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Conserved domains on  [gi|767950641|ref|XP_011542734|]
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serine protease HTRA4 isoform X2 [Homo sapiens]

Protein Classification

Do family serine endopeptidase( domain architecture ID 13622476)

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 ...
 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
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950641 201 SGSGFIVSEDGLIITNAHVVRNQQWIEVVLQNGARYEAVVKDIDLKLDLAVIKIESnAELPVLMLGRSSDLRAGEFVVAL 280
Cdd:COG0265    2 LGSGVIISPDGYILTNNHVVEGADEITVTLADGREYPAKVVGRDPLTDLAVLKIDA-KDLPAAPLGDSDKLRVGDWVLAI 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 767950641 281 GSPFSLQNTATAGIVSTKQRGGkELGMKDSDMDYVQIDATINYGNSGGPLVNL 333
Cdd:COG0265   81 GNPFGLGQTVTAGIVSALGRSI-GSSGGGTYDDFIQTDAAINPGNSGGPLVNL 132
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
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767950641   40 CPAVCQPTRCPALP-TCALGTTPvfDLCRCCRVCPAAEREVCGGAQGqPCAPGLQC 94
Cdd:pfam00219   1 CPPPCDPERCPPPPpGCPAGVVL--DGCGCCKVCARQEGEPCGVYTP-PCGKGLRC 53
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
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 767950641  104 STCGCPTLGGA-VCGSDRRTYPSMCALRAENRAARRLGKVPAVpVQWGNC 152
Cdd:pfam07648   2 CNCQCPKTEYEpVCGSDGVTYPSPCALCAAGCKLGKEVKEEKV-KYDGSC 50
 
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
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950641 201 SGSGFIVSEDGLIITNAHVVRNQQWIEVVLQNGARYEAVVKDIDLKLDLAVIKIESnAELPVLMLGRSSDLRAGEFVVAL 280
Cdd:COG0265    2 LGSGVIISPDGYILTNNHVVEGADEITVTLADGREYPAKVVGRDPLTDLAVLKIDA-KDLPAAPLGDSDKLRVGDWVLAI 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 767950641 281 GSPFSLQNTATAGIVSTKQRGGkELGMKDSDMDYVQIDATINYGNSGGPLVNL 333
Cdd:COG0265   81 GNPFGLGQTVTAGIVSALGRSI-GSSGGGTYDDFIQTDAAINPGNSGGPLVNL 132
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
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950641  170 IAAVVEKVAPSVVHV--------------------QLWGRLL------HGSRLVPVYsGSGFIVSEDGLIITNAHVVRNQ 223
Cdd:TIGR02037   3 FAPLVEKVAPAVVNIsvegtvkrrnrppalppffrQFFGDDMpdfprqQREQKVRGL-GSGVIISADGYVLTNNHVVDGA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950641  224 QWIEVVLQNGARYEAVVKDIDLKLDLAVIKIESNAELPVLMLGRSSDLRAGEFVVALGSPFSLQNTATAGIVSTKQRGGk 303
Cdd:TIGR02037  82 DEITVTLSDGREFKAKLVGKDPRTDIAVLKIDAKKNLPVIKLGDSDKLRVGDWVLAIGNPFGLGQTVTSGIVSALGRSG- 160

                         170       180       190
                  ....*....|....*....|....*....|
gi 767950641  304 eLGMKDSDmDYVQIDATINYGNSGGPLVNL 333
Cdd:TIGR02037 161 -LGIGDYE-NFIQTDAAINPGNSGGPLVNL 188
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
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950641 174 VEKVAPSVVHV--QLWGRLLHGSRLVPVYsGSGFIVSEDGLIITNAHVVRNQQWIEVVLQNGARYEAVVKDIDLKLDLAV 251
Cdd:PRK10898  51 VRRAAPAVVNVynRSLNSTSHNQLEIRTL-GSGVIMDQRGYILTNKHVINDADQIIVALQDGRVFEALLVGSDSLTDLAV 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950641 252 IKIESnAELPVLMLGRSSDLRAGEFVVALGSPFSLQNTATAGIVSTKQRggkeLGMKDSD-MDYVQIDATINYGNSGGPL 330
Cdd:PRK10898 130 LKINA-TNLPVIPINPKRVPHIGDVVLAIGNPYNLGQTITQGIISATGR----IGLSPTGrQNFLQTDASINHGNSGGAL 204


