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Database: UniProt
Entry: A0A226D6Z6_FOLCA
LinkDB: A0A226D6Z6_FOLCA
Original site: A0A226D6Z6_FOLCA 
ID   A0A226D6Z6_FOLCA        Unreviewed;       500 AA.
AC   A0A226D6Z6;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   08-MAY-2019, entry version 7.
DE   SubName: Full=Trypsin-1 {ECO:0000313|EMBL:OXA40890.1};
GN   ORFNames=Fcan01_24255 {ECO:0000313|EMBL:OXA40890.1};
OS   Folsomia candida (Springtail).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Collembola;
OC   Entomobryomorpha; Isotomoidea; Isotomidae; Proisotominae; Folsomia.
OX   NCBI_TaxID=158441 {ECO:0000313|EMBL:OXA40890.1, ECO:0000313|Proteomes:UP000198287};
RN   [1] {ECO:0000313|EMBL:OXA40890.1, ECO:0000313|Proteomes:UP000198287}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VU population {ECO:0000313|EMBL:OXA40890.1,
RC   ECO:0000313|Proteomes:UP000198287};
RC   TISSUE=Whole body {ECO:0000313|EMBL:OXA40890.1};
RA   Faddeeva A., Derks M.F., Anvar Y., Smit S., Van Straalen N.,
RA   Roelofs D.;
RT   "The genome of Folsomia candida.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family.
CC       {ECO:0000256|SAAS:SAAS00559343}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00059}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:OXA40890.1}.
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DR   EMBL; LNIX01000031; OXA40890.1; -; Genomic_DNA.
DR   Proteomes; UP000198287; Unassembled WGS sequence.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   CDD; cd00041; CUB; 1.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 2.60.120.290; -; 1.
DR   InterPro; IPR000859; CUB_dom.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   InterPro; IPR035914; Sperma_CUB_dom_sf.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR018114; TRYPSIN_HIS.
DR   InterPro; IPR033116; TRYPSIN_SER.
DR   Pfam; PF00431; CUB; 1.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00042; CUB; 1.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF49854; SSF49854; 1.
DR   SUPFAM; SSF50494; SSF50494; 1.
DR   PROSITE; PS01180; CUB; 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   Complete proteome {ECO:0000313|Proteomes:UP000198287};
KW   Disulfide bond {ECO:0000256|SAAS:SAAS00037407};
KW   Hydrolase {ECO:0000256|RuleBase:RU363034};
KW   Protease {ECO:0000256|RuleBase:RU363034};
KW   Serine protease {ECO:0000256|RuleBase:RU363034};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     20       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        21    500       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5011968504.
FT   DOMAIN       35    260       Peptidase S1. {ECO:0000259|PROSITE:
FT                                PS50240}.
FT   DOMAIN      388    500       CUB. {ECO:0000259|PROSITE:PS01180}.
SQ   SEQUENCE   500 AA;  54774 MW;  39D1E314794EEDF7 CRC64;
     MKSSTPLISF IYTLVVVTYG APPPSDFRGL NTGKIVGGVE ADRHEFKFLV DIRLQNIHLC
     GGSIVTPEWV VTAAHCAHSA PSGYTLSAGE HNINVTEGTE QVRQVTQINI HPNYLSYQYE
     NDIALMRVSP PFEFNEYVQP VVIPNVNFAP TTLATVTGWG SISEGGGSPP NDNLMKVVVP
     FVDDVTCQRN HYGEIAPSMV CYGEAGKDSC HGDSGSPLLC GDNQTLCGIV SWGEGCARPN
     LFRVYTETSF FSEWIRSSTI KFEEDSNPAQ FITTCGARID ASSAEITFQL GASIPAGQKC
     VWVVKTRYDS VRFRLSSSGL GENDGLYLTN FAHSEPGTQK RMTSVGQNYT VASGFVLVTL
     SIGSAPSSGF RLEFFSSGFS DQTRDFSEFA RFTTNTGRLS YPIDGGITRP NEDALFVINP
     TMSAVRTLRL TRMDVETDTD PSCRYDAVTI YDWFDNQYRH LDRRCGYSLP PSFTLESGLG
     LVTFQSDSGV GGTGFDFEWV
//
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