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Conserved domains on  [gi|662236739|ref|NP_001284488|]
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serine protease HTRA3 isoform 2 precursor [Homo sapiens]

Protein Classification

Kazal-type serine protease inhibitor family protein; Do family serine endopeptidase( domain architecture ID 13622484)

Kazal-type serine protease inhibitor family protein may function as a serine protease inhibitor| Do/DeqQ family serine endopeptidase belonging to the peptidase S1C family, contains a PDZ-domain, similar to Lactococcus lactis Do-like HtrA (High-temperature requirement A), which is a surface protease responsible for the housekeeping of exported proteins and plays a role in stress resistance during active exponential growth

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DegQ COG0265
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ...
 173-343 6.74e-69

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: 217.32  E-value: 6.74e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662236739 173 SSGSGFIMSEAGLIITNAHVVSsnsaapGRQQLKVQLQNGDSYEATIKDIDKKSDIATIKIHPKKkLPVLLLGHSADLRP 252
Cdd:COG0265    1 GLGSGVIISPDGYILTNNHVVE------GADEITVTLADGREYPAKVVGRDPLTDLAVLKIDAKD-LPAAPLGDSDKLRV 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662236739 253 GEFVVAIGSPFALQNTVTTGIVSTAqreGRELGLRDSD--MDYIQTDAIINYGNSGGPLVNLDGEVIGINTLKVT----- 325
Cdd:COG0265   74 GDWVLAIGNPFGLGQTVTAGIVSAL---GRSIGSSGGGtyDDFIQTDAAINPGNSGGPLVNLNGEVIGINTAIISrsggs 150

                        170
                 ....*....|....*...
gi 662236739 326 AGISFAIPSDRITRFLTE 343
Cdd:COG0265  151 QGIGFAIPINLAKRVVEQ 168
IGFBP pfam00219
Insulin-like growth factor binding protein;
25-76 2.34e-17

Insulin-like growth factor binding protein;


:

Pssm-ID: 459717  Cd Length: 53  Bit Score: 75.05  E-value: 2.34e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 662236739   25 CPARCDVSRCPS--PRCPGGYVPDLCNCCLVCAASEGEPCGGpLDSPCGESLEC 76
Cdd:pfam00219   1 CPPPCDPERCPPppPGCPAGVVLDGCGCCKVCARQEGEPCGV-YTPPCGKGLRC 53
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 89-126 1.57e-06

Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains.


:

Pssm-ID: 197624  Cd Length: 46  Bit Score: 44.59  E-value: 1.57e-06
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 662236739    89 VCGTDGHTYANVCALQAASRRalqlSGTPVRQLQKGAC 126
Cdd:smart00280  13 VCGSDGVTYSNECHLCKAACE----SGKSIEVKHDGPC 46
 
Name Accession Description Interval E-value
DegQ COG0265
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ...
 173-343 6.74e-69

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: 217.32  E-value: 6.74e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662236739 173 SSGSGFIMSEAGLIITNAHVVSsnsaapGRQQLKVQLQNGDSYEATIKDIDKKSDIATIKIHPKKkLPVLLLGHSADLRP 252
Cdd:COG0265    1 GLGSGVIISPDGYILTNNHVVE------GADEITVTLADGREYPAKVVGRDPLTDLAVLKIDAKD-LPAAPLGDSDKLRV 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662236739 253 GEFVVAIGSPFALQNTVTTGIVSTAqreGRELGLRDSD--MDYIQTDAIINYGNSGGPLVNLDGEVIGINTLKVT----- 325
Cdd:COG0265   74 GDWVLAIGNPFGLGQTVTAGIVSAL---GRSIGSSGGGtyDDFIQTDAAINPGNSGGPLVNLNGEVIGINTAIISrsggs 150

                        170
                 ....*....|....*...
gi 662236739 326 AGISFAIPSDRITRFLTE 343
Cdd:COG0265  151 QGIGFAIPINLAKRVVEQ 168
degP_htrA_DO TIGR02037
periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ...
 143-356 1.23e-67

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: 219.02  E-value: 1.23e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662236739  143 IADVVEKIAPAVVHIEL---------------FLRHPlFGRNVPL-----------SSGSGFIMSEAGLIITNAHVVSsn 196
Cdd:TIGR02037   3 FAPLVEKVAPAVVNISVegtvkrrnrppalppFFRQF-FGDDMPDfprqqreqkvrGLGSGVIISADGYVLTNNHVVD-- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662236739  197 saapGRQQLKVQLQNGDSYEATIKDIDKKSDIATIKIHPKKKLPVLLLGHSADLRPGEFVVAIGSPFALQNTVTTGIVST 276
Cdd:TIGR02037  80 ----GADEITVTLSDGREFKAKLVGKDPRTDIAVLKIDAKKNLPVIKLGDSDKLRVGDWVLAIGNPFGLGQTVTSGIVSA 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662236739  277 AQREGreLGLRDSDmDYIQTDAIINYGNSGGPLVNLDGEVIGINTLKVT-----AGISFAIPSDRITRFLTEF-QDKQIK 350
Cdd:TIGR02037 156 LGRSG--LGIGDYE-NFIQTDAAINPGNSGGPLVNLRGEVIGINTAILSpsggnVGIGFAIPSNMAKNVVDQLiEGGKVK 232


                  ....*.
gi 662236739  351 APSLAV 356
Cdd:TIGR02037 233 RGWLGV 238
PRK10942 PRK10942
serine endoprotease DegP;
175-335 1.64e-38

serine endoprotease DegP;


Pssm-ID: 236802 [Multi-domain]  Cd Length: 473  Bit Score: 142.98  E-value: 1.64e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662236739 175 GSGFIMSEA-GLIITNAHVVSSNSaapgrqQLKVQLQNGDSYEATIKDIDKKSDIATIKIHPKKKLPVLLLGHSADLRPG 253
Cdd:PRK10942 113 GSGVIIDADkGYVVTNNHVVDNAT------KIKVQLSDGRKFDAKVVGKDPRSDIALIQLQNPKNLTAIKMADSDALRVG 186

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662236739 254 EFVVAIGSPFALQNTVTTGIVSTAQREGreLGLRDSDmDYIQTDAIINYGNSGGPLVNLDGEVIGINTLKVTA-----GI 328
Cdd:PRK10942 187 DYTVAIGNPYGLGETVTSGIVSALGRSG--LNVENYE-NFIQTDAAINRGNSGGALVNLNGELIGINTAILAPdggniGI 263


                 ....*..
gi 662236739 329 SFAIPSD 335
Cdd:PRK10942 264 GFAIPSN 270
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
 175-319 2.50e-30

Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 112.90  E-value: 2.50e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662236739  175 GSGFIMSEAGLIITNAHVVSSNSAAPgRQQLKVQLQNGDSYEATIKDIDKKSDIATIKI-HPKKKLPVLLLGHSADLRPG 253
Cdd:pfam13365   1 GTGFVVSSDGLVLTNAHVVDDAEEAA-VELVSVVLADGREYPATVVARDPDLDLALLRVsGDGRGLPPLPLGDSEPLVGG 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 662236739  254 EFVVAIGSPFALQ-NTVTTGIVSTAQREGRElglrDSDMDYIQTDAIINYGNSGGPLVNLDGEVIGI 319
Cdd:pfam13365  80 ERVYAVGYPLGGEkLSLSEGIVSGVDEGRDG----GDDGRVIQTDAALSPGSSGGPVFDADGRVVGI 142
IGFBP pfam00219
Insulin-like growth factor binding protein;
25-76 2.34e-17

Insulin-like growth factor binding protein;


Pssm-ID: 459717  Cd Length: 53  Bit Score: 75.05  E-value: 2.34e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 662236739   25 CPARCDVSRCPS--PRCPGGYVPDLCNCCLVCAASEGEPCGGpLDSPCGESLEC 76
Cdd:pfam00219   1 CPPPCDPERCPPppPGCPAGVVLDGCGCCKVCARQEGEPCGV-YTPPCGKGLRC 53
IB smart00121
Insulin growth factor-binding protein homologues; High affinity binding partners of ...
 23-79 6.84e-13

Insulin growth factor-binding protein homologues; High affinity binding partners of insulin-like growth factors.


