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Conserved domains on  [gi|442630141|ref|NP_001261408|]
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masquerade, isoform C [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 802-1040 8.65e-87

Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.


:

Pssm-ID: 238113 [Multi-domain]  Cd Length: 232  Bit Score: 278.78  E-value: 8.65e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630141  802 VVGGEDGENGEWCWQVALINSLNQYLCGAALIGTQWVLTAAHCVTNIVRSgdAIYVRVGDYDLTRkyGSPGAQTLRVATT 881
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVYSSAPS--NYTVRLGSHDLSS--NEGGGQVIKVKKV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630141  882 YIHHNHNSQTLDNDIALLKLHGQAELRDGVCLVCLPARGVSHAAGKRCTVTGYGYMGEAGPIPLRVREAEIPIVSDTECI 961
Cdd:cd00190    77 IVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECK 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630141  962 RKvnavTEKIFILPASSFCAGGEE-GHDACQGDGGGPLVCQDDGFYELAGLVSWGFGCGRQDVPGVYVKTSSFIGWINQI 1040
Cdd:cd00190   157 RA----YSYGGTITDNMLCAGGLEgGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
CLIP_SPH_mas pfam18398
Clip-domain serine protease homolog masquerade; The clip domain is a structural/regulatory ...
 456-491 3.49e-08

Clip-domain serine protease homolog masquerade; The clip domain is a structural/regulatory unit in many arthropod serine proteases. The clip domain super-family also includes serine protease homologs (SPHs). This entry describes clip domains in the SPHs (CLIP subfamily A), which belong to group-3. SPHs usually carry between 1 to 5 clip domains. One of the most prominent family members is masquerade (mas). Deletion in drosophila models lead to defects in somatic muscle attachment and in the formation of the nervous system during embryogenesis.


:

Pssm-ID: 465746  Cd Length: 32  Bit Score: 49.92  E-value: 3.49e-08
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 442630141   456 RCPGFCLLNIMAAFCERPSVlvstPTTCAKGSVCCD 491
Cdd:pfam18398    1 RCPGVCVHTLLALFCDRVLE----DASCPSGGKCCV 32
CLIP_SPH_mas pfam18398
Clip-domain serine protease homolog masquerade; The clip domain is a structural/regulatory ...
 342-373 3.67e-08

Clip-domain serine protease homolog masquerade; The clip domain is a structural/regulatory unit in many arthropod serine proteases. The clip domain super-family also includes serine protease homologs (SPHs). This entry describes clip domains in the SPHs (CLIP subfamily A), which belong to group-3. SPHs usually carry between 1 to 5 clip domains. One of the most prominent family members is masquerade (mas). Deletion in drosophila models lead to defects in somatic muscle attachment and in the formation of the nervous system during embryogenesis.


:

Pssm-ID: 465746  Cd Length: 32  Bit Score: 49.92  E-value: 3.67e-08
                           10        20        30
                   ....*....|....*....|....*....|..
gi 442630141   342 ECEGECMNGIFAIFCDDIDSDAFCPGEESCCV 373
Cdd:pfam18398    1 RCPGVCVHTLLALFCDRVLEDASCPSGGKCCV 32
CLIP_SPH_mas pfam18398
Clip-domain serine protease homolog masquerade; The clip domain is a structural/regulatory ...
 55-87 4.55e-08

Clip-domain serine protease homolog masquerade; The clip domain is a structural/regulatory unit in many arthropod serine proteases. The clip domain super-family also includes serine protease homologs (SPHs). This entry describes clip domains in the SPHs (CLIP subfamily A), which belong to group-3. SPHs usually carry between 1 to 5 clip domains. One of the most prominent family members is masquerade (mas). Deletion in drosophila models lead to defects in somatic muscle attachment and in the formation of the nervous system during embryogenesis.


