ID A0A1J1IU61_9DIPT Unreviewed; 501 AA.
AC A0A1J1IU61;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=CLUMA_CG016953, isoform A {ECO:0000313|EMBL:CRL03727.1};
GN Name=similar to Serine protease gd {ECO:0000313|EMBL:CRL03727.1};
GN ORFNames=CLUMA_CG016953 {ECO:0000313|EMBL:CRL03727.1};
OS Clunio marinus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Chironomoidea; Chironomidae;
OC Clunio.
OX NCBI_TaxID=568069 {ECO:0000313|EMBL:CRL03727.1, ECO:0000313|Proteomes:UP000183832};
RN [1] {ECO:0000313|EMBL:CRL03727.1, ECO:0000313|Proteomes:UP000183832}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Syromyatnikov M.Y., Popov V.N.;
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. CLIP subfamily.
CC {ECO:0000256|ARBA:ARBA00024195}.
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DR EMBL; CVRI01000059; CRL03727.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J1IU61; -.
DR STRING; 568069.A0A1J1IU61; -.
DR OrthoDB; 3473805at2759; -.
DR Proteomes; UP000183832; 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; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR InterPro; IPR032675; LRR_dom_sf.
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; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF52058; L domain-like; 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 Reference proteome {ECO:0000313|Proteomes:UP000183832};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..501
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012859667"
FT DOMAIN 46..274
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
SQ SEQUENCE 501 AA; 56807 MW; 708D90E3CA9D8924 CRC64;
MISNASVVLK FLLILFAITQ ILSDELFKGS NAENQCDVSL SASGLIYNGK VVKRNQWPFL
VALMMVADMK FFCGGTLISR SHVLTAAHCL QEKSQETPLT PSEFVLHLGK YNLSLVYERG
SITAFPEKIK IHPNWNIHQV KYDSDIALIK IDGTVPLRSN IYPACLWTSA LGMRNVQTGT
VIGWGVIEDQ LTTQHQLVPR QIKLKIVTNE ICYEDEFMAS DSGGGLYMKD NIKWFIKGIV
SSSLFTDEGM CDVESYSIFT DVSKFSNWIA KEMDIETDMT CEFKSEDGTR YQCWPKNFVI
QQPNVKVSVV MGVHLGQSNN NDVKEFCLKD QDTSYLPHGI PELFPNLTRY YAQGTKLKHI
QRSDFSGFQF LTNIDIADNE FVNIPADTFY DVPGLIMLSL RGSPIVSFDA DLLINSPNLI
VFYAFMNKIE YLDGRLFRKN FNLEGIHMDH NKLKHIDLEL FTPLKKLKVV NFRHNTCISE
HFPETKDLDS FKAIIAASCS I
//
