ID A0A1J1HLE5_9DIPT Unreviewed; 521 AA.
AC A0A1J1HLE5;
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_CG002636, isoform A {ECO:0000313|EMBL:CRK88880.1};
GN Name=similar to Serine protease gd {ECO:0000313|EMBL:CRK88880.1};
GN ORFNames=CLUMA_CG002636 {ECO:0000313|EMBL:CRK88880.1};
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:CRK88880.1, ECO:0000313|Proteomes:UP000183832};
RN [1] {ECO:0000313|EMBL:CRK88880.1, 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; CVRI01000010; CRK88880.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J1HLE5; -.
DR STRING; 568069.A0A1J1HLE5; -.
DR OrthoDB; 3474910at2759; -.
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; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
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; PF13855; LRR_8; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00369; LRR_TYP; 2.
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 Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Reference proteome {ECO:0000313|Proteomes:UP000183832};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..521
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009619045"
FT DOMAIN 46..294
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
SQ SEQUENCE 521 AA; 59243 MW; 7C10A773823DEA2C CRC64;
MILNSPVVLK FLLILFVITK IQSGNLVEGT NSESQCGVSL KISGRIYNGK VVEKNQWPFL
VALTYNPDGE FFCGGTLISR SHVLTAAHCL QEKRQQTPLT PSQFVLHLGK YNLSLAHERG
SITAFPENIK IHPNWNIFQI KYDYDIALIK MDGIVPLRSN IFPACLWTSA LGMRNIQTGT
VVGWGIIEDQ LTSQHQLIPR QIELKIVTNE VCYEVEPMAN LISSRTFCAI GENGSGPCKG
DSGGGFFMKE NSKWLIKGIV SSSLVTEEGN CDVESYSIFT DISKFSNWIA KEMSVETDMT
CKFFLEDGKR YHCFPKNLVI QQPNVEVSVI MGVHLGQRSN NDVTKFSILF QETSYLPHGI
PELFPNLTRY CAFKTNLKHI QRSDFSGFQS LTTIEMGYNE LTNIPADTFY DVPGLKKLHL
QRNQIVSFDV DLFINNPNLK EFFAYKNQIE YLDGRLFRKN LNLELIVMDY NKLKHIDFEL
FTPLKKLKVV NFRHNTCISE FFSEMKDFEG FKAIIATNCS I
//
