ID A0A232EXA8_9HYME Unreviewed; 1269 AA.
AC A0A232EXA8;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=ZAD domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=TSAR_004029 {ECO:0000313|EMBL:OXU23016.1};
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:OXU23016.1, ECO:0000313|Proteomes:UP000215335};
RN [1] {ECO:0000313|EMBL:OXU23016.1, ECO:0000313|Proteomes:UP000215335}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Alberta {ECO:0000313|EMBL:OXU23016.1,
RC ECO:0000313|Proteomes:UP000215335};
RC TISSUE=Whole body {ECO:0000313|EMBL:OXU23016.1};
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 -!- 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:OXU23016.1}.
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DR EMBL; NNAY01001757; OXU23016.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A232EXA8; -.
DR STRING; 543379.A0A232EXA8; -.
DR Proteomes; UP000215335; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 3.
DR InterPro; IPR012934; Znf_AD.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR16515; PR DOMAIN ZINC FINGER PROTEIN; 1.
DR PANTHER; PTHR16515:SF26; PR DOMAIN ZINC FINGER PROTEIN 1; 1.
DR Pfam; PF07776; zf-AD; 1.
DR Pfam; PF00096; zf-C2H2; 1.
DR SMART; SM00868; zf-AD; 1.
DR SMART; SM00355; ZnF_C2H2; 7.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 2.
DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR PROSITE; PS51915; ZAD; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 7.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 6.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU01263}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000215335};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU01263};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00042}.
FT DOMAIN 12..85
FT /note="ZAD"
FT /evidence="ECO:0000259|PROSITE:PS51915"
FT DOMAIN 1006..1029
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1087..1114
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1122..1149
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1171..1198
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1219..1246
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1246..1269
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT REGION 106..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 220..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 288..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 660..701
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 718..741
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 897..923
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 953..974
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..133
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..164
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..206
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..242
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..352
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..377
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 660..676
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 677..701
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 722..737
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 905..920
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 14
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01263"
FT BINDING 17
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01263"
FT BINDING 58
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01263"
FT BINDING 61
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01263"
SQ SEQUENCE 1269 AA; 142785 MW; 8FA522C398E629EF CRC64;
MSRKRKLSNL ADRCRFCLAR DVCMNDLFVD WLKPKLHDLE KCSSVEVLDK PNYPKSICYV
CLYKIEMWSE FKSQFLETNK TLSSHFKYAE PSQENVADKL INLNDTEDLN SDNNQKRLKI
DIQRAEPVET SEKPNETSIR SAPLAEPLLA TQNEGSNENI LSDTLRGSNK EDKGTASASK
TQPSDSSVTN SRKGGRSRKI EREAYTKRWE ERKNALIAAT GEVPSESDSD NGAQLSPVQK
ARARSNNEKE QENQRRKIEK ALKNLQTNMT EKYRINQDDI IIDVERKTRS RRTHVDDKQS
KETKIESSKS TLNDMKLEHS KISTKENDKK KDAKESSKSP IKESEKKSLP NKELEQSVTN
DVEAMELSTP ANETENQPEH FENIEEHFEA LDNNTGSADV DNDAMDVVSG ENKFNESFTP
QLVSSEVSIG NATYIITTTL DFPDSFSSKS DISLKTNGLN IDATSQDGQK VDVLNAVELQ
RVQSKNTNDS VNKQNSDVQK CLKIEIEGME VEALQRVQLE LDHFVKEEIK KRVMDETLAN
RKTDKKSIKF KDTYQTLDHQ LKTIIEKILR TNYEAEKNCE RNWSINNKKI SAEFLKAAKK
SPVFQPKVAI SRLNISKLCK TYQINNLHIL EKAKRQKGLV GPLSRTLGKR KHVLPKKYDG
FSLSLKPEDD ERSQTTTKSV ANKPSTPAPA APSKIVETNS DTSMNTSQFC VDDDIEDSTL
SVNDKPSETN KTAQKTAVEA APTIGCSESA VEERRSPIIK ETSNKPLPEI VDISSESPAD
LIENQVKSTP LSAEKAIESS VFIKEKATKP SSLSVEKSTK STSEVNEQPI LTPSGVTELP
VIKSKPLPVI YPKMKDIARP VITVMNSNKS VSSLPSIASR QTNTIVNSAN KVPASPAKLP
LPSIMNKNSL KNSTPVNNTH KPGKRQRHIC GICGLELFSK EDAETHVKNH TVEPTPVAKS
PPTANIAPTP LLQSTKPKPK LMRCKRCQAI VEARNVKTHV CDSVKYKCRL CDCSFGAEHL
LVAHLETHTQ IVTKPNTMKP PATSTVKKNA VKEPQRMVIT KENYRKIPEH DQEDLEEMLS
EKEPQGYSCF VCDKVFVDEE QMKDHLQMHC EEISDESNEK GFQCAFCGEK FQTEESLETH
VGDHLLEDGD EKINMLISMG TRRDKQKKSM FRCEQCSETF SSSLLLAMHL PMHEEEEAAT
MIAEYEKQQQ QEDAEQDHHF CVVCDEVFDT AEELSEHQDV HNGNAHVCIL CEKSFSSIKD
LQEHVSTHL
//