The Tryp_SPc domain within your query sequence starts at position 867 and ends at position 1093, and its E-value is 1.62e-92.

Some of the required catalytic sites were not detected in this domain, and are marked red in the sequence below. The domain is probably inactive. Check the literature (PubMed 95010055 ) for details.

Catalytic residues
Position
Domain	Protein	Amino acid	Present?
43	909	H	Yes
90	956	D	Yes
183	1049	S	No

RIVGGSAASLGEWPWQVSLWLRRREHRCGAVLVAERWLLSAAHCFDIYGDPMQWAAFLGTPFLSSTEGQLERVARIYRHPFYNIYTLDYDVALLELAGPVRRSRLVRPICLPGPARPPDGARCVITGWGSLREGGSMARQLQKAAVRVLSEQTCRRFYPVQISSRMLCAGFPQGGVDSCSGDAGGPLACREPSGQWVLTGVTSWGYGCGRPHFPGVYTRVAAVLGWI

Tryp_SPc Trypsin-like serine protease
SMART ACC:	SM000020
Description:	Many of these are synthesised as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. A few, however, are active as single chain molecules, and others are inactive due to substitutions of the catalytic triad residues.
InterPro ACC:	IPR001254
InterPro abstract:	This entry represents the active-site-containing domain found in the trypsin family members. The catalytic activity of the serine proteases from the trypsin family is provided by a charge relay system involving an aspartic acid residue hydrogen-bonded to a histidine, which itself is hydrogen-bonded to a serine. The sequences in the vicinity of the active site serine and histidine residues are … expand This entry represents the active-site-containing domain found in the trypsin family members. The catalytic activity of the serine proteases from the trypsin family is provided by a charge relay system involving an aspartic acid residue hydrogen-bonded to a histidine, which itself is hydrogen-bonded to a serine. The sequences in the vicinity of the active site serine and histidine residues are well conserved in this family of proteases [ PUBMED:3136396 ]. A partial list of proteases known to belong to the trypsin family is shown below. Acrosin. Blood coagulation factors VII, IX, X, XI and XII, thrombin, plasminogen, and protein C. Cathepsin G. Chymotrypsins. Complement components C1r, C1s, C2, and complement factors B, D and I. Complement-activating component of RA-reactive factor. Cytotoxic cell proteases (granzymes A to H). Duodenase I. Elastases 1, 2, 3A, 3B (protease E), leukocyte (medullasin). Enterokinase (EC 3.4.21.9) (enteropeptidase). Hepatocyte growth factor activator. Hepsin. Glandular (tissue) kallikreins (including EGF-binding protein types A, B, and C, NGF-gamma chain, gamma-renin, prostate specific antigen (PSA) and tonin). Plasma kallikrein. Mast cell proteases (MCP) 1 (chymase) to 8. Myeloblastin (proteinase 3) (Wegener's autoantigen). Plasminogen activators (urokinase-type, and tissue-type). Trypsins I, II, III, and IV. Tryptases. All the above proteins belong to family S1 in the classification of peptidases [ PUBMED:7845208 ] and originate from eukaryotic species. It should be noted that bacterial proteases that belong to family S2A are similar enough in the regions of the active site residues that they can be picked up by the same patterns. These proteases are listed below. Achromobacter lyticus protease I. Lysobacter alpha-lytic protease. Streptogrisin A and B (Streptomyces proteases A and B). Streptomyces griseus glutamyl endopeptidase II. Streptomyces fradiae proteases 1 and 2. collapse
GO process:	proteolysis (GO:0006508)
GO function:	serine-type endopeptidase activity (GO:0004252)
Family alignment:	View the Family alignment or the Alignment consensus sequence
There are 111 555 Tryp_SPc domains in 106 560 proteins in SMART's NRDB database.

Taxonomic distribution of proteins containing Tryp_SPc domains

The tree below includes only several representative species and genera. The complete taxonomic breakdown of all proteins containing Tryp_SPc domains can be accessed here. Click the counts or percentage values to display the corresponding proteins.

Predicted cellular role

Binding / catalysis:	Peptidase, Hydrolase

Disease genes where sequence variants are found in this domain

UniRef sequences and OMIM curated human diseases associated with missense mutations within the Tryp_SPc domain.

Protein	Description	Disease / phenotype
CFAB_HUMAN		OMIM:138470 : PROPERDIN FACTOR B; BF
FA12_HUMAN		OMIM:234000 : Factor XII deficiency
ELNE_HUMAN		OMIM:130130 : Hematopoiesis, cyclic
		OMIM:162800 : Neutropenia, congenital
		OMIM:202700 : no description
PLMN_HUMAN		OMIM:173350 : Plasminogen Tochigi disease ; Thrombophilia, dysplasminogenemic ; Plasminogen deficiency, types I and II ; Conjunctivitis, ligneous
PLMN_HUMAN		OMIM:217090 : no description
PROC_HUMAN		OMIM:176860 : Thrombophilia due to protein C deficiency ; Purpura fulminans, neonatal
FA9_HUMAN		OMIM:306900 : Hemophilia B ; Warfarin sensitivity
TRY1_HUMAN		OMIM:276000 : Trypsinogen deficiency ; Pancreatitis, hereditary
TRY1_HUMAN		OMIM:167800 : no description
CO2_HUMAN		OMIM:217000 : C2 deficiency
THRB_HUMAN		OMIM:176930 : Hypoprothrombinemia ; Dysprothrombinemia
FA7_HUMAN		OMIM:227500 : Factor VII deficiency ; {Myocardial infarction, decreased susceptibility to}

KEGG pathways involving proteins which contain this domain

This information is based on the mapping of SMART genomic protein database to KEGG orthologous groups. Percentages are related to the number of proteins containing a Tryp_SPc domain which could be assigned to a KEGG orthologous group, and not all proteins containing Tryp_SPc domains. Please note that proteins can be included in multiple pathways, ie. the numbers below will not add to 100%.

KEGG pathways

Some of these pathways are included in the interactive Pathways Explorer overview maps. Select an overview map and click the button below to highlight them in iPath.

KEGG orthologous groups

Some of these KOs are included in the interactive Pathways Explorer overview maps. Select an overview map and click the button below to highlight them in iPath.

3D structures in PDB containing this domain

Links to other resources describing this domain

InterPro	IPR001254