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Conserved domains on  [gi|540344553|ref|NP_001269386|]
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complement C2 isoform 4 [Homo sapiens]

Protein Classification

vWFA and Tryp_SPc domain-containing protein( domain architecture ID 10208018)

vWFA and Tryp_SPc domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
vWFA super family cl00057
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 38-204 1.70e-81

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: 251.82  E-value: 1.70e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344553  38 IFSFEINVSVAIITFASEPKVLMSVLNDNSRDMTEVISSLENANYKDHENGTGTNTYAALNSVYLMmnnqMRLLGME-TM 116
Cdd:cd01470   32 ISSYEVSPRYEIISYASDPKEIVSIRDFNSNDADDVIKRLEDFNYDDHGDKTGTNTAAALKKVYER----MALEKVRnKE 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344553 117 AWQEIRHAIILLTDGKSNMGGSPKTAVDHIREILNINQK----RNDYLDIYAIGVGKlDVDWRELNELGSKKDGERHAFI 192
Cdd:cd01470  108 AFNETRHVIILFTDGKSNMGGSPLPTVDKIKNLVYKNNKsdnpREDYLDVYVFGVGD-DVNKEELNDLASKKDNERHFFK 186

                        170
                 ....*....|..
gi 540344553 193 LQDTKALHQVFE 204
Cdd:cd01470  187 LKDYEDLQEVFD 198
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 227-496 2.87e-41

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: 147.81  E-value: 2.87e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344553 227 SDQERTPWHVTIKPKS-QETCRGALISDQWVLTAAHCFRdGNDHSLWRVNVGD----PKSQWGKEFLIEKAVISPGFDVF 301
Cdd:cd00190    7 AKIGSFPWQVSLQYTGgRHFCGGSLISPRWVLTAAHCVY-SSAPSNYTVRLGShdlsSNEGGGQVIKVKKVIVHPNYNPS 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344553 302 akknqgileFYGDDIALLKLAQKVKMSTHARPICLPCTMEANlalrrPQGSTCR-----DHENEllnkqsvpahfVALNG 376
Cdd:cd00190   86 ---------TYDNDIALLKLKRPVTLSDNVRPICLPSSGYNL-----PAGTTCTvsgwgRTSEG-----------GPLPD 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344553 377 SKLNINLKMgVEWTSCAEVVSQektmfpnltdvREVVTDQFLCSGTQE-DESPCKGESGGAVFLERRFRFFQVGLVSWGl 455
Cdd:cd00190  141 VLQEVNVPI-VSNAECKRAYSY-----------GGTITDNMLCAGGLEgGKDACQGDSGGPLVCNDNGRGVLVGIVSWG- 207

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 540344553 456 ynpcLGSADKNSrkraprskvppPRDFHiNLFRMQPWLRQH 496
Cdd:cd00190  208 ----SGCARPNY-----------PGVYT-RVSSYLDWIQKT 232
 
Name Accession Description Interval E-value
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
 38-204 1.70e-81

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: 251.82  E-value: 1.70e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344553  38 IFSFEINVSVAIITFASEPKVLMSVLNDNSRDMTEVISSLENANYKDHENGTGTNTYAALNSVYLMmnnqMRLLGME-TM 116
Cdd:cd01470   32 ISSYEVSPRYEIISYASDPKEIVSIRDFNSNDADDVIKRLEDFNYDDHGDKTGTNTAAALKKVYER----MALEKVRnKE 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344553 117 AWQEIRHAIILLTDGKSNMGGSPKTAVDHIREILNINQK----RNDYLDIYAIGVGKlDVDWRELNELGSKKDGERHAFI 192
Cdd:cd01470  108 AFNETRHVIILFTDGKSNMGGSPLPTVDKIKNLVYKNNKsdnpREDYLDVYVFGVGD-DVNKEELNDLASKKDNERHFFK 186

                        170
                 ....*....|..
gi 540344553 193 LQDTKALHQVFE 204
Cdd:cd01470  187 LKDYEDLQEVFD 198
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 227-496 2.87e-41

