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Conserved domains on  [gi|239781746]
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Chain L, COMPLEMENT FACTOR B

Protein Classification

Graphical summary

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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 ...
 10-207 3.23e-114

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 [Multi-domain]  Cd Length: 198  Bit Score: 335.41  E-value: 3.23e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239781746  10 MNIYLVLDGSDSIGASNFTGAKKCLVNLIEKVASYGVKPRYGLVTYATYPKIWVKVSEADSSNADWVTKQLNEINYEDHK 89
Cdd:cd01470    1 LNIYIALDASDSIGEEDFDEAKNAIKTLIEKISSYEVSPRYEIISYASDPKEIVSIRDFNSNDADDVIKRLEDFNYDDHG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239781746  90 LKSGTNTKKALQAVYSMMSWPDDVPPEGWNRTRHVIILMTDGLHNMGGDPITVIDEIRDLLYIGKDRKNPREDYLDVYVF 169
Cdd:cd01470   81 DKTGTNTAAALKKVYERMALEKVRNKEAFNETRHVIILFTDGKSNMGGSPLPTVDKIKNLVYKNNKSDNPREDYLDVYVF 160

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 239781746 170 GVGPLVNQVNINALASKKDNEQHVFKVKDMENLEDVFY 207
Cdd:cd01470  161 GVGDDVNKEELNDLASKKDNERHFFKLKDYEDLQEVFD 198
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 229-496 5.27e-49

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: 168.22  E-value: 5.27e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239781746 229 TDYHKQPWQAKIsviRPSKGHESCMGAVVSEYFVLTAAHCFtVDDKEHSIKVSVG--------GEKRDLEIEVVLFHPNY 300
Cdd:cd00190    7 AKIGSFPWQVSL---QYTGGRHFCGGSLISPRWVLTAAHCV-YSSAPSNYTVRLGshdlssneGGGQVIKVKKVIVHPNY 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239781746 301 NingkkeagiPEFYDYDVALIKLKNKLKYGQTIRPICLPCTEGTtralrLPPTTTCQqqkeellpaqdikalfVS----- 375
Cdd:cd00190   83 N---------PSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYN-----LPAGTTCT----------------VSgwgrt 132

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239781746 376 EEEKKLTR--KEVYIKNGDKKgSCERDAQYAPgydkvkdiseVVTPRFLCTGGvsPYADPNTCRGDSGGPLIVHKRSRFI 453
Cdd:cd00190  133 SEGGPLPDvlQEVNVPIVSNA-ECKRAYSYGG----------TITDNMLCAGG--LEGGKDACQGDSGGPLVCNDNGRGV 199

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 239781746 454 QVGVISWGVvdVCknqkRQKQVPAhardFHINLFQVLPWLKEK 496
Cdd:cd00190  200 LVGIVSWGS--GC----ARPNYPG----VYTRVSSYLDWIQKT 232
 
Name Accession Description Interval E-value
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
 10-207 3.23e-114

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 [Multi-domain]  Cd Length: 198  Bit Score: 335.41  E-value: 3.23e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239781746  10 MNIYLVLDGSDSIGASNFTGAKKCLVNLIEKVASYGVKPRYGLVTYATYPKIWVKVSEADSSNADWVTKQLNEINYEDHK 89
Cdd:cd01470    1 LNIYIALDASDSIGEEDFDEAKNAIKTLIEKISSYEVSPRYEIISYASDPKEIVSIRDFNSNDADDVIKRLEDFNYDDHG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239781746  90 LKSGTNTKKALQAVYSMMSWPDDVPPEGWNRTRHVIILMTDGLHNMGGDPITVIDEIRDLLYIGKDRKNPREDYLDVYVF 169
Cdd:cd01470   81 DKTGTNTAAALKKVYERMALEKVRNKEAFNETRHVIILFTDGKSNMGGSPLPTVDKIKNLVYKNNKSDNPREDYLDVYVF 160

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 239781746 170 GVGPLVNQVNINALASKKDNEQHVFKVKDMENLEDVFY 207
Cdd:cd01470  161 GVGDDVNKEELNDLASKKDNERHFFKLKDYEDLQEVFD 198
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 229-496 5.27e-49

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: 168.22  E-value: 5.27e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239781746 229 TDYHKQPWQAKIsviRPSKGHESCMGAVVSEYFVLTAAHCFtVDDKEHSIKVSVG--------GEKRDLEIEVVLFHPNY 300
Cdd:cd00190    7 AKIGSFPWQVSL---QYTGGRHFCGGSLISPRWVLTAAHCV-YSSAPSNYTVRLGshdlssneGGGQVIKVKKVIVHPNY 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239781746 301 NingkkeagiPEFYDYDVALIKLKNKLKYGQTIRPICLPCTEGTtralrLPPTTTCQqqkeellpaqdikalfVS----- 375
Cdd:cd00190   83 N---------PSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYN-----LPAGTTCT----------------VSgwgrt 132

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239781746 376 EEEKKLTR--KEVYIKNGDKKgSCERDAQYAPgydkvkdiseVVTPRFLCTGGvsPYADPNTCRGDSGGPLIVHKRSRFI 453
Cdd:cd00190  133 SEGGPLPDvlQEVNVPIVSNA-ECKRAYSYGG----------TITDNMLCAGG--LEGGKDACQGDSGGPLVCNDNGRGV 199

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 239781746 454 QVGVISWGVvdVCknqkRQKQVPAhardFHINLFQVLPWLKEK 496
Cdd:cd00190  200 LVGIVSWGS--GC----ARPNYPG----VYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 229-462 1.18e-45

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: 159.38  E-value: 1.18e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239781746   229 TDYHKQPWQAKIsviRPSKGHESCMGAVVSEYFVLTAAHCFTvDDKEHSIKVSVG-------GEKRDLEIEVVLFHPNYN 301
Cdd:smart00020   8 ANIGSFPWQVSL---QYGGGRHFCGGSLISPRWVLTAAHCVR-GSDPSNIRVRLGshdlssgEEGQVIKVSKVIIHPNYN 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239781746   302 ingkkeagiPEFYDYDVALIKLKNKLKYGQTIRPICLPCTegttrALRLPPTTTCQqqkeellpaqdikalfVS------ 375
Cdd:smart00020  84 ---------PSTYDNDIALLKLKEPVTLSDNVRPICLPSS-----NYNVPAGTTCT----------------VSgwgrts 133

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239781746   376 EEEKKLTR--KEVYIKNGDKKgSCERDAQYapgydkvkdiSEVVTPRFLCTGGvsPYADPNTCRGDSGGPLiVHKRSRFI 453
Cdd:smart00020 134 EGAGSLPDtlQEVNVPIVSNA-TCRRAYSG----------GGAITDNMLCAGG--LEGGKDACQGDSGGPL-VCNDGRWV 199


                   ....*....
gi 239781746   454 QVGVISWGV 462
Cdd:smart00020 200 LVGIVSWGS 208
Trypsin pfam00089
Trypsin;
232-493 9.69e-38

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 137.96  E-value: 9.69e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239781746  232 HKQPWQAKISVirpSKGHESCMGAVVSEYFVLTAAHCF------TVDDKEHSIKVSVGGEKRdLEIEVVLFHPNYNingk 305
Cdd:pfam00089  10 GSFPWQVSLQL---SSGKHFCGGSLISENWVLTAAHCVsgasdvKVVLGAHNIVLREGGEQK-FDVEKIIVHPNYN---- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239781746  306 keagiPEFYDYDVALIKLKNKLKYGQTIRPICLPCTEGTtralrLPPTTTCQQQKEELlpaqdikalfVSEEEKKLTRKE 385
Cdd:pfam00089  82 -----PDTLDNDIALLKLESPVTLGDTVRPICLPDASSD-----LPVGTTCTVSGWGN----------TKTLGPSDTLQE 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239781746  386 VYIKNGDkKGSCERdaqyapgydkvkDISEVVTPRFLCTGGVSPYAdpntCRGDSGGPLIVHKRsrfIQVGVISWGvvDV 465
Cdd:pfam00089 142 VTVPVVS-RETCRS------------AYGGTVTDTMICAGAGGKDA----CQGDSGGPLVCSDG---ELIGIVSWG--YG 199

                         250       260
                  ....*....|....*....|....*...
gi 239781746  466 CKNQKRqkqvpahaRDFHINLFQVLPWL 493
Cdd:pfam00089 200 CASGNY--------PGVYTPVSSYLDWI 219
VWA pfam00092
von Willebrand factor type A domain;
11-208 2.78e-32

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 121.61  E-value: 2.78e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239781746   11 NIYLVLDGSDSIGASNFTGAKKCLVNLIEKVASYGVKPRYGLVTYATYPKIWVKVSeaDSSNADWVTKQLNEINYEDHKL 90
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLN--DYSSKEELLSAVDNLRYLGGGT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239781746   91 KS-GTNTKKALQAVYSMMSWPDDvppegwnRTRHVIILMTDGlHNMGGDPITVIDEIRDllyigkdrknpreDYLDVYVF 169
Cdd:pfam00092  79 TNtGKALKYALENLFSSAAGARP-------GAPKVVVLLTDG-RSQDGDPEEVARELKS-------------AGVTVFAV 137

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 239781746  170 GVGPLVNQvNINALASKKDnEQHVFKVKDMENLEDVFYQ 208
Cdd:pfam00092 138 GVGNADDE-ELRKIASEPG-EGHVFTVSDFEALEDLQDQ 174
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 11-204 6.80e-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 [Multi-domain]  Cd Length: 175  Bit Score: 109.47  E-value: 6.80e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239781746    11 NIYLVLDGSDSIGASNFTGAKKCLVNLIEKVASYGVKPRYGLVTYATYPKIWVKVSeaDSSNADWVTKQLNEINYedhKL 90
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLN--DSRSKDALLEALASLSY---KL 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239781746    91 KSGTNTKKALQAVYSMMSwpddVPPEGWNR-TRHVIILMTDGLHNMGGDPItvIDEIRDLlyigkdrknpREDYLDVYVF 169
Cdd:smart00327  76 GGGTNLGAALQYALENLF----SKSAGSRRgAPKVVILITDGESNDGPKDL--LKAAKEL----------KRSGVKVFVV 139

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 239781746   170 GVGPLVNQVNINALASKKDNEqHVFKVKDMENLED 204
Cdd:smart00327 140 GVGNDVDEEELKKLASAPGGV-YVFLPELLDLLID 173
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 235-461 1.08e-19

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 88.55  E-value: 1.08e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239781746 235 PWQAKISVIRPSKGHeSCMGAVVSEYFVLTAAHCfTVDDKEHSIKVSVGGEKRD------LEIEVVLFHPNYNingkkea 308
Cdd:COG5640   43 PWMVALQSSNGPSGQ-FCGGTLIAPRWVLTAAHC-VDGDGPSDLRVVIGSTDLStsggtvVKVARIVVHPDYD------- 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239781746 309 giPEFYDYDVALIKLKnklkygqtiRPIclpcteGTTRALRLPPTTTcqqqkeelLPAQDIKALFV-----SEEEKKL-- 381
Cdd:COG5640  114 --PATPGNDIALLKLA---------TPV------PGVAPAPLATSAD--------AAAPGTPATVAgwgrtSEGPGSQsg 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239781746 382 TRKEVYIKNGDkkgscERDAQYAPGYDkvkdisevvTPRFLCTGGVSPYADpnTCRGDSGGPLIVHKRSRFIQVGVISWG 461
Cdd:COG5640  169 TLRKADVPVVS-----DATCAAYGGFD---------GGTMLCAGYPEGGKD--ACQGDSGGPLVVKDGGGWVLVGVVSWG 232
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 5-206 9.03e-09

vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and metabolism];


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 56.49  E-value: 9.03e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239781746   5 DPSGSMNIYLVLDGSDSIGASN-FTGAKKCLVNLIEkvaSYGVKPRYGLVTYATYPKIWVKVSeadsSNADWVTKQLNEI 83
Cdd:COG1240   88 RPQRGRDVVLVVDASGSMAAENrLEAAKGALLDFLD---DYRPRDRVGLVAFGGEAEVLLPLT----RDREALKRALDEL 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239781746  84 nyedhKLKSGTNTKKALQAVYSMMswpDDVPPEGwnrtRHVIILMTDGLHNMG-GDPITVIDEIrdllyigkdrknpRED 162
Cdd:COG1240  161 -----PPGGGTPLGDALALALELL---KRADPAR----RKVIVLLTDGRDNAGrIDPLEAAELA-------------AAA 215

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 239781746 163 YLDVYVFGVG-PLVNQVNINALAskkdnEQ---HVFKVKDMENLEDVF 206
Cdd:COG1240  216 GIRIYTIGVGtEAVDEGLLREIA-----EAtggRYFRADDLSELAAIY 258
 
Name Accession Description Interval E-value
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
 10-207 3.23e-114

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 [Multi-domain]  Cd Length: 198  Bit Score: 335.41  E-value: 3.23e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239781746  10 MNIYLVLDGSDSIGASNFTGAKKCLVNLIEKVASYGVKPRYGLVTYATYPKIWVKVSEADSSNADWVTKQLNEINYEDHK 89
Cdd:cd01470    1 LNIYIALDASDSIGEEDFDEAKNAIKTLIEKISSYEVSPRYEIISYASDPKEIVSIRDFNSNDADDVIKRLEDFNYDDHG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239781746  90 LKSGTNTKKALQAVYSMMSWPDDVPPEGWNRTRHVIILMTDGLHNMGGDPITVIDEIRDLLYIGKDRKNPREDYLDVYVF 169
Cdd:cd01470   81 DKTGTNTAAALKKVYERMALEKVRNKEAFNETRHVIILFTDGKSNMGGSPLPTVDKIKNLVYKNNKSDNPREDYLDVYVF 160

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 239781746 170 GVGPLVNQVNINALASKKDNEQHVFKVKDMENLEDVFY 207
Cdd:cd01470  161 GVGDDVNKEELNDLASKKDNERHFFKLKDYEDLQEVFD 198
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 229-496 5.27e-49

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: 168.22  E-value: 5.27e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239781746 229 TDYHKQPWQAKIsviRPSKGHESCMGAVVSEYFVLTAAHCFtVDDKEHSIKVSVG--------GEKRDLEIEVVLFHPNY 300
Cdd:cd00190    7 AKIGSFPWQVSL---QYTGGRHFCGGSLISPRWVLTAAHCV-YSSAPSNYTVRLGshdlssneGGGQVIKVKKVIVHPNY 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239781746 301 NingkkeagiPEFYDYDVALIKLKNKLKYGQTIRPICLPCTEGTtralrLPPTTTCQqqkeellpaqdikalfVS----- 375
Cdd:cd00190   83 N---------PSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYN-----LPAGTTCT----------------VSgwgrt 132

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239781746 376 EEEKKLTR--KEVYIKNGDKKgSCERDAQYAPgydkvkdiseVVTPRFLCTGGvsPYADPNTCRGDSGGPLIVHKRSRFI 453
Cdd:cd00190  133 SEGGPLPDvlQEVNVPIVSNA-ECKRAYSYGG----------TITDNMLCAGG--LEGGKDACQGDSGGPLVCNDNGRGV 199

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 239781746 454 QVGVISWGVvdVCknqkRQKQVPAhardFHINLFQVLPWLKEK 496
Cdd:cd00190  200 LVGIVSWGS--GC----ARPNYPG----VYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 229-462 1.18e-45

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: 159.38  E-value: 1.18e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239781746   229 TDYHKQPWQAKIsviRPSKGHESCMGAVVSEYFVLTAAHCFTvDDKEHSIKVSVG-------GEKRDLEIEVVLFHPNYN 301
Cdd:smart00020   8 ANIGSFPWQVSL---QYGGGRHFCGGSLISPRWVLTAAHCVR-GSDPSNIRVRLGshdlssgEEGQVIKVSKVIIHPNYN 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239781746   302 ingkkeagiPEFYDYDVALIKLKNKLKYGQTIRPICLPCTegttrALRLPPTTTCQqqkeellpaqdikalfVS------ 375
Cdd:smart00020  84 ---------PSTYDNDIALLKLKEPVTLSDNVRPICLPSS-----NYNVPAGTTCT----------------VSgwgrts 133

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239781746   376 EEEKKLTR--KEVYIKNGDKKgSCERDAQYapgydkvkdiSEVVTPRFLCTGGvsPYADPNTCRGDSGGPLiVHKRSRFI 453
Cdd:smart00020 134 EGAGSLPDtlQEVNVPIVSNA-TCRRAYSG----------GGAITDNMLCAGG--LEGGKDACQGDSGGPL-VCNDGRWV 199


                   ....*....
gi 239781746   454 QVGVISWGV 462
Cdd:smart00020 200 LVGIVSWGS 208
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 10-194 2.91e-39

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 [Multi-domain]  Cd Length: 161  Bit Score: 140.12  E-value: 2.91e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239781746  10 MNIYLVLDGSDSIGASNFTGAKKCLVNLIEKVASYGVKPRYGLVTYATYPKIWVKVSeaDSSNADWVTKQLNEINYEDHk 89
Cdd:cd01450    1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLN--DYKSKDDLLKAVKNLKYLGG- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239781746  90 lkSGTNTKKALQAVYSMMSWPDdvppEGWNRTRHVIILMTDGLHNMGGDPITVIDEIRDLlyigkdrknpredYLDVYVF 169
Cdd:cd01450   78 --GGTNTGKALQYALEQLFSES----NARENVPKVIIVLTDGRSDDGGDPKEAAAKLKDE-------------GIKVFVV 138

                        170       180
                 ....*....|....*....|....*
gi 239781746 170 GVGPlVNQVNINALASKKdNEQHVF 194
Cdd:cd01450  139 GVGP-ADEEELREIASCP-SERHVF 161
Trypsin pfam00089
Trypsin;
232-493 9.69e-38

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 137.96  E-value: 9.69e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239781746  232 HKQPWQAKISVirpSKGHESCMGAVVSEYFVLTAAHCF------TVDDKEHSIKVSVGGEKRdLEIEVVLFHPNYNingk 305
Cdd:pfam00089  10 GSFPWQVSLQL---SSGKHFCGGSLISENWVLTAAHCVsgasdvKVVLGAHNIVLREGGEQK-FDVEKIIVHPNYN---- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239781746  306 keagiPEFYDYDVALIKLKNKLKYGQTIRPICLPCTEGTtralrLPPTTTCQQQKEELlpaqdikalfVSEEEKKLTRKE 385
Cdd:pfam00089  82 -----PDTLDNDIALLKLESPVTLGDTVRPICLPDASSD-----LPVGTTCTVSGWGN----------TKTLGPSDTLQE 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239781746  386 VYIKNGDkKGSCERdaqyapgydkvkDISEVVTPRFLCTGGVSPYAdpntCRGDSGGPLIVHKRsrfIQVGVISWGvvDV 465
Cdd:pfam00089 142 VTVPVVS-RETCRS------------AYGGTVTDTMICAGAGGKDA----CQGDSGGPLVCSDG---ELIGIVSWG--YG 199

                         250       260
                  ....*....|....*....|....*...
gi 239781746  466 CKNQKRqkqvpahaRDFHINLFQVLPWL 493
Cdd:pfam00089 200 CASGNY--------PGVYTPVSSYLDWI 219
VWA pfam00092
von Willebrand factor type A domain;
11-208 2.78e-32

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 121.61  E-value: 2.78e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239781746   11 NIYLVLDGSDSIGASNFTGAKKCLVNLIEKVASYGVKPRYGLVTYATYPKIWVKVSeaDSSNADWVTKQLNEINYEDHKL 90
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLN--DYSSKEELLSAVDNLRYLGGGT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239781746   91 KS-GTNTKKALQAVYSMMSWPDDvppegwnRTRHVIILMTDGlHNMGGDPITVIDEIRDllyigkdrknpreDYLDVYVF 169
Cdd:pfam00092  79 TNtGKALKYALENLFSSAAGARP-------GAPKVVVLLTDG-RSQDGDPEEVARELKS-------------AGVTVFAV 137

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 239781746  170 GVGPLVNQvNINALASKKDnEQHVFKVKDMENLEDVFYQ 208
Cdd:pfam00092 138 GVGNADDE-ELRKIASEPG-EGHVFTVSDFEALEDLQDQ 174
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 11-204 6.80e-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 [Multi-domain]  Cd Length: 175  Bit Score: 109.47  E-value: 6.80e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239781746    11 NIYLVLDGSDSIGASNFTGAKKCLVNLIEKVASYGVKPRYGLVTYATYPKIWVKVSeaDSSNADWVTKQLNEINYedhKL 90
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLN--DSRSKDALLEALASLSY---KL 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239781746    91 KSGTNTKKALQAVYSMMSwpddVPPEGWNR-TRHVIILMTDGLHNMGGDPItvIDEIRDLlyigkdrknpREDYLDVYVF 169
Cdd:smart00327  76 GGGTNLGAALQYALENLF----SKSAGSRRgAPKVVILITDGESNDGPKDL--LKAAKEL----------KRSGVKVFVV 139

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 239781746   170 GVGPLVNQVNINALASKKDNEqHVFKVKDMENLED 204
Cdd:smart00327 140 GVGNDVDEEELKKLASAPGGV-YVFLPELLDLLID 173
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 11-194 3.56e-23

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 [Multi-domain]  Cd Length: 161  Bit Score: 95.71  E-value: 3.56e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239781746  11 NIYLVLDGSDSIGASNFTGAKKCLVNLIEKVASYGVKPRYGLVTYATYPKIWVKVSeaDSSNADWVTKQLNEINYedhKL 90
Cdd:cd00198    2 DIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLT--TDTDKADLLEAIDALKK---GL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239781746  91 KSGTNTKKALQAVYSMMSWPDDvppegwNRTRHVIILMTDGLHNmgGDPITVIDEIRDLlyigkdrknpREDYLDVYVFG 170
Cdd:cd00198   77 GGGTNIGAALRLALELLKSAKR------PNARRVIILLTDGEPN--DGPELLAEAAREL----------RKLGITVYTIG 138

                        170       180
                 ....*....|....*....|....
gi 239781746 171 VGPLVNQVNINALASkKDNEQHVF 194
Cdd:cd00198  139 IGDDANEDELKEIAD-KTTGGAVF 161
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 235-461 1.08e-19

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 88.55  E-value: 1.08e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239781746 235 PWQAKISVIRPSKGHeSCMGAVVSEYFVLTAAHCfTVDDKEHSIKVSVGGEKRD------LEIEVVLFHPNYNingkkea 308
Cdd:COG5640   43 PWMVALQSSNGPSGQ-FCGGTLIAPRWVLTAAHC-VDGDGPSDLRVVIGSTDLStsggtvVKVARIVVHPDYD------- 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239781746 309 giPEFYDYDVALIKLKnklkygqtiRPIclpcteGTTRALRLPPTTTcqqqkeelLPAQDIKALFV-----SEEEKKL-- 381
Cdd:COG5640  114 --PATPGNDIALLKLA---------TPV------PGVAPAPLATSAD--------AAAPGTPATVAgwgrtSEGPGSQsg 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239781746 382 TRKEVYIKNGDkkgscERDAQYAPGYDkvkdisevvTPRFLCTGGVSPYADpnTCRGDSGGPLIVHKRSRFIQVGVISWG 461
Cdd:COG5640  169 TLRKADVPVVS-----DATCAAYGGFD---------GGTMLCAGYPEGGKD--ACQGDSGGPLVVKDGGGWVLVGVVSWG 232
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 10-205 4.28e-09

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 [Multi-domain]  Cd Length: 177  Bit Score: 55.82  E-value: 4.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239781746  10 MNIYLVLDGSDSIGASNFTGAKKCLVNLIEKVASYGVKPRYGLVTYATYPKIWVKVSE-ADSSNADWVTKQLneinyedH 88
Cdd:cd01469    1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEyRTKEEPLSLVKHI-------S 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239781746  89 KLKSGTNTKKALQAVYSmmswpddvppEGWNRTR-------HVIILMTDGLHNMGGDPITVIDEirdllyigkdrknPRE 161
Cdd:cd01469   74 QLLGLTNTATAIQYVVT----------ELFSESNgarkdatKVLVVITDGESHDDPLLKDVIPQ-------------AER 130

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 239781746 162 DYLDVYVFGVGPLVNQVN----INALASKKDnEQHVFKVKDMENLEDV 205
Cdd:cd01469  131 EGIIRYAIGVGGHFQRENsreeLKTIASKPP-EEHFFNVTDFAALKDI 177
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 5-206 9.03e-09

vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and metabolism];


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 56.49  E-value: 9.03e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239781746   5 DPSGSMNIYLVLDGSDSIGASN-FTGAKKCLVNLIEkvaSYGVKPRYGLVTYATYPKIWVKVSeadsSNADWVTKQLNEI 83
Cdd:COG1240   88 RPQRGRDVVLVVDASGSMAAENrLEAAKGALLDFLD---DYRPRDRVGLVAFGGEAEVLLPLT----RDREALKRALDEL 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239781746  84 nyedhKLKSGTNTKKALQAVYSMMswpDDVPPEGwnrtRHVIILMTDGLHNMG-GDPITVIDEIrdllyigkdrknpRED 162
Cdd:COG1240  161 -----PPGGGTPLGDALALALELL---KRADPAR----RKVIVLLTDGRDNAGrIDPLEAAELA-------------AAA 215

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 239781746 163 YLDVYVFGVG-PLVNQVNINALAskkdnEQ---HVFKVKDMENLEDVF 206
Cdd:COG1240  216 GIRIYTIGVGtEAVDEGLLREIA-----EAtggRYFRADDLSELAAIY 258
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 10-176 7.70e-08

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 [Multi-domain]  Cd Length: 186  Bit Score: 52.39  E-value: 7.70e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239781746  10 MNIYLVLDGSDSIGASN-FTGAKKCLVNLIEKVASYGVKPRYGLVTYATYPKIWVKVSEADSSNAD---WVTKQLNEINY 85
Cdd:cd01471    1 LDLYLLVDGSGSIGYSNwVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSPNSTNKDlalNAIRALLSLYY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239781746  86 EdhklKSGTNTKKALQAV----YSMMSWPDDVPpegwnrtrHVIILMTDGLHNMGGDPITVIDEIRDLLYIgkdrknpre 161
Cdd:cd01471   81 P----NGSTNTTSALLVVekhlFDTRGNRENAP--------QLVIIMTDGIPDSKFRTLKEARKLRERGVI--------- 139

                        170
                 ....*....|....*
gi 239781746 162 dyldVYVFGVGPLVN 176
Cdd:cd01471  140 ----IAVLGVGQGVN 150
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 11-131 2.69e-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 [Multi-domain]  Cd Length: 164  Bit Score: 50.30  E-value: 2.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239781746  11 NIYLVLDGSDSIGASNFTGAKKCLVNLIEKVASYGVKPRYGLVTYATYPKIwvkvsEADS---SNADWVTKQLNEINYed 87
Cdd:cd01472    2 DIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRT-----EFYLntyRSKDDVLEAVKNLRY-- 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 239781746  88 hkLKSGTNTKKALQAVYSMMSWPDDVPPEGWNRtrhVIILMTDG 131
Cdd:cd01472   75 --IGGGTNTGKALKYVRENLFTEASGSREGVPK---VLVVITDG 113
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 2-206 2.95e-07

Secreted protein containing bacterial Ig-like domain and vWFA domain [General function prediction only];


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 52.03  E-value: 2.95e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239781746   2 IVLDPSGSMNiylvldgSDSIGAsnftgAKKCLVNLIEKVasygvKP--RYGLVTYATYPKIWVKVSEADSsnadwVTKQ 79
Cdd:COG2304   96 FVIDVSGSMS-------GDKLEL-----AKEAAKLLVDQL-----RPgdRVSIVTFAGDARVLLPPTPATD-----RAKI 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239781746  80 LNEINyedhKLKSG--TNTKKALQAVYSMmswPDDVPPEGWNRtrhVIILMTDGLHNMGgdpITVIDEIRDLLyigkdrK 157
Cdd:COG2304  154 LAAID----RLQAGggTALGAGLELAYEL---ARKHFIPGRVN---RVILLTDGDANVG---ITDPEELLKLA------E 214

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 239781746 158 NPREDYLDVYVFGVGPLVNQVNINALASKKDNEqhVFKVKDMENLEDVF 206
Cdd:COG2304  215 EAREEGITLTTLGVGSDYNEDLLERLADAGGGN--YYYIDDPEEAEKVF 261
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 8-191 6.32e-07

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 [Multi-domain]  Cd Length: 186  Bit Score: 49.69  E-value: 6.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239781746   8 GSMNIYLVLDGSDSIGASNFTGAKKCLVNLIEKVAS-YGVKP-----RYGLVTYATYPKIwVKVSEADSSNADWVTKQLN 81
Cdd:cd01480    1 GPVDITFVLDSSESVGLQNFDITKNFVKRVAERFLKdYYRKDpagswRVGVVQYSDQQEV-EAGFLRDIRNYTSLKEAVD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239781746  82 EINYedhkLKSGTNTKKALQAVYSMMSwpdDVPPEGWNRtrhVIILMTDGlHNMGGDPITVIDEIRDLLYIGkdrknpre 161
Cdd:cd01480   80 NLEY----IGGGTFTDCALKYATEQLL---EGSHQKENK---FLLVITDG-HSDGSPDGGIEKAVNEADHLG-------- 140

                        170       180       190
                 ....*....|....*....|....*....|
gi 239781746 162 dyLDVYVFGVGPLVNQVNINALASKKDNEQ 191
Cdd:cd01480  141 --IKIFFVAVGSQNEEPLSRIACDGKSALY 168
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 12-198 1.36e-05

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 [Multi-domain]  Cd Length: 164  Bit Score: 45.36  E-value: 1.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239781746  12 IYLVLDGSDSIGASNFTGAKKCLVNLIEKVASYGVKPRYGLVTYATYPKIWVKVSeADSSNADwVTKQLNEINYedhklK 91
Cdd:cd01482    3 IVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLN-AYTSKED-VLAAIKNLPY-----K 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239781746  92 SG-TNTKKALQAVYSMMSWPDDVPPEGwnrTRHVIILMTDGLHNmggdpitviDEIRDllyIGKDRKNpredyLDVYVFG 170
Cdd:cd01482   76 GGnTRTGKALTHVREKNFTPDAGARPG---VPKVVILITDGKSQ---------DDVEL---PARVLRN-----LGVNVFA 135

                        170       180       190
                 ....*....|....*....|....*....|
gi 239781746 171 VGplVNQVNINALAS--KKDNEQHVFKVKD 198
Cdd:cd01482  136 VG--VKDADESELKMiaSKPSETHVFNVAD 163
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
 251-465 2.60e-05

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 45.05  E-value: 2.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239781746 251 SCMGAVVSEYFVLTAAHCFTVDDKEH---SIKVSVGGEKRD---LEIEVVLFHPNYNINGKkeagipefYDYDVALIKLK 324
Cdd:COG3591   13 VCTGTLIGPNLVLTAGHCVYDGAGGGwatNIVFVPGYNGGPygtATATRFRVPPGWVASGD--------AGYDYALLRLD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239781746 325 NKLkygqtirpiclpctEGTTRALRLPPTTTcqqqkeellpaqdikalfvseeekKLTRKEVYIkngdkkgscerdAQYa 404
Cdd:COG3591   85 EPL--------------GDTTGWLGLAFNDA------------------------PLAGEPVTI------------IGY- 113

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 239781746 405 pGYDKVKDISevvtprFLCTGGVSPYADP------NTCRGDSGGPLIVHKRSRFIQVGVISWGVVDV 465
Cdd:COG3591  114 -PGDRPKDLS------LDCSGRVTGVQGNrlsydcDTTGGSSGSPVLDDSDGGGRVVGVHSAGGADR 173
VWA_2 pfam13519
von Willebrand factor type A domain;
2-127 4.12e-04

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 39.58  E-value: 4.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239781746    2 IVLDPSGSMniylvldGSDSIGASNFTGAKKCLVNLIEKVAsyGVkpRYGLVTYATYPKIWVKVseadSSNADWVTKQLN 81
Cdd:pfam13519   3 FVLDTSGSM-------RNGDYGPTRLEAAKDAVLALLKSLP--GD--RVGLVTFGDGPEVLIPL----TKDRAKILRALR 67

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 239781746   82 EINYEDhklkSGTNTKKALQAVYSMMswpddvpPEGWNRTRHVIIL 127
Cdd:pfam13519  68 RLEPKG----GGTNLAAALQLARAAL-------KHRRKNQPRRIVL 102
 
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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