ID   A0A3Q0IJC2_DIACI        Unreviewed;       872 AA.
AC   A0A3Q0IJC2;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=LOW QUALITY PROTEIN: probable WRKY transcription factor protein 1 {ECO:0000313|RefSeq:XP_026676351.1};
GN   Name=LOC103505209 {ECO:0000313|RefSeq:XP_026676351.1};
OS   Diaphorina citri (Asian citrus psyllid).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Paraneoptera; Hemiptera; Sternorrhyncha; Psylloidea; Psyllidae;
OC   Diaphorininae; Diaphorina.
OX   NCBI_TaxID=121845 {ECO:0000313|Proteomes:UP000079169, ECO:0000313|RefSeq:XP_026676351.1};
RN   [1] {ECO:0000313|RefSeq:XP_026676351.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   RefSeq; XP_026676351.1; XM_026820550.1.
DR   AlphaFoldDB; A0A3Q0IJC2; -.
DR   STRING; 121845.A0A3Q0IJC2; -.
DR   PaxDb; 121845-A0A3Q0IJC2; -.
DR   KEGG; dci:103505209; -.
DR   OrthoDB; 3149366at2759; -.
DR   Proteomes; UP000079169; Unplaced.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR   InterPro; IPR031986; GD_N.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR018114; TRYPSIN_HIS.
DR   PANTHER; PTHR24260; -; 1.
DR   PANTHER; PTHR24260:SF153; GH19262P-RELATED; 1.
DR   Pfam; PF16030; GD_N; 1.
DR   Pfam; PF00089; Trypsin; 2.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 2.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00134; TRYPSIN_HIS; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Reference proteome {ECO:0000313|Proteomes:UP000079169}.
FT   DOMAIN          376..868
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000259|PROSITE:PS50240"
FT   REGION          79..185
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          205..251
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          283..362
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          573..806
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        79..101
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        113..175
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        205..220
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        221..242
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        283..298
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        299..320
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        321..362
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        597..632
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        652..806
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   872 AA;  97285 MW;  CC38D84B45A3897A CRC64;
     MDKPMRFRFG RPHLLHKTEP HDSLGEVTTS NNKEFTILNL EQVLDPSRPM TTRIMVRFEP
     NGGSPKVKTI WLNGKQICPA ETPKSSYNTK PQQTYEESYR PQGNVGGSGG YQPGNVGYNS
     NTGYNTQPQP TVNTGYSTSS SNSRPVVYQG QKPSSQSEIS YNGKKPSQNS NTPDIGDIAE
     HLIDDGDSNN KTVIITVIKH NAQETTTENY KTTTWKAKTT GKPNNKDKDR DNRDKDKDNN
     SGNKGHPLNT QHSQDIAEHL IDDGDSNNKT VIITVIKHNA QETTTENYKT TTWKAKTTAK
     PNNKDKDRDN RDKDKDNNSG NKGHPLNTQH SQKRPAESNN KNTNNNNNNN NGQSSGNSNK
     DVSCGTVVYN KAQPLVTYGQ KTARGQWPWH VALYRTEGIN LSYVCGGSLV SVNYVITAAH
     CVTKKPYDKP VDSDTLVIYL GKYHQHQFSD EGGVQNKQVK RVHIYPTFNS SNYLGDIALL
     QLSSDVDYSM YVRPVCLWDD STAPLQLSAV EGVLIFQFKR IGLKRPDPIF ITDTLYNGSV
     TTNDDYYNEF FNINQQNAMK QNPDKVYANT ESSVLEPGGY SKPQQRPQKP PRKKGQTESV
     DNTYTIPSSN TEYNAGQNEQ SSYNQGTIDK PLTSPVYNKK PQEPEYQAKP QTYPAPDNSY
     NSYSNTDAYG SNGRPQTVTN SETSHARPQK SPESSYNTRP QTNSDSNYNS RPQTNPDNVY
     YVKPQTETSY NTRPQTNPEP SYNTRPQSNS DSNYNSRPQT NPEPSYNTRP QSSPDTSYNT
     RPQSSPDTSY NTRPQSNSLG NSFSASGTSV CNGDSGGGMV FKIDSAWYLR GIVSITVARD
     GLRVCDTKHY VVFTDVAKYL GWIRPILASG SR
//