:

Pssm-ID: 465746  Cd Length: 32  Bit Score: 49.92  E-value: 4.55e-08
                           10        20        30
                   ....*....|....*....|....*....|...
gi 442630141    55 DCPGVCVHTLATLICYEVLDDVACPSpSMKCCI 87
Cdd:pfam18398    1 RCPGVCVHTLLALFCDRVLEDASCPS-GGKCCV 32
CLIP_SPH_mas pfam18398
Clip-domain serine protease homolog masquerade; The clip domain is a structural/regulatory ...
 191-223 5.59e-06

Clip-domain serine protease homolog masquerade; The clip domain is a structural/regulatory unit in many arthropod serine proteases. The clip domain super-family also includes serine protease homologs (SPHs). This entry describes clip domains in the SPHs (CLIP subfamily A), which belong to group-3. SPHs usually carry between 1 to 5 clip domains. One of the most prominent family members is masquerade (mas). Deletion in drosophila models lead to defects in somatic muscle attachment and in the formation of the nervous system during embryogenesis.


:

Pssm-ID: 465746  Cd Length: 32  Bit Score: 43.76  E-value: 5.59e-06
                           10        20        30
                   ....*....|....*....|....*....|...
gi 442630141   191 NCTGVCVADRIAEYCEAYLtSDGLCKEGTKCCV 223
Cdd:pfam18398    1 RCPGVCVHTLLALFCDRVL-EDASCPSGGKCCV 32
CLIP_SPH_mas pfam18398
Clip-domain serine protease homolog masquerade; The clip domain is a structural/regulatory ...
 531-566 8.85e-03

Clip-domain serine protease homolog masquerade; The clip domain is a structural/regulatory unit in many arthropod serine proteases. The clip domain super-family also includes serine protease homologs (SPHs). This entry describes clip domains in the SPHs (CLIP subfamily A), which belong to group-3. SPHs usually carry between 1 to 5 clip domains. One of the most prominent family members is masquerade (mas). Deletion in drosophila models lead to defects in somatic muscle attachment and in the formation of the nervous system during embryogenesis.


:

Pssm-ID: 465746  Cd Length: 32  Bit Score: 34.90  E-value: 8.85e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 442630141   531 ECPGSCIVSLLSFTCFKNAEMTDlfrCKRSGqICCA 566
Cdd:pfam18398    1 RCPGVCVHTLLALFCDRVLEDAS---CPSGG-KCCV 32
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 802-1040 8.65e-87

Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.


Pssm-ID: 238113 [Multi-domain]  Cd Length: 232  Bit Score: 278.78  E-value: 8.65e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630141  802 VVGGEDGENGEWCWQVALINSLNQYLCGAALIGTQWVLTAAHCVTNIVRSgdAIYVRVGDYDLTRkyGSPGAQTLRVATT 881
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVYSSAPS--NYTVRLGSHDLSS--NEGGGQVIKVKKV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630141  882 YIHHNHNSQTLDNDIALLKLHGQAELRDGVCLVCLPARGVSHAAGKRCTVTGYGYMGEAGPIPLRVREAEIPIVSDTECI 961
Cdd:cd00190    77 IVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECK 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630141  962 RKvnavTEKIFILPASSFCAGGEE-GHDACQGDGGGPLVCQDDGFYELAGLVSWGFGCGRQDVPGVYVKTSSFIGWINQI 1040
Cdd:cd00190   157 RA----YSYGGTITDNMLCAGGLEgGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 801-1037 8.26e-81

Trypsin-like serine protease; 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.


