ID E2ACM3_CAMFO Unreviewed; 257 AA.
AC E2ACM3;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Chymotrypsin-1 {ECO:0000313|EMBL:EFN68767.1};
GN ORFNames=EAG_15846 {ECO:0000313|EMBL:EFN68767.1};
OS Camponotus floridanus (Florida carpenter ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Formicinae; Camponotus.
OX NCBI_TaxID=104421 {ECO:0000313|Proteomes:UP000000311};
RN [1] {ECO:0000313|EMBL:EFN68767.1, ECO:0000313|Proteomes:UP000000311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C129 {ECO:0000313|Proteomes:UP000000311};
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 -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.; EC=3.4.21.4;
CC Evidence={ECO:0000256|ARBA:ARBA00036320};
CC -!- SIMILARITY: Belongs to the peptidase S1 family.
CC {ECO:0000256|ARBA:ARBA00007664}.
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DR EMBL; GL438568; EFN68767.1; -; Genomic_DNA.
DR RefSeq; XP_011255560.1; XM_011257258.2.
DR AlphaFoldDB; E2ACM3; -.
DR STRING; 104421.E2ACM3; -.
DR MEROPS; S01.438; -.
DR EnsemblMetazoa; XM_011257258.3; XP_011255560.1; LOC105250899.
DR GeneID; 105250899; -.
DR KEGG; cfo:105250899; -.
DR InParanoid; E2ACM3; -.
DR OMA; VIDQKQC; -.
DR OrthoDB; 3659930at2759; -.
DR Proteomes; UP000000311; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 InterPro; IPR033116; TRYPSIN_SER.
DR PANTHER; PTHR24276:SF100; AT20289P-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.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000256|RuleBase:RU363034};
KW Protease {ECO:0000256|RuleBase:RU363034};
KW Reference proteome {ECO:0000313|Proteomes:UP000000311};
KW Serine protease {ECO:0000256|RuleBase:RU363034};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..257
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003157066"
FT DOMAIN 33..252
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
SQ SEQUENCE 257 AA; 28247 MW; 380D1F3D5CA5CC03 CRC64;
MLLIFCILGV VAIHELSGVS SMDTDSPNQI PKIVGGNLAA EGEYPYQASL RYRNQHFCGG
SVIKKRWILT AAHCLSGFND TAINVVLGTN TLDKGGDEYS SIKRLVHPYY NSAFIRNDIG
LIKLDKDIVF GDKVKPIALP TQNFNKVDYP ATLSGWGTTS YPGETPNELQ HIKLTVIDQK
QCLSTSFRVS SNNICTLNKK GEGVCHGDSG GPLVADGEQI GVVSWGIPCA KGRPDVFTRI
YHYMDWIEQH LKEDNSI
//
