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Database: UniProt
Entry: A0A232F5G3_9HYME
LinkDB: A0A232F5G3_9HYME
Original site: A0A232F5G3_9HYME 
ID   A0A232F5G3_9HYME        Unreviewed;      1317 AA.
AC   A0A232F5G3;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=RING-type domain-containing protein {ECO:0000259|PROSITE:PS50089};
GN   ORFNames=TSAR_002184 {ECO:0000313|EMBL:OXU25719.1};
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:OXU25719.1, ECO:0000313|Proteomes:UP000215335};
RN   [1] {ECO:0000313|EMBL:OXU25719.1, ECO:0000313|Proteomes:UP000215335}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Alberta {ECO:0000313|EMBL:OXU25719.1,
RC   ECO:0000313|Proteomes:UP000215335};
RC   TISSUE=Whole body {ECO:0000313|EMBL:OXU25719.1};
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   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:OXU25719.1}.
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DR   EMBL; NNAY01000960; OXU25719.1; -; Genomic_DNA.
DR   STRING; 543379.A0A232F5G3; -.
DR   Proteomes; UP000215335; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0060255; P:regulation of macromolecule metabolic process; IEA:UniProt.
DR   CDD; cd17082; RAWUL_PCGF2_like; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR032443; RAWUL.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR10825:SF75; POLYCOMB COMPLEX PROTEIN BMI-1-LIKE PROTEIN; 1.
DR   PANTHER; PTHR10825; RING FINGER DOMAIN-CONTAINING, POLYCOMB GROUP COMPONENT; 1.
DR   Pfam; PF16207; RAWUL; 1.
DR   Pfam; PF13923; zf-C3HC4_2; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000215335};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          19..58
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          280..411
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          427..452
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          479..639
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          696..757
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          778..813
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          825..867
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          883..922
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1021..1045
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1070..1269
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        280..307
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        347..362
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        489..504
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        527..543
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        551..632
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        711..739
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        793..813
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1021..1041
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1071..1108
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1109..1126
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1127..1221
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1229..1269
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1317 AA;  141644 MW;  63E4E137968C9A73 CRC64;
     MAGIGKRTYL REVNPHLICP LCRGYLIDAT TVVECLHSFC RSCILKHLNK NAQCPTCKHL
     LNTAKPNIKA DKALQDIVYK LVPGLYHKEM RKRREFYSKH PEHGFAAMSL NHLGGADSAT
     PEQRGEDVSG RLIFAPEDAI SLSLEYLPMG ADPLTLLSNN SDVDASQVNS PKTKINNGMA
     NRRYLQCPAL VTIAHLKKFL ALKYSVDMTR YNIDVCHRRA PLPEHWTLMD VAYIFAWKRN
     APIRFFYRIT QEEQQLEAPP NDRPSTPGLG ASQPIADEQA IEPKDKEPES NKEPLNKPSD
     EESKQQAAEP KIPQISPQKP EIKRNESEKV RGFLAKRSAP NPKENLPVTT KPLPPLLPKP
     EPQVKSPIKI MKNSDGRYQV LRGPATPLRT TDSGTISSPK PSPPSPTPAE FSVVSIADGV
     NSNSVKITLK QCPPGSTTPG STNSTNASKK PKVISNVLLR SPTQVDKSSP MSIVEQLQEQ
     KQKRKVTFVD NVESSPLTAP KQAKKSTEQA EKKQFLQGFR LTAAAAKQQH QEVSNSEQMS
     SKKKNEQISV EEQVRSIITK NDPSKLLTSP NQQATTNNSE ETSPTKKLQT EMKINSTNIA
     DRLSDPKQLA TTGDNASQAQ TISSSNEQQP IDVYAFPNDP PSALPAGAVK RKCPPGLPIF
     DVRKKPQSYQ TGKRAGVNTT RGGGAVKCYR NQSAKPMVYA KPPPSPARPL QSLNAIGNVG
     NVNAGSPSTH PNNNPTVTST SPKNPPPPSS VMISNDTRNL LDGCGLNIPA SLSITLTAPK
     SPSRVNDPVI DSRGSKEAQS TLDKVNPSIT LNDKSVDPKV LKALKSGQMR MPAANAGAKT
     KGRQPASLEP TPQGQGPAAK RKKEEQLMQQ AKNILDLSGT KKVDTHPLKI PTPIGKFKPK
     PPTWSQANSP KPPTKDDAPS YTTNGQVVTV TGGQRFYRAP PGSLTPAAHR IGDIPTPSRA
     PVYAPCFSSP SPPTSRPPPV NLSSVFPSLQ SLYALSQSPS LEQFHMDSRI RMAAAANAAA
     NANKDSKNGS SNNSGSVGQK SHLAAQCAPI KPARSSIGSF AVPIAKQISG TPAKLPSSNK
     PGKATASTPV STAKDSETTT SSTDSGNTEQ KDTKVESSKE DSSKTNTEQS ETCTTSSAAE
     EGNSQGSASP RVTSTASPSP PPSASEAATS NSSTSESKSS KPENRQQQPS SGSEVTSSNK
     SPESPDSSSV VTESISNLVD STKPVMEKAG DASTEKDDTK TTSEEKSSDE AKSKEKLDTT
     EFKKPVSSET LQKRFLDAFP STEWANDPVT AEQFGNFLKR LSSMQAEAQS KNAKAVD
//
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