Pssm-ID: 214473  Cd Length: 229  Bit Score: 262.61  E-value: 8.26e-81
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630141    801 RVVGGEDGENGEWCWQVALINSLNQYLCGAALIGTQWVLTAAHCVTNIVRSgdAIYVRVGDYDLTRkygSPGAQTLRVAT 880
Cdd:smart00020    1 RIVGGSEANIGSFPWQVSLQYGGGRHFCGGSLISPRWVLTAAHCVRGSDPS--NIRVRLGSHDLSS---GEEGQVIKVSK 75

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630141    881 TYIHHNHNSQTLDNDIALLKLHGQAELRDGVCLVCLPARGVSHAAGKRCTVTGYGYMGE-AGPIPLRVREAEIPIVSDTE 959
Cdd:smart00020   76 VIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEgAGSLPDTLQEVNVPIVSNAT 155

                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442630141    960 CIRKVnavtEKIFILPASSFCAGGEE-GHDACQGDGGGPLVCQDDGFYeLAGLVSWGFGCGRQDVPGVYVKTSSFIGWI 1037
Cdd:smart00020  156 CRRAY----SGGGAITDNMLCAGGLEgGKDACQGDSGGPLVCNDGRWV-LVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 800-1044 7.24e-59

Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 202.96  E-value: 7.24e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630141  800 ARVVGGEDGENGEWCWQVALI--NSLNQYLCGAALIGTQWVLTAAHCVTNivRSGDAIYVRVGDYDLTrkygSPGAQTLR 877
Cdd:COG5640    29 PAIVGGTPATVGEYPWMVALQssNGPSGQFCGGTLIAPRWVLTAAHCVDG--DGPSDLRVVIGSTDLS----TSGGTVVK 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630141  878 VATTYIHHNHNSQTLDNDIALLKLhgqAELRDGVCLVCLPARGVSHAAGKRCTVTGYGYMGE-AGPIPLRVREAEIPIVS 956
Cdd:COG5640   103 VARIVVHPDYDPATPGNDIALLKL---ATPVPGVAPAPLATSADAAAPGTPATVAGWGRTSEgPGSQSGTLRKADVPVVS 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630141  957 DTECIRKVNavtekifILPASSFCAGGEEG-HDACQGDGGGPLVCQDDGFYELAGLVSWGFGCGRQDVPGVYVKTSSFIG 1035
Cdd:COG5640   180 DATCAAYGG-------FDGGTMLCAGYPEGgKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRD 252


                  ....*....
gi 442630141 1036 WINQIISVN 1044
Cdd:COG5640   253 WIKSTAGGL 261
Trypsin pfam00089
Trypsin;
802-1037 1.32e-58

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 200.75  E-value: 1.32e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630141   802 VVGGEDGENGEWCWQVALINSLNQYLCGAALIGTQWVLTAAHCVTNivrsGDAIYVRVGDYDLTRKYGspGAQTLRVATT 881
Cdd:pfam00089    1 IVGGDEAQPGSFPWQVSLQLSSGKHFCGGSLISENWVLTAAHCVSG----ASDVKVVLGAHNIVLREG--GEQKFDVEKI 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630141   882 YIHHNHNSQTLDNDIALLKLHGQAELRDGVCLVCLPARGVSHAAGKRCTVTGYGYMGEAGPiPLRVREAEIPIVSDTECI 961
Cdd:pfam00089   75 IVHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSRETCR 153

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442630141   962 RKVNAVTEKIFIlpassfCAGGeEGHDACQGDGGGPLVCqDDGfyELAGLVSWGFGCGRQDVPGVYVKTSSFIGWI 1037
Cdd:pfam00089  154 SAYGGTVTDTMI------CAGA-GGKDACQGDSGGPLVC-SDG--ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
CLIP_SPH_mas pfam18398
Clip-domain serine protease homolog masquerade; The clip domain is a structural/regulatory ...
 456-491 3.49e-08

Clip-domain serine protease homolog masquerade; The clip domain is a structural/regulatory unit in many arthropod serine proteases. The clip domain super-family also includes serine protease homologs (SPHs). This entry describes clip domains in the SPHs (CLIP subfamily A), which belong to group-3. SPHs usually carry between 1 to 5 clip domains. One of the most prominent family members is masquerade (mas). Deletion in drosophila models lead to defects in somatic muscle attachment and in the formation of the nervous system during embryogenesis.