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: 147.81  E-value: 2.87e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344553 227 SDQERTPWHVTIKPKS-QETCRGALISDQWVLTAAHCFRdGNDHSLWRVNVGD----PKSQWGKEFLIEKAVISPGFDVF 301
Cdd:cd00190    7 AKIGSFPWQVSLQYTGgRHFCGGSLISPRWVLTAAHCVY-SSAPSNYTVRLGShdlsSNEGGGQVIKVKKVIVHPNYNPS 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344553 302 akknqgileFYGDDIALLKLAQKVKMSTHARPICLPCTMEANlalrrPQGSTCR-----DHENEllnkqsvpahfVALNG 376
Cdd:cd00190   86 ---------TYDNDIALLKLKRPVTLSDNVRPICLPSSGYNL-----PAGTTCTvsgwgRTSEG-----------GPLPD 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344553 377 SKLNINLKMgVEWTSCAEVVSQektmfpnltdvREVVTDQFLCSGTQE-DESPCKGESGGAVFLERRFRFFQVGLVSWGl 455
Cdd:cd00190  141 VLQEVNVPI-VSNAECKRAYSY-----------GGTITDNMLCAGGLEgGKDACQGDSGGPLVCNDNGRGVLVGIVSWG- 207

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 540344553 456 ynpcLGSADKNSrkraprskvppPRDFHiNLFRMQPWLRQH 496
Cdd:cd00190  208 ----SGCARPNY-----------PGVYT-RVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 227-459 2.68e-39

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: 142.43  E-value: 2.68e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344553   227 SDQERTPWHVTIKPKS-QETCRGALISDQWVLTAAHCFRdGNDHSLWRVNVGDPKSQWGKE---FLIEKAVISPGFDvfa 302
Cdd:smart00020   8 ANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVR-GSDPSNIRVRLGSHDLSSGEEgqvIKVSKVIIHPNYN--- 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344553   303 kknqgiLEFYGDDIALLKLAQKVKMSTHARPICLPCTmeanlALRRPQGSTCRD----HENEllnkqSVPAHFVALNGSK 378
Cdd:smart00020  84 ------PSTYDNDIALLKLKEPVTLSDNVRPICLPSS-----NYNVPAGTTCTVsgwgRTSE-----GAGSLPDTLQEVN 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344553   379 LNInlkmgVEWTSCAEVVSQektmfpnltdvREVVTDQFLCSGTQE-DESPCKGESGGAVFLERRfRFFQVGLVSWGlyN 457
Cdd:smart00020 148 VPI-----VSNATCRRAYSG-----------GGAITDNMLCAGGLEgGKDACQGDSGGPLVCNDG-RWVLVGIVSWG--S 208


                   ..
gi 540344553   458 PC 459
Cdd:smart00020 209 GC 210
Trypsin pfam00089
Trypsin;
233-454 9.96e-24

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 99.05  E-value: 9.96e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344553  233 PWHVTIK-PKSQETCRGALISDQWVLTAAHCFRDGNDhslWRVNVGDP----KSQWGKEFLIEKAVISPGFDVFAKKNqg 307
Cdd:pfam00089  13 PWQVSLQlSSGKHFCGGSLISENWVLTAAHCVSGASD---VKVVLGAHnivlREGGEQKFDVEKIIVHPNYNPDTLDN-- 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344553  308 ilefygdDIALLKLAQKVKMSTHARPICLPCTmeanlALRRPQGSTC------RDHEN---ELLNKQSVPahfvalngsk 378
Cdd:pfam00089  88 -------DIALLKLESPVTLGDTVRPICLPDA-----SSDLPVGTTCtvsgwgNTKTLgpsDTLQEVTVP---------- 145

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 540344553  379 lninlkmgvewtscaeVVSQEKtmfpNLTDVREVVTDQFLCSGTQeDESPCKGESGGAVFLERRfrfFQVGLVSWG 454
Cdd:pfam00089 146 ----------------VVSRET----CRSAYGGTVTDTMICAGAG-GKDACQGDSGGPLVCSDG---ELIGIVSWG 197
VWA pfam00092
von Willebrand factor type A domain;
44-205 1.25e-21

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 91.95  E-value: 1.25e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344553   44 NVSVAIITFASEPKVLMSvLNDNsRDMTEVISSLENANYKDH-ENGTGTNTYAALNSVYLMMNNQMRllgmetmawqEIR 122
Cdd:pfam00092  37 GTRVGLVQYSSDVRTEFP-LNDY-SSKEELLSAVDNLRYLGGgTTNTGKALKYALENLFSSAAGARP----------GAP 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344553  123 HAIILLTDGKSNMgGSPKTAVDHIREiLNINqkrndyldIYAIGVGklDVDWRELNELGSKKDgERHAFILQDTKALHQV 202
Cdd:pfam00092 105 KVVVLLTDGRSQD-GDPEEVARELKS-AGVT--------VFAVGVG--NADDEELRKIASEPG-EGHVFTVSDFEALEDL 171


                  ...
gi 540344553  203 FEH 205
Cdd:pfam00092 172 QDQ 174
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 225-463 6.82e-21

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 92.02  E-value: 6.82e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344553 225 NASDQERtPWHVTIKPKS---QETCRGALISDQWVLTAAHCFRDGNDHSLwRVNVG--DPKSQWGKEFLIEKAVISPGFD 299
Cdd:COG5640   36 PATVGEY-PWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDGPSDL-RVVIGstDLSTSGGTVVKVARIVVHPDYD 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344553 300 VFAkknqgilefYGDDIALLKLAQKVkmsTHARPICLPctmEANLALRRPQ-------GSTCRDHEN--ELLNKQSVPAh 370
Cdd:COG5640  114 PAT---------PGNDIALLKLATPV---PGVAPAPLA---TSADAAAPGTpatvagwGRTSEGPGSqsGTLRKADVPV- 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344553 371 fvalngsklninlkmgVEWTSCAevvsqektmfpnltDVREVVTDQFLCSGTQE-DESPCKGESGGAVFLERRFRFFQVG 449
Cdd:COG5640  178 ----------------VSDATCA--------------AYGGFDGGTMLCAGYPEgGKDACQGDSGGPLVVKDGGGWVLVG 227

                        250
                 ....*....|....
gi 540344553 450 LVSWGlYNPCLGSA 463
Cdd:COG5640  228 VVSWG-GGPCAAGY 240
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 37-201 1.28e-16

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: 77.49  E-value: 1.28e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344553    37 AIFSFEINVSVAIITFASEPKVLMSVlnDNSRDMTEVISSLENANYKDhenGTGTNTYAALNSVYLMMNNQMRllgmetm 116
Cdd:smart00327  30 QLDIGPDGDRVGLVTFSDDARVLFPL--NDSRSKDALLEALASLSYKL---GGGTNLGAALQYALENLFSKSA------- 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344553   117 AWQE-IRHAIILLTDGKSNMGGSpktavdhiREILNINQKRNDYLDIYAIGVGKlDVDWRELNELgSKKDGERHAFILQD 195
Cdd:smart00327  98 GSRRgAPKVVILITDGESNDGPK--------DLLKAAKELKRSGVKVFVVGVGN-DVDEEELKKL-ASAPGGVYVFLPEL 167


                   ....*.
gi 540344553   196 TKALHQ 201
Cdd:smart00327 168 LDLLID 173
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 47-204 4.77e-10

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: 60.34  E-value: 4.77e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344553  47 VAIITFASEPKVLMSVlndnSRDMTEVISSLENANYkdhenGTGTNTYAALNSVYLMMNNQMrllgmetmawQEIRHAII 126
Cdd:COG1240  131 VGLVAFGGEAEVLLPL----TRDREALKRALDELPP-----GGGTPLGDALALALELLKRAD----------PARRKVIV 191

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 540344553 127 LLTDGKSNMG-GSPKTAVDHIREiLNInqkrndylDIYAIGVGKLDVDWRELNELGSKKDGErhAFILQDTKALHQVFE 204
Cdd:COG1240  192 LLTDGRDNAGrIDPLEAAELAAA-AGI--------RIYTIGVGTEAVDEGLLREIAEATGGR--YFRADDLSELAAIYR 259
 
Name Accession Description Interval E-value
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
 38-204 1.70e-81

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: 251.82  E-value: 1.70e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344553  38 IFSFEINVSVAIITFASEPKVLMSVLNDNSRDMTEVISSLENANYKDHENGTGTNTYAALNSVYLMmnnqMRLLGME-TM 116
Cdd:cd01470   32 ISSYEVSPRYEIISYASDPKEIVSIRDFNSNDADDVIKRLEDFNYDDHGDKTGTNTAAALKKVYER----MALEKVRnKE 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344553 117 AWQEIRHAIILLTDGKSNMGGSPKTAVDHIREILNINQK----RNDYLDIYAIGVGKlDVDWRELNELGSKKDGERHAFI 192
Cdd:cd01470  108 AFNETRHVIILFTDGKSNMGGSPLPTVDKIKNLVYKNNKsdnpREDYLDVYVFGVGD-DVNKEELNDLASKKDNERHFFK 186

                        170
                 ....*....|..
gi 540344553 193 LQDTKALHQVFE 204
Cdd:cd01470  187 LKDYEDLQEVFD 198
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 227-496 2.87e-41

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: 147.81  E-value: 2.87e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344553 227 SDQERTPWHVTIKPKS-QETCRGALISDQWVLTAAHCFRdGNDHSLWRVNVGD----PKSQWGKEFLIEKAVISPGFDVF 301
Cdd:cd00190    7 AKIGSFPWQVSLQYTGgRHFCGGSLISPRWVLTAAHCVY-SSAPSNYTVRLGShdlsSNEGGGQVIKVKKVIVHPNYNPS 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344553 302 akknqgileFYGDDIALLKLAQKVKMSTHARPICLPCTMEANlalrrPQGSTCR-----DHENEllnkqsvpahfVALNG 376
Cdd:cd00190   86 ---------TYDNDIALLKLKRPVTLSDNVRPICLPSSGYNL-----PAGTTCTvsgwgRTSEG-----------GPLPD 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344553 377 SKLNINLKMgVEWTSCAEVVSQektmfpnltdvREVVTDQFLCSGTQE-DESPCKGESGGAVFLERRFRFFQVGLVSWGl 455
Cdd:cd00190  141 VLQEVNVPI-VSNAECKRAYSY-----------GGTITDNMLCAGGLEgGKDACQGDSGGPLVCNDNGRGVLVGIVSWG- 207

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 540344553 456 ynpcLGSADKNSrkraprskvppPRDFHiNLFRMQPWLRQH 496
Cdd:cd00190  208 ----SGCARPNY-----------PGVYT-RVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 227-459 2.68e-39

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: 142.43  E-value: 2.68e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344553   227 SDQERTPWHVTIKPKS-QETCRGALISDQWVLTAAHCFRdGNDHSLWRVNVGDPKSQWGKE---FLIEKAVISPGFDvfa 302
Cdd:smart00020   8 ANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVR-GSDPSNIRVRLGSHDLSSGEEgqvIKVSKVIIHPNYN--- 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344553   303 kknqgiLEFYGDDIALLKLAQKVKMSTHARPICLPCTmeanlALRRPQGSTCRD----HENEllnkqSVPAHFVALNGSK 378
Cdd:smart00020  84 ------PSTYDNDIALLKLKEPVTLSDNVRPICLPSS-----NYNVPAGTTCTVsgwgRTSE-----GAGSLPDTLQEVN 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344553   379 LNInlkmgVEWTSCAEVVSQektmfpnltdvREVVTDQFLCSGTQE-DESPCKGESGGAVFLERRfRFFQVGLVSWGlyN 457
Cdd:smart00020 148 VPI-----VSNATCRRAYSG-----------GGAITDNMLCAGGLEgGKDACQGDSGGPLVCNDG-RWVLVGIVSWG--S 208


                   ..
gi 540344553   458 PC 459
Cdd:smart00020 209 GC 210
Trypsin pfam00089
Trypsin;
233-454 9.96e-24

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 99.05  E-value: 9.96e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344553  233 PWHVTIK-PKSQETCRGALISDQWVLTAAHCFRDGNDhslWRVNVGDP----KSQWGKEFLIEKAVISPGFDVFAKKNqg 307
Cdd:pfam00089  13 PWQVSLQlSSGKHFCGGSLISENWVLTAAHCVSGASD---VKVVLGAHnivlREGGEQKFDVEKIIVHPNYNPDTLDN-- 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344553  308 ilefygdDIALLKLAQKVKMSTHARPICLPCTmeanlALRRPQGSTC------RDHEN---ELLNKQSVPahfvalngsk 378
Cdd:pfam00089  88 -------DIALLKLESPVTLGDTVRPICLPDA-----SSDLPVGTTCtvsgwgNTKTLgpsDTLQEVTVP---------- 145

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 540344553  379 lninlkmgvewtscaeVVSQEKtmfpNLTDVREVVTDQFLCSGTQeDESPCKGESGGAVFLERRfrfFQVGLVSWG 454
Cdd:pfam00089 146 ----------------VVSRET----CRSAYGGTVTDTMICAGAG-GKDACQGDSGGPLVCSDG---ELIGIVSWG 197
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 38-191 4.50e-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: 238727 [Multi-domain]  Cd Length: 161  Bit Score: 95.44  E-value: 4.50e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344553  38 IFSFEINVSVAIITFASEPKVLMSVLