ID A0A232EXH5_9HYME Unreviewed; 1076 AA.
AC A0A232EXH5;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 13-SEP-2023, entry version 25.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=TSAR_011597 {ECO:0000313|EMBL:OXU23045.1};
OS Trichomalopsis sarcophagae.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Proctotrupomorpha;
OC Chalcidoidea; Pteromalidae; Pteromalinae; Trichomalopsis.
OX NCBI_TaxID=543379 {ECO:0000313|EMBL:OXU23045.1, ECO:0000313|Proteomes:UP000215335};
RN [1] {ECO:0000313|EMBL:OXU23045.1, ECO:0000313|Proteomes:UP000215335}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Alberta {ECO:0000313|EMBL:OXU23045.1,
RC ECO:0000313|Proteomes:UP000215335};
RC TISSUE=Whole body {ECO:0000313|EMBL:OXU23045.1};
RX PubMed=28648823; DOI=10.1016/j.cub.2017.05.032;
RA Martinson E.O., Mrinalini, Kelkar Y.D., Chang C.H., Werren J.H.;
RT "The Evolution of Venom by Co-option of Single-Copy Genes.";
RL Curr. Biol. 27:2007-2013(2017).
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: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00358}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00500}.
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:OXU23045.1}.
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DR EMBL; NNAY01001745; OXU23045.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A232EXH5; -.
DR STRING; 543379.A0A232EXH5; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000215335; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; 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; cd15525; PHD_UHRF1_2; 1.
DR CDD; cd20387; Tudor_UHRF_rpt1; 1.
DR CDD; cd20388; Tudor_UHRF_rpt2; 1.
DR CDD; cd00191; TY; 1.
DR Gene3D; 2.30.30.1150; -; 1.
DR Gene3D; 2.30.30.140; -; 1.
DR Gene3D; 2.30.280.10; SRA-YDG; 1.
DR Gene3D; 4.10.800.10; Thyroglobulin type-1; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR015947; PUA-like_sf.
DR InterPro; IPR036987; SRA-YDG_sf.
DR InterPro; IPR003105; SRA_YDG.
DR InterPro; IPR000716; Thyroglobulin_1.
DR InterPro; IPR036857; Thyroglobulin_1_sf.
DR InterPro; IPR021991; TTD_dom.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR045134; UHRF1/2-like.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR14140; E3 UBIQUITIN-PROTEIN LIGASE UHRF-RELATED; 1.
DR PANTHER; PTHR14140:SF45; RING-TYPE E3 UBIQUITIN TRANSFERASE; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF02182; SAD_SRA; 1.
DR Pfam; PF00086; Thyroglobulin_1; 1.
DR Pfam; PF12148; TTD; 1.
DR Pfam; PF00240; ubiquitin; 1.
DR Pfam; PF13920; zf-C3HC4_3; 1.
DR SMART; SM00249; PHD; 1.
DR SMART; SM00184; RING; 2.
DR SMART; SM00466; SRA; 1.
DR SMART; SM00211; TY; 2.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF88697; PUA domain-like; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF57610; Thyroglobulin type-1 domain; 3.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS51162; THYROGLOBULIN_1_2; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
DR PROSITE; PS51015; YDG; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW ProRule:PRU00358}; Reference proteome {ECO:0000313|Proteomes:UP000215335};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT TRANSMEM 12..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 123..193
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS50053"
FT DOMAIN 409..460
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 509..672
FT /note="YDG"
FT /evidence="ECO:0000259|PROSITE:PS51015"
FT DOMAIN 783..822
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 866..931
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000259|PROSITE:PS51162"
FT REGION 203..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..220
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1076 AA; 121980 MW; EEF59AEEC79158FB CRC64;
MIEDQYSTMF GRLYLKVFVI FLIIFPNYLV SSSGDVTKAC DPAGLNEPCK NCDKCLPGLI
CNEAKICAIA YGTCESHQWL NNIWKPSCEK DGTYSAVQCK GEYSNGRGEN QFAKRMSITP
DAIHLVVTID GKKKTVLNVS KLTKIAALKA DIEEEFGIKK AKQGLFFRGK HLEDDCTLYD
YSININNVIQ VMIMSDKDIA AEKKGKKQVD KKPNEEKKEK ENEEEEVDAE SQYYKVGDAV
DCTDNALGAW FEAVIVKIFT KSEKLFHKVR WDLPETKNDE PFNIEEKFIR PRAWKVLNFN
DLDIGQKVMV NYNLEDPKEI GNWYDFTISK IKNTKSAKEL IGTIHIGDST RSVDDCTINT
KLDILEIEKP ILLSERDDEL ISKRVPKTRR RIPVKCTKCH DNPKKRCKEC SCRVCGKKND
PHLTLLCDEC DDAYHLACLN PPLTELPADD DWYCPHCKVN TNEIVKVGEK VQNKKKHSNV
VGTNRDWGKG MACVGRTKIC TIVPLSHRGP IPGIEVGTMW KFRFQVSEAG VHRPHVAGIH
GRAEDGAYSI ALSGGYEDDV DNGEEFFYTG SGGRDLSGNK RTAKQSSDQQ LTLMNRALAV
NCNAKINEKD GAEATDWKAG SPIRVVRNFK LAKHSKYAPE DGNRYDGIYK VVKYWPEKGQ
SGFRVWRYLL RRDDPTPAPW TKAGKARIAQ LGLEMIYPEG YQEAQEKKAG IKKRKSDDED
DPAVADEFVS AKKKRKVSFK LSSEMKNLIK KDLPNTKLWN QCNEFLSEGK QAYFEKISTE
FACIVCQDLV IKPITTPCGH NICITCLKRS FAASSYACPM CRAALDKNYE MNVNETLSSL
LLCFCFSPDG HRIFGWSWWN SAKNMTCACS RRQYEIKKQT LKREDVSLHC TQNGNYEELQ
CDNGLCWCVE PLTGRPTQRA YPESLMTYLP CYNQKLSEFQ YLRQCESKLI AIAKIVQKVK
HHGHNYYHPD NVLCDDDGSY GSVQVDRAGI KCTWKDGKKI FTYLTENVGN IADINCNCAR
DSVIYSNENL EFRLQCNPDG NYKPQQSING RPFCVDKDGF ATSDKLGNIG ENLKCT
//
