![](files/infoQ.gif)
serine protease HTRA4 isoform X2 [Homo sapiens]
IGFBP and cpPDZ_HtrA-like domain-containing protein( domain architecture ID 13622476)
protein containing domains IGFBP, KAZAL_FS, and cpPDZ_HtrA-like
List of domain hits
![](files/help.png)
Name | Accession | Description | Interval | E-value | |||
DegQ | COG0265 | Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ... |
201-333 | 7.81e-54 | |||
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational modification, protein turnover, chaperones]; : Pssm-ID: 440035 [Multi-domain] Cd Length: 274 Bit Score: 178.03 E-value: 7.81e-54
|
|||||||
IGFBP | pfam00219 | Insulin-like growth factor binding protein; |
40-94 | 1.58e-12 | |||
Insulin-like growth factor binding protein; : Pssm-ID: 459717 Cd Length: 53 Bit Score: 61.57 E-value: 1.58e-12
|
|||||||
Kazal_2 | pfam07648 | Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ... |
104-152 | 1.75e-07 | |||
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. However, kazal-like domains are also seen in the extracellular part of agrins, which are not known to be protease inhibitors. Kazal domains often occur in tandem arrays. Small alpha+beta fold containing three disulphides. : Pssm-ID: 400135 Cd Length: 50 Bit Score: 47.10 E-value: 1.75e-07
|
|||||||
Name | Accession | Description | Interval | E-value | ||||
DegQ | COG0265 | Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ... |
201-333 | 7.81e-54 | ||||
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440035 [Multi-domain] Cd Length: 274 Bit Score: 178.03 E-value: 7.81e-54
|
||||||||
degP_htrA_DO | TIGR02037 | periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ... |
170-333 | 9.36e-50 | ||||
periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various designated DegP, heat shock protein HtrA, and protease DO. The ortholog in Pseudomonas aeruginosa is designated MucD and is found in an operon that controls mucoid phenotype. This family also includes the DegQ (HhoA) paralog in E. coli which can rescue a DegP mutant, but not the smaller DegS paralog, which cannot. Members of this family are located in the periplasm and have separable functions as both protease and chaperone. Members have a trypsin domain and two copies of a PDZ domain. This protein protects bacteria from thermal and other stresses and may be important for the survival of bacterial pathogens.// The chaperone function is dominant at low temperatures, whereas the proteolytic activity is turned on at elevated temperatures. [Protein fate, Protein folding and stabilization, Protein fate, Degradation of proteins, peptides, and glycopeptides] Pssm-ID: 273938 [Multi-domain] Cd Length: 428 Bit Score: 171.64 E-value: 9.36e-50
|
||||||||
PRK10898 | PRK10898 | serine endoprotease DegS; |
174-332 | 7.69e-29 | ||||
serine endoprotease DegS; Pssm-ID: 182820 [Multi-domain] Cd Length: 353 Bit Score: 113.94 E-value: 7.69e-29
|
||||||||
Trypsin_2 | pfam13365 | Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains. |
202-332 | 1.31e-27 | ||||
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains. Pssm-ID: 433149 [Multi-domain] Cd Length: 142 Bit Score: 105.20 E-value: 1.31e-27
|
||||||||
MarP_fam_protase | NF033740 | MarP family serine protease; The founding member of this family of membrane-spanning serine ... |
171-332 | 1.24e-13 | ||||
MarP family serine protease; The founding member of this family of membrane-spanning serine proteases, which is restricted to Actinobacteria, is the acid resistance periplasmic serine protease MarP of Mycobacterium tuberculosis. Recent work shows that MarP is required to cleave and activate the peptidoglycan hydrolase RipA, and loss of RipA activity creates a defect in progeny separation during cell division. Therefore, the requirement for MarP in order to survive acidic conditions may be a consequence of peptidoglycan hydrolysis requirements, explaining why MarP family members are distributed more broadly in the Actinobacteria than the subset of species capable of surviving intracellularly as pathogens. Pssm-ID: 468161 [Multi-domain] Cd Length: 390 Bit Score: 70.98 E-value: 1.24e-13
|
||||||||
IGFBP | pfam00219 | Insulin-like growth factor binding protein; |
40-94 | 1.58e-12 | ||||
Insulin-like growth factor binding protein; Pssm-ID: 459717 Cd Length: 53 Bit Score: 61.57 E-value: 1.58e-12
|
||||||||
IB | smart00121 | Insulin growth factor-binding protein homologues; High affinity binding partners of ... |
40-94 | 1.39e-07 | ||||
Insulin growth factor-binding protein homologues; High affinity binding partners of insulin-like growth factors. Pssm-ID: 197525 Cd Length: 75 Bit Score: 48.23 E-value: 1.39e-07
|
||||||||
Kazal_2 | pfam07648 | Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ... |
104-152 | 1.75e-07 | ||||
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. However, kazal-like domains are also seen in the extracellular part of agrins, which are not known to be protease inhibitors. Kazal domains often occur in tandem arrays. Small alpha+beta fold containing three disulphides. Pssm-ID: 400135 Cd Length: 50 Bit Score: 47.10 E-value: 1.75e-07
|
||||||||
KAZAL_FS | cd00104 | Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ... |
108-152 | 5.86e-04 | ||||
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit serine proteases, such as, trypsin, chyomotrypsin, avian ovomucoids, and elastases. The inhibitory domain has one reactive site peptide bond, which serves the cognate enzyme as substrate. The reactive site peptide bond is a combining loop which has an identical conformation in all Kazal inhibitors and in all enzyme/inhibitor complexes. These Kazal domains (small hydrophobic core of alpha/beta structure with 3 to 4 disulfide bonds) often occur in tandem arrays. Similar domains are also present in follistatin (FS) and follistatin-like family members, which play an important role in tissue specific regulation. The FS domain consists of an N-terminal beta hairpin (FOLN/EGF-like domain) and a Kazal-like domain and has five disulfide bonds. Although the Kazal-like FS substructure is similar to Kazal proteinase inhibitors, no FS domain has yet been shown to be a proteinase inhibitor. Follistatin-like family members include SPARC, also known as, BM-40 or osteonectin, the Gallus gallus Flik protein, as well as, agrin which has a long array of FS domains. The kazal-type inhibitor domain has also been detected in an extracellular loop region of solute carrier 21 (SLC21) family members (organic anion transporters) , which may regulate the specificity of anion uptake. The distant homolog, Ascidian trypsin inhibitor, is included in this CD. Pssm-ID: 238052 [Multi-domain] Cd Length: 41 Bit Score: 36.86 E-value: 5.86e-04
|
||||||||
KAZAL | smart00280 | Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ... |
108-134 | 1.83e-03 | ||||
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains. Pssm-ID: 197624 Cd Length: 46 Bit Score: 35.73 E-value: 1.83e-03
|
||||||||
Name | Accession | Description | Interval | E-value | ||||
DegQ | COG0265 | Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ... |
201-333 | 7.81e-54 | ||||
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440035 [Multi-domain] Cd Length: 274 Bit Score: 178.03 E-value: 7.81e-54
|
||||||||
degP_htrA_DO | TIGR02037 | periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ... |
170-333 | 9.36e-50 | ||||
periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various designated DegP, heat shock protein HtrA, and protease DO. The ortholog in Pseudomonas aeruginosa is designated MucD and is found in an operon that controls mucoid phenotype. This family also includes the DegQ (HhoA) paralog in E. coli which can rescue a DegP mutant, but not the smaller DegS paralog, which cannot. Members of this family are located in the periplasm and have separable functions as both protease and chaperone. Members have a trypsin domain and two copies of a PDZ domain. This protein protects bacteria from thermal and other stresses and may be important for the survival of bacterial pathogens.// The chaperone function is dominant at low temperatures, whereas the proteolytic activity is turned on at elevated temperatures. [Protein fate, Protein folding and stabilization, Protein fate, Degradation of proteins, peptides, and glycopeptides] Pssm-ID: 273938 [Multi-domain] Cd Length: 428 Bit Score: 171.64 E-value: 9.36e-50
|
||||||||
PRK10898 | PRK10898 | serine endoprotease DegS; |
174-332 | 7.69e-29 | ||||
serine endoprotease DegS; Pssm-ID: 182820 [Multi-domain] Cd Length: 353 Bit Score: 113.94 E-value: 7.69e-29
|
||||||||
Trypsin_2 | pfam13365 | Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains. |
202-332 | 1.31e-27 | ||||
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains. Pssm-ID: 433149 [Multi-domain] Cd Length: 142 Bit Score: 105.20 E-value: 1.31e-27
|
||||||||
PRK10942 | PRK10942 | serine endoprotease DegP; |
202-333 | 5.23e-27 | ||||
serine endoprotease DegP; Pssm-ID: 236802 [Multi-domain] Cd Length: 473 Bit Score: 110.63 E-value: 5.23e-27
|
||||||||
PRK10139 | PRK10139 | serine endoprotease DegQ; |
170-333 | 9.56e-27 | ||||
serine endoprotease DegQ; Pssm-ID: 182262 [Multi-domain] Cd Length: 455 Bit Score: 110.04 E-value: 9.56e-27
|
||||||||
MarP_fam_protase | NF033740 | MarP family serine protease; The founding member of this family of membrane-spanning serine ... |
171-332 | 1.24e-13 | ||||
MarP family serine protease; The founding member of this family of membrane-spanning serine proteases, which is restricted to Actinobacteria, is the acid resistance periplasmic serine protease MarP of Mycobacterium tuberculosis. Recent work shows that MarP is required to cleave and activate the peptidoglycan hydrolase RipA, and loss of RipA activity creates a defect in progeny separation during cell division. Therefore, the requirement for MarP in order to survive acidic conditions may be a consequence of peptidoglycan hydrolysis requirements, explaining why MarP family members are distributed more broadly in the Actinobacteria than the subset of species capable of surviving intracellularly as pathogens. Pssm-ID: 468161 [Multi-domain] Cd Length: 390 Bit Score: 70.98 E-value: 1.24e-13
|
||||||||
IGFBP | pfam00219 | Insulin-like growth factor binding protein; |
40-94 | 1.58e-12 | ||||
Insulin-like growth factor binding protein; Pssm-ID: 459717 Cd Length: 53 Bit Score: 61.57 E-value: 1.58e-12
|
||||||||
Trypsin | pfam00089 | Trypsin; |
204-333 | 5.87e-09 | ||||
Trypsin; Pssm-ID: 459667 [Multi-domain] Cd Length: 219 Bit Score: 55.53 E-value: 5.87e-09
|
||||||||
IB | smart00121 | Insulin growth factor-binding protein homologues; High affinity binding partners of ... |
40-94 | 1.39e-07 | ||||
Insulin growth factor-binding protein homologues; High affinity binding partners of insulin-like growth factors. Pssm-ID: 197525 Cd Length: 75 Bit Score: 48.23 E-value: 1.39e-07
|
||||||||
Kazal_2 | pfam07648 | Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ... |
104-152 | 1.75e-07 | ||||
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. However, kazal-like domains are also seen in the extracellular part of agrins, which are not known to be protease inhibitors. Kazal domains often occur in tandem arrays. Small alpha+beta fold containing three disulphides. Pssm-ID: 400135 Cd Length: 50 Bit Score: 47.10 E-value: 1.75e-07
|
||||||||
eMpr | COG3591 | V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ... |
200-332 | 2.22e-05 | ||||
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 442810 [Multi-domain] Cd Length: 194 Bit Score: 44.67 E-value: 2.22e-05
|
||||||||
KAZAL_FS | cd00104 | Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ... |
108-152 | 5.86e-04 | ||||
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit serine proteases, such as, trypsin, chyomotrypsin, avian ovomucoids, and elastases. The inhibitory domain has one reactive site peptide bond, which serves the cognate enzyme as substrate. The reactive site peptide bond is a combining loop which has an identical conformation in all Kazal inhibitors and in all enzyme/inhibitor complexes. These Kazal domains (small hydrophobic core of alpha/beta structure with 3 to 4 disulfide bonds) often occur in tandem arrays. Similar domains are also present in follistatin (FS) and follistatin-like family members, which play an important role in tissue specific regulation. The FS domain consists of an N-terminal beta hairpin (FOLN/EGF-like domain) and a Kazal-like domain and has five disulfide bonds. Although the Kazal-like FS substructure is similar to Kazal proteinase inhibitors, no FS domain has yet been shown to be a proteinase inhibitor. Follistatin-like family members include SPARC, also known as, BM-40 or osteonectin, the Gallus gallus Flik protein, as well as, agrin which has a long array of FS domains. The kazal-type inhibitor domain has also been detected in an extracellular loop region of solute carrier 21 (SLC21) family members (organic anion transporters) , which may regulate the specificity of anion uptake. The distant homolog, Ascidian trypsin inhibitor, is included in this CD. Pssm-ID: 238052 [Multi-domain] Cd Length: 41 Bit Score: 36.86 E-value: 5.86e-04
|
||||||||
KAZAL | smart00280 | Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ... |
108-134 | 1.83e-03 | ||||
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains. Pssm-ID: 197624 Cd Length: 46 Bit Score: 35.73 E-value: 1.83e-03
|
||||||||
Blast search parameters | ||||
|