Pssm-ID: 197525  Cd Length: 75  Bit Score: 63.25  E-value: 6.84e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 662236739    23 APCPaRCDVSRCPS--PRCPGGYVPDLCNCCLVCAASEGEPCGGPLDsPCGESLECVRG 79
Cdd:smart00121   1 ARCP-PCDPARCPPcpPGCAELVRLDGCGCCPVCARQEGEPCGVYTP-RCAPGLRCQPP 57
MarP_fam_protase NF033740
MarP family serine protease; The founding member of this family of membrane-spanning serine ...
 144-319 1.16e-11

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: 65.21  E-value: 1.16e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662236739 144 ADVVEKIAPAVVHIELflRHPLFGRNvplSSGSGFIMSEaGLIITNAHVVSsnsaapGRQQLKVQLQNGDSYEATIKDID 223
Cdd:NF033740 187 SPAVRRARPSVVKVRG--TAPSCGRA---LEGSGFVVAP-DRVMTNAHVVA------GTDEVTVETVGGGTLDARVVYYD 254

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662236739 224 KKSDIATIKIhPKKKLPVLLLGhSADLRPGEFVVAIG----SPFalqnTVT-TGIVSTAQREGREL-GLRDSDMDYIQTD 297
Cdd:NF033740 255 PDRDIAVLAV-PGLGLPPLPFA-DEPAETGDDAIVLGypegGPF----TATpARVRERIALSGPDIyGSGTVTREVYTLR 328

                        170       180
                 ....*....|....*....|..
gi 662236739 298 AIINYGNSGGPLVNLDGEVIGI 319
Cdd:NF033740 329 GTVRPGNSGGPLLDPDGRVLGV 350
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 89-126 1.57e-06

Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains.


Pssm-ID: 197624  Cd Length: 46  Bit Score: 44.59  E-value: 1.57e-06
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 662236739    89 VCGTDGHTYANVCALQAASRRalqlSGTPVRQLQKGAC 126
Cdd:smart00280  13 VCGSDGVTYSNECHLCKAACE----SGKSIEVKHDGPC 46
Kazal_2 pfam07648
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
 76-126 2.90e-06

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: 44.02  E-value: 2.90e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 662236739   76 CVRGLCRCRWSHAVCGTDGHTYANVCALQAASRRALQLSGTPVrQLQKGAC 126
Cdd:pfam07648   1 NCNCQCPKTEYEPVCGSDGVTYPSPCALCAAGCKLGKEVKEEK-VKYDGSC 50
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
 89-126 7.36e-05

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: 39.56  E-value: 7.36e-05
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 662236739  89 VCGTDGHTYANVCALQAASRRalqlSGTPVRQLQKGAC 126
Cdd:cd00104    8 VCGSDGKTYSNECHLGCAACR----SGRSITVAHNGPC 41
 
Name Accession Description Interval E-value
DegQ COG0265
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ...
 173-343 6.74e-69

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: 217.32  E-value: 6.74e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662236739 173 SSGSGFIMSEAGLIITNAHVVSsnsaapGRQQLKVQLQNGDSYEATIKDIDKKSDIATIKIHPKKkLPVLLLGHSADLRP 252
Cdd:COG0265    1 GLGSGVIISPDGYILTNNHVVE------GADEITVTLADGREYPAKVVGRDPLTDLAVLKIDAKD-LPAAPLGDSDKLRV 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662236739 253 GEFVVAIGSPFALQNTVTTGIVSTAqreGRELGLRDSD--MDYIQTDAIINYGNSGGPLVNLDGEVIGINTLKVT----- 325
Cdd:COG0265   74 GDWVLAIGNPFGLGQTVTAGIVSAL---GRSIGSSGGGtyDDFIQTDAAINPGNSGGPLVNLNGEVIGINTAIISrsggs 150

                        170
                 ....*....|....*...
gi 662236739 326 AGISFAIPSDRITRFLTE 343
Cdd:COG0265  151 QGIGFAIPINLAKRVVEQ 168
degP_htrA_DO TIGR02037
periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ...
 143-356 1.23e-67

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: 219.02  E-value: 1.23e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662236739  143 IADVVEKIAPAVVHIEL---------------FLRHPlFGRNVPL-----------SSGSGFIMSEAGLIITNAHVVSsn 196
Cdd:TIGR02037   3 FAPLVEKVAPAVVNISVegtvkrrnrppalppFFRQF-FGDDMPDfprqqreqkvrGLGSGVIISADGYVLTNNHVVD-- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662236739  197 saapGRQQLKVQLQNGDSYEATIKDIDKKSDIATIKIHPKKKLPVLLLGHSADLRPGEFVVAIGSPFALQNTVTTGIVST 276
Cdd:TIGR02037  80 ----GADEITVTLSDGREFKAKLVGKDPRTDIAVLKIDAKKNLPVIKLGDSDKLRVGDWVLAIGNPFGLGQTVTSGIVSA 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662236739  277 AQREGreLGLRDSDmDYIQTDAIINYGNSGGPLVNLDGEVIGINTLKVT-----AGISFAIPSDRITRFLTEF-QDKQIK 350
Cdd:TIGR02037 156 LGRSG--LGIGDYE-NFIQTDAAINPGNSGGPLVNLRGEVIGINTAILSpsggnVGIGFAIPSNMAKNVVDQLiEGGKVK 232


                  ....*.
gi 662236739  351 APSLAV 356
Cdd:TIGR02037 233 RGWLGV 238
PRK10942 PRK10942
serine endoprotease DegP;
175-335 1.64e-38

serine endoprotease DegP;


Pssm-ID: 236802 [Multi-domain]  Cd Length: 473  Bit Score: 142.98  E-value: 1.64e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662236739 175 GSGFIMSEA-GLIITNAHVVSSNSaapgrqQLKVQLQNGDSYEATIKDIDKKSDIATIKIHPKKKLPVLLLGHSADLRPG 253
Cdd:PRK10942 113 GSGVIIDADkGYVVTNNHVVDNAT------KIKVQLSDGRKFDAKVVGKDPRSDIALIQLQNPKNLTAIKMADSDALRVG 186

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662236739 254 EFVVAIGSPFALQNTVTTGIVSTAQREGreLGLRDSDmDYIQTDAIINYGNSGGPLVNLDGEVIGINTLKVTA-----GI 328
Cdd:PRK10942 187 DYTVAIGNPYGLGETVTSGIVSALGRSG--LNVENYE-NFIQTDAAINRGNSGGALVNLNGELIGINTAILAPdggniGI 263


                 ....*..
gi 662236739 329 SFAIPSD 335
Cdd:PRK10942 264 GFAIPSN 270
PRK10898 PRK10898
serine endoprotease DegS;
147-350 2.61e-38

serine endoprotease DegS;


Pssm-ID: 182820 [Multi-domain]  Cd Length: 353  Bit Score: 140.14  E-value: 2.61e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662236739 147 VEKIAPAVVHIelflrhplFGRNVPLSS---------GSGFIMSEAGLIITNAHVVssNSAapgrQQLKVQLQNGDSYEA 217
Cdd:PRK10898  51 VRRAAPAVVNV--------YNRSLNSTShnqleirtlGSGVIMDQRGYILTNKHVI--NDA----DQIIVALQDGRVFEA 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662236739 218 TIKDIDKKSDIATIKIHPKKkLPVLLLGHSADLRPGEFVVAIGSPFALQNTVTTGIVSTAQRegreLGLRDSD-MDYIQT 296
Cdd:PRK10898 117 LLVGSDSLTDLAVLKINATN-LPVIPINPKRVPHIGDVVLAIGNPYNLGQTITQGIISATGR----IGLSPTGrQNFLQT 191

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 662236739 297 DAIINYGNSGGPLVNLDGEVIGINTL--------KVTAGISFAIPsdriTRFLTEFQDKQIK 350
Cdd:PRK10898 192 DASINHGNSGGALVNSLGELMGINTLsfdksndgETPEGIGFAIP----TQLATKIMDKLIR 249
PRK10139 PRK10139
serine endoprotease DegQ;
143-335 3.97e-37

serine endoprotease DegQ;


Pssm-ID: 182262 [Multi-domain]  Cd Length: 455  Bit Score: 138.93  E-value: 3.97e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662236739 143 IADVVEKIAPAVVHIEL------FLRHP-----LFGRNVPLSS-------GSGFIMSEA-GLIITNAHVVSSnsaapgRQ 203
Cdd:PRK10139  42 LAPMLEKVLPAVVSVRVegtasqGQKIPeefkkFFGDDLPDQPaqpfeglGSGVIIDAAkGYVLTNNHVINQ------AQ 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662236739 204 QLKVQLQNGDSYEATIKDIDKKSDIATIKIHPKKKLPVLLLGHSADLRPGEFVVAIGSPFALQNTVTTGIVSTAQREGRE 283
Cdd:PRK10139 116 KISIQLNDGREFDAKLIGSDDQSDIALLQIQNPSKLTQIAIADSDKLRVGDFAVAVGNPFGLGQTATSGIISALGRSGLN 195

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 662236739 284 L-GLRdsdmDYIQTDAIINYGNSGGPLVNLDGEVIGINTLKV-----TAGISFAIPSD 335
Cdd:PRK10139 196 LeGLE----NFIQTDASINRGNSGGALLNLNGELIGINTAILapgggSVGIGFAIPSN 249
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
 175-319 2.50e-30

Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 112.90  E-value: 2.50e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662236739  175 GSGFIMSEAGLIITNAHVVSSNSAAPgRQQLKVQLQNGDSYEATIKDIDKKSDIATIKI-HPKKKLPVLLLGHSADLRPG 253
Cdd:pfam13365   1 GTGFVVSSDGLVLTNAHVVDDAEEAA-VELVSVVLADGREYPATVVARDPDLDLALLRVsGDGRGLPPLPLGDSEPLVGG 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 662236739  254 EFVVAIGSPFALQ-NTVTTGIVSTAQREGRElglrDSDMDYIQTDAIINYGNSGGPLVNLDGEVIGI 319
Cdd:pfam13365  80 ERVYAVGYPLGGEkLSLSEGIVSGVDEGRDG----GDDGRVIQTDAALSPGSSGGPVFDADGRVVGI 142
IGFBP pfam00219
Insulin-like growth factor binding protein;
25-76 2.34e-17

Insulin-like growth factor binding protein;


Pssm-ID: 459717  Cd Length: 53  Bit Score: 75.05  E-value: 2.34e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 662236739   25 CPARCDVSRCPS--PRCPGGYVPDLCNCCLVCAASEGEPCGGpLDSPCGESLEC 76
Cdd:pfam00219   1 CPPPCDPERCPPppPGCPAGVVLDGCGCCKVCARQEGEPCGV-YTPPCGKGLRC 53
Trypsin pfam00089
Trypsin;
177-341 2.68e-13

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 68.24  E-value: 2.68e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662236739  177 GFIMSEaGLIITNAHVVSSNSAAPGRQ-QLKVQLQNGDSYEATIKDI---------DKKSDIATIKIHPKKKL-----PV 241
Cdd:pfam00089  29 GSLISE-NWVLTAAHCVSGASDVKVVLgAHNIVLREGGEQKFDVEKIivhpnynpdTLDNDIALLKLESPVTLgdtvrPI 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662236739  242 LLLGHSADLRPGE--FVVAIGSPFALQ-----NTVTTGIVSTAQREGRELGLRDSDMdyIQTDAI---INYGNSGGPLVN 311
Cdd:pfam00089 108 CLPDASSDLPVGTtcTVSGWGNTKTLGpsdtlQEVTVPVVSRETCRSAYGGTVTDTM--ICAGAGgkdACQGDSGGPLVC 185

                         170       180       190
                  ....*....|....*....|....*....|....
gi 662236739  312 LDGEVIGINTLK----VTAGISFAIPSDRITRFL 341
Cdd:pfam00089 186 SDGELIGIVSWGygcaSGNYPGVYTPVSSYLDWI 219
IB smart00121
Insulin growth factor-binding protein homologues; High affinity binding partners of ...
 23-79 6.84e-13

Insulin growth factor-binding protein homologues; High affinity binding partners of insulin-like growth factors.


Pssm-ID: 197525  Cd Length: 75  Bit Score: 63.25  E-value: 6.84e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 662236739    23 APCPaRCDVSRCPS--PRCPGGYVPDLCNCCLVCAASEGEPCGGPLDsPCGESLECVRG 79
Cdd:smart00121   1 ARCP-PCDPARCPPcpPGCAELVRLDGCGCCPVCARQEGEPCGVYTP-RCAPGLRCQPP 57
MarP_fam_protase NF033740
MarP family serine protease; The founding member of this family of membrane-spanning serine ...
 144-319 1.16e-11

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: 65.21  E-value: 1.16e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662236739 144 ADVVEKIAPAVVHIELflRHPLFGRNvplSSGSGFIMSEaGLIITNAHVVSsnsaapGRQQLKVQLQNGDSYEATIKDID 223
Cdd:NF033740 187 SPAVRRARPSVVKVRG--TAPSCGRA---LEGSGFVVAP-DRVMTNAHVVA------GTDEVTVETVGGGTLDARVVYYD 254

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662236739 224 KKSDIATIKIhPKKKLPVLLLGhSADLRPGEFVVAIG----SPFalqnTVT-TGIVSTAQREGREL-GLRDSDMDYIQTD 297
Cdd:NF033740 255 PDRDIAVLAV-PGLGLPPLPFA-DEPAETGDDAIVLGypegGPF----TATpARVRERIALSGPDIyGSGTVTREVYTLR 328

                        170       180
                 ....*....|....*....|..
gi 662236739 298 AIINYGNSGGPLVNLDGEVIGI 319
Cdd:NF033740 329 GTVRPGNSGGPLLDPDGRVLGV 350
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 89-126 1.57e-06

Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains.


Pssm-ID: 197624  Cd Length: 46  Bit Score: 44.59  E-value: 1.57e-06
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 662236739    89 VCGTDGHTYANVCALQAASRRalqlSGTPVRQLQKGAC 126
Cdd:smart00280  13 VCGSDGVTYSNECHLCKAACE----SGKSIEVKHDGPC 46
Kazal_2 pfam07648
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
 76-126 2.90e-06

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: 44.02  E-value: 2.90e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 662236739   76 CVRGLCRCRWSHAVCGTDGHTYANVCALQAASRRALQLSGTPVrQLQKGAC 126
Cdd:pfam07648   1 NCNCQCPKTEYEPVCGSDGVTYPSPCALCAAGCKLGKEVKEEK-VKYDGSC 50
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
 173-333 3.03e-05

V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 44.28  E-value: 3.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662236739 173 SSGSGFIMSEaGLIITNAHVVSSNSAAPGRQQLKVQL-QNGDSYEAT-----------IKDIDKKSDIATIKIHPKKKLP 240
Cdd:COG3591   12 GVCTGTLIGP-NLVLTAGHCVYDGAGGGWATNIVFVPgYNGGPYGTAtatrfrvppgwVASGDAGYDYALLRLDEPLGDT 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662236739 241 V--LLLGHSADLRPGEFVVAIGSPFALQNTVttgivsTAQREGRelgLRDSDMDYIQTDAIINYGNSGGPLVNLD---GE 315
Cdd:COG3591   91 TgwLGLAFNDAPLAGEPVTIIGYPGDRPKDL------SLDCSGR---VTGVQGNRLSYDCDTTGGSSGSPVLDDSdggGR 161

                        170
                 ....*....|....*...
gi 662236739 316 VIGINTLKVTAGISFAIP 333
Cdd:COG3591  162 VVGVHSAGGADRANTGVR 179
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
 89-126 7.36e-05

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: 39.56  E-value: 7.36e-05
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 662236739  89 VCGTDGHTYANVCALQAASRRalqlSGTPVRQLQKGAC 126
Cdd:cd00104    8 VCGSDGKTYSNECHLGCAACR----SGRSITVAHNGPC 41
KAZAL_PSTI cd01327
Kazal-type pancreatic secretory trypsin inhibitors (PSTI) and related proteins, including the ...
 89-126 2.11e-03

Kazal-type pancreatic secretory trypsin inhibitors (PSTI) and related proteins, including the second domain of the ovomucoid turkey inhibitor and the C-terminal domain of the esophagus cancer-related gene-2 protein (ECRG-2), are members of the superfamily of kazal-type proteinase inhibitors and follistatin-like proteins.


Pssm-ID: 238648  Cd Length: 45  Bit Score: 35.72  E-value: 2.11e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 662236739  89 VCGTDGHTYANVCALQAASrralQLSGTPVRQLQKGAC 126
Cdd:cd01327   12 VCGTDGVTYSNECLLCAEN----LKRQTNIRIKHDGEC 45
Kazal_1 pfam00050
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
 89-126 3.36e-03

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. Alignment also includes a single domain from transporters in the OATP/PGT family.


Pssm-ID: 395004  Cd Length: 49  Bit Score: 35.34  E-value: 3.36e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 662236739   89 VCGTDGHTYANVCALQAASRralqLSGTPVRQLQKGAC 126
Cdd:pfam00050  16 VCGTDGKTYSNECLFCAENG----KRGTNLHKVHDGEC 49
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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