITE GIKLQSQNRP QRSRKNANES ENASNATSYN NTPNISAPTT
     PNPSTNIANQ SDSSQSATGP LNSGGTTSRN STTPSPNPAN QISKPSKRQK SLQNSENDSS
     SAEAETGGGD SMVDTEGEGP SEPLMLNEIE LVFKPHPTEM AGDNSLIKAL KENSIRYIKT
     TANATVDHLS KYLAMRLTLD LDTELSESDR LLNFCIYIAP SPGQLVVLSG SQTLRQVNDK
     FWRVNRPLEM YYSWKKT
//
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