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Conserved domains on  [gi|289547636|ref|NP_057630|]
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complement C1r subcomponent-like protein isoform 1 precursor [Homo sapiens]

Protein Classification

CUB and Tryp_SPc domain-containing protein( domain architecture ID 10035942)

CUB and Tryp_SPc domain-containing protein

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 ...
247-480 8.34e-62

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: 201.35  E-value: 8.34e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547636 247 GSSRAKLGNFPWQAFTSIHGRG---GGALLGDRWILTAAHTIYPKDSVSLRknqsvnVFLGHTAIDEMLKLG-NHPVHRV 322
Cdd:cd00190    3 GGSEAKIGSFPWQVSLQYTGGRhfcGGSLISPRWVLTAAHCVYSSAPSNYT------VRLGSHDLSSNEGGGqVIKVKKV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547636 323 VVHPDYRQNESHNfsgDIALLELQHSIPLGPNVLPVCLPDNETLYRSGLLGYVSGFG--MEMGWLTTELKYSRLPVAPRE 400
Cdd:cd00190   77 IVHPNYNPSTYDN---DIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGrtSEGGPLPDVLQEVNVPIVSNA 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547636 401 ACNawlQKRQRPEVFSDNMFCVGDETQRHSVCQGDSGSVYVVWDNhaHHWVATGIVSWGIGCGEG--YDFYTKVLSYVDW 478
Cdd:cd00190  154 ECK---RAYSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDN--GRGVLVGIVSWGSGCARPnyPGVYTRVSSYLDW 228

                 ..
gi 289547636 479 IK 480
Cdd:cd00190  229 IQ 230
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
40-162 2.99e-20

CUB domain; extracellular domain; present in proteins mostly known to be involved in development; not found in prokaryotes, plants and yeast.


:

Pssm-ID: 238001 [Multi-domain]  Cd Length: 113  Bit Score: 85.93  E-value: 2.99e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547636  40 GSVLLAQElPQQLTSPGYPEPYGKGQESSTDIKAPEGFAVRLVFQDFDLEPSQDCAGDSVTIsFVGSDPS-----QFCGQ 114
Cdd:cd00041    2 GGTLTAST-SGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESSPNCSYDYLEI-YDGPSTSspllgRFCGS 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 289547636 115 QGSPlgrppgqrEFVSSGRSLRLTFRTQPSSEnktahlHKGFLALYQT 162
Cdd:cd00041   80 TLPP--------PIISSGNSLTVRFRSDSSVT------GRGFKATYSA 113
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
247-480 8.34e-62

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: 201.35  E-value: 8.34e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547636 247 GSSRAKLGNFPWQAFTSIHGRG---GGALLGDRWILTAAHTIYPKDSVSLRknqsvnVFLGHTAIDEMLKLG-NHPVHRV 322
Cdd:cd00190    3 GGSEAKIGSFPWQVSLQYTGGRhfcGGSLISPRWVLTAAHCVYSSAPSNYT------VRLGSHDLSSNEGGGqVIKVKKV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547636 323 VVHPDYRQNESHNfsgDIALLELQHSIPLGPNVLPVCLPDNETLYRSGLLGYVSGFG--MEMGWLTTELKYSRLPVAPRE 400
Cdd:cd00190   77 IVHPNYNPSTYDN---DIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGrtSEGGPLPDVLQEVNVPIVSNA 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547636 401 ACNawlQKRQRPEVFSDNMFCVGDETQRHSVCQGDSGSVYVVWDNhaHHWVATGIVSWGIGCGEG--YDFYTKVLSYVDW 478
Cdd:cd00190  154 ECK---RAYSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDN--GRGVLVGIVSWGSGCARPnyPGVYTRVSSYLDW 228

                 ..
gi 289547636 479 IK 480
Cdd:cd00190  229 IQ 230
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
247-479 2.63e-60

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: 197.52  E-value: 2.63e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547636   247 GSSRAKLGNFPWQAFTSIHGRG---GGALLGDRWILTAAHTIYPKDsvslrkNQSVNVFLGHTAIDEMLKLGNHPVHRVV 323
Cdd:smart00020   4 GGSEANIGSFPWQVSLQYGGGRhfcGGSLISPRWVLTAAHCVRGSD------PSNIRVRLGSHDLSSGEEGQVIKVSKVI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547636   324 VHPDYRQNESHNfsgDIALLELQHSIPLGPNVLPVCLPDNETLYRSGLLGYVSGFG---MEMGWLTTELKYSRLPVAPRE 400
Cdd:smart00020  78 IHPNYNPSTYDN---DIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGrtsEGAGSLPDTLQEVNVPIVSNA 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547636   401 ACNawlQKRQRPEVFSDNMFCVGDETQRHSVCQGDSGSVYVVWDNhahHWVATGIVSWGIGCGEG--YDFYTKVLSYVDW 478
Cdd:smart00020 155 TCR---RAYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCNDG---RWVLVGIVSWGSGCARPgkPGVYTRVSSYLDW 228

                   .
gi 289547636   479 I 479
Cdd:smart00020 229 I 229
Trypsin pfam00089
Trypsin;
247-479 6.16e-42

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 148.74  E-value: 6.16e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547636  247 GSSRAKLGNFPWQAFTSIHGRG---GGALLGDRWILTAAHTIYPKDSVslrknqsvNVFLGHTAIDEMLKLGNH-PVHRV 322
Cdd:pfam00089   3 GGDEAQPGSFPWQVSLQLSSGKhfcGGSLISENWVLTAAHCVSGASDV--------KVVLGAHNIVLREGGEQKfDVEKI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547636  323 VVHPDYRQNESHNfsgDIALLELQHSIPLGPNVLPVCLPDNETLYRSGLLGYVSGFG-MEMGWLTTELKYSRLPVAPREA 401
Cdd:pfam00089  75 IVHPNYNPDTLDN---DIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGnTKTLGPSDTLQEVTVPVVSRET 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547636  402 CNawlqkRQRPEVFSDNMFCVGdeTQRHSVCQGDSGSVYVVWDNHAHhwvatGIVSWGIGCGEG--YDFYTKVLSYVDWI 479
Cdd:pfam00089 152 CR-----SAYGGTVTDTMICAG--AGGKDACQGDSGGPLVCSDGELI-----GIVSWGYGCASGnyPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
247-485 4.18e-39

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 142.48  E-value: 4.18e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547636 247 GSSRAKLGNFPWQAftSIHGRGG-------GALLGDRWILTAAHTIYPKDSVSLRknqsvnVFLGHTAIDEmlKLGN-HP 318
Cdd:COG5640   33 GGTPATVGEYPWMV--ALQSSNGpsgqfcgGTLIAPRWVLTAAHCVDGDGPSDLR------VVIGSTDLST--SGGTvVK 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547636 319 VHRVVVHPDYRqneSHNFSGDIALLELQHSIPLGPnvlPVCLPDNETLYRSGLLGYVSGFGM---EMGWLTTELKYSRLP 395
Cdd:COG5640  103 VARIVVHPDYD---PATPGNDIALLKLATPVPGVA---PAPLATSADAAAPGTPATVAGWGRtseGPGSQSGTLRKADVP 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547636 396 VAPREACNAWlqkrqrPEVFSDNMFCVGDETQRHSVCQGDSGSVYVVWDNHAhhWVATGIVSWGIG-CGEG-YDFYTKVL 473
Cdd:COG5640  177 VVSDATCAAY------GGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGG--WVLVGVVSWGGGpCAAGyPGVYTRVS 248
                        250
                 ....*....|..
gi 289547636 474 SYVDWIKGVMNG 485
Cdd:COG5640  249 AYRDWIKSTAGG 260
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
40-162 2.99e-20

CUB domain; extracellular domain; present in proteins mostly known to be involved in development; not found in prokaryotes, plants and yeast.


Pssm-ID: 238001 [Multi-domain]  Cd Length: 113  Bit Score: 85.93  E-value: 2.99e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547636  40 GSVLLAQElPQQLTSPGYPEPYGKGQESSTDIKAPEGFAVRLVFQDFDLEPSQDCAGDSVTIsFVGSDPS-----QFCGQ 114
Cdd:cd00041    2 GGTLTAST-SGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESSPNCSYDYLEI-YDGPSTSspllgRFCGS 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 289547636 115 QGSPlgrppgqrEFVSSGRSLRLTFRTQPSSEnktahlHKGFLALYQT 162
Cdd:cd00041   80 TLPP--------PIISSGNSLTVRFRSDSSVT------GRGFKATYSA 113
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
52-160 3.02e-19

Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found mostly among developmentally-regulated proteins. Spermadhesins contain only this domain.


Pssm-ID: 214483 [Multi-domain]  Cd Length: 102  Bit Score: 82.82  E-value: 3.02e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547636    52 LTSPGYPEPYGKGQESSTDIKAPEGFAVRLVFQDFDLEPSQDCAGDSVTIsFVGSDPS-----QFCGQQGSPlgrppgqR 126
Cdd:smart00042   3 ITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTDFDLESSDNCEYDYVEI-YDGPSASspllgRFCGSEAPP-------P 74
                           90       100       110
                   ....*....|....*....|....*....|....
gi 289547636   127 EFVSSGRSLRLTFRTQPSSENktahlhKGFLALY 160
Cdd:smart00042  75 VISSSSNSLTLTFVSDSSVQK------RGFSARY 102
CUB pfam00431
CUB domain;
47-160 3.87e-14

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 68.48  E-value: 3.87e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547636   47 ELPQQLTSPGYPEPYGKGQESSTDIKAPEGFAVRLVFQDFDLEPSQDCAGDSVTIsFVGSDPSQ-----FCGQQGSPlgr 121
Cdd:pfam00431   7 DSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDECGYDYVEI-RDGPSASSpllgrFCGSGIPE--- 82
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 289547636  122 ppgqrEFVSSGRSLRLTFRTQPSSENktahlhKGFLALY 160
Cdd:pfam00431  83 -----DIVSSSNQMTIKFVSDASVQK------RGFKATY 110
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
247-480 8.34e-62

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: 201.35  E-value: 8.34e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547636 247 GSSRAKLGNFPWQAFTSIHGRG---GGALLGDRWILTAAHTIYPKDSVSLRknqsvnVFLGHTAIDEMLKLG-NHPVHRV 322
Cdd:cd00190    3 GGSEAKIGSFPWQVSLQYTGGRhfcGGSLISPRWVLTAAHCVYSSAPSNYT------VRLGSHDLSSNEGGGqVIKVKKV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547636 323 VVHPDYRQNESHNfsgDIALLELQHSIPLGPNVLPVCLPDNETLYRSGLLGYVSGFG--MEMGWLTTELKYSRLPVAPRE 400
Cdd:cd00190   77 IVHPNYNPSTYDN---DIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGrtSEGGPLPDVLQEVNVPIVSNA 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547636 401 ACNawlQKRQRPEVFSDNMFCVGDETQRHSVCQGDSGSVYVVWDNhaHHWVATGIVSWGIGCGEG--YDFYTKVLSYVDW 478
Cdd:cd00190  154 ECK---RAYSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDN--GRGVLVGIVSWGSGCARPnyPGVYTRVSSYLDW 228

                 ..
gi 289547636 479 IK 480
Cdd:cd00190  229 IQ 230
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
247-479 2.63e-60

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: 197.52  E-value: 2.63e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547636   247 GSSRAKLGNFPWQAFTSIHGRG---GGALLGDRWILTAAHTIYPKDsvslrkNQSVNVFLGHTAIDEMLKLGNHPVHRVV 323
Cdd:smart00020   4 GGSEANIGSFPWQVSLQYGGGRhfcGGSLISPRWVLTAAHCVRGSD------PSNIRVRLGSHDLSSGEEGQVIKVSKVI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547636   324 VHPDYRQNESHNfsgDIALLELQHSIPLGPNVLPVCLPDNETLYRSGLLGYVSGFG---MEMGWLTTELKYSRLPVAPRE 400
Cdd:smart00020  78 IHPNYNPSTYDN---DIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGrtsEGAGSLPDTLQEVNVPIVSNA 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547636   401 ACNawlQKRQRPEVFSDNMFCVGDETQRHSVCQGDSGSVYVVWDNhahHWVATGIVSWGIGCGEG--YDFYTKVLSYVDW 478
Cdd:smart00020 155 TCR---RAYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCNDG---RWVLVGIVSWGSGCARPgkPGVYTRVSSYLDW 228

                   .
gi 289547636   479 I 479
Cdd:smart00020 229 I 229
Trypsin pfam00089
Trypsin;
247-479 6.16e-42

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 148.74  E-value: 6.16e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547636  247 GSSRAKLGNFPWQAFTSIHGRG---GGALLGDRWILTAAHTIYPKDSVslrknqsvNVFLGHTAIDEMLKLGNH-PVHRV 322
Cdd:pfam00089   3 GGDEAQPGSFPWQVSLQLSSGKhfcGGSLISENWVLTAAHCVSGASDV--------KVVLGAHNIVLREGGEQKfDVEKI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547636  323 VVHPDYRQNESHNfsgDIALLELQHSIPLGPNVLPVCLPDNETLYRSGLLGYVSGFG-MEMGWLTTELKYSRLPVAPREA 401
Cdd:pfam00089  75 IVHPNYNPDTLDN---DIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGnTKTLGPSDTLQEVTVPVVSRET 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547636  402 CNawlqkRQRPEVFSDNMFCVGdeTQRHSVCQGDSGSVYVVWDNHAHhwvatGIVSWGIGCGEG--YDFYTKVLSYVDWI 479
Cdd:pfam00089 152 CR-----SAYGGTVTDTMICAG--AGGKDACQGDSGGPLVCSDGELI-----GIVSWGYGCASGnyPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
247-485 4.18e-39

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 142.48  E-value: 4.18e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547636 247 GSSRAKLGNFPWQAftSIHGRGG-------GALLGDRWILTAAHTIYPKDSVSLRknqsvnVFLGHTAIDEmlKLGN-HP 318
Cdd:COG5640   33 GGTPATVGEYPWMV--ALQSSNGpsgqfcgGTLIAPRWVLTAAHCVDGDGPSDLR------VVIGSTDLST--SGGTvVK 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547636 319 VHRVVVHPDYRqneSHNFSGDIALLELQHSIPLGPnvlPVCLPDNETLYRSGLLGYVSGFGM---EMGWLTTELKYSRLP 395
Cdd:COG5640  103 VARIVVHPDYD---PATPGNDIALLKLATPVPGVA---PAPLATSADAAAPGTPATVAGWGRtseGPGSQSGTLRKADVP 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547636 396 VAPREACNAWlqkrqrPEVFSDNMFCVGDETQRHSVCQGDSGSVYVVWDNHAhhWVATGIVSWGIG-CGEG-YDFYTKVL 473
Cdd:COG5640  177 VVSDATCAAY------GGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGG--WVLVGVVSWGGGpCAAGyPGVYTRVS 248
                        250
                 ....*....|..
gi 289547636 474 SYVDWIKGVMNG 485
Cdd:COG5640  249 AYRDWIKSTAGG 260
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
40-162 2.99e-20

CUB domain; extracellular domain; present in proteins mostly known to be involved in development; not found in prokaryotes, plants and yeast.


Pssm-ID: 238001 [Multi-domain]  Cd Length: 113  Bit Score: 85.93  E-value: 2.99e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547636  40 GSVLLAQElPQQLTSPGYPEPYGKGQESSTDIKAPEGFAVRLVFQDFDLEPSQDCAGDSVTIsFVGSDPS-----QFCGQ 114
Cdd:cd00041    2 GGTLTAST-SGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESSPNCSYDYLEI-YDGPSTSspllgRFCGS 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 289547636 115 QGSPlgrppgqrEFVSSGRSLRLTFRTQPSSEnktahlHKGFLALYQT 162
Cdd:cd00041   80 TLPP--------PIISSGNSLTVRFRSDSSVT------GRGFKATYSA 113
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
52-160 3.02e-19

Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found mostly among developmentally-regulated proteins. Spermadhesins contain only this domain.


Pssm-ID: 214483 [Multi-domain]  Cd Length: 102  Bit Score: 82.82  E-value: 3.02e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547636    52 LTSPGYPEPYGKGQESSTDIKAPEGFAVRLVFQDFDLEPSQDCAGDSVTIsFVGSDPS-----QFCGQQGSPlgrppgqR 126
Cdd:smart00042   3 ITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTDFDLESSDNCEYDYVEI-YDGPSASspllgRFCGSEAPP-------P 74
                           90       100       110
                   ....*....|....*....|....*....|....
gi 289547636   127 EFVSSGRSLRLTFRTQPSSENktahlhKGFLALY 160
Cdd:smart00042  75 VISSSSNSLTLTFVSDSSVQK------RGFSARY 102
CUB pfam00431
CUB domain;
47-160 3.87e-14

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 68.48  E-value: 3.87e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547636   47 ELPQQLTSPGYPEPYGKGQESSTDIKAPEGFAVRLVFQDFDLEPSQDCAGDSVTIsFVGSDPSQ-----FCGQQGSPlgr 121
Cdd:pfam00431   7 DSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDECGYDYVEI-RDGPSASSpllgrFCGSGIPE--- 82
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 289547636  122 ppgqrEFVSSGRSLRLTFRTQPSSENktahlhKGFLALY 160
Cdd:pfam00431  83 -----DIVSSSNQMTIKFVSDASVQK------RGFKATY 110
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
270-459 1.67e-06

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 48.52  E-value: 1.67e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547636 270 GALLGDRWILTAAHTIYPKDsvSLRKNQSVNVFLGHTAIDEmlklGNHPVHRVVVHPDYRQNESHNFsgDIALLELQHSI 349
Cdd:COG3591   16 GTLIGPNLVLTAGHCVYDGA--GGGWATNIVFVPGYNGGPY----GTATATRFRVPPGWVASGDAGY--DYALLRLDEPL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547636 350 PLGPNVLPVclpDNETLYRSGLLGYVSGFGMEmgwlttelkysrlpvapreacnawlqkrqRPEVFSDNMFC----VGDE 425
Cdd:COG3591   88 GDTTGWLGL---AFNDAPLAGEPVTIIGYPGD-----------------------------RPKDLSLDCSGrvtgVQGN 135
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 289547636 426 TQRHS--VCQGDSGSvyVVWDNHAHHWVATGIVSWG 459
Cdd:COG3591  136 RLSYDcdTTGGSSGS--PVLDDSDGGGRVVGVHSAG 169
 
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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