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Conserved domains on  [gi|148230547|ref|NP_001081234.1|]
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complement factor B precursor

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List of domain hits

Name Accession Description Interval E-value
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
240-442 1.64e-102

Complement factors B and C2 are two critical proteases for complement activation. They both contain three CCP or Sushi domains, a trypsin-type serine protease domain and a single VWA domain with a conserved metal ion dependent adhesion site referred commonly as the MIDAS motif. Orthologues of these molecules are found from echinoderms to chordates. During complement activation, the CCP domains are cleaved off, resulting in the formation of an active protease that cleaves and activates complement C3. Complement C2 is in the classical pathway and complement B is in the alternative pathway. The interaction of C2 with C4 and of factor B with C3b are both dependent on Mg2+ binding sites within the VWA domains and the VWA domain of factor B has been shown to mediate the binding of C3. This is consistent with the common inferred function of VWA domains as magnesium-dependent protein interaction domains.


:

Pssm-ID: 238747  Cd Length: 198  Bit Score: 315.38  E-value: 1.64e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230547 240 MNIFIVLDTSKSVGQNRFDEAKSASILFIEKMSNYDIKPRYCIISYASKAISVVSLRDPDSNNADAVMEHLEEFQYDRHE 319
Cdd:cd01470    1 LNIYIALDASDSIGEEDFDEAKNAIKTLIEKISSYEVSPRYEIISYASDPKEIVSIRDFNSNDADDVIKRLEDFNYDDHG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230547 320 DKQGTNTRAALHAIYEHLieqelAYEREGKKEDFMKIHNVILLMTDGKFNMGGDPREEMKLIKRFLDVGIRKDNPREEYL 399
Cdd:cd01470   81 DKTGTNTAAALKKVYERM-----ALEKVRNKEAFNETRHVIILFTDGKSNMGGSPLPTVDKIKNLVYKNNKSDNPREDYL 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 148230547 400 DVYVFGLGSDIDQPEINDLASKKEKEVHTFHLQNVEKMKEFFE 442
Cdd:cd01470  156 DVYVFGVGDDVNKEELNDLASKKDNERHFFKLKDYEDLQEVFD 198
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
474-734 1.69e-46

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: 165.14  E-value: 1.69e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230547 474 FPWIVKITITHNGiQYCKGTILSQYFILTAAHCFDLDDKTQ-KIHV--------KIDGKEYLVKDFYRHPKYDPiskkdk 544
Cdd:cd00190   12 FPWQVSLQYTGGR-HFCGGSLISPRWVLTAAHCVYSSAPSNyTVRLgshdlssnEGGGQVIKVKKVIVHPNYNP------ 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230547 545 gikRAFDYDVALLELQRndKIEFSENARPICIPCTQGTAqalkQPGAPCSshektllseeevkavfIA------EESNKP 618
Cdd:cd00190   85 ---STYDNDIALLKLKR--PVTLSDNVRPICLPSSGYNL----PAGTTCT----------------VSgwgrtsEGGPLP 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230547 619 MKEMHVLIKRgQKRSACLEAAKKAPelknvtniedAVTDQFLCTGGIVPVADPpvCKGDSGGPLLIQVKRRYVQVGIISW 698
Cdd:cd00190  140 DVLQEVNVPI-VSNAECKRAYSYGG----------TITDNMLCAGGLEGGKDA--CQGDSGGPLVCNDNGRGVLVGIVSW 206
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 148230547 699 GTVdhCdkgtrikqTQKNARDFYQDIFKVLPWIQKV 734
Cdd:cd00190  207 GSG--C--------ARPNYPGVYTRVSSYLDWIQKT 232
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
80-135 5.88e-14

Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) have been identified in several proteins of the complement system; SUSHI repeats (short complement-like repeat, SCR) are abundant in complement control proteins. The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. Typically, 2 to 4 modules contribute to a binding site, implying that the orientation of the modules to each other is critical for function.


:

Pssm-ID: 153056  Cd Length: 57  Bit Score: 67.87  E-value: 5.88e-14
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 148230547  80 CPRPVTFEDGDYEPRQPFYKVGDTLYFECYSGFTMKGPQNRTCQENAKWTGETTIC 135
Cdd:cd00033    1 CPPPPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTC 56
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
142-196 9.33e-10

Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) have been identified in several proteins of the complement system; SUSHI repeats (short complement-like repeat, SCR) are abundant in complement control proteins. The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. Typically, 2 to 4 modules contribute to a binding site, implying that the orientation of the modules to each other is critical for function.


:

Pssm-ID: 153056  Cd Length: 57  Bit Score: 55.93  E-value: 9.33e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 148230547 142 CPNPGIPIGASKSGS--SYKMENKVSYNCQQGLVMFGSKERECLEDKSWSGTEPSCR 196
Cdd:cd00033    1 CPPPPVPENGTVTGSkgSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
24-72 4.40e-04

Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat (SCR); The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. A missense mutation in seventh CCP domain causes deficiency of the b subunit of factor XIII.


:

Pssm-ID: 214478  Cd Length: 56  Bit Score: 39.05  E-value: 4.40e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 148230547    24 AIIGGSYTVSDGG-NVGSKVEYQCPKGKYPYPKYTRECQYNGFWTDQKAK 72
Cdd:smart00032   6 DIENGTVTSSSGTySYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPT 55
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
474-731 7.19e-42

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 [Multi-domain]  Cd Length: 229  Bit Score: 152.45  E-value: 7.19e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230547   474 FPWIVKITITHNGiQYCKGTILSQYFILTAAHCFDLDDKTQ--------KIHVKIDGKEYLVKDFYRHPKYDPiskkdkg 545
Cdd:smart00020  13 FPWQVSLQYGGGR-HFCGGSLISPRWVLTAAHCVRGSDPSNirvrlgshDLSSGEEGQVIKVSKVIIHPNYNP------- 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230547   546 ikRAFDYDVALLELQRndKIEFSENARPICIPCTQGTAqalkQPGAPCSshektllseeevkavfIA-------EESNKP 618
Cdd:smart00020  85 --STYDNDIALLKLKE--PVTLSDNVRPICLPSSNYNV----PAGTTCT----------------VSgwgrtseGAGSLP 140
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230547   619 MKEMHVLIKRgQKRSACLEAAKKAPelknvtniedAVTDQFLCTGGIVPVADPpvCKGDSGGPLLIQvKRRYVQVGIISW 698
Cdd:smart00020 141 DTLQEVNVPI-VSNATCRRAYSGGG----------AITDNMLCAGGLEGGKDA--CQGDSGGPLVCN-DGRWVLVGIVSW 206
                          250       260       270
                   ....*....|....*....|....*....|...
gi 148230547   699 GtvDHCDkgtrikqtQKNARDFYQDIFKVLPWI 731
Cdd:smart00020 207 G--SGCA--------RPGKPGVYTRVSSYLDWI 229
 
Name Accession Description Interval E-value
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
240-442 1.64e-102

Complement factors B and C2 are two critical proteases for complement activation. They both contain three CCP or Sushi domains, a trypsin-type serine protease domain and a single VWA domain with a conserved metal ion dependent adhesion site referred commonly as the MIDAS motif. Orthologues of these molecules are found from echinoderms to chordates. During complement activation, the CCP domains are cleaved off, resulting in the formation of an active protease that cleaves and activates complement C3. Complement C2 is in the classical pathway and complement B is in the alternative pathway. The interaction of C2 with C4 and of factor B with C3b are both dependent on Mg2+ binding sites within the VWA domains and the VWA domain of factor B has been shown to mediate the binding of C3. This is consistent with the common inferred function of VWA domains as magnesium-dependent protein interaction domains.


Pssm-ID: 238747  Cd Length: 198  Bit Score: 315.38  E-value: 1.64e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230547 240 MNIFIVLDTSKSVGQNRFDEAKSASILFIEKMSNYDIKPRYCIISYASKAISVVSLRDPDSNNADAVMEHLEEFQYDRHE 319
Cdd:cd01470    1 LNIYIALDASDSIGEEDFDEAKNAIKTLIEKISSYEVSPRYEIISYASDPKEIVSIRDFNSNDADDVIKRLEDFNYDDHG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230547 320 DKQGTNTRAALHAIYEHLieqelAYEREGKKEDFMKIHNVILLMTDGKFNMGGDPREEMKLIKRFLDVGIRKDNPREEYL 399
Cdd:cd01470   81 DKTGTNTAAALKKVYERM-----ALEKVRNKEAFNETRHVIILFTDGKSNMGGSPLPTVDKIKNLVYKNNKSDNPREDYL 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 148230547 400 DVYVFGLGSDIDQPEINDLASKKEKEVHTFHLQNVEKMKEFFE 442
Cdd:cd01470  156 DVYVFGVGDDVNKEELNDLASKKDNERHFFKLKDYEDLQEVFD 198
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
474-734 1.69e-46

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: 165.14  E-value: 1.69e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230547 474 FPWIVKITITHNGiQYCKGTILSQYFILTAAHCFDLDDKTQ-KIHV--------KIDGKEYLVKDFYRHPKYDPiskkdk 544
Cdd:cd00190   12 FPWQVSLQYTGGR-HFCGGSLISPRWVLTAAHCVYSSAPSNyTVRLgshdlssnEGGGQVIKVKKVIVHPNYNP------ 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230547 545 gikRAFDYDVALLELQRndKIEFSENARPICIPCTQGTAqalkQPGAPCSshektllseeevkavfIA------EESNKP 618
Cdd:cd00190   85 ---STYDNDIALLKLKR--PVTLSDNVRPICLPSSGYNL----PAGTTCT----------------VSgwgrtsEGGPLP 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230547 619 MKEMHVLIKRgQKRSACLEAAKKAPelknvtniedAVTDQFLCTGGIVPVADPpvCKGDSGGPLLIQVKRRYVQVGIISW 698
Cdd:cd00190  140 DVLQEVNVPI-VSNAECKRAYSYGG----------TITDNMLCAGGLEGGKDA--CQGDSGGPLVCNDNGRGVLVGIVSW 206
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 148230547 699 GTVdhCdkgtrikqTQKNARDFYQDIFKVLPWIQKV 734
Cdd:cd00190  207 GSG--C--------ARPNYPGVYTRVSSYLDWIQKT 232
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
80-135 5.88e-14

Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) have been identified in several proteins of the complement system; SUSHI repeats (short complement-like repeat, SCR) are abundant in complement control proteins. The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. Typically, 2 to 4 modules contribute to a binding site, implying that the orientation of the modules to each other is critical for function.


Pssm-ID: 153056  Cd Length: 57  Bit Score: 67.87  E-value: 5.88e-14
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 148230547  80 CPRPVTFEDGDYEPRQPFYKVGDTLYFECYSGFTMKGPQNRTCQENAKWTGETTIC 135
Cdd:cd00033    1 CPPPPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTC 56
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
142-196 9.33e-10

Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) have been identified in several proteins of the complement system; SUSHI repeats (short complement-like repeat, SCR) are abundant in complement control proteins. The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. Typically, 2 to 4 modules contribute to a binding site, implying that the orientation of the modules to each other is critical for function.


Pssm-ID: 153056  Cd Length: 57  Bit Score: 55.93  E-value: 9.33e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 148230547 142 CPNPGIPIGASKSGS--SYKMENKVSYNCQQGLVMFGSKERECLEDKSWSGTEPSCR 196
Cdd:cd00033    1 CPPPPVPENGTVTGSkgSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57
VWA pfam00092
von Willebrand factor type A domain;
241-444 4.92e-31

von Willebrand factor type A domain;


Pssm-ID: 249581  Cd Length: 177  Bit Score: 120.19  E-value: 4.92e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230547  241 NIFIVLDTSKSVGQNRFDEAKSASILFIEKMSNYDIKPRYCIISYASKAISVVSLRdpDSNNADAVMEHLeefQYDRHED 320
Cdd:pfam00092   1 DIVFLLDGSGSIGEANFEKVKEFIKKLVERLDIGPDGTRVGLVQYSSDVTTEFSLN--DYKSKDDLLSAV---LKNIYYL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230547  321 KQGTNTRAALHAIYEHLIEqelayeregKKEDFMKIHNVILLMTDGKFNMGGDPREEMKLIKRFldvgirkdnpreeyLD 400
Cdd:pfam00092  76 GGGTNTGKALKYALENLFR---------SAGSRPNAPKVVILLTDGKSNDGGLVEAAAAALRRK--------------VG 132
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 148230547  401 VYVFGLGS-DIDQPEINDLASKKEKEVHTFHLQNVEKMKEFFELM 444
Cdd:pfam00092 133 IIVFGVGVgDVDEEELRLIASEPCSEGHVFYVTDFDALSEIQEEL 177
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
241-444 1.51e-28

von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins mediate adhesion via metal ion-dependent adhesion sites (MIDAS). Intracellular VWA domains and homologues in prokaryotes have recently been identified. The proposed VWA domains in integrin beta subunits have recently been substantiated using sequence-based methods.


Pssm-ID: 214621  Cd Length: 175  Bit Score: 113.32  E-value: 1.51e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230547   241 NIFIVLDTSKSVGQNRFDEAKSASILFIEKMSNYDIKPRYCIISYASKAISVVSLRdpDSNNADAVMEHLEEFQYDRhed 320
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLN--DSRSKDALLEALASLSYKL--- 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230547   321 KQGTNTRAALHAIYEHLIEQELAYEREGKKedfmkihnVILLMTDGKFNMGG-DPREEMKLIKRfldvgirkdnpreEYL 399
Cdd:smart00327  76 GGGTNLGAALQYALENLFSKSAGSRRGAPK--------VVILITDGESNDGPkDLLKAAKELKR-------------SGV 134
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 148230547   400 DVYVFGLGSDIDQPEINDLASKKeKEVHTFhlqNVEKMKEFFELM 444
Cdd:smart00327 135 KVFVVGVGNDVDEEELKKLASAP-GGVYVF---LPELLDLLIDLL 175
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
80-135 1.20e-13

Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat (SCR); The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. A missense mutation in seventh CCP domain causes deficiency of the b subunit of factor XIII.


Pssm-ID: 214478  Cd Length: 56  Bit Score: 67.17  E-value: 1.20e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 148230547    80 CPRPVTFEDGDYEPRQPFYKVGDTLYFECYSGFTMKGPQNRTCQENAKWTGETTIC 135
Cdd:smart00032   1 CPPPPDIENGTVTSSSGTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
Sushi pfam00084
Sushi domain (SCR repeat);
80-135 2.11e-10

Sushi domain (SCR repeat);


Pssm-ID: 249573  Cd Length: 56  Bit Score: 57.59  E-value: 2.11e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 148230547   80 CPRPVTFEDGDYEPRQPFYKVGDTLYFECYSGFTMKGPQNRTCQENAKWTGETTIC 135
Cdd:pfam00084   1 CPAPPPIPHGVISTTKNSYQVGSVVRYECDPGYVLVGSSVITCQDDGTWSPPLPEC 56
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
142-195 4.20e-09

Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat (SCR); The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. A missense mutation in seventh CCP domain causes deficiency of the b subunit of factor XIII.