Pssm-ID: 465746  Cd Length: 32  Bit Score: 49.92  E-value: 3.49e-08
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 442630141   456 RCPGFCLLNIMAAFCERPSVlvstPTTCAKGSVCCD 491
Cdd:pfam18398    1 RCPGVCVHTLLALFCDRVLE----DASCPSGGKCCV 32
CLIP_SPH_mas pfam18398
Clip-domain serine protease homolog masquerade; The clip domain is a structural/regulatory ...
 342-373 3.67e-08

Clip-domain serine protease homolog masquerade; The clip domain is a structural/regulatory unit in many arthropod serine proteases. The clip domain super-family also includes serine protease homologs (SPHs). This entry describes clip domains in the SPHs (CLIP subfamily A), which belong to group-3. SPHs usually carry between 1 to 5 clip domains. One of the most prominent family members is masquerade (mas). Deletion in drosophila models lead to defects in somatic muscle attachment and in the formation of the nervous system during embryogenesis.


Pssm-ID: 465746  Cd Length: 32  Bit Score: 49.92  E-value: 3.67e-08
                           10        20        30
                   ....*....|....*....|....*....|..
gi 442630141   342 ECEGECMNGIFAIFCDDIDSDAFCPGEESCCV 373
Cdd:pfam18398    1 RCPGVCVHTLLALFCDRVLEDASCPSGGKCCV 32
CLIP_SPH_mas pfam18398
Clip-domain serine protease homolog masquerade; The clip domain is a structural/regulatory ...
 55-87 4.55e-08

Clip-domain serine protease homolog masquerade; The clip domain is a structural/regulatory unit in many arthropod serine proteases. The clip domain super-family also includes serine protease homologs (SPHs). This entry describes clip domains in the SPHs (CLIP subfamily A), which belong to group-3. SPHs usually carry between 1 to 5 clip domains. One of the most prominent family members is masquerade (mas). Deletion in drosophila models lead to defects in somatic muscle attachment and in the formation of the nervous system during embryogenesis.


Pssm-ID: 465746  Cd Length: 32  Bit Score: 49.92  E-value: 4.55e-08
                           10        20        30
                   ....*....|....*....|....*....|...
gi 442630141    55 DCPGVCVHTLATLICYEVLDDVACPSpSMKCCI 87
Cdd:pfam18398    1 RCPGVCVHTLLALFCDRVLEDASCPS-GGKCCV 32
CLIP_SPH_mas pfam18398
Clip-domain serine protease homolog masquerade; The clip domain is a structural/regulatory ...
 191-223 5.59e-06

Clip-domain serine protease homolog masquerade; The clip domain is a structural/regulatory unit in many arthropod serine proteases. The clip domain super-family also includes serine protease homologs (SPHs). This entry describes clip domains in the SPHs (CLIP subfamily A), which belong to group-3. SPHs usually carry between 1 to 5 clip domains. One of the most prominent family members is masquerade (mas). Deletion in drosophila models lead to defects in somatic muscle attachment and in the formation of the nervous system during embryogenesis.


Pssm-ID: 465746  Cd Length: 32  Bit Score: 43.76  E-value: 5.59e-06
                           10        20        30
                   ....*....|....*....|....*....|...
gi 442630141   191 NCTGVCVADRIAEYCEAYLtSDGLCKEGTKCCV 223
Cdd:pfam18398    1 RCPGVCVHTLLALFCDRVL-EDASCPSGGKCCV 32
CLIP_SPH_mas pfam18398
Clip-domain serine protease homolog masquerade; The clip domain is a structural/regulatory ...
 531-566 8.85e-03

Clip-domain serine protease homolog masquerade; The clip domain is a structural/regulatory unit in many arthropod serine proteases. The clip domain super-family also includes serine protease homologs (SPHs). This entry describes clip domains in the SPHs (CLIP subfamily A), which belong to group-3. SPHs usually carry between 1 to 5 clip domains. One of the most prominent family members is masquerade (mas). Deletion in drosophila models lead to defects in somatic muscle attachment and in the formation of the nervous system during embryogenesis.


Pssm-ID: 465746  Cd Length: 32  Bit Score: 34.90  E-value: 8.85e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 442630141   531 ECPGSCIVSLLSFTCFKNAEMTDlfrCKRSGqICCA 566
Cdd:pfam18398    1 RCPGVCVHTLLALFCDRVLEDAS---CPSGG-KCCV 32
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 802-1040 8.65e-87

Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.


Pssm-ID: 238113 [Multi-domain]  Cd Length: 232  Bit Score: 278.78  E-value: 8.65e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630141  802 VVGGEDGENGEWCWQVALINSLNQYLCGAALIGTQWVLTAAHCVTNIVRSgdAIYVRVGDYDLTRkyGSPGAQTLRVATT 881
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVYSSAPS--NYTVRLGSHDLSS--NEGGGQVIKVKKV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630141  882 YIHHNHNSQTLDNDIALLKLHGQAELRDGVCLVCLPARGVSHAAGKRCTVTGYGYMGEAGPIPLRVREAEIPIVSDTECI 961
Cdd:cd00190    77 IVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECK 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630141  962 RKvnavTEKIFILPASSFCAGGEE-GHDACQGDGGGPLVCQDDGFYELAGLVSWGFGCGRQDVPGVYVKTSSFIGWINQI 1040
Cdd:cd00190   157 RA----YSYGGTITDNMLCAGGLEgGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 801-1037 8.26e-81

Trypsin-like serine protease; 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.


Pssm-ID: 214473  Cd Length: 229  Bit Score: 262.61  E-value: 8.26e-81
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630141    801 RVVGGEDGENGEWCWQVALINSLNQYLCGAALIGTQWVLTAAHCVTNIVRSgdAIYVRVGDYDLTRkygSPGAQTLRVAT 880
Cdd:smart00020    1 RIVGGSEANIGSFPWQVSLQYGGGRHFCGGSLISPRWVLTAAHCVRGSDPS--NIRVRLGSHDLSS---GEEGQVIKVSK 75

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630141    881 TYIHHNHNSQTLDNDIALLKLHGQAELRDGVCLVCLPARGVSHAAGKRCTVTGYGYMGE-AGPIPLRVREAEIPIVSDTE 959
Cdd:smart00020   76 VIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEgAGSLPDTLQEVNVPIVSNAT 155

                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442630141    960 CIRKVnavtEKIFILPASSFCAGGEE-GHDACQGDGGGPLVCQDDGFYeLAGLVSWGFGCGRQDVPGVYVKTSSFIGWI 1037
Cdd:smart00020  156 CRRAY----SGGGAITDNMLCAGGLEgGKDACQGDSGGPLVCNDGRWV-LVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 800-1044 7.24e-59

Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 202.96  E-value: 7.24e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630141  800 ARVVGGEDGENGEWCWQVALI--NSLNQYLCGAALIGTQWVLTAAHCVTNivRSGDAIYVRVGDYDLTrkygSPGAQTLR 877
Cdd:COG5640    29 PAIVGGTPATVGEYPWMVALQssNGPSGQFCGGTLIAPRWVLTAAHCVDG--DGPSDLRVVIGSTDLS----TSGGTVVK 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630141  878 VATTYIHHNHNSQTLDNDIALLKLhgqAELRDGVCLVCLPARGVSHAAGKRCTVTGYGYMGE-AGPIPLRVREAEIPIVS 956
Cdd:COG5640   103 VARIVVHPDYDPATPGNDIALLKL---ATPVPGVAPAPLATSADAAAPGTPATVAGWGRTSEgPGSQSGTLRKADVPVVS 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630141  957 DTECIRKVNavtekifILPASSFCAGGEEG-HDACQGDGGGPLVCQDDGFYELAGLVSWGFGCGRQDVPGVYVKTSSFIG 1035
Cdd:COG5640   180 DATCAAYGG-------FDGGTMLCAGYPEGgKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRD 252


                  ....*....
gi 442630141 1036 WINQIISVN 1044
Cdd:COG5640   253 WIKSTAGGL 261
Trypsin pfam00089
Trypsin;
802-1037 1.32e-58

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 200.75  E-value: 1.32e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630141   802 VVGGEDGENGEWCWQVALINSLNQYLCGAALIGTQWVLTAAHCVTNivrsGDAIYVRVGDYDLTRKYGspGAQTLRVATT 881
Cdd:pfam00089    1 IVGGDEAQPGSFPWQVSLQLSSGKHFCGGSLISENWVLTAAHCVSG----ASDVKVVLGAHNIVLREG--GEQKFDVEKI 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630141   882 YIHHNHNSQTLDNDIALLKLHGQAELRDGVCLVCLPARGVSHAAGKRCTVTGYGYMGEAGPiPLRVREAEIPIVSDTECI 961
Cdd:pfam00089   75 IVHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSRETCR 153

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442630141   962 RKVNAVTEKIFIlpassfCAGGeEGHDACQGDGGGPLVCqDDGfyELAGLVSWGFGCGRQDVPGVYVKTSSFIGWI 1037
Cdd:pfam00089  154 SAYGGTVTDTMI------CAGA-GGKDACQGDSGGPLVC-SDG--ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
 817-1042 4.32e-12

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 66.24  E-value: 4.32e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630141  817 VALINSLNQ-YLCGAALIGTQWVLTAAHCVTNIVRSGDAIYVRVG-DYDLTRkYGSPGAQTLRVATTYIhhnhNSQTLDN 894
Cdd:COG3591     2 VGRLETDGGgGVCTGTLIGPNLVLTAGHCVYDGAGGGWATNIVFVpGYNGGP-YGTATATRFRVPPGWV----ASGDAGY 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630141  895 DIALLKLHGQAELRDGVCLVclpARGVSHAAGKRCTVTGYGymgeagpiplrvreAEIPIVSDTECIRKVNAVTEKIFIL 974
Cdd:COG3591    77 DYALLRLDEPLGDTTGWLGL---AFNDAPLAGEPVTIIGYP--------------GDRPKDLSLDCSGRVTGVQGNRLSY 139

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442630141  975 PAssfcaggeeghDACQGDGGGPLVCQDDGFYELAGLVSWGFGCGRQDvpGVYVkTSSFIGWINQIIS 1042
Cdd:COG3591   140 DC-----------DTTGGSSGSPVLDDSDGGGRVVGVHSAGGADRANT--GVRL-TSAIVAALRAWAS 193
CLIP_SPH_mas pfam18398
Clip-domain serine protease homolog masquerade; The clip domain is a structural/regulatory ...
 456-491 3.49e-08

Clip-domain serine protease homolog masquerade; The clip domain is a structural/regulatory unit in many arthropod serine proteases. The clip domain super-family also includes serine protease homologs (SPHs). This entry describes clip domains in the SPHs (CLIP subfamily A), which belong to group-3. SPHs usually carry between 1 to 5 clip domains. One of the most prominent family members is masquerade (mas). Deletion in drosophila models lead to defects in somatic muscle attachment and in the formation of the nervous system during embryogenesis.


Pssm-ID: 465746  Cd Length: 32  Bit Score: 49.92  E-value: 3.49e-08
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 442630141   456 RCPGFCLLNIMAAFCERPSVlvstPTTCAKGSVCCD 491
Cdd:pfam18398    1 RCPGVCVHTLLALFCDRVLE----DASCPSGGKCCV 32
CLIP_SPH_mas pfam18398
Clip-domain serine protease homolog masquerade; The clip domain is a structural/regulatory ...
 342-373 3.67e-08

Clip-domain serine protease homolog masquerade; The clip domain is a structural/regulatory unit in many arthropod serine proteases. The clip domain super-family also includes serine protease homologs (SPHs). This entry describes clip domains in the SPHs (CLIP subfamily A), which belong to group-3. SPHs usually carry between 1 to 5 clip domains. One of the most prominent family members is masquerade (mas). Deletion in drosophila models lead to defects in somatic muscle attachment and in the formation of the nervous system during embryogenesis.


