NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1331817272|gb|PNI76680|]
View 

T0023928 isoform 2 [Pan troglodytes]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 620-817 2.13e-111

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: 344.66  E-value: 2.13e-111
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272  620 MNIYLVLDGSDSIGASNFTGAKKCLVNLIEKVASYGVKPRYGLVTYATHPKIWVKVSDPDSSNADWVTKQLNEINYEDHK 699
Cdd:cd01470      1 LNIYIALDASDSIGEEDFDEAKNAIKTLIEKISSYEVSPRYEIISYASDPKEIVSIRDFNSNDADDVIKRLEDFNYDDHG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272  700 LKSGTNTKKALQAVYSMMSWPDDIPPEGWNRTRHVIILMTDGLHNMGGDPITVIDEIRDLLYIGKDRKNPREDYLDVYVF 779
Cdd:cd01470     81 DKTGTNTAAALKKVYERMALEKVRNKEAFNETRHVIILFTDGKSNMGGSPLPTVDKIKNLVYKNNKSDNPREDYLDVYVF 160

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1331817272  780 GVGPLVNQVNINALASKKDNEQHVFKVKDMENLEDVFY 817
Cdd:cd01470    161 GVGDDVNKEELNDLASKKDNERHFFKLKDYEDLQEVFD 198
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 839-1106 1.04e-45

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: 164.37  E-value: 1.04e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272  839 TDYHKQPWQAKIsviRPSKGHESCMGAVVSEYFVLTAAHCFtVDDKEHSIKVSVG--------GEKRDLEIEVVLFHPNY 910
Cdd:cd00190      7 AKIGSFPWQVSL---QYTGGRHFCGGSLISPRWVLTAAHCV-YSSAPSNYTVRLGshdlssneGGGQVIKVKKVIVHPNY 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272  911 NingkkaagiPEFYDYDVALIKLKNKLKYGQTIRPICLPCTEGTtralrLPPTTTCQqqkeellpaqdikalfVS----- 985
Cdd:cd00190     83 N---------PSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYN-----LPAGTTCT----------------VSgwgrt 132

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272  986 EEEKKLTR--KEVYIKNGDKKgSCERDAQYAPgydkvkdiseVVTPRFLCTGGvsPYADPNTCRGDSGGPLIVHKRSRFI 1063
Cdd:cd00190    133 SEGGPLPDvlQEVNVPIVSNA-ECKRAYSYGG----------TITDNMLCAGG--LEGGKDACQGDSGGPLVCNDNGRGV 199

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1331817272 1064 QVGVISWGVvdVCknqkRQKQVPAhardFHINLFQVLPWLKEK 1106
Cdd:cd00190    200 LVGIVSWGS--GC----ARPNYPG----VYTRVSSYLDWIQKT 232
vWFA super family cl00057
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 147-226 5.67e-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.


The actual alignment was detected with superfamily member cd01470:

Pssm-ID: 469594 [Multi-domain]  Cd Length: 198  Bit Score: 123.55  E-value: 5.67e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272  147 GDHENGTGTNTYAALNSVYLMMnnqmRLLGME-TMAWQEIRHAIILLTDGKSNMGGSPKTAVDHIREILNINQK----RN 221
Cdd:cd01470     77 DDHGDKTGTNTAAALKKVYERM----ALEKVRnKEAFNETRHVIILFTDGKSNMGGSPLPTVDKIKNLVYKNNKsdnpRE 152


                   ....*
gi 1331817272  222 DYLDV 226
Cdd:cd01470    153 DYLDV 157
Tryp_SPc super family cl21584
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 244-448 1.79e-27

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.


The actual alignment was detected with superfamily member smart00020:

Pssm-ID: 473915  Cd Length: 229  Bit Score: 111.62  E-value: 1.79e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272   244 SDQERTPWHVTIKPKS-QETCRGALISDQWVLTAAHCFRdGNDHSLWRVNVGDPKSRWGKE---FLIEKAVISPGFDvfa 319
Cdd:smart00020    8 ANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVR-GSDPSNIRVRLGSHDLSSGEEgqvIKVSKVIIHPNYN--- 83

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272   320 kknqgiLEFYGDDIALLKLAQKVKMSTHARPICLPCTmeanlALRRPQGSTCRD----HENEllnkqSVPAHFVALNGSK 395
Cdd:smart00020   84 ------PSTYDNDIALLKLKEPVTLSDNVRPICLPSS-----NYNVPAGTTCTVsgwgRTSE-----GAGSLPDTLQEVN 147

                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|....
gi 1331817272   396 LNInlkmgVEWTSCAEVVSQektmfpnltdvREVVTDQFLCSGTQE-DESPCKG 448
Cdd:smart00020  148 VPI-----VSNATCRRAYSG-----------GGAITDNMLCAGGLEgGKDACQG 185
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 89-144 1.28e-15

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 [Multi-domain]  Cd Length: 57  Bit Score: 72.11  E-value: 1.28e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1331817272   89 CPAPVSFENGIYTPRLGSYPVGGNVSFECEDGFILRGSPVRQCRPNGMWDGETAVC 144
Cdd:cd00033      1 CPPPPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTC 56
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 454-509 1.77e-15

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 [Multi-domain]  Cd Length: 57  Bit Score: 71.73  E-value: 1.77e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1331817272  454 CPRPHDFENGEYWPRSPYYNVSDEISFHCYDGYTLRGSANRTCQVNGRWSGQTAIC 509
Cdd:cd00033      1 CPPPPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTC 56
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 516-570 2.68e-12

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 [Multi-domain]  Cd Length: 57  Bit Score: 62.48  E-value: 2.68e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1331817272  516 CSNPGIPIGTRKVGSQ--YRLEDSVTYHCSRGLTLRGSQRRTCQEGGSWSGTEPSCQ 570
Cdd:cd00033      1 CPPPPVPENGTVTGSKgsYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57
PHA02927 super family cl33700
secreted complement-binding protein; Provisional
 24-144 2.73e-09

secreted complement-binding protein; Provisional


The actual alignment was detected with superfamily member PHA02927:

Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 59.28  E-value: 2.73e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272   24 CPQNVNISGGTFT-LSHGWAPGSLLTYSCPQGLYPSPASRLCKSSGQWQTPgatrslskAVCKPVRCPAPvSFENGIYTP 102
Cdd:PHA02927   148 CQSPPSISNGRHNgYEDFYTDGSVVTYSCNSGYSLIGNSGVLCSGGEWSDP--------PTCQIVKCPHP-TISNGYLSS 218

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1331817272  103 RLG-SYPVGGNVSFECEDGFILRGSPVRQCRPNGMWDGETAVC 144
Cdd:PHA02927   219 GFKrSYSYNDNVDFKCKYGYKLSGSSSSTCSPGNTWQPELPKC 261
 
Name Accession Description Interval E-value
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
 620-817 2.13e-111

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: 344.66  E-value: 2.13e-111
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272  620 MNIYLVLDGSDSIGASNFTGAKKCLVNLIEKVASYGVKPRYGLVTYATHPKIWVKVSDPDSSNADWVTKQLNEINYEDHK 699
Cdd:cd01470      1 LNIYIALDASDSIGEEDFDEAKNAIKTLIEKISSYEVSPRYEIISYASDPKEIVSIRDFNSNDADDVIKRLEDFNYDDHG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272  700 LKSGTNTKKALQAVYSMMSWPDDIPPEGWNRTRHVIILMTDGLHNMGGDPITVIDEIRDLLYIGKDRKNPREDYLDVYVF 779
Cdd:cd01470     81 DKTGTNTAAALKKVYERMALEKVRNKEAFNETRHVIILFTDGKSNMGGSPLPTVDKIKNLVYKNNKSDNPREDYLDVYVF 160

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1331817272  780 GVGPLVNQVNINALASKKDNEQHVFKVKDMENLEDVFY 817
Cdd:cd01470    161 GVGDDVNKEELNDLASKKDNERHFFKLKDYEDLQEVFD 198
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 839-1106 1.04e-45

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: 164.37  E-value: 1.04e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272  839 TDYHKQPWQAKIsviRPSKGHESCMGAVVSEYFVLTAAHCFtVDDKEHSIKVSVG--------GEKRDLEIEVVLFHPNY 910
Cdd:cd00190      7 AKIGSFPWQVSL---QYTGGRHFCGGSLISPRWVLTAAHCV-YSSAPSNYTVRLGshdlssneGGGQVIKVKKVIVHPNY 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272  911 NingkkaagiPEFYDYDVALIKLKNKLKYGQTIRPICLPCTEGTtralrLPPTTTCQqqkeellpaqdikalfVS----- 985
Cdd:cd00190     83 N---------PSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYN-----LPAGTTCT----------------VSgwgrt 132

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272  986 EEEKKLTR--KEVYIKNGDKKgSCERDAQYAPgydkvkdiseVVTPRFLCTGGvsPYADPNTCRGDSGGPLIVHKRSRFI 1063
Cdd:cd00190    133 SEGGPLPDvlQEVNVPIVSNA-ECKRAYSYGG----------TITDNMLCAGG--LEGGKDACQGDSGGPLVCNDNGRGV 199

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1331817272 1064 QVGVISWGVvdVCknqkRQKQVPAhardFHINLFQVLPWLKEK 1106
Cdd:cd00190    200 LVGIVSWGS--GC----ARPNYPG----VYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 839-1072 1.63e-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  Cd Length: 229  Bit Score: 155.14  E-value: 1.63e-42
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272   839 TDYHKQPWQAKIsviRPSKGHESCMGAVVSEYFVLTAAHCFTvDDKEHSIKVSVG-------GEKRDLEIEVVLFHPNYN 911
Cdd:smart00020    8 ANIGSFPWQVSL---QYGGGRHFCGGSLISPRWVLTAAHCVR-GSDPSNIRVRLGshdlssgEEGQVIKVSKVIIHPNYN 83

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272   912 ingkkaagiPEFYDYDVALIKLKNKLKYGQTIRPICLPCTegttrALRLPPTTTCQqqkeellpaqdikalfVS------ 985
Cdd:smart00020   84 ---------PSTYDNDIALLKLKEPVTLSDNVRPICLPSS-----NYNVPAGTTCT----------------VSgwgrts 133

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272   986 EEEKKLTR--KEVYIKNGDKKgSCERDAQYapgydkvkdiSEVVTPRFLCTGGvsPYADPNTCRGDSGGPLiVHKRSRFI 1063
Cdd:smart00020  134 EGAGSLPDtlQEVNVPIVSNA-TCRRAYSG----------GGAITDNMLCAGG--LEGGKDACQGDSGGPL-VCNDGRWV 199


                    ....*....
gi 1331817272  1064 QVGVISWGV 1072
Cdd:smart00020  200 LVGIVSWGS 208
Trypsin pfam00089
Trypsin;
842-1103 3.15e-35

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 133.72  E-value: 3.15e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272  842 HKQPWQAKISVirpSKGHESCMGAVVSEYFVLTAAHCF------TVDDKEHSIKVSVGGEKRdLEIEVVLFHPNYNingk 915
Cdd:pfam00089   10 GSFPWQVSLQL---SSGKHFCGGSLISENWVLTAAHCVsgasdvKVVLGAHNIVLREGGEQK-FDVEKIIVHPNYN---- 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272  916 kaagiPEFYDYDVALIKLKNKLKYGQTIRPICLPCTEGTtralrLPPTTTCQQQKEELlpaqdikalfVSEEEKKLTRKE 995
Cdd:pfam00089   82 -----PDTLDNDIALLKLESPVTLGDTVRPICLPDASSD-----LPVGTTCTVSGWGN----------TKTLGPSDTLQE 141

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272  996 VYIKNGDkKGSCERdaqyapgydkvkDISEVVTPRFLCTGGVSPYAdpntCRGDSGGPLIVHKRsrfIQVGVISWGvvDV 1075
Cdd:pfam00089  142 VTVPVVS-RETCRS------------AYGGTVTDTMICAGAGGKDA----CQGDSGGPLVCSDG---ELIGIVSWG--YG 199

                          250       260
                   ....*....|....*....|....*...
gi 1331817272 1076 CKNQKRqkqvpahaRDFHINLFQVLPWL 1103
Cdd:pfam00089  200 CASGNY--------PGVYTPVSSYLDWI 219
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
 147-226 5.67e-32

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: 123.55  E-value: 5.67e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272  147 GDHENGTGTNTYAALNSVYLMMnnqmRLLGME-TMAWQEIRHAIILLTDGKSNMGGSPKTAVDHIREILNINQK----RN 221
Cdd:cd01470     77 DDHGDKTGTNTAAALKKVYERM----ALEKVRnKEAFNETRHVIILFTDGKSNMGGSPLPTVDKIKNLVYKNNKsdnpRE 152


                   ....*
gi 1331817272  222 DYLDV 226
Cdd:cd01470    153 DYLDV 157
VWA pfam00092
von Willebrand factor type A domain;
621-818 1.26e-31

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 122.00  E-value: 1.26e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272  621 NIYLVLDGSDSIGASNFTGAKKCLVNLIEKVASYGVKPRYGLVTYATHPKIWVKVSDPdsSNADWVTKQLNEINYEDHKL 700
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDY--SSKEELLSAVDNLRYLGGGT 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272  701 KS-GTNTKKALQAVYSMMSWPDDippegwnRTRHVIILMTDGlHNMGGDPITVIDEIRDllyigkdrknpreDYLDVYVF 779
Cdd:pfam00092   79 TNtGKALKYALENLFSSAAGARP-------GAPKVVVLLTDG-RSQDGDPEEVARELKS-------------AGVTVFAV 137

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1331817272  780 GVGPLVNQvNINALASKKDnEQHVFKVKDMENLEDVFYQ 818
Cdd:pfam00092  138 GVGNADDE-ELRKIASEPG-EGHVFTVSDFEALEDLQDQ 174
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 244-448 1.79e-27

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: 111.62  E-value: 1.79e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272   244 SDQERTPWHVTIKPKS-QETCRGALISDQWVLTAAHCFRdGNDHSLWRVNVGDPKSRWGKE---FLIEKAVISPGFDvfa 319
Cdd:smart00020    8 ANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVR-GSDPSNIRVRLGSHDLSSGEEgqvIKVSKVIIHPNYN--- 83

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272   320 kknqgiLEFYGDDIALLKLAQKVKMSTHARPICLPCTmeanlALRRPQGSTCRD----HENEllnkqSVPAHFVALNGSK 395
Cdd:smart00020   84 ------PSTYDNDIALLKLKEPVTLSDNVRPICLPSS-----NYNVPAGTTCTVsgwgRTSE-----GAGSLPDTLQEVN 147

                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|....
gi 1331817272   396 LNInlkmgVEWTSCAEVVSQektmfpnltdvREVVTDQFLCSGTQE-DESPCKG 448
Cdd:smart00020  148 VPI-----VSNATCRRAYSG-----------GGAITDNMLCAGGLEgGKDACQG 185
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 621-814 4.24e-27

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: 109.08  E-value: 4.24e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272   621 NIYLVLDGSDSIGASNFTGAKKCLVNLIEKVASYGVKPRYGLVTYATHPKIWVKVSDPDSSNAdwVTKQLNEINYedhKL 700
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDA--LLEALASLSY---KL 75

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272   701 KSGTNTKKALQAVYSMMSwpddIPPEGWNR-TRHVIILMTDGLHNMGGDPItvIDEIRDLlyigkdrknpREDYLDVYVF 779
Cdd:smart00327   76 GGGTNLGAALQYALENLF----SKSAGSRRgAPKVVILITDGESNDGPKDL--LKAAKEL----------KRSGVKVFVV 139

                           170       180       190
                    ....*....|....*....|....*....|....*
gi 1331817272   780 GVGPLVNQVNINALASKKDNEqHVFKVKDMENLED 814
Cdd:smart00327  140 GVGNDVDEEELKKLASAPGGV-YVFLPELLDLLID 173
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 244-448 1.41e-26

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: 109.29  E-value: 1.41e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272  244 SDQERTPWHVTIKPKS-QETCRGALISDQWVLTAAHCFRdGNDHSLWRVNVGD----PKSRWGKEFLIEKAVISPGFDVF 318
Cdd:cd00190      7 AKIGSFPWQVSLQYTGgRHFCGGSLISPRWVLTAAHCVY-SSAPSNYTVRLGShdlsSNEGGGQVIKVKKVIVHPNYNPS 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272  319 akknqgileFYGDDIALLKLAQKVKMSTHARPICLPCTMEANlalrrPQGSTCR-----DHENEllnkqsvpahfVALNG 393
Cdd:cd00190     86 ---------TYDNDIALLKLKRPVTLSDNVRPICLPSSGYNL-----PAGTTCTvsgwgRTSEG-----------GPLPD 140

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1331817272  394 SKLNINLKMgVEWTSCAEVVSQektmfpnltdvREVVTDQFLCSGTQE-DESPCKG 448
Cdd:cd00190    141 VLQEVNVPI-VSNAECKRAYSY-----------GGTITDNMLCAGGLEgGKDACQG 184
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 845-1071 4.61e-19

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 88.17  E-value: 4.61e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272  845 PWQAKISVIRPSKGHeSCMGAVVSEYFVLTAAHCfTVDDKEHSIKVSVGGEKRD------LEIEVVLFHPNYNingkkaa 918
Cdd:COG5640     43 PWMVALQSSNGPSGQ-FCGGTLIAPRWVLTAAHC-VDGDGPSDLRVVIGSTDLStsggtvVKVARIVVHPDYD------- 113

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272  919 giPEFYDYDVALIKLKnklkygqtiRPIclpcteGTTRALRLPPTTTcqqqkeelLPAQDIKALFV-----SEEEKKL-- 991
Cdd:COG5640    114 --PATPGNDIALLKLA---------TPV------PGVAPAPLATSAD--------AAAPGTPATVAgwgrtSEGPGSQsg 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272  992 TRKEVYIKNGDkkgscERDAQYAPGYDkvkdisevvTPRFLCTGGVSPYADpnTCRGDSGGPLIVHKRSRFIQVGVISWG 1071
Cdd:COG5640    169 TLRKADVPVVS-----DATCAAYGGFD---------GGTMLCAGYPEGGKD--ACQGDSGGPLVVKDGGGWVLVGVVSWG 232
Trypsin pfam00089
Trypsin;
250-356 6.11e-17

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 80.95  E-value: 6.11e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272  250 PWHVTIK-PKSQETCRGALISDQWVLTAAHCFRDGNDhslWRVNVGDPKSR----WGKEFLIEKAVISPGFDVFAKKNqg 324
Cdd:pfam00089   13 PWQVSLQlSSGKHFCGGSLISENWVLTAAHCVSGASD---VKVVLGAHNIVlregGEQKFDVEKIIVHPNYNPDTLDN-- 87

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1331817272  325 ilefygdDIALLKLAQKVKMSTHARPICLPCT 356
Cdd:pfam00089   88 -------DIALLKLESPVTLGDTVRPICLPDA 112
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 89-144 1.28e-15

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 [Multi-domain]  Cd Length: 57  Bit Score: 72.11  E-value: 1.28e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1331817272   89 CPAPVSFENGIYTPRLGSYPVGGNVSFECEDGFILRGSPVRQCRPNGMWDGETAVC 144
Cdd:cd00033      1 CPPPPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTC 56
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 454-509 1.77e-15

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 [Multi-domain]  Cd Length: 57  Bit Score: 71.73  E-value: 1.77e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1331817272  454 CPRPHDFENGEYWPRSPYYNVSDEISFHCYDGYTLRGSANRTCQVNGRWSGQTAIC 509
Cdd:cd00033      1 CPPPPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTC 56
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 454-509 1.89e-14

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 [Multi-domain]  Cd Length: 56  Bit Score: 68.71  E-value: 1.89e-14
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 1331817272   454 CPRPHDFENGEYWPRSPYYNVSDEISFHCYDGYTLRGSANRTCQVNGRWSGQTAIC 509
Cdd:smart00032    1 CPPPPDIENGTVTSSSGTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 242-354 2.60e-14

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 74.30  E-value: 2.60e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272  242 NASDQERtPWHVTIKPKS---QETCRGALISDQWVLTAAHCFRDGNDHSLwRVNVG--DPKSRWGKEFLIEKAVISPGFD 316
Cdd:COG5640     36 PATVGEY-PWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDGPSDL-RVVIGstDLSTSGGTVVKVARIVVHPDYD 113

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1331817272  317 VFAkknqgilefYGDDIALLKLAQKVkmsTHARPICLP 354
Cdd:COG5640    114 PAT---------PGNDIALLKLATPV---PGVAPAPLA 139
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 89-144 2.05e-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 [Multi-domain]  Cd Length: 56  Bit Score: 65.63  E-value: 2.05e-13
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 1331817272    89 CPAPVSFENGIYTPRLGSYPVGGNVSFECEDGFILRGSPVRQCRPNGMWDGETAVC 144
Cdd:smart00032    1 CPPPPDIENGTVTSSSGTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 516-570 2.68e-12

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 [Multi-domain]  Cd Length: 57  Bit Score: 62.48  E-value: 2.68e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1331817272  516 CSNPGIPIGTRKVGSQ--YRLEDSVTYHCSRGLTLRGSQRRTCQEGGSWSGTEPSCQ 570
Cdd:cd00033      1 CPPPPVPENGTVTGSKgsYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57
Sushi pfam00084
Sushi repeat (SCR repeat);
89-144 2.38e-11

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 59.82  E-value: 2.38e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1331817272   89 CPAPVSFENGIYTPRLGSYPVGGNVSFECEDGFILRGSPVRQCRPNGMWDGETAVC 144
Cdd:pfam00084    1 CPPPPDIPNGKVSATKNEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 516-569 3.49e-11

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 [Multi-domain]  Cd Length: 56  Bit Score: 59.46  E-value: 3.49e-11
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 1331817272   516 CSNPGIPIGTRKVGSQ--YRLEDSVTYHCSRGLTLRGSQRRTCQEGGSWSGTEPSC 569
Cdd:smart00032    1 CPPPPDIENGTVTSSSgtYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
Sushi pfam00084
Sushi repeat (SCR repeat);
454-509 4.10e-10

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 56.35  E-value: 4.10e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1331817272  454 CPRPHDFENGEYWPRSPYYNVSDEISFHCYDGYTLRGSANRTCQVNGRWSGQTAIC 509
Cdd:pfam00084    1 CPPPPDIPNGKVSATKNEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
PHA02927 PHA02927
secreted complement-binding protein; Provisional
 24-144 2.73e-09

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 59.28  E-value: 2.73e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272   24 CPQNVNISGGTFT-LSHGWAPGSLLTYSCPQGLYPSPASRLCKSSGQWQTPgatrslskAVCKPVRCPAPvSFENGIYTP 102
Cdd:PHA02927   148 CQSPPSISNGRHNgYEDFYTDGSVVTYSCNSGYSLIGNSGVLCSGGEWSDP--------PTCQIVKCPHP-TISNGYLSS 218

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1331817272  103 RLG-SYPVGGNVSFECEDGFILRGSPVRQCRPNGMWDGETAVC 144
Cdd:PHA02927   219 GFKrSYSYNDNVDFKCKYGYKLSGSSSSTCSPGNTWQPELPKC 261
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 576-816 3.39e-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: 59.18  E-value: 3.39e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272  576 DTPQEVAEAFLSSLTETIEGVDAEDGHGPGEQQKRKIVLDPSGSMNIYLVLDGSDSIGASN-FTGAKKCLVNLIEkvaSY 654
Cdd:COG1240     49 LLLGLAGLGLLALLLAALLLLLAVLLLLLALALAPLALARPQRGRDVVLVVDASGSMAAENrLEAAKGALLDFLD---DY 125

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272  655 GVKPRYGLVTYATHPKIWVkvsdPDSSNADWVTKQLNEInyedhKLKSGTNTKKALQAVYSMMswpDDIPPEGwnrtRHV 734
Cdd:COG1240    126 RPRDRVGLVAFGGEAEVLL----PLTRDREALKRALDEL-----PPGGGTPLGDALALALELL---KRADPAR----RKV 189

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272  735 IILMTDGLHNMG-GDPITVIDEIrdllyigkdrknpREDYLDVYVFGVG-PLVNQVNINALAskkdnEQ---HVFKVKDM 809
Cdd:COG1240    190 IVLLTDGRDNAGrIDPLEAAELA-------------AAAGIRIYTIGVGtEAVDEGLLREIA-----EAtggRYFRADDL 251


                   ....*..
gi 1331817272  810 ENLEDVF 816
Cdd:COG1240    252 SELAAIY 258
PHA02927 PHA02927
secreted complement-binding protein; Provisional
 451-569 5.97e-09

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 58.13  E-value: 5.97e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272  451 AIHCPRPHDFENGEYWPRSPYYNVSDEISFHCYDGYTLRGSANRTCQvNGRWSgQTAICDngAGYCSNPGIPIGTRKVG- 529
Cdd:PHA02927   145 SVKCQSPPSISNGRHNGYEDFYTDGSVVTYSCNSGYSLIGNSGVLCS-GGEWS-DPPTCQ--IVKCPHPTISNGYLSSGf 220

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1331817272  530 -SQYRLEDSVTYHCSRGLTLRGSQRRTCQEGGSWSGTEPSC 569
Cdd:PHA02927   221 kRSYSYNDNVDFKCKYGYKLSGSSSSTCSPGNTWQPELPKC 261
Sushi pfam00084
Sushi repeat (SCR repeat);
531-569 1.20e-07

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 49.42  E-value: 1.20e-07
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1331817272  531 QYRLEDSVTYHCSRGLTLRGSQRRTCQEGGSWSGTEPSC 569
Cdd:pfam00084   18 EYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
PHA02831 PHA02831
EEV host range protein; Provisional
 83-137 2.42e-04

EEV host range protein; Provisional


Pssm-ID: 165176 [Multi-domain]  Cd Length: 268  Bit Score: 44.21  E-value: 2.42e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1331817272   83 VCKPVRCPAPvSFENGIYTPRLGSYPVGGNVSFECEDGFILRGSPVRQCRPNGMW 137
Cdd:PHA02831   135 VCKLIRCKYP-ALQNGFLNVFEKKFYYGDIVNFKCKKGFILLGSSVSTCDINSIW 188
 
Name Accession Description Interval E-value
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
 620-817 2.13e-111

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: 344.66  E-value: 2.13e-111
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272  620 MNIYLVLDGSDSIGASNFTGAKKCLVNLIEKVASYGVKPRYGLVTYATHPKIWVKVSDPDSSNADWVTKQLNEINYEDHK 699
Cdd:cd01470      1 LNIYIALDASDSIGEEDFDEAKNAIKTLIEKISSYEVSPRYEIISYASDPKEIVSIRDFNSNDADDVIKRLEDFNYDDHG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272  700 LKSGTNTKKALQAVYSMMSWPDDIPPEGWNRTRHVIILMTDGLHNMGGDPITVIDEIRDLLYIGKDRKNPREDYLDVYVF 779
Cdd:cd01470     81 DKTGTNTAAALKKVYERMALEKVRNKEAFNETRHVIILFTDGKSNMGGSPLPTVDKIKNLVYKNNKSDNPREDYLDVYVF 160

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1331817272  780 GVGPLVNQVNINALASKKDNEQHVFKVKDMENLEDVFY 817
Cdd:cd01470    161 GVGDDVNKEELNDLASKKDNERHFFKLKDYEDLQEVFD 198
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 839-1106 1.04e-45

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: 164.37  E-value: 1.04e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272  839 TDYHKQPWQAKIsviRPSKGHESCMGAVVSEYFVLTAAHCFtVDDKEHSIKVSVG--------GEKRDLEIEVVLFHPNY 910
Cdd:cd00190      7 AKIGSFPWQVSL---QYTGGRHFCGGSLISPRWVLTAAHCV-YSSAPSNYTVRLGshdlssneGGGQVIKVKKVIVHPNY 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272  911 NingkkaagiPEFYDYDVALIKLKNKLKYGQTIRPICLPCTEGTtralrLPPTTTCQqqkeellpaqdikalfVS----- 985
Cdd:cd00190     83 N---------PSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYN-----LPAGTTCT----------------VSgwgrt 132

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272  986 EEEKKLTR--KEVYIKNGDKKgSCERDAQYAPgydkvkdiseVVTPRFLCTGGvsPYADPNTCRGDSGGPLIVHKRSRFI 1063
Cdd:cd00190    133 SEGGPLPDvlQEVNVPIVSNA-ECKRAYSYGG----------TITDNMLCAGG--LEGGKDACQGDSGGPLVCNDNGRGV 199

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1331817272 1064 QVGVISWGVvdVCknqkRQKQVPAhardFHINLFQVLPWLKEK 1106
Cdd:cd00190    200 LVGIVSWGS--GC----ARPNYPG----VYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 839-1072 1.63e-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  Cd Length: 229  Bit Score: 155.14  E-value: 1.63e-42
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272   839 TDYHKQPWQAKIsviRPSKGHESCMGAVVSEYFVLTAAHCFTvDDKEHSIKVSVG-------GEKRDLEIEVVLFHPNYN 911
Cdd:smart00020    8 ANIGSFPWQVSL---QYGGGRHFCGGSLISPRWVLTAAHCVR-GSDPSNIRVRLGshdlssgEEGQVIKVSKVIIHPNYN 83

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272   912 ingkkaagiPEFYDYDVALIKLKNKLKYGQTIRPICLPCTegttrALRLPPTTTCQqqkeellpaqdikalfVS------ 985
Cdd:smart00020   84 ---------PSTYDNDIALLKLKEPVTLSDNVRPICLPSS-----NYNVPAGTTCT----------------VSgwgrts 133

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272   986 EEEKKLTR--KEVYIKNGDKKgSCERDAQYapgydkvkdiSEVVTPRFLCTGGvsPYADPNTCRGDSGGPLiVHKRSRFI 1063
Cdd:smart00020  134 EGAGSLPDtlQEVNVPIVSNA-TCRRAYSG----------GGAITDNMLCAGG--LEGGKDACQGDSGGPL-VCNDGRWV 199


                    ....*....
gi 1331817272  1064 QVGVISWGV 1072
Cdd:smart00020  200 LVGIVSWGS 208
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 620-804 1.66e-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: 143.97  E-value: 1.66e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272  620 MNIYLVLDGSDSIGASNFTGAKKCLVNLIEKVASYGVKPRYGLVTYATHPKIWVKVSdpDSSNADWVTKQLNEINYEDHk 699
Cdd:cd01450      1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLN--DYKSKDDLLKAVKNLKYLGG- 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272  700 lkSGTNTKKALQAVYSMMSWPDDIppegWNRTRHVIILMTDGLHNMGGDPITVIDEIRDLlyigkdrknpredYLDVYVF 779
Cdd:cd01450     78 --GGTNTGKALQYALEQLFSESNA----RENVPKVIIVLTDGRSDDGGDPKEAAAKLKDE-------------GIKVFVV 138

                          170       180
                   ....*....|....*....|....*
gi 1331817272  780 GVGPlVNQVNINALASKKdNEQHVF 804
Cdd:cd01450    139 GVGP-ADEEELREIASCP-SERHVF 161
Trypsin pfam00089
Trypsin;
842-1103 3.15e-35

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 133.72  E-value: 3.15e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272  842 HKQPWQAKISVirpSKGHESCMGAVVSEYFVLTAAHCF------TVDDKEHSIKVSVGGEKRdLEIEVVLFHPNYNingk 915
Cdd:pfam00089   10 GSFPWQVSLQL---SSGKHFCGGSLISENWVLTAAHCVsgasdvKVVLGAHNIVLREGGEQK-FDVEKIIVHPNYN---- 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272  916 kaagiPEFYDYDVALIKLKNKLKYGQTIRPICLPCTEGTtralrLPPTTTCQQQKEELlpaqdikalfVSEEEKKLTRKE 995
Cdd:pfam00089   82 -----PDTLDNDIALLKLESPVTLGDTVRPICLPDASSD-----LPVGTTCTVSGWGN----------TKTLGPSDTLQE 141

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272  996 VYIKNGDkKGSCERdaqyapgydkvkDISEVVTPRFLCTGGVSPYAdpntCRGDSGGPLIVHKRsrfIQVGVISWGvvDV 1075
Cdd:pfam00089  142 VTVPVVS-RETCRS------------AYGGTVTDTMICAGAGGKDA----CQGDSGGPLVCSDG---ELIGIVSWG--YG 199

                          250       260
                   ....*....|....*....|....*...
gi 1331817272 1076 CKNQKRqkqvpahaRDFHINLFQVLPWL 1103
Cdd:pfam00089  200 CASGNY--------PGVYTPVSSYLDWI 219
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
 147-226 5.67e-32

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: 123.55  E-value: 5.67e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272  147 GDHENGTGTNTYAALNSVYLMMnnqmRLLGME-TMAWQEIRHAIILLTDGKSNMGGSPKTAVDHIREILNINQK----RN 221
Cdd:cd01470     77 DDHGDKTGTNTAAALKKVYERM----ALEKVRnKEAFNETRHVIILFTDGKSNMGGSPLPTVDKIKNLVYKNNKsdnpRE 152


                   ....*
gi 1331817272  222 DYLDV 226
Cdd:cd01470    153 DYLDV 157
VWA pfam00092
von Willebrand factor type A domain;
621-818 1.26e-31

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 122.00  E-value: 1.26e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272  621 NIYLVLDGSDSIGASNFTGAKKCLVNLIEKVASYGVKPRYGLVTYATHPKIWVKVSDPdsSNADWVTKQLNEINYEDHKL 700
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDY--SSKEELLSAVDNLRYLGGGT 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272  701 KS-GTNTKKALQAVYSMMSWPDDippegwnRTRHVIILMTDGlHNMGGDPITVIDEIRDllyigkdrknpreDYLDVYVF 779
Cdd:pfam00092   79 TNtGKALKYALENLFSSAAGARP-------GAPKVVVLLTDG-RSQDGDPEEVARELKS-------------AGVTVFAV 137

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1331817272  780 GVGPLVNQvNINALASKKDnEQHVFKVKDMENLEDVFYQ 818
Cdd:pfam00092  138 GVGNADDE-ELRKIASEPG-EGHVFTVSDFEALEDLQDQ 174
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 244-448 1.79e-27

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: 111.62  E-value: 1.79e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272   244 SDQERTPWHVTIKPKS-QETCRGALISDQWVLTAAHCFRdGNDHSLWRVNVGDPKSRWGKE---FLIEKAVISPGFDvfa 319
Cdd:smart00020    8 ANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVR-GSDPSNIRVRLGSHDLSSGEEgqvIKVSKVIIHPNYN--- 83

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272   320 kknqgiLEFYGDDIALLKLAQKVKMSTHARPICLPCTmeanlALRRPQGSTCRD----HENEllnkqSVPAHFVALNGSK 395
Cdd:smart00020   84 ------PSTYDNDIALLKLKEPVTLSDNVRPICLPSS-----NYNVPAGTTCTVsgwgRTSE-----GAGSLPDTLQEVN 147

                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|....
gi 1331817272   396 LNInlkmgVEWTSCAEVVSQektmfpnltdvREVVTDQFLCSGTQE-DESPCKG 448
Cdd:smart00020  148 VPI-----VSNATCRRAYSG-----------GGAITDNMLCAGGLEgGKDACQG 185
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 621-814 4.24e-27

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: 109.08  E-value: 4.24e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272   621 NIYLVLDGSDSIGASNFTGAKKCLVNLIEKVASYGVKPRYGLVTYATHPKIWVKVSDPDSSNAdwVTKQLNEINYedhKL 700
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDA--LLEALASLSY---KL 75

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272   701 KSGTNTKKALQAVYSMMSwpddIPPEGWNR-TRHVIILMTDGLHNMGGDPItvIDEIRDLlyigkdrknpREDYLDVYVF 779
Cdd:smart00327   76 GGGTNLGAALQYALENLF----SKSAGSRRgAPKVVILITDGESNDGPKDL--LKAAKEL----------KRSGVKVFVV 139

                           170       180       190
                    ....*....|....*....|....*....|....*
gi 1331817272   780 GVGPLVNQVNINALASKKDNEqHVFKVKDMENLED 814
Cdd:smart00327  140 GVGNDVDEEELKKLASAPGGV-YVFLPELLDLLID 173
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 244-448 1.41e-26

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: 109.29  E-value: 1.41e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272  244 SDQERTPWHVTIKPKS-QETCRGALISDQWVLTAAHCFRdGNDHSLWRVNVGD----PKSRWGKEFLIEKAVISPGFDVF 318
Cdd:cd00190      7 AKIGSFPWQVSLQYTGgRHFCGGSLISPRWVLTAAHCVY-SSAPSNYTVRLGShdlsSNEGGGQVIKVKKVIVHPNYNPS 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272  319 akknqgileFYGDDIALLKLAQKVKMSTHARPICLPCTMEANlalrrPQGSTCR-----DHENEllnkqsvpahfVALNG 393
Cdd:cd00190     86 ---------TYDNDIALLKLKRPVTLSDNVRPICLPSSGYNL-----PAGTTCTvsgwgRTSEG-----------GPLPD 140

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1331817272  394 SKLNINLKMgVEWTSCAEVVSQektmfpnltdvREVVTDQFLCSGTQE-DESPCKG 448
Cdd:cd00190    141 VLQEVNVPI-VSNAECKRAYSY-----------GGTITDNMLCAGGLEgGKDACQG 184
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 621-804 3.68e-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: 97.25  E-value: 3.68e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272  621 NIYLVLDGSDSIGASNFTGAKKCLVNLIEKVASYGVKPRYGLVTYATHPKIWVKVSDPDSSnadwvTKQLNEINYEDHKL 700
Cdd:cd00198      2 DIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDK-----ADLLEAIDALKKGL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272  701 KSGTNTKKALQAVYSMMSWPDDippegwNRTRHVIILMTDGLHNmgGDPITVIDEIRDLlyigkdrknpREDYLDVYVFG 780
Cdd:cd00198     77 GGGTNIGAALRLALELLKSAKR------PNARRVIILLTDGEPN--DGPELLAEAAREL----------RKLGITVYTIG 138

                          170       180
                   ....*....|....*....|....
gi 1331817272  781 VGPLVNQVNINALASkKDNEQHVF 804
Cdd:cd00198    139 IGDDANEDELKEIAD-KTTGGAVF 161
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 845-1071 4.61e-19

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 88.17  E-value: 4.61e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272  845 PWQAKISVIRPSKGHeSCMGAVVSEYFVLTAAHCfTVDDKEHSIKVSVGGEKRD------LEIEVVLFHPNYNingkkaa 918
Cdd:COG5640     43 PWMVALQSSNGPSGQ-FCGGTLIAPRWVLTAAHC-VDGDGPSDLRVVIGSTDLStsggtvVKVARIVVHPDYD------- 113

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272  919 giPEFYDYDVALIKLKnklkygqtiRPIclpcteGTTRALRLPPTTTcqqqkeelLPAQDIKALFV-----SEEEKKL-- 991
Cdd:COG5640    114 --PATPGNDIALLKLA---------TPV------PGVAPAPLATSAD--------AAAPGTPATVAgwgrtSEGPGSQsg 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272  992 TRKEVYIKNGDkkgscERDAQYAPGYDkvkdisevvTPRFLCTGGVSPYADpnTCRGDSGGPLIVHKRSRFIQVGVISWG 1071
Cdd:COG5640    169 TLRKADVPVVS-----DATCAAYGGFD---------GGTMLCAGYPEGGKD--ACQGDSGGPLVVKDGGGWVLVGVVSWG 232
Trypsin pfam00089
Trypsin;
250-356 6.11e-17

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 80.95  E-value: 6.11e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272  250 PWHVTIK-PKSQETCRGALISDQWVLTAAHCFRDGNDhslWRVNVGDPKSR----WGKEFLIEKAVISPGFDVFAKKNqg 324
Cdd:pfam00089   13 PWQVSLQlSSGKHFCGGSLISENWVLTAAHCVSGASD---VKVVLGAHNIVlregGEQKFDVEKIIVHPNYNPDTLDN-- 87

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1331817272  325 ilefygdDIALLKLAQKVKMSTHARPICLPCT 356
Cdd:pfam00089   88 -------DIALLKLESPVTLGDTVRPICLPDA 112
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 89-144 1.28e-15

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 [Multi-domain]  Cd Length: 57  Bit Score: 72.11  E-value: 1.28e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1331817272   89 CPAPVSFENGIYTPRLGSYPVGGNVSFECEDGFILRGSPVRQCRPNGMWDGETAVC 144
Cdd:cd00033      1 CPPPPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTC 56
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 454-509 1.77e-15

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 [Multi-domain]  Cd Length: 57  Bit Score: 71.73  E-value: 1.77e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1331817272  454 CPRPHDFENGEYWPRSPYYNVSDEISFHCYDGYTLRGSANRTCQVNGRWSGQTAIC 509
Cdd:cd00033      1 CPPPPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTC 56
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 454-509 1.89e-14

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 [Multi-domain]  Cd Length: 56  Bit Score: 68.71  E-value: 1.89e-14
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 1331817272   454 CPRPHDFENGEYWPRSPYYNVSDEISFHCYDGYTLRGSANRTCQVNGRWSGQTAIC 509
Cdd:smart00032    1 CPPPPDIENGTVTSSSGTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 242-354 2.60e-14

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 74.30  E-value: 2.60e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272  242 NASDQERtPWHVTIKPKS---QETCRGALISDQWVLTAAHCFRDGNDHSLwRVNVG--DPKSRWGKEFLIEKAVISPGFD 316
Cdd:COG5640     36 PATVGEY-PWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDGPSDL-RVVIGstDLSTSGGTVVKVARIVVHPDYD 113

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1331817272  317 VFAkknqgilefYGDDIALLKLAQKVkmsTHARPICLP 354
Cdd:COG5640    114 PAT---------PGNDIALLKLATPV---PGVAPAPLA 139
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 89-144 2.05e-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 [Multi-domain]  Cd Length: 56  Bit Score: 65.63  E-value: 2.05e-13
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 1331817272    89 CPAPVSFENGIYTPRLGSYPVGGNVSFECEDGFILRGSPVRQCRPNGMWDGETAVC 144
Cdd:smart00032    1 CPPPPDIENGTVTSSSGTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 516-570 2.68e-12

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 [Multi-domain]  Cd Length: 57  Bit Score: 62.48  E-value: 2.68e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1331817272  516 CSNPGIPIGTRKVGSQ--YRLEDSVTYHCSRGLTLRGSQRRTCQEGGSWSGTEPSCQ 570
Cdd:cd00033      1 CPPPPVPENGTVTGSKgsYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57
Sushi pfam00084
Sushi repeat (SCR repeat);
89-144 2.38e-11

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 59.82  E-value: 2.38e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1331817272   89 CPAPVSFENGIYTPRLGSYPVGGNVSFECEDGFILRGSPVRQCRPNGMWDGETAVC 144
Cdd:pfam00084    1 CPPPPDIPNGKVSATKNEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 516-569 3.49e-11

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 [Multi-domain]  Cd Length: 56  Bit Score: 59.46  E-value: 3.49e-11
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 1331817272   516 CSNPGIPIGTRKVGSQ--YRLEDSVTYHCSRGLTLRGSQRRTCQEGGSWSGTEPSC 569
Cdd:smart00032    1 CPPPPDIENGTVTSSSgtYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
Sushi pfam00084
Sushi repeat (SCR repeat);
454-509 4.10e-10

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 56.35  E-value: 4.10e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1331817272  454 CPRPHDFENGEYWPRSPYYNVSDEISFHCYDGYTLRGSANRTCQVNGRWSGQTAIC 509
Cdd:pfam00084    1 CPPPPDIPNGKVSATKNEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 620-786 1.81e-09

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: 58.55  E-value: 1.81e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272  620 MNIYLVLDGSDSIGASN-FTGAKKCLVNLIEKVASYGVKPRYGLVTYATHPKIWVKVSDPDSSNAD---WVTKQLNEINY 695
Cdd:cd01471      1 LDLYLLVDGSGSIGYSNwVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSPNSTNKDlalNAIRALLSLYY 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272  696 EdhklKSGTNTKKALQAVYSMMSwpdDIPPEGWNRTRHVIIlMTDGLHNMGGDPITVIDEIRDLLYIgkdrknpredyld 775
Cdd:cd01471     81 P----NGSTNTTSALLVVEKHLF---DTRGNRENAPQLVII-MTDGIPDSKFRTLKEARKLRERGVI------------- 139

                          170
                   ....*....|.
gi 1331817272  776 VYVFGVGPLVN 786
Cdd:cd01471    140 IAVLGVGQGVN 150
PHA02927 PHA02927
secreted complement-binding protein; Provisional
 24-144 2.73e-09

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 59.28  E-value: 2.73e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272   24 CPQNVNISGGTFT-LSHGWAPGSLLTYSCPQGLYPSPASRLCKSSGQWQTPgatrslskAVCKPVRCPAPvSFENGIYTP 102
Cdd:PHA02927   148 CQSPPSISNGRHNgYEDFYTDGSVVTYSCNSGYSLIGNSGVLCSGGEWSDP--------PTCQIVKCPHP-TISNGYLSS 218

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1331817272  103 RLG-SYPVGGNVSFECEDGFILRGSPVRQCRPNGMWDGETAVC 144
Cdd:PHA02927   219 GFKrSYSYNDNVDFKCKYGYKLSGSSSSTCSPGNTWQPELPKC 261
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 576-816 3.39e-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: 59.18  E-value: 3.39e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272  576 DTPQEVAEAFLSSLTETIEGVDAEDGHGPGEQQKRKIVLDPSGSMNIYLVLDGSDSIGASN-FTGAKKCLVNLIEkvaSY 654
Cdd:COG1240     49 LLLGLAGLGLLALLLAALLLLLAVLLLLLALALAPLALARPQRGRDVVLVVDASGSMAAENrLEAAKGALLDFLD---DY 125

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272  655 GVKPRYGLVTYATHPKIWVkvsdPDSSNADWVTKQLNEInyedhKLKSGTNTKKALQAVYSMMswpDDIPPEGwnrtRHV 734
Cdd:COG1240    126 RPRDRVGLVAFGGEAEVLL----PLTRDREALKRALDEL-----PPGGGTPLGDALALALELL---KRADPAR----RKV 189

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272  735 IILMTDGLHNMG-GDPITVIDEIrdllyigkdrknpREDYLDVYVFGVG-PLVNQVNINALAskkdnEQ---HVFKVKDM 809
Cdd:COG1240    190 IVLLTDGRDNAGrIDPLEAAELA-------------AAAGIRIYTIGVGtEAVDEGLLREIA-----EAtggRYFRADDL 251


                   ....*..
gi 1331817272  810 ENLEDVF 816
Cdd:COG1240    252 SELAAIY 258
PHA02927 PHA02927
secreted complement-binding protein; Provisional
 451-569 5.97e-09

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 58.13  E-value: 5.97e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272  451 AIHCPRPHDFENGEYWPRSPYYNVSDEISFHCYDGYTLRGSANRTCQvNGRWSgQTAICDngAGYCSNPGIPIGTRKVG- 529
Cdd:PHA02927   145 SVKCQSPPSISNGRHNGYEDFYTDGSVVTYSCNSGYSLIGNSGVLCS-GGEWS-DPPTCQ--IVKCPHPTISNGYLSSGf 220

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1331817272  530 -SQYRLEDSVTYHCSRGLTLRGSQRRTCQEGGSWSGTEPSC 569
Cdd:PHA02927   221 kRSYSYNDNVDFKCKYGYKLSGSSSSTCSPGNTWQPELPKC 261
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 620-815 7.88e-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: 56.21  E-value: 7.88e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272  620 MNIYLVLDGSDSIGASNFTGAKKCLVNLIEKVASYGVKPRYGLVTYATHPKI------WVKVSDPDSsnadwVTKQLnei 693
Cdd:cd01469      1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTeftlneYRTKEEPLS-----LVKHI--- 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272  694 nyedHKLKSGTNTKKALQAVYSmmswpddippEGWNRTR-------HVIILMTDGLHNMGGDPITVIDEirdllyigkdr 766
Cdd:cd01469     73 ----SQLLGLTNTATAIQYVVT----------ELFSESNgarkdatKVLVVITDGESHDDPLLKDVIPQ----------- 127

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1331817272  767 knPREDYLDVYVFGVGPLVNQVN----INALASKKDnEQHVFKVKDMENLEDV 815
Cdd:cd01469    128 --AEREGIIRYAIGVGGHFQRENsreeLKTIASKPP-EEHFFNVTDFAALKDI 177
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 621-741 8.41e-08

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: 53.00  E-value: 8.41e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272  621 NIYLVLDGSDSIGASNFTGAKKCLVNLIEKVASYGVKPRYGLVTYATHPKIWVKVSDPdsSNADWVTKQLNEINYedhkL 700
Cdd:cd01472      2 DIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTY--RSKDDVLEAVKNLRY----I 75

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1331817272  701 KSGTNTKKALQAVYSMMSWPDDIPPEGWNRtrhVIILMTDG 741
Cdd:cd01472     76 GGGTNTGKALKYVRENLFTEASGSREGVPK---VLVVITDG 113
Sushi pfam00084
Sushi repeat (SCR repeat);
531-569 1.20e-07

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 49.42  E-value: 1.20e-07
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1331817272  531 QYRLEDSVTYHCSRGLTLRGSQRRTCQEGGSWSGTEPSC 569
Cdd:pfam00084   18 EYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 149-212 1.45e-07

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: 52.29  E-value: 1.45e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1331817272  149 HENGTGTNTYAALNSVYLMMNNqmrllgmETMAWQEIRHAIILLTDGKSNMGGSPKTAVDHIRE 212
Cdd:cd01450     74 YLGGGGTNTGKALQYALEQLFS-------ESNARENVPKVIIVLTDGRSDDGGDPKEAAAKLKD 130
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 612-816 3.87e-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: 53.18  E-value: 3.87e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272  612 IVLDPSGSMNiylvldgSDSIGAsnftgAKKCLVNLIEKVasygvKP--RYGLVTYATHPKIWV---KVSDPDSsnadwV 686
Cdd:COG2304     96 FVIDVSGSMS-------GDKLEL-----AKEAAKLLVDQL-----RPgdRVSIVTFAGDARVLLpptPATDRAK-----I 153

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272  687 TKQLNEInyedhKLKSGTNTKKALQAVYSMMSwpddiPPEGWNRTRHVIiLMTDGLHNMGgdpITVIDEIRDLLyigkdr 766
Cdd:COG2304    154 LAAIDRL-----QAGGGTALGAGLELAYELAR-----KHFIPGRVNRVI-LLTDGDANVG---ITDPEELLKLA------ 213

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1331817272  767 KNPREDYLDVYVFGVGPLVNQVNINALASKKDNEqhVFKVKDMENLEDVF 816
Cdd:COG2304    214 EEAREEGITLTTLGVGSDYNEDLLERLADAGGGN--YYYIDDPEEAEKVF 261
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 618-801 4.82e-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: 51.23  E-value: 4.82e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272  618 GSMNIYLVLDGSDSIGASNFTGAKKCLVNLIEKVAS-YGVKP-----RYGLVTYATHPKIwVKVSDPDSSNADWVTKQLN 691
Cdd:cd01480      1 GPVDITFVLDSSESVGLQNFDITKNFVKRVAERFLKdYYRKDpagswRVGVVQYSDQQEV-EAGFLRDIRNYTSLKEAVD 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272  692 EINYedhkLKSGTNTKKALQAVYSMMSwpdDIPPEGWNRtrhVIILMTDGlHNMGGDPITVIDEIRDLLYIGkdrknpre 771
Cdd:cd01480     80 NLEY----IGGGTFTDCALKYATEQLL---EGSHQKENK---FLLVITDG-HSDGSPDGGIEKAVNEADHLG-------- 140

                          170       180       190
                   ....*....|....*....|....*....|
gi 1331817272  772 dyLDVYVFGVGPLVNQVNINALASKKDNEQ 801
Cdd:cd01480    141 --IKIFFVAVGSQNEEPLSRIACDGKSALY 168
PHA02817 PHA02817
EEV Host range protein; Provisional
 454-569 5.58e-07

EEV Host range protein; Provisional


Pssm-ID: 165167 [Multi-domain]  Cd Length: 225  Bit Score: 51.87  E-value: 5.58e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272  454 CPRPHDFENGEYWPRSPYYNVSDEISFHCYDG-----YTLRGSANRTCQVNGRWSGQTAICDngAGYCSNP--------G 520
Cdd:PHA02817    24 CCYPPSIKNGYIYNKKTEYNIGSNVTFFCGNNtrgvrYTLVGEKNIICEKDGKWNKEFPVCK--IIRCRFPalqngfvnG 101

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1331817272  521 IPigtrkVGSQYRLEDSVTYHCSRGLTLRGSQRRTCQEGGSWSGTEPSC 569
Cdd:PHA02817   102 IP-----DSKKFYYESEVSFSCKPGFVLIGTKYSVCGINSSWIPKVPIC 145
PHA02927 PHA02927
secreted complement-binding protein; Provisional
 454-570 1.06e-06

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 51.58  E-value: 1.06e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272  454 CPRPHDFENGEYWPRSPYYNVSdeISFHCYDGYTLRGSANRTCQVNGR----WSGQTAICDNGAgyC-SNPGIPIGTRKV 528
Cdd:PHA02927    86 CPSPRDIDNGQLDIGGVDFGSS--ITYSCNSGYQLIGESKSYCELGSTgsmvWNPEAPICESVK--CqSPPSISNGRHNG 161

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1331817272  529 GSQYRLEDS-VTYHCSRGLTLRGSQRRTCQeGGSWSgTEPSCQ 570
Cdd:PHA02927   162 YEDFYTDGSvVTYSCNSGYSLIGNSGVLCS-GGEWS-DPPTCQ 202
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 622-808 4.08e-06

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: 48.05  E-value: 4.08e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272  622 IYLVLDGSDSIGASNFTGAKKCLVNLIEKVASYGVKPRYGLVTYATHPKIWVKVsDPDSSNADwVTKQLNEINYedhklK 701
Cdd:cd01482      3 IVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDL-NAYTSKED-VLAAIKNLPY-----K 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272  702 SG-TNTKKALQAVYSMMSWPDDIPPEGwnrTRHVIILMTDGLHNmggdpitviDEIRDllyIGKDRKNpredyLDVYVFG 780
Cdd:cd01482     76 GGnTRTGKALTHVREKNFTPDAGARPG---VPKVVILITDGKSQ---------DDVEL---PARVLRN-----LGVNVFA 135

                          170       180       190
                   ....*....|....*....|....*....|
gi 1331817272  781 VGplVNQVNINALAS--KKDNEQHVFKVKD 808
Cdd:cd01482    136 VG--VKDADESELKMiaSKPSETHVFNVAD 163
PHA02639 PHA02639
EEV host range protein; Provisional
 448-570 5.82e-06

EEV host range protein; Provisional


Pssm-ID: 165022 [Multi-domain]  Cd Length: 295  Bit Score: 49.66  E-value: 5.82e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272  448 GGSAIHCPRPHDFENGEYWPRSPYYNVSDEISFHCYDGYTLRGSANRTC---QVNGRWSGQTAICdnGAGYCSNPGIPIG 524
Cdd:PHA02639    16 GVKSIYCDKPDDISNGFITELMEKYEIGKLIEYTCNTDYALIGDRFRTCikdKNNAIWSNKAPFC--MLKECNDPPSIIN 93

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1331817272  525 TRKVGSQ--YRLEDSVTYHCS--RGL--TLRGSQRRTCQEGGSWSGTEPSCQ 570
Cdd:PHA02639    94 GKIYNKRemYKVGDEIYYVCNehKGVqySLVGNEKITCIQDKSWKPDPPICK 145
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
 263-342 9.72e-06

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 47.75  E-value: 9.72e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272  263 CRGALISDQWVLTAAHCF---RDGNDHSLWRVNVGDPKSRWGkEFLIEKAVISPGFDVFAKknqgilefYGDDIALLKLA 339
Cdd:COG3591     14 CTGTLIGPNLVLTAGHCVydgAGGGWATNIVFVPGYNGGPYG-TATATRFRVPPGWVASGD--------AGYDYALLRLD 84


                   ...
gi 1331817272  340 QKV 342
Cdd:COG3591     85 EPL 87
PHA02927 PHA02927
secreted complement-binding protein; Provisional
 24-137 4.56e-05

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 46.57  E-value: 4.56e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272   24 CPQNVNISGGTFTLShGWAPGSLLTYSCPQGLYpspasrLCKSSGQWQTPGATRSL----SKAVCKPVRCPAPVSFENGI 99
Cdd:PHA02927    86 CPSPRDIDNGQLDIG-GVDFGSSITYSCNSGYQ------LIGESKSYCELGSTGSMvwnpEAPICESVKCQSPPSISNGR 158

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1331817272  100 YTPRLGSYPVGGNVSFECEDGFILRGSPVRQCRpNGMW 137
Cdd:PHA02927   159 HNGYEDFYTDGSVVTYSCNSGYSLIGNSGVLCS-GGEW 195
PHA02817 PHA02817
EEV Host range protein; Provisional
 4-148 5.72e-05

EEV Host range protein; Provisional


Pssm-ID: 165167 [Multi-domain]  Cd Length: 225  Bit Score: 45.70  E-value: 5.72e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272    4 LMVLFCLLFLYPGL----ADSAPSC--PQNVNisGGTFTLSHGWAPGSLLTYSCPQGLYPSPASRL------CKSSGQWQ 71
Cdd:PHA02817     1 MKNIHMLLILLCNKvyslCDLNKCCypPSIKN--GYIYNKKTEYNIGSNVTFFCGNNTRGVRYTLVgekniiCEKDGKWN 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272   72 TpgatrslSKAVCKPVRCPAPV---SFENGIytPRLGSYPVGGNVSFECEDGFILRGSPVRQCRPNGMWDGETAVCDNGD 148
Cdd:PHA02817    79 K-------EFPVCKIIRCRFPAlqnGFVNGI--PDSKKFYYESEVSFSCKPGFVLIGTKYSVCGINSSWIPKVPICSRDN 149
PHA02639 PHA02639
EEV host range protein; Provisional
 454-569 1.27e-04

EEV host range protein; Provisional


Pssm-ID: 165022 [Multi-domain]  Cd Length: 295  Bit Score: 45.43  E-value: 1.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272  454 CPRPHDFENGEYWPRSPYYNVSDEISFHCYD----GYTLRGSANRTCQVNGRWSGQTAICDngAGYCSNPGIP---IGTR 526
Cdd:PHA02639    85 CNDPPSIINGKIYNKREMYKVGDEIYYVCNEhkgvQYSLVGNEKITCIQDKSWKPDPPICK--MINCRFPALQngyINGI 162

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1331817272  527 KVGSQYRLEDSVTYHCSRGLTLRGSQRRTCQEGGSWSGTEPSC 569
Cdd:PHA02639   163 PSNKKFYYKTRVGFSCKSGFDLVGEKYSTCNINATWFPSIPTC 205
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
 861-1075 1.32e-04

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 44.28  E-value: 1.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272  861 SCMGAVVSEYFVLTAAHCFTVDDKEH---SIKVSVGGEKRD---LEIEVVLFHPNYNINGKkaagipefYDYDVALIKLK 934
Cdd:COG3591     13 VCTGTLIGPNLVLTAGHCVYDGAGGGwatNIVFVPGYNGGPygtATATRFRVPPGWVASGD--------AGYDYALLRLD 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272  935 NKLkygqtirpiclpctEGTTRALRLPPTTTcqqqkeellpaqdikalfvseeekKLTRKEVYIkngdkkgscerdAQYa 1014
Cdd:COG3591     85 EPL--------------GDTTGWLGLAFNDA------------------------PLAGEPVTI------------IGY- 113

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1331817272 1015 pGYDKVKDISevvtprFLCTGGVSPYADP------NTCRGDSGGPLIVHKRSRFIQVGVISWGVVDV 1075
Cdd:COG3591    114 -PGDRPKDLS------LDCSGRVTGVQGNrlsydcDTTGGSSGSPVLDDSDGGGRVVGVHSAGGADR 173
PHA02831 PHA02831
EEV host range protein; Provisional
 83-137 2.42e-04

EEV host range protein; Provisional


Pssm-ID: 165176 [Multi-domain]  Cd Length: 268  Bit Score: 44.21  E-value: 2.42e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1331817272   83 VCKPVRCPAPvSFENGIYTPRLGSYPVGGNVSFECEDGFILRGSPVRQCRPNGMW 137
Cdd:PHA02831   135 VCKLIRCKYP-ALQNGFLNVFEKKFYYGDIVNFKCKKGFILLGSSVSTCDINSIW 188
VWA_2 pfam13519
von Willebrand factor type A domain;
612-737 3.58e-04

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 41.12  E-value: 3.58e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272  612 IVLDPSGSMniylvldGSDSIGASNFTGAKKCLVNLIEKVAsyGVkpRYGLVTYATHPKIWVkvsdPDSSNADWVTKQLN 691
Cdd:pfam13519    3 FVLDTSGSM-------RNGDYGPTRLEAAKDAVLALLKSLP--GD--RVGLVTFGDGPEVLI----PLTKDRAKILRALR 67

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1331817272  692 EINYEDhklkSGTNTKKALQAVYSMMswpddipPEGWNRTRHVIIL 737
Cdd:pfam13519   68 RLEPKG----GGTNLAAALQLARAAL-------KHRRKNQPRRIVL 102
vWA_BatA_type cd01467
VWA BatA type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 612-782 1.93e-03

VWA BatA type: 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. Members of this subgroup are bacterial in origin. They are typified by the presence of a MIDAS motif.


Pssm-ID: 238744 [Multi-domain]  Cd Length: 180  Bit Score: 40.39  E-value: 1.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272  612 IVLDPSGSMNIylvldgSDSIGASNFTGAKKCLVNLIEKVASygvkPRYGLVTYATHPKIWVkvsdPDSSNADWVTKQLN 691
Cdd:cd01467      7 IALDVSGSMLA------QDFVKPSRLEAAKEVLSDFIDRREN----DRIGLVVFAGAAFTQA----PLTLDRESLKELLE 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272  692 EINYEDhkLKSGTNTKKALQ-AVYSMMswpddiPPEGWNRtrhVIILMTDGLHNMGG-DPITVIDeirdllyIGKDRKnp 769
Cdd:cd01467     73 DIKIGL--AGQGTAIGDAIGlAIKRLK------NSEAKER---VIVLLTDGENNAGEiDPATAAE-------LAKNKG-- 132

                          170
                   ....*....|...
gi 1331817272  770 redyLDVYVFGVG 782
Cdd:cd01467    133 ----VRIYTIGVG 141
PHA02831 PHA02831
EEV host range protein; Provisional
 437-569 4.25e-03

EEV host range protein; Provisional


Pssm-ID: 165176 [Multi-domain]  Cd Length: 268  Bit Score: 40.36  E-value: 4.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272  437 SGTQEDESPCKGGSaiHCPRPHDFENGEYWPRSPYYNVSDEISFHC----YDGYTLRGSANRTCqVNGRWSGQTAICDng 512
Cdd:PHA02831    63 NGSWSTKNMCIGKR--NCKDPVTILNGYIKNKKDQYSFGDSVTYACkvnkLEKYSIVGNETVKC-INKQWVPKYPVCK-- 137

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1331817272  513 AGYCSNPGIPIGTRKV-GSQYRLEDSVTYHCSRGLTLRGSQRRTCQEGGSWSGTEPSC 569
Cdd:PHA02831   138 LIRCKYPALQNGFLNVfEKKFYYGDIVNFKCKKGFILLGSSVSTCDINSIWYPGIPKC 195
PHA02954 PHA02954
EEV membrane glycoprotein; Provisional
 431-569 5.36e-03

EEV membrane glycoprotein; Provisional


Pssm-ID: 165263 [Multi-domain]  Cd Length: 317  Bit Score: 40.45  E-value: 5.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331817272  431 TDQFLCsgtQEDESPCKGGSAIHCP----RPHDFENGEYWPRSPYYNVSDEISFHCYDGYTLRGSANRTCQVNGrWSgqt 506
Cdd:PHA02954   105 TKYFRC---EEKNGNTSWNDTVTCPnaecQPLQLEHGSCQPVKEKYSFGEHITINCDVGYEVIGASYISCTANS-WN--- 177

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1331817272  507 aICDNGAGYCSNPGIPIGTRKvGSQYRLEDSVTYHCSRGLTLRGSQRRTCQEgGSWSGTEPSC 569
Cdd:PHA02954   178 -VIPSCQQKCDIPSLSNGLIS-GSTFSIGGVIHLSCKSGFTLTGSPSSTCID-GKWNPVLPIC 237
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH