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Database: UniProt
Entry: A0A1I8PHT3_STOCA
LinkDB: A0A1I8PHT3_STOCA
Original site: A0A1I8PHT3_STOCA 
ID   A0A1I8PHT3_STOCA        Unreviewed;       528 AA.
AC   A0A1I8PHT3;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=C2H2-type domain-containing protein {ECO:0000259|PROSITE:PS50157};
GN   Name=106087448 {ECO:0000313|EnsemblMetazoa:SCAU008160-PJ};
OS   Stomoxys calcitrans (Stable fly) (Conops calcitrans).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Muscoidea;
OC   Muscidae; Stomoxys.
OX   NCBI_TaxID=35570 {ECO:0000313|EnsemblMetazoa:SCAU008160-PJ, ECO:0000313|Proteomes:UP000095300};
RN   [1] {ECO:0000313|EnsemblMetazoa:SCAU008160-PJ}
RP   IDENTIFICATION.
RC   STRAIN=USDA {ECO:0000313|EnsemblMetazoa:SCAU008160-PJ};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
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DR   RefSeq; XP_013107945.1; XM_013252491.1.
DR   AlphaFoldDB; A0A1I8PHT3; -.
DR   EnsemblMetazoa; SCAU008160-RJ; SCAU008160-PJ; SCAU008160.
DR   VEuPathDB; VectorBase:SCAU008160; -.
DR   OrthoDB; 3242563at2759; -.
DR   Proteomes; UP000095300; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 7.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR24399:SF69; FINGER PUTATIVE TRANSCRIPTION FACTOR FAMILY-RELATED; 1.
DR   PANTHER; PTHR24399; ZINC FINGER AND BTB DOMAIN-CONTAINING; 1.
DR   Pfam; PF00096; zf-C2H2; 4.
DR   Pfam; PF13912; zf-C2H2_6; 1.
DR   SMART; SM00355; ZnF_C2H2; 9.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 4.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 7.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 8.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00042};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00042};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00042}.
FT   DOMAIN          234..262
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          274..298
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          299..326
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          327..350
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          353..380
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          381..408
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          409..436
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          437..464
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   REGION          90..230
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          457..528
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        90..133
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        170..187
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        188..209
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        470..513
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   528 AA;  60694 MW;  3ECF4BFE1504C939 CRC64;
     MLRTACGPQP YKCGEVFCVS QPAVLKVTCL ICNRKLAFDK FMDHFKSQHL NIGEENINIV
     EIEEILIKED LGDDPIKEEE IVVEQTMMEQ EYEDEDYAQP QTDDEEDEHD QQYEDDLLQE
     QPMTDESEEE DEEDYNKNIS KSLEEEEYIE DVEAVAENSN VSTNIEIEIV KNPPEDDDKP
     QGSSKQNEED EENEDEGEGD GDDDDDDDWK DPNAKCGGGD GDGNANLPNV TARPKCEKCQ
     RTYSSMNSYK KHIRNYHTDR KKVVRIVDKS TYKYKCQECD ERFRTMQSLE AHKYKHTGIV
     CDICGQSFTQ LATMKRHRLT HTGIKPHKCS ECPKAFYSAI SLKIHMQGHT LSAVCEICGK
     RFRNSNVLAI HMRQHTGEKP AKCDICFKTY TTVFGLKIHK TVHSDERPFT CEICGDKFKR
     MHYLKNHRYT HVVERNYVCE ICNKDFTSPS YLNAHRNKHS KAEKEAAKTN PWQSYHNSGT
     EESAGHGKPS NLNSESECDS QNLSPSPYST AELMEDTYES IEIEVVND
//
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