Pssm-ID: 465746  Cd Length: 32  Bit Score: 49.92  E-value: 3.67e-08
                           10        20        30
                   ....*....|....*....|....*....|..
gi 442630141   342 ECEGECMNGIFAIFCDDIDSDAFCPGEESCCV 373
Cdd:pfam18398    1 RCPGVCVHTLLALFCDRVLEDASCPSGGKCCV 32
CLIP_SPH_mas pfam18398
Clip-domain serine protease homolog masquerade; The clip domain is a structural/regulatory ...
 55-87 4.55e-08

Clip-domain serine protease homolog masquerade; The clip domain is a structural/regulatory unit in many arthropod serine proteases. The clip domain super-family also includes serine protease homologs (SPHs). This entry describes clip domains in the SPHs (CLIP subfamily A), which belong to group-3. SPHs usually carry between 1 to 5 clip domains. One of the most prominent family members is masquerade (mas). Deletion in drosophila models lead to defects in somatic muscle attachment and in the formation of the nervous system during embryogenesis.


Pssm-ID: 465746  Cd Length: 32  Bit Score: 49.92  E-value: 4.55e-08
                           10        20        30
                   ....*....|....*....|....*....|...
gi 442630141    55 DCPGVCVHTLATLICYEVLDDVACPSpSMKCCI 87
Cdd:pfam18398    1 RCPGVCVHTLLALFCDRVLEDASCPS-GGKCCV 32
CLIP_SPH_mas pfam18398
Clip-domain serine protease homolog masquerade; The clip domain is a structural/regulatory ...
 191-223 5.59e-06

Clip-domain serine protease homolog masquerade; The clip domain is a structural/regulatory unit in many arthropod serine proteases. The clip domain super-family also includes serine protease homologs (SPHs). This entry describes clip domains in the SPHs (CLIP subfamily A), which belong to group-3. SPHs usually carry between 1 to 5 clip domains. One of the most prominent family members is masquerade (mas). Deletion in drosophila models lead to defects in somatic muscle attachment and in the formation of the nervous system during embryogenesis.


Pssm-ID: 465746  Cd Length: 32  Bit Score: 43.76  E-value: 5.59e-06
                           10        20        30
                   ....*....|....*....|....*....|...
gi 442630141   191 NCTGVCVADRIAEYCEAYLtSDGLCKEGTKCCV 223
Cdd:pfam18398    1 RCPGVCVHTLLALFCDRVL-EDASCPSGGKCCV 32
CLIP_SPH_mas pfam18398
Clip-domain serine protease homolog masquerade; The clip domain is a structural/regulatory ...
 531-566 8.85e-03

Clip-domain serine protease homolog masquerade; The clip domain is a structural/regulatory unit in many arthropod serine proteases. The clip domain super-family also includes serine protease homologs (SPHs). This entry describes clip domains in the SPHs (CLIP subfamily A), which belong to group-3. SPHs usually carry between 1 to 5 clip domains. One of the most prominent family members is masquerade (mas). Deletion in drosophila models lead to defects in somatic muscle attachment and in the formation of the nervous system during embryogenesis.


Pssm-ID: 465746  Cd Length: 32  Bit Score: 34.90  E-value: 8.85e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 442630141   531 ECPGSCIVSLLSFTCFKNAEMTDlfrCKRSGqICCA 566
Cdd:pfam18398    1 RCPGVCVHTLLALFCDRVLEDAS---CPSGG-KCCV 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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