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Database: UniProt
Entry: E2B507_HARSA
LinkDB: E2B507_HARSA
Original site: E2B507_HARSA 
ID   E2B507_HARSA            Unreviewed;       253 AA.
AC   E2B507;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   24-JAN-2024, entry version 48.
DE   SubName: Full=Chymotrypsin-1 {ECO:0000313|EMBL:EFN89215.1};
GN   ORFNames=EAI_07718 {ECO:0000313|EMBL:EFN89215.1};
OS   Harpegnathos saltator (Jerdon's jumping ant).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Ponerinae; Ponerini; Harpegnathos.
OX   NCBI_TaxID=610380 {ECO:0000313|Proteomes:UP000008237};
RN   [1] {ECO:0000313|EMBL:EFN89215.1, ECO:0000313|Proteomes:UP000008237}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R22 G/1 {ECO:0000313|EMBL:EFN89215.1,
RC   ECO:0000313|Proteomes:UP000008237};
RX   PubMed=20798317; DOI=10.1126/science.1192428;
RA   Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G.,
RA   Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D.,
RA   Wang J., Liebig J.;
RT   "Genomic comparison of the ants Camponotus floridanus and Harpegnathos
RT   saltator.";
RL   Science 329:1068-1071(2010).
CC   -!- SIMILARITY: Belongs to the peptidase S1 family.
CC       {ECO:0000256|ARBA:ARBA00007664}.
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DR   EMBL; GL445685; EFN89215.1; -; Genomic_DNA.
DR   RefSeq; XP_011144480.1; XM_011146178.1.
DR   AlphaFoldDB; E2B507; -.
DR   STRING; 610380.E2B507; -.
DR   EnsemblMetazoa; XM_011146178.2; XP_011144480.1; LOC105186146.
DR   GeneID; 105186146; -.
DR   KEGG; hst:105186146; -.
DR   InParanoid; E2B507; -.
DR   OMA; TINWMIS; -.
DR   OrthoDB; 3601399at2759; -.
DR   Proteomes; UP000008237; Unassembled WGS sequence.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
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; PTHR24276:SF98; FI18310P1-RELATED; 1.
DR   PANTHER; PTHR24276; POLYSERASE-RELATED; 1.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00134; TRYPSIN_HIS; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022825};
KW   Protease {ECO:0000256|ARBA:ARBA00022825};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008237};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..253
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003157846"
FT   DOMAIN          25..251
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000259|PROSITE:PS50240"
SQ   SEQUENCE   253 AA;  27641 MW;  B1F9D793B6EAEA04 CRC64;
     MMKLAILLVV AAIAKQTYGD EPEAIVGGDY AVLGQIKYIA SLQTNGGHMC GGSLISDTHV
     LTAAHCVEGL HSVNDMTVVT GTINWMISGQ THKIKCIRIH PKYNGDPMGA YKYDIAVITL
     VKPIIINANQ APIPLANMNY ATGNYRGTVC GWGLINERWN IPIFRLRCVE MKILETAHCM
     KEHTYPQTSK GHMCTKAEVD KAFCSGDSGG PLVANGQLCG IVSWSKRCGG DSPDVYTSVY
     DYRDFIKESQ MMC
//
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