Pssm-ID: 214478  Cd Length: 56  Bit Score: 53.68  E-value: 4.20e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 148230547   142 CPNPGIPIGASKSGSS--YKMENKVSYNCQQGLVMFGSKERECLEDKSWSGTEPSC 195
Cdd:smart00032   1 CPPPPDIENGTVTSSSgtYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
Sushi pfam00084
Sushi domain (SCR repeat);
142-195 5.23e-05

Sushi domain (SCR repeat);


Pssm-ID: 249573  Cd Length: 56  Bit Score: 41.80  E-value: 5.23e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 148230547  142 CPNPGIPIGASKS--GSSYKMENKVSYNCQQGLVMFGSKERECLEDKSWSGTEPSC 195
Cdd:pfam00084   1 CPAPPPIPHGVISttKNSYQVGSVVRYECDPGYVLVGSSVITCQDDGTWSPPLPEC 56
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
24-72 4.40e-04

Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat (SCR); The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. A missense mutation in seventh CCP domain causes deficiency of the b subunit of factor XIII.


Pssm-ID: 214478  Cd Length: 56  Bit Score: 39.05  E-value: 4.40e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 148230547    24 AIIGGSYTVSDGG-NVGSKVEYQCPKGKYPYPKYTRECQYNGFWTDQKAK 72
Cdd:smart00032   6 DIENGTVTSSSGTySYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPT 55
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
474-731 7.19e-42

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 [Multi-domain]  Cd Length: 229  Bit Score: 152.45  E-value: 7.19e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230547   474 FPWIVKITITHNGiQYCKGTILSQYFILTAAHCFDLDDKTQ--------KIHVKIDGKEYLVKDFYRHPKYDPiskkdkg 545
Cdd:smart00020  13 FPWQVSLQYGGGR-HFCGGSLISPRWVLTAAHCVRGSDPSNirvrlgshDLSSGEEGQVIKVSKVIIHPNYNP------- 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230547   546 ikRAFDYDVALLELQRndKIEFSENARPICIPCTQGTAqalkQPGAPCSshektllseeevkavfIA-------EESNKP 618
Cdd:smart00020  85 --STYDNDIALLKLKE--PVTLSDNVRPICLPSSNYNV----PAGTTCT----------------VSgwgrtseGAGSLP 140
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230547   619 MKEMHVLIKRgQKRSACLEAAKKAPelknvtniedAVTDQFLCTGGIVPVADPpvCKGDSGGPLLIQvKRRYVQVGIISW 698
Cdd:smart00020 141 DTLQEVNVPI-VSNATCRRAYSGGG----------AITDNMLCAGGLEGGKDA--CQGDSGGPLVCN-DGRWVLVGIVSW 206
                          250       260       270
                   ....*....|....*....|....*....|...
gi 148230547   699 GtvDHCDkgtrikqtQKNARDFYQDIFKVLPWI 731
Cdd:smart00020 207 G--SGCA--------RPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
474-731 2.45e-28

Trypsin;


Pssm-ID: 249578 [Multi-domain]  Cd Length: 219  Bit Score: 113.69  E-value: 2.45e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230547  474 FPWIVKITITHNGIQyCKGTILSQYFILTAAHCFDLDDKTQ-----KIHVKIDGKE--YLVKDFYRHPKYDPiskkdkgi 546
Cdd:pfam00089  12 FPWQVSLQVSSGKHF-CGGSLISENWVLTAAHCVSNAKSVRvvlgaHNIVLREGGEqkFDVEKIIVHPNYNP-------- 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230547  547 kRAFDYDVALLELqrNDKIEFSENARPICIPctqgTAQALKQPGAPCsshektllseeevkavFIA----EESNKPMKEM 622
Cdd:pfam00089  83 -DTLDNDIALLKL--KSPVTLGDTVRPICLP----TASSDLPVGTTC----------------TVSgwgnTKTLGLSDTL 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230547  623 HVLIKRGQKRSACLEAAKkapelknvtnieDAVTDQFLCTGGIVPVAdppvCKGDSGGPLLiqVKRRYVQvGIISWGtvD 702
Cdd:pfam00089 140 QEVTVPVVSRETCRSAYG------------GTVTDTMICAGAGGKDA----CQGDSGGPLV--CSDGELI-GIVSWG--Y 198
                         250       260
                  ....*....|....*....|....*....
gi 148230547  703 HCDKGTRIkqtqknarDFYQDIFKVLPWI 731
Cdd:pfam00089 199 GCASGNKP--------GVYTPVSSYLDWI 219
PHA02927 PHA02927
secreted complement-binding protein; Provisional
35-195 1.56e-15

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 76.23  E-value: 1.56e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230547  35 GGNVGSKVEYQCPKGKYPYPKYTRECQ--YNGFWTDQKAKTICKDVRCPRPVTFEDGDYEPRQPFYKVGDTLYFECYSGF 112
Cdd:PHA02927 101 GVDFGSSITYSCNSGYQLIGESKSYCElgSTGSMVWNPEAPICESVKCQSPPSISNGRHNGYEDFYTDGSVVTYSCNSGY 180
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230547 113 TMKGPQNRTCQeNAKWTGETTiCDDNNgyCPNPGIPIGASKSG--SSYKMENKVSYNCQQGLVMFGSKERECLEDKSWSG 190
Cdd:PHA02927 181 SLIGNSGVLCS-GGEWSDPPT-CQIVK--CPHPTISNGYLSSGfkRSYSYNDNVDFKCKYGYKLSGSSSSTCSPGNTWQP 256

                 ....*
gi 148230547 191 TEPSC 195
Cdd:PHA02927 257 ELPKC 261
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
474-699 1.13e-06

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


Pssm-ID: 227927 [Multi-domain]  Cd Length: 413  Bit Score: 50.26  E-value: 1.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230547 474 FPWIVKITIT---HNGIQYCKGTILSQYFILTAAHCFDLDD--KTQKIHVKID------GKEYLVKDFYRHPKYDPISK- 541
Cdd:COG5640   44 YPSLVALVDRisdYVSGTFCGGSKLGGRYVLTAAHCADASSpiSSDVNRVVVDlndssqAERGHVRTIYVHEFYSPGNLg 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230547 542 KDKGIKRAFDYDVALLE-LQRNDKIEFSENARPICIPCTQGTAQALKQPGAPCSSHEKTLLSEEEVKAVFIAEESNKpmk 620
Cdd:COG5640  124 NDIAVLELARAASLPRVkITSFDASDTFLNSVTTVSPMTNGTFGVTTPSDVPRSSPKGTILHEVAVLFVPLSTCAQY--- 200
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230547 621 emhvlikrgqkrSACLEAAKKAPELKNVTniedavtdqflctggivpVADPP--VCKGDSGGPLLIQVKRRYVQVGIISW 698
Cdd:COG5640  201 ------------KGCANASDGATGLTGFC------------------AGRPPkdACQGDSGGPIFHKGEEGRVQRGVVSW 250

                 .
gi 148230547 699 G 699
Cdd:COG5640  251 G 251
 
Name Accession Description Interval E-value
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
240-442 1.64e-102

Complement factors B and C2 are two critical proteases for complement activation. They both contain three CCP or Sushi domains, a trypsin-type serine protease domain and a single VWA domain with a conserved metal ion dependent adhesion site referred commonly as the MIDAS motif. Orthologues of these molecules are found from echinoderms to chordates. During complement activation, the CCP domains are cleaved off, resulting in the formation of an active protease that cleaves and activates complement C3. Complement C2 is in the classical pathway and complement B is in the alternative pathway. The interaction of C2 with C4 and of factor B with C3b are both dependent on Mg2+ binding sites within the VWA domains and the VWA domain of factor B has been shown to mediate the binding of C3. This is consistent with the common inferred function of VWA domains as magnesium-dependent protein interaction domains.