                 ..
gi 767950641 331 VN 332
Cdd:PRK10898 205 VN 206
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
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950641  202 GSGFIVSEDGLIITNAHVVRNQQWIEV-----VLQNGARYEAVVKDIDLKLDLAVIKI-ESNAELPVLMLGRSSDLRAGE 275
Cdd:pfam13365   1 GTGFVVSSDGLVLTNAHVVDDAEEAAVelvsvVLADGREYPATVVARDPDLDLALLRVsGDGRGLPPLPLGDSEPLVGGE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767950641  276 FVVALGSPFSLQ-NTATAGIVSTKQRGGKElgmkDSDMDYVQIDATINYGNSGGPLVN 332
Cdd:pfam13365  81 RVYAVGYPLGGEkLSLSEGIVSGVDEGRDG----GDDGRVIQTDAALSPGSSGGPVFD 134
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
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950641 171 AAVVEKVAPSVVHVQlwGRLLHGSRLVpvySGSGFIVSeDGLIITNAHVVRNQQWIEVVLQNGARYEAVVKDIDLKLDLA 250
Cdd:NF033740 187 SPAVRRARPSVVKVR--GTAPSCGRAL---EGSGFVVA-PDRVMTNAHVVAGTDEVTVETVGGGTLDARVVYYDPDRDIA 260

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950641 251 VIKIESNAeLPVLMLGrSSDLRAGEFVVALGSPFSLQNTATAGIVSTKQ--RGGKELGMKDSDMDYVQIDATINYGNSGG 328
Cdd:NF033740 261 VLAVPGLG-LPPLPFA-DEPAETGDDAIVLGYPEGGPFTATPARVRERIalSGPDIYGSGTVTREVYTLRGTVRPGNSGG 338


                 ....
gi 767950641 329 PLVN 332
Cdd:NF033740 339 PLLD 342
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
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767950641   40 CPAVCQPTRCPALP-TCALGTTPvfDLCRCCRVCPAAEREVCGGAQGqPCAPGLQC 94
Cdd:pfam00219   1 CPPPCDPERCPPPPpGCPAGVVL--DGCGCCKVCARQEGEPCGVYTP-PCGKGLRC 53
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
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 767950641    40 CPaVCQPTRCPALP-TCALGTTPvfDLCRCCRVCPAAEREVCgGAQGQPCAPGLQC 94
Cdd:smart00121   3 CP-PCDPARCPPCPpGCAELVRL--DGCGCCPVCARQEGEPC-GVYTPRCAPGLRC 54
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
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 767950641  104 STCGCPTLGGA-VCGSDRRTYPSMCALRAENRAARRLGKVPAVpVQWGNC 152
Cdd:pfam07648   2 CNCQCPKTEYEpVCGSDGVTYPSPCALCAAGCKLGKEVKEEKV-KYDGSC 50
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
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 767950641 108 CPTLGGAVCGSDRRTYPSMCALRAENRAARRLGKVpavpVQWGNC 152
Cdd:cd00104    1 CPKEYDPVCGSDGKTYSNECHLGCAACRSGRSITV----AHNGPC 41
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
                           10        20
                   ....*....|....*....|....*..
gi 767950641   108 CPTLGGAVCGSDRRTYPSMCALRAENR 134
Cdd:smart00280   6 CPREYDPVCGSDGVTYSNECHLCKAAC 32
 
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
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950641 201 SGSGFIVSEDGLIITNAHVVRNQQWIEVVLQNGARYEAVVKDIDLKLDLAVIKIESnAELPVLMLGRSSDLRAGEFVVAL 280
Cdd:COG0265    2 LGSGVIISPDGYILTNNHVVEGADEITVTLADGREYPAKVVGRDPLTDLAVLKIDA-KDLPAAPLGDSDKLRVGDWVLAI 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 767950641 281 GSPFSLQNTATAGIVSTKQRGGkELGMKDSDMDYVQIDATINYGNSGGPLVNL 333
Cdd:COG0265   81 GNPFGLGQTVTAGIVSALGRSI-GSSGGGTYDDFIQTDAAINPGNSGGPLVNL 132
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
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950641  170 IAAVVEKVAPSVVHV--------------------QLWGRLL------HGSRLVPVYsGSGFIVSEDGLIITNAHVVRNQ 223
Cdd:TIGR02037   3 FAPLVEKVAPAVVNIsvegtvkrrnrppalppffrQFFGDDMpdfprqQREQKVRGL-GSGVIISADGYVLTNNHVVDGA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950641  224 QWIEVVLQNGARYEAVVKDIDLKLDLAVIKIESNAELPVLMLGRSSDLRAGEFVVALGSPFSLQNTATAGIVSTKQRGGk 303
Cdd:TIGR02037  82 DEITVTLSDGREFKAKLVGKDPRTDIAVLKIDAKKNLPVIKLGDSDKLRVGDWVLAIGNPFGLGQTVTSGIVSALGRSG- 160

                         170       180       190
                  ....*....|....*....|....*....|
gi 767950641  304 eLGMKDSDmDYVQIDATINYGNSGGPLVNL 333
Cdd:TIGR02037 161 -LGIGDYE-NFIQTDAAINPGNSGGPLVNL 188
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
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950641 174 VEKVAPSVVHV--QLWGRLLHGSRLVPVYsGSGFIVSEDGLIITNAHVVRNQQWIEVVLQNGARYEAVVKDIDLKLDLAV 251
Cdd:PRK10898  51 VRRAAPAVVNVynRSLNSTSHNQLEIRTL-GSGVIMDQRGYILTNKHVINDADQIIVALQDGRVFEALLVGSDSLTDLAV 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950641 252 IKIESnAELPVLMLGRSSDLRAGEFVVALGSPFSLQNTATAGIVSTKQRggkeLGMKDSD-MDYVQIDATINYGNSGGPL 330
Cdd:PRK10898 130 LKINA-TNLPVIPINPKRVPHIGDVVLAIGNPYNLGQTITQGIISATGR----IGLSPTGrQNFLQTDASINHGNSGGAL 204


                 ..
gi 767950641 331 VN 332
Cdd:PRK10898 205 VN 206
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
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950641  202 GSGFIVSEDGLIITNAHVVRNQQWIEV-----VLQNGARYEAVVKDIDLKLDLAVIKI-ESNAELPVLMLGRSSDLRAGE 275
Cdd:pfam13365   1 GTGFVVSSDGLVLTNAHVVDDAEEAAVelvsvVLADGREYPATVVARDPDLDLALLRVsGDGRGLPPLPLGDSEPLVGGE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767950641  276 FVVALGSPFSLQ-NTATAGIVSTKQRGGKElgmkDSDMDYVQIDATINYGNSGGPLVN 332
Cdd:pfam13365  81 RVYAVGYPLGGEkLSLSEGIVSGVDEGRDG----GDDGRVIQTDAALSPGSSGGPVFD 134
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
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950641 202 GSGFIV-SEDGLIITNAHVVRNQQWIEVVLQNGARYEAVVKDIDLKLDLAVIKIESNAELPVLMLGRSSDLRAGEFVVAL 280
Cdd:PRK10942 113 GSGVIIdADKGYVVTNNHVVDNATKIKVQLSDGRKFDAKVVGKDPRSDIALIQLQNPKNLTAIKMADSDALRVGDYTVAI 192

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 767950641 281 GSPFSLQNTATAGIVSTKQRGGkeLGMKDSDmDYVQIDATINYGNSGGPLVNL 333
Cdd:PRK10942 193 GNPYGLGETVTSGIVSALGRSG--LNVENYE-NFIQTDAAINRGNSGGALVNL 242
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
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950641 170 IAAVVEKVAPSVVHVQLWGRLLHGSRLVPVYS------------------GSGFIV-SEDGLIITNAHVVRNQQWIEVVL 230
Cdd:PRK10139  42 LAPMLEKVLPAVVSVRVEGTASQGQKIPEEFKkffgddlpdqpaqpfeglGSGVIIdAAKGYVLTNNHVINQAQKISIQL 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950641 231 QNGARYEAVVKDIDLKLDLAVIKIESNAELPVLMLGRSSDLRAGEFVVALGSPFSLQNTATAGIVSTKQRGGKEL-GMKd 309
Cdd:PRK10139 122 NDGREFDAKLIGSDDQSDIALLQIQNPSKLTQIAIADSDKLRVGDFAVAVGNPFGLGQTATSGIISALGRSGLNLeGLE- 200

                        170       180
                 ....*....|....*....|....
gi 767950641 310 sdmDYVQIDATINYGNSGGPLVNL 333
Cdd:PRK10139 201 ---NFIQTDASINRGNSGGALLNL 221
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
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950641 171 AAVVEKVAPSVVHVQlwGRLLHGSRLVpvySGSGFIVSeDGLIITNAHVVRNQQWIEVVLQNGARYEAVVKDIDLKLDLA 250
Cdd:NF033740 187 SPAVRRARPSVVKVR--GTAPSCGRAL---EGSGFVVA-PDRVMTNAHVVAGTDEVTVETVGGGTLDARVVYYDPDRDIA 260

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950641 251 VIKIESNAeLPVLMLGrSSDLRAGEFVVALGSPFSLQNTATAGIVSTKQ--RGGKELGMKDSDMDYVQIDATINYGNSGG 328
Cdd:NF033740 261 VLAVPGLG-LPPLPFA-DEPAETGDDAIVLGYPEGGPFTATPARVRERIalSGPDIYGSGTVTREVYTLRGTVRPGNSGG 338


                 ....
gi 767950641 329 PLVN 332
Cdd:NF033740 339 PLLD 342
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
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767950641   40 CPAVCQPTRCPALP-TCALGTTPvfDLCRCCRVCPAAEREVCGGAQGqPCAPGLQC 94
Cdd:pfam00219   1 CPPPCDPERCPPPPpGCPAGVVL--DGCGCCKVCARQEGEPCGVYTP-PCGKGLRC 53
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
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950641  204 GFIVSEDGlIITNAHVVRNQQWIEVVL--QNGARYEAVVKDIDLK--------------LDLAVIKIESNAELPVLM--- 264
Cdd:pfam00089  29 GSLISENW-VLTAAHCVSGASDVKVVLgaHNIVLREGGEQKFDVEkiivhpnynpdtldNDIALLKLESPVTLGDTVrpi 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950641  265 -LGRSSDL---RAGEFVVA------LGSPFSLQnTATAGIVSTKQRGGKELGMKDSDMdyVQIDAT---INYGNSGGPLV 331
Cdd:pfam00089 108 cLPDASSDlpvGTTCTVSGwgntktLGPSDTLQ-EVTVPVVSRETCRSAYGGTVTDTM--ICAGAGgkdACQGDSGGPLV 184


                  ..
gi 767950641  332 NL 333
Cdd:pfam00089 185 CS 186
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
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 767950641    40 CPaVCQPTRCPALP-TCALGTTPvfDLCRCCRVCPAAEREVCgGAQGQPCAPGLQC 94
Cdd:smart00121   3 CP-PCDPARCPPCPpGCAELVRL--DGCGCCPVCARQEGEPC-GVYTPRCAPGLRC 54
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
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 767950641  104 STCGCPTLGGA-VCGSDRRTYPSMCALRAENRAARRLGKVPAVpVQWGNC 152
Cdd:pfam07648   2 CNCQCPKTEYEpVCGSDGVTYPSPCALCAAGCKLGKEVKEEKV-KYDGSC 50
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
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950641 200 YSGSGFIVSEDgLIITNAHVVRNQ------QWIEVVL-QNGARYEAV-----------VKDIDLKLDLAVIKIESNAELP 261
Cdd:COG3591   12 GVCTGTLIGPN-LVLTAGHCVYDGagggwaTNIVFVPgYNGGPYGTAtatrfrvppgwVASGDAGYDYALLRLDEPLGDT 90

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767950641 262 V--LMLGRSSDLRAGEFVVALGSPFSLQNTATAgivstkQRGGKELGMKDSDMDYvQIDATinYGNSGGPLVN 332
Cdd:COG3591   91 TgwLGLAFNDAPLAGEPVTIIGYPGDRPKDLSL------DCSGRVTGVQGNRLSY-DCDTT--GGSSGSPVLD 154
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
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 767950641 108 CPTLGGAVCGSDRRTYPSMCALRAENRAARRLGKVpavpVQWGNC 152
Cdd:cd00104    1 CPKEYDPVCGSDGKTYSNECHLGCAACRSGRSITV----AHNGPC 41
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
                           10        20
                   ....*....|....*....|....*..
gi 767950641   108 CPTLGGAVCGSDRRTYPSMCALRAENR 134
Cdd:smart00280   6 CPREYDPVCGSDGVTYSNECHLCKAAC 32
 
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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