Pssm-ID: 238747  Cd Length: 198  Bit Score: 315.38  E-value: 1.64e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230547 240 MNIFIVLDTSKSVGQNRFDEAKSASILFIEKMSNYDIKPRYCIISYASKAISVVSLRDPDSNNADAVMEHLEEFQYDRHE 319
Cdd:cd01470    1 LNIYIALDASDSIGEEDFDEAKNAIKTLIEKISSYEVSPRYEIISYASDPKEIVSIRDFNSNDADDVIKRLEDFNYDDHG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230547 320 DKQGTNTRAALHAIYEHLieqelAYEREGKKEDFMKIHNVILLMTDGKFNMGGDPREEMKLIKRFLDVGIRKDNPREEYL 399
Cdd:cd01470   81 DKTGTNTAAALKKVYERM-----ALEKVRNKEAFNETRHVIILFTDGKSNMGGSPLPTVDKIKNLVYKNNKSDNPREDYL 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 148230547 400 DVYVFGLGSDIDQPEINDLASKKEKEVHTFHLQNVEKMKEFFE 442
Cdd:cd01470  156 DVYVFGVGDDVNKEELNDLASKKDNERHFFKLKDYEDLQEVFD 198
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
474-734 1.69e-46

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: 165.14  E-value: 1.69e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230547 474 FPWIVKITITHNGiQYCKGTILSQYFILTAAHCFDLDDKTQ-KIHV--------KIDGKEYLVKDFYRHPKYDPiskkdk 544
Cdd:cd00190   12 FPWQVSLQYTGGR-HFCGGSLISPRWVLTAAHCVYSSAPSNyTVRLgshdlssnEGGGQVIKVKKVIVHPNYNP------ 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230547 545 gikRAFDYDVALLELQRndKIEFSENARPICIPCTQGTAqalkQPGAPCSshektllseeevkavfIA------EESNKP 618
Cdd:cd00190   85 ---STYDNDIALLKLKR--PVTLSDNVRPICLPSSGYNL----PAGTTCT----------------VSgwgrtsEGGPLP 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230547 619 MKEMHVLIKRgQKRSACLEAAKKAPelknvtniedAVTDQFLCTGGIVPVADPpvCKGDSGGPLLIQVKRRYVQVGIISW 698
Cdd:cd00190  140 DVLQEVNVPI-VSNAECKRAYSYGG----------TITDNMLCAGGLEGGKDA--CQGDSGGPLVCNDNGRGVLVGIVSW 206
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 148230547 699 GTVdhCdkgtrikqTQKNARDFYQDIFKVLPWIQKV 734
Cdd:cd00190  207 GSG--C--------ARPNYPGVYTRVSSYLDWIQKT 232
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
80-135 5.88e-14

Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) have been identified in several proteins of the complement system; SUSHI repeats (short complement-like repeat, SCR) are abundant in complement control proteins. The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. Typically, 2 to 4 modules contribute to a binding site, implying that the orientation of the modules to each other is critical for function.


Pssm-ID: 153056  Cd Length: 57  Bit Score: 67.87  E-value: 5.88e-14
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 148230547  80 CPRPVTFEDGDYEPRQPFYKVGDTLYFECYSGFTMKGPQNRTCQENAKWTGETTIC 135
Cdd:cd00033    1 CPPPPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTC 56
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
142-196 9.33e-10

Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) have been identified in several proteins of the complement system; SUSHI repeats (short complement-like repeat, SCR) are abundant in complement control proteins. The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. Typically, 2 to 4 modules contribute to a binding site, implying that the orientation of the modules to each other is critical for function.


Pssm-ID: 153056  Cd Length: 57  Bit Score: 55.93  E-value: 9.33e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 148230547 142 CPNPGIPIGASKSGS--SYKMENKVSYNCQQGLVMFGSKERECLEDKSWSGTEPSCR 196
Cdd:cd00033    1 CPPPPVPENGTVTGSkgSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
240-429 1.67e-32

Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains


Pssm-ID: 238727  Cd Length: 161  Bit Score: 123.94  E-value: 1.67e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230547 240 MNIFIVLDTSKSVGQNRFDEAKSASILFIEKMSNYDIKPRYCIISYASKAISVVSLRdpDSNNADAVMEHLEEFQYDrhe 319
Cdd:cd01450    1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLN--DYKSKDDLLKAVKNLKYL--- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230547 320 DKQGTNTRAALHAIYEHLIEqelayeregKKEDFMKIHNVILLMTDGKFNMGGDPREEMKLIKRfldvgirkdnpreEYL 399
Cdd:cd01450   76 GGGGTNTGKALQYALEQLFS---------ESNARENVPKVIIVLTDGRSDDGGDPKEAAAKLKD-------------EGI 133
                        170       180       190
                 ....*....|....*....|....*....|
gi 148230547 400 DVYVFGLGsDIDQPEINDLASKKEkEVHTF 429
Cdd:cd01450  134 KVFVVGVG-PADEEELREIASCPS-ERHVF 161
VWA pfam00092
von Willebrand factor type A domain;
241-444 4.92e-31

von Willebrand factor type A domain;


Pssm-ID: 249581  Cd Length: 177  Bit Score: 120.19  E-value: 4.92e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230547  241 NIFIVLDTSKSVGQNRFDEAKSASILFIEKMSNYDIKPRYCIISYASKAISVVSLRdpDSNNADAVMEHLeefQYDRHED 320
Cdd:pfam00092   1 DIVFLLDGSGSIGEANFEKVKEFIKKLVERLDIGPDGTRVGLVQYSSDVTTEFSLN--DYKSKDDLLSAV---LKNIYYL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230547  321 KQGTNTRAALHAIYEHLIEqelayeregKKEDFMKIHNVILLMTDGKFNMGGDPREEMKLIKRFldvgirkdnpreeyLD 400
Cdd:pfam00092  76 GGGTNTGKALKYALENLFR---------SAGSRPNAPKVVILLTDGKSNDGGLVEAAAAALRRK--------------VG 132
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 148230547  401 VYVFGLGS-DIDQPEINDLASKKEKEVHTFHLQNVEKMKEFFELM 444
Cdd:pfam00092 133 IIVFGVGVgDVDEEELRLIASEPCSEGHVFYVTDFDALSEIQEEL 177
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
241-444 1.51e-28

von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins mediate adhesion via metal ion-dependent adhesion sites (MIDAS). Intracellular VWA domains and homologues in prokaryotes have recently been identified. The proposed VWA domains in integrin beta subunits have recently been substantiated using sequence-based methods.


Pssm-ID: 214621  Cd Length: 175  Bit Score: 113.32  E-value: 1.51e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230547   241 NIFIVLDTSKSVGQNRFDEAKSASILFIEKMSNYDIKPRYCIISYASKAISVVSLRdpDSNNADAVMEHLEEFQYDRhed 320
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLN--DSRSKDALLEALASLSYKL--- 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230547   321 KQGTNTRAALHAIYEHLIEQELAYEREGKKedfmkihnVILLMTDGKFNMGG-DPREEMKLIKRfldvgirkdnpreEYL 399
Cdd:smart00327  76 GGGTNLGAALQYALENLFSKSAGSRRGAPK--------VVILITDGESNDGPkDLLKAAKELKR-------------SGV 134
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 148230547   400 DVYVFGLGSDIDQPEINDLASKKeKEVHTFhlqNVEKMKEFFELM 444
Cdd:smart00327 135 KVFVVGVGNDVDEEELKKLASAP-GGVYVF---LPELLDLLIDLL 175
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
241-421 2.13e-19

Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains.


Pssm-ID: 238119  Cd Length: 161  Bit Score: 86.47  E-value: 2.13e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230547 241 NIFIVLDTSKSVGQNRFDEAKSASILFIEKMSNYDIKPRYCIISYASKAISVVSLRDPDSNNadavmEHLEEFQYDRHED 320
Cdd:cd00198    2 DIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKA-----DLLEAIDALKKGL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230547 321 KQGTNTRAALHAIYEHLieqelayeregKKEDFMKIHNVILLMTDGKFNmgGDPREEMKLIKRFLDVGIRkdnpreeyld 400
Cdd:cd00198   77 GGGTNIGAALRLALELL-----------KSAKRPNARRVIILLTDGEPN--DGPELLAEAARELRKLGIT---------- 133
                        170       180
                 ....*....|....*....|.
gi 148230547 401 VYVFGLGSDIDQPEINDLASK 421
Cdd:cd00198  134 VYTIGIGDDANEDELKEIADK 154
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
80-135 1.20e-13

Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat (SCR); The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. A missense mutation in seventh CCP domain causes deficiency of the b subunit of factor XIII.


Pssm-ID: 214478  Cd Length: 56  Bit Score: 67.17  E-value: 1.20e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 148230547    80 CPRPVTFEDGDYEPRQPFYKVGDTLYFECYSGFTMKGPQNRTCQENAKWTGETTIC 135
Cdd:smart00032   1 CPPPPDIENGTVTSSSGTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
Sushi pfam00084
Sushi domain (SCR repeat);
80-135 2.11e-10

Sushi domain (SCR repeat);


Pssm-ID: 249573  Cd Length: 56  Bit Score: 57.59  E-value: 2.11e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 148230547   80 CPRPVTFEDGDYEPRQPFYKVGDTLYFECYSGFTMKGPQNRTCQENAKWTGETTIC 135
Cdd:pfam00084   1 CPAPPPIPHGVISTTKNSYQVGSVVRYECDPGYVLVGSSVITCQDDGTWSPPLPEC 56
VWA_2 pfam13519
von Willebrand factor type A domain;
241-421 3.45e-09

von Willebrand factor type A domain;


Pssm-ID: 257839  Cd Length: 172  Bit Score: 55.82  E-value: 3.45e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230547  241 NIFIVLDTSKS-----VGQNRFDEAKSASILFIEKMSNYDIKprycIISYASKAisvvSLRDPDSNNADAVMEHLEEFQY 315
Cdd:pfam13519   1 DLVIVLDVSGSmnatdLSPSRLTRAKAALADLLAALPGDRVG----LVAFAGSA----YLVLPLTDDRAALLAALPALDP 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230547  316 DRHeDKQGTNTRAALHAIYEHLIEQELAyeregkkedfmkiHNVILLMTDgkfnmGGDPREEMKLIKRFLDVGIRkdnpr 395
Cdd:pfam13519  73 RIM-PGGGTNLAAALALALRLLAGAGGG-------------SGAIVLITD-----GEDTPSLLEAASALKQAGVR----- 128
                         170       180
                  ....*....|....*....|....*..
gi 148230547  396 eeyldVYVFGLGSDID-QPEINDLASK 421
Cdd:pfam13519 129 -----LYVLGVGTDEGaEALLQRLAKA 150
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
142-195 4.20e-09

Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat (SCR); The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. A missense mutation in seventh CCP domain causes deficiency of the b subunit of factor XIII.


Pssm-ID: 214478  Cd Length: 56  Bit Score: 53.68  E-value: 4.20e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 148230547   142 CPNPGIPIGASKSGSS--YKMENKVSYNCQQGLVMFGSKERECLEDKSWSGTEPSC 195
Cdd:smart00032   1 CPPPPDIENGTVTSSSgtYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
241-366 4.35e-08

VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable members of diverse protein families defining structural integrity and various physiological functions. The most abundant family is the collagens with more than 20 different collagen types identified thus far. Collagens are centrally involved in the formation of fibrillar and microfibrillar networks of the extracellular matrix, basement membranes as well as other structures of the extracellular matrix. Some collagens have about 15-18 vWA domains in them. The VWA domains present in these collagens mediate protein-protein interactions.


Pssm-ID: 238757  Cd Length: 186  Bit Score: 52.39  E-value: 4.35e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230547 241 NIFIVLDTSKSVGQNRFDEAKSASILFIEKMSNYDIKP------RYCIISYaSKAISVVSLRDPDSNNADAVMEHLEEFQ 314
Cdd:cd01480    4 DITFVLDSSESVGLQNFDITKNFVKRVAERFLKDYYRKdpagswRVGVVQY-SDQQEVEAGFLRDIRNYTSLKEAVDNLE 82
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 148230547 315 YDRhedkQGTNTRAALHAIYEHLIEQELAYERegkkedfmkihNVILLMTDG 366
Cdd:cd01480   83 YIG----GGTFTDCALKYATEQLLEGSHQKEN-----------KFLLVITDG 119
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
241-367 1.13e-07

von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This domain has a variety of functions including: intermolecular adhesion, cell migration, signalling, transcription, and DNA repair. In integrins these domains form heterodimers while in vWF it forms homodimers and multimers. There are different interaction surfaces of this domain as seen by its complexes with collagen with either integrin or human vWFA. In integrins collagen binding occurs via the metal ion-dependent adhesion site (MIDAS) and involves three surface loops located on the upper surface of the molecule. In human vWFA, collagen binding is thought to occur on the bottom of the molecule and does not involve the vestigial MIDAS motif.


Pssm-ID: 238749  Cd Length: 164  Bit Score: 51.07  E-value: 1.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230547 241 NIFIVLDTSKSVGQNRFDEAKSasilFIEKM-SNYDI---KPRYCIISYASKAISVVSLRDPdsNNADAVMEHLEEFQYD 316
Cdd:cd01472    2 DIVFLVDGSESIGLSNFNLVKD----FVKRVvERLDIgpdGVRVGVVQYSDDPRTEFYLNTY--RSKDDVLEAVKNLRYI 75
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 148230547 317 RhedkQGTNTRAALHAIYEHLIEQELAYEREGKKedfmkihnVILLMTDGK 367
Cdd:cd01472   76 G----GGTNTGKALKYVRENLFTEASGSREGVPK--------VLVVITDGK 114
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
240-439 1.66e-06

Integrins are a class of adhesion receptors that link the extracellular matrix to the cytoskeleton and cooperate with growth factor receptors to promote celll survival, cell cycle progression and cell migration. Integrins consist of an alpha and a beta sub-unit. Each sub-unit has a large extracellular portion, a single transmembrane segment and a short cytoplasmic domain. The N-terminal domains of the alpha and beta subunits associate to form the integrin headpiece, which contains the ligand binding site, whereas the C-terminal segments traverse the plasma membrane and mediate interaction with the cytoskeleton and with signalling proteins.The VWA domains present in the alpha subunits of integrins seem to be a chordate specific radiation of the gene family being found only in vertebrates. They mediate protein-protein interactions.


Pssm-ID: 238746  Cd Length: 177  Bit Score: 47.74  E-value: 1.66e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230547 240 MNIFIVLDTSKSVGQNRFDEAKSasilFIEK-MSNYDIKPRYC---IISYASKAISVVSLRD-PDSNNADAVMEHLEEFQ 314
Cdd:cd01469    1 MDIVFVLDGSGSIYPDDFQKVKN----FLSTvMKKLDIGPTKTqfgLVQYSESFRTEFTLNEyRTKEEPLSLVKHISQLL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230547 315 YDrhedkqgTNTRAALHAIYEHLIEQELAYEREGKKedfmkihnVILLMTDGKFNmgGDPRE-------EMKLIKRFLdV 387
Cdd:cd01469   77 GL-------TNTATAIQYVVTELFSESNGARKDATK--------VLVVITDGESH--DDPLLkdvipqaEREGIIRYA-I 138
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 148230547 388 GIRKDNPREEYLDvyvfglgsdidqpEINDLASKKeKEVHTFHLQNVEKMKE 439
Cdd:cd01469  139 GVGGHFQRENSRE-------------ELKTIASKP-PEEHFFNVTDFAALKD 176
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
240-383 3.63e-06

Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a target cell. In association with invasion, T. gondii sequentially discharges three sets of secretory organelles beginning with the micronemes, which contain adhesive proteins involved in parasite attachment to a host cell. Deployed as protein complexes, several micronemal proteins possess vertebrate-derived adhesive sequences that function in binding receptors. The VWA domain likely mediates the protein-protein interactions of these with their interacting partners.


Pssm-ID: 238748  Cd Length: 186  Bit Score: 46.61  E-value: 3.63e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230547 240 MNIFIVLDTSKSVG-QNRFDEAKSASILFIEKM--SNYDIkpRYCIISYASKAISVVSLRDPDSNNAD---AVMEHLEEF 313
Cdd:cd01471    1 LDLYLLVDGSGSIGySNWVTHVVPFLHTFVQNLniSPDEI--NLYLVTFSTNAKELIRLSSPNSTNKDlalNAIRALLSL 78
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148230547 314 QYdrhedKQG-TNTRAALHAIYEHLieqelaYEREGKKEDFMKIhnvILLMTDGKFNMGGDPREEMKLIKR 383
Cdd:cd01471   79 YY-----PNGsTNTTSALLVVEKHL------FDTRGNRENAPQL---VIIMTDGIPDSKFRTLKEARKLRE 135
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
241-441 3.25e-05

VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains. Not much is known about the function of the VWA domain in these proteins. The members do have a conserved MIDAS motif. The biochemical function however is not known.


Pssm-ID: 238742  Cd Length: 170  Bit Score: 43.80  E-value: 3.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230547 241 NIFIVLDTSKSVGQNRFDEAKSASILFIEKMSNYDikpRYCIISYASKA---ISVVSLRDPDSNnADAVmehleefqyDR 317
Cdd:cd01465    2 NLVFVIDRSGSMDGPKLPLVKSALKLLVDQLRPDD---RLAIVTYDGAAetvLPATPVRDKAAI-LAAI---------DR 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230547 318 HEDKQGTNTRAALhaiyehlieqELAYErEGKKEDFMKIHNVILLMTDGKFNMG-GDPREEMKLIKRFLDVGIRkdnpre 396
Cdd:cd01465   69 LTAGGSTAGGAGI----------QLGYQ-EAQKHFVPGGVNRILLATDGDFNVGeTDPDELARLVAQKRESGIT------ 131
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 148230547 397 eyldVYVFGLGSDIDQPEINDLASKKEKevHTFHLQNVEKMKEFF 441
Cdd:cd01465  132 ----LSTLGFGDNYNEDLMEAIADAGNG--NTAYIDNLAEARKVF 170
Sushi pfam00084
Sushi domain (SCR repeat);
142-195 5.23e-05

Sushi domain (SCR repeat);


Pssm-ID: 249573  Cd Length: 56  Bit Score: 41.80  E-value: 5.23e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 148230547  142 CPNPGIPIGASKS--GSSYKMENKVSYNCQQGLVMFGSKERECLEDKSWSGTEPSC 195
Cdd:pfam00084   1 CPAPPPIPHGVISttKNSYQVGSVVRYECDPGYVLVGSSVITCQDDGTWSPPLPEC 56
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
24-72 4.40e-04

Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat (SCR); The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. A missense mutation in seventh CCP domain causes deficiency of the b subunit of factor XIII.


Pssm-ID: 214478  Cd Length: 56  Bit Score: 39.05  E-value: 4.40e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 148230547    24 AIIGGSYTVSDGG-NVGSKVEYQCPKGKYPYPKYTRECQYNGFWTDQKAK 72
Cdd:smart00032   6 DIENGTVTSSSGTySYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPT 55
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
242-367 8.36e-04

Collagen: The extracellular matrix represents a complex alloy of variable members of diverse protein families defining structural integrity and various physiological functions. The most abundant family is the collagens with more than 20 different collagen types identified thus far. Collagens are centrally involved in the formation of fibrillar and microfibrillar networks of the extracellular matrix, basement membranes as well as other structures of the extracellular matrix. Some collagens have about 15-18 vWA domains in them. The VWA domains present in these collagens mediate protein-protein interactions.


Pssm-ID: 238759  Cd Length: 164  Bit Score: 39.58  E-value: 8.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230547 242 IFIVlDTSKSVGQNRFDEAKSasilFIEKM-SNYDI---KPRYCIISYASkaisvvslrDPDS-------NNADAVMEHL 310
Cdd:cd01482    4 VFLV-DGSWSIGRSNFNLVRS----FLSSVvEAFEIgpdGVQVGLVQYSD---------DPRTefdlnayTSKEDVLAAI 69
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 148230547 311 EEFQYdrhedKQG-TNTRAALhaiyEHLIEQELAyEREGKKEDFMKihnVILLMTDGK 367
Cdd:cd01482   70 KNLPY-----KGGnTRTGKAL----THVREKNFT-PDAGARPGVPK---VVILITDGK 114
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
241-420 2.93e-03

vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- two heavy chains and one light chain (bikunin). Bikunin confers the protease-inhibitor function while the heavy chains are involved in rendering stability to the extracellular matrix by binding to hyaluronic acid. The heavy chains carry the VWA domain with a conserved MIDAS motif. Although the exact role of the VWA domains remains unknown, it has been speculated to be involved in mediating protein-protein interactions with the components of the extracellular matrix.


Pssm-ID: 238738  Cd Length: 171  Bit Score: 37.96  E-value: 2.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230547 241 NIFIVLDTSKSVGQNRFDEAKSASILFIEKMSNYDikpRYCIISYASkaiSVVSLRD-PDSNNADAV---MEHLEEFQYD 316
Cdd:cd01461    4 EVVFVIDTSGSMSGTKIEQTKEALLTALKDLPPGD---YFNIIGFSD---TVEEFSPsSVSATAENVaaaIEYVNRLQAL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230547 317 rhedkQGTNTRAALHAIYEHLIeqelayeregkkedfmKIHNV---ILLMTDGKFnmgGDPREEMKLIKRFLDVGIRkdn 393
Cdd:cd01461   78 -----GGTNMNDALEAALELLN----------------SSPGSvpqIILLTDGEV---TNESQILKNVREALSGRIR--- 130
                        170       180
                 ....*....|....*....|....*..
gi 148230547 394 preeyldVYVFGLGSDIDQPEINDLAS 420
Cdd:cd01461  131 -------LFTFGIGSDVNTYLLERLAR 150
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
242-440 3.69e-03

VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and matrix-matrix interactions thereby providing tissue integrity. Some members of the matrilin family are expressed specifically in developing cartilage rudiments. The matrilin family consists of at least four members. All the members of the matrilin family contain VWA domains, EGF-like domains and a heptad repeat coiled-coiled domain at the carboxy terminus which is responsible for the oligomerization of the matrilins. The VWA domains have been shown to be essential for matrilin network formation by interacting with matrix ligands.


Pssm-ID: 238752 [Multi-domain]  Cd Length: 224  Bit Score: 38.13  E-value: 3.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230547 242 IFIVlDTSKSVGQNRFDEAKSASILFIEKMsnyDIKP---RYCIISYASKAISVVSL----RDPDSNNADAVMEHLEefq 314
Cdd:cd01475    6 VFLI-DSSRSVRPENFELVKQFLNQIIDSL---DVGPdatRVGLVQYSSTVKQEFPLgrfkSKADLKRAVRRMEYLE--- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230547 315 ydrhedkQGTNTRAALhaiyEHLIEQELAyEREGKKEDFMKIHNVILLMTDGKfnmggdPREemklikrflDVGIRKDNP 394
Cdd:cd01475   79 -------TGTMTGLAI----QYAMNNAFS-EAEGARPGSERVPRVGIVVTDGR------PQD---------DVSEVAAKA 131
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 148230547 395 REEYLDVYVFGLGSdIDQPEINDLASKKEKEvHTFHLQNVEKMKEF 440
Cdd:cd01475  132 RALGIEMFAVGVGR-ADEEELREIASEPLAD-HVFYVEDFSTIEEL 175
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
474-731 7.19e-42

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 [Multi-domain]  Cd Length: 229  Bit Score: 152.45  E-value: 7.19e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230547   474 FPWIVKITITHNGiQYCKGTILSQYFILTAAHCFDLDDKTQ--------KIHVKIDGKEYLVKDFYRHPKYDPiskkdkg 545
Cdd:smart00020  13 FPWQVSLQYGGGR-HFCGGSLISPRWVLTAAHCVRGSDPSNirvrlgshDLSSGEEGQVIKVSKVIIHPNYNP------- 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230547   546 ikRAFDYDVALLELQRndKIEFSENARPICIPCTQGTAqalkQPGAPCSshektllseeevkavfIA-------EESNKP 618
Cdd:smart00020  85 --STYDNDIALLKLKE--PVTLSDNVRPICLPSSNYNV----PAGTTCT----------------VSgwgrtseGAGSLP 140
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230547   619 MKEMHVLIKRgQKRSACLEAAKKAPelknvtniedAVTDQFLCTGGIVPVADPpvCKGDSGGPLLIQvKRRYVQVGIISW 698
Cdd:smart00020 141 DTLQEVNVPI-VSNATCRRAYSGGG----------AITDNMLCAGGLEGGKDA--CQGDSGGPLVCN-DGRWVLVGIVSW 206
                          250       260       270
                   ....*....|....*....|....*....|...
gi 148230547   699 GtvDHCDkgtrikqtQKNARDFYQDIFKVLPWI 731
Cdd:smart00020 207 G--SGCA--------RPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
474-731 2.45e-28

Trypsin;


Pssm-ID: 249578 [Multi-domain]  Cd Length: 219  Bit Score: 113.69  E-value: 2.45e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230547  474 FPWIVKITITHNGIQyCKGTILSQYFILTAAHCFDLDDKTQ-----KIHVKIDGKE--YLVKDFYRHPKYDPiskkdkgi 546
Cdd:pfam00089  12 FPWQVSLQVSSGKHF-CGGSLISENWVLTAAHCVSNAKSVRvvlgaHNIVLREGGEqkFDVEKIIVHPNYNP-------- 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230547  547 kRAFDYDVALLELqrNDKIEFSENARPICIPctqgTAQALKQPGAPCsshektllseeevkavFIA----EESNKPMKEM 622
Cdd:pfam00089  83 -DTLDNDIALLKL--KSPVTLGDTVRPICLP----TASSDLPVGTTC----------------TVSgwgnTKTLGLSDTL 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230547  623 HVLIKRGQKRSACLEAAKkapelknvtnieDAVTDQFLCTGGIVPVAdppvCKGDSGGPLLiqVKRRYVQvGIISWGtvD 702
Cdd:pfam00089 140 QEVTVPVVSRETCRSAYG------------GTVTDTMICAGAGGKDA----CQGDSGGPLV--CSDGELI-GIVSWG--Y 198
                         250       260
                  ....*....|....*....|....*....
gi 148230547  703 HCDKGTRIkqtqknarDFYQDIFKVLPWI 731
Cdd:pfam00089 199 GCASGNKP--------GVYTPVSSYLDWI 219
PHA02927 PHA02927
secreted complement-binding protein; Provisional
35-195 1.56e-15

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 76.23  E-value: 1.56e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230547  35 GGNVGSKVEYQCPKGKYPYPKYTRECQ--YNGFWTDQKAKTICKDVRCPRPVTFEDGDYEPRQPFYKVGDTLYFECYSGF 112
Cdd:PHA02927 101 GVDFGSSITYSCNSGYQLIGESKSYCElgSTGSMVWNPEAPICESVKCQSPPSISNGRHNGYEDFYTDGSVVTYSCNSGY 180
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230547 113 TMKGPQNRTCQeNAKWTGETTiCDDNNgyCPNPGIPIGASKSG--SSYKMENKVSYNCQQGLVMFGSKERECLEDKSWSG 190
Cdd:PHA02927 181 SLIGNSGVLCS-GGEWSDPPT-CQIVK--CPHPTISNGYLSSGfkRSYSYNDNVDFKCKYGYKLSGSSSSTCSPGNTWQP 256

                 ....*
gi 148230547 191 TEPSC 195
Cdd:PHA02927 257 ELPKC 261
PHA02639 PHA02639
EEV host range protein; Provisional
38-195 3.81e-09

EEV host range protein; Provisional


Pssm-ID: 165022 [Multi-domain]  Cd Length: 295  Bit Score: 57.37  E-value: 3.81e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230547  38 VGSKVEYQCPKGKYPYPKYTREC---QYNGFWTDQKAKTICKDvrCPRPVTFEDGDYEPRQPFYKVGDTLYFEC--YSG- 111
Cdd:PHA02639  42 IGKLIEYTCNTDYALIGDRFRTCikdKNNAIWSNKAPFCMLKE--CNDPPSIINGKIYNKREMYKVGDEIYYVCneHKGv 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230547 112 -FTMKGPQNRTCQENAKWTGETTICDDNNgyCPNPGIP---IGASKSGSSYKMENKVSYNCQQGLVMFGSKERECLEDKS 187
Cdd:PHA02639 120 qYSLVGNEKITCIQDKSWKPDPPICKMIN--CRFPALQngyINGIPSNKKFYYKTRVGFSCKSGFDLVGEKYSTCNINAT 197

                 ....*...
gi 148230547 188 WSGTEPSC 195
Cdd:PHA02639 198 WFPSIPTC 205
PHA02817 PHA02817
EEV Host range protein; Provisional
75-195 2.22e-07

EEV Host range protein; Provisional


Pssm-ID: 165167 [Multi-domain]  Cd Length: 225  Bit Score: 51.09  E-value: 2.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230547  75 CKDVRCPRPVTFEDGDYEPRQPFYKVGDTLYFECYSG-----FTMKGPQNRTCQENAKWTGETTICDD--------NNGY 141
Cdd:PHA02817  19 CDLNKCCYPPSIKNGYIYNKKTEYNIGSNVTFFCGNNtrgvrYTLVGEKNIICEKDGKWNKEFPVCKIircrfpalQNGF 98
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 148230547 142 CPnpGIPigaskSGSSYKMENKVSYNCQQGLVMFGSKERECLEDKSWSGTEPSC 195
Cdd:PHA02817  99 VN--GIP-----DSKKFYYESEVSFSCKPGFVLIGTKYSVCGINSSWIPKVPIC 145
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
474-699 1.13e-06

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


Pssm-ID: 227927 [Multi-domain]  Cd Length: 413  Bit Score: 50.26  E-value: 1.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230547 474 FPWIVKITIT---HNGIQYCKGTILSQYFILTAAHCFDLDD--KTQKIHVKID------GKEYLVKDFYRHPKYDPISK- 541
Cdd:COG5640   44 YPSLVALVDRisdYVSGTFCGGSKLGGRYVLTAAHCADASSpiSSDVNRVVVDlndssqAERGHVRTIYVHEFYSPGNLg 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230547 542 KDKGIKRAFDYDVALLE-LQRNDKIEFSENARPICIPCTQGTAQALKQPGAPCSSHEKTLLSEEEVKAVFIAEESNKpmk 620
Cdd:COG5640  124 NDIAVLELARAASLPRVkITSFDASDTFLNSVTTVSPMTNGTFGVTTPSDVPRSSPKGTILHEVAVLFVPLSTCAQY--- 200
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230547 621 emhvlikrgqkrSACLEAAKKAPELKNVTniedavtdqflctggivpVADPP--VCKGDSGGPLLIQVKRRYVQVGIISW 698
Cdd:COG5640  201 ------------KGCANASDGATGLTGFC------------------AGRPPkdACQGDSGGPIFHKGEEGRVQRGVVSW 250

                 .
gi 148230547 699 G 699
Cdd:COG5640  251 G 251
PHA02639 PHA02639
EEV host range protein; Provisional
76-196 6.44e-05

EEV host range protein; Provisional


Pssm-ID: 165022 [Multi-domain]  Cd Length: 295  Bit Score: 44.27  E-value: 6.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230547  76 KDVRCPRPVTFEDGDYEPRQPFYKVGDTLYFECYSGFTMKGPQNRTC---QENAKWTGETTICDDNNGYCPNPGIPIGAS 152
Cdd:PHA02639  18 KSIYCDKPDDISNGFITELMEKYEIGKLIEYTCNTDYALIGDRFRTCikdKNNAIWSNKAPFCMLKECNDPPSIINGKIY 97
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 148230547 153 KSGSSYKMENKVSYNCQQ----GLVMFGSKERECLEDKSWSGTEPSCR 196
Cdd:PHA02639  98 NKREMYKVGDEIYYVCNEhkgvQYSLVGNEKITCIQDKSWKPDPPICK 145
PHA02954 PHA02954
EEV membrane glycoprotein; Provisional
55-195 6.93e-05

EEV membrane glycoprotein; Provisional


Pssm-ID: 165263 [Multi-domain]  Cd Length: 317  Bit Score: 44.31  E-value: 6.93e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230547  55 KYTRECQYNG--FWTDQkakTICKDVRCpRPVTFEDGDYEPRQPFYKVGDTLYFECYSGFTMKGPQNRTCQENAkWTget 132
Cdd:PHA02954 106 KYFRCEEKNGntSWNDT---VTCPNAEC-QPLQLEHGSCQPVKEKYSFGEHITINCDVGYEVIGASYISCTANS-WN--- 177
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148230547 133 tICDDNNGYCPNPGIPIGASkSGSSYKMENKVSYNCQQGLVMFGSKERECLEDKsWSGTEPSC 195
Cdd:PHA02954 178 -VIPSCQQKCDIPSLSNGLI-SGSTFSIGGVIHLSCKSGFTLTGSPSSTCIDGK-WNPVLPIC 237
PHA02831 PHA02831
EEV host range protein; Provisional
41-195 1.60e-04

EEV host range protein; Provisional


Pssm-ID: 165176 [Multi-domain]  Cd Length: 268  Bit Score: 42.67  E-value: 1.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230547  41 KVEYQCpkgKYPYPKYTRECQyNGFWTDQK---AKTICKDvrcprPVTFEDGDYEPRQPFYKVGDTLYFEC----YSGFT 113
Cdd:PHA02831  45 NLEYKC---NNNFDKVFVTCN-NGSWSTKNmciGKRNCKD-----PVTILNGYIKNKKDQYSFGDSVTYACkvnkLEKYS 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230547 114 MKGPQNRTCQeNAKWTGETTICDDNNgyCPNPGIPIGASKS-GSSYKMENKVSYNCQQGLVMFGSKERECLEDKSWSGTE 192
Cdd:PHA02831 116 IVGNETVKCI-NKQWVPKYPVCKLIR--CKYPALQNGFLNVfEKKFYYGDIVNFKCKKGFILLGSSVSTCDINSIWYPGI 192

                 ...
gi 148230547 193 PSC 195
Cdd:PHA02831 193 PKC 195
PHA02817 PHA02817
EEV Host range protein; Provisional
1-139 7.56e-04

EEV Host range protein; Provisional


Pssm-ID: 165167 [Multi-domain]  Cd Length: 225  Bit Score: 40.31  E-value: 7.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230547   1 MLLLLLITHVSVSlavqCDLTKVAII-----GGSYTVSDGGNVGSKVEYQCPKGKYPYPkYTR------ECQYNGFWtdQ 69
Cdd:PHA02817   6 MLLILLCNKVYSL----CDLNKCCYPpsiknGYIYNKKTEYNIGSNVTFFCGNNTRGVR-YTLvgekniICEKDGKW--N 78
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148230547  70 KAKTICKDVRCPRPVT---FEDGDYEPRQPFYKvgDTLYFECYSGFTMKGPQNRTCQENAKWTGETTICDDNN 139
Cdd:PHA02817  79 KEFPVCKIIRCRFPALqngFVNGIPDSKKFYYE--SEVSFSCKPGFVLIGTKYSVCGINSSWIPKVPICSRDN 149
PHA02831 PHA02831
EEV host range protein; Provisional
34-128 2.86e-03

EEV host range protein; Provisional


Pssm-ID: 165176 [Multi-domain]  Cd Length: 268  Bit Score: 38.82  E-value: 2.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148230547  34 DGGNVGSKVEYQCPKGKYPypKY------TRECqYNGFWTDQKAktICKDVRCPRPvTFEDGDYEPRQPFYKVGDTLYFE 107
Cdd:PHA02831  94 DQYSFGDSVTYACKVNKLE--KYsivgneTVKC-INKQWVPKYP--VCKLIRCKYP-ALQNGFLNVFEKKFYYGDIVNFK 167
                         90       100
                 ....*....|....*....|.
gi 148230547 108 CYSGFTMKGPQNRTCQENAKW 128
Cdd:PHA02831 168 CKKGFILLGSSVSTCDINSIW 188
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.14
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A et al. (2009), "CDD: specific functional annotation with the Conserved Domain Database.", Nucleic Acids Res.37(D)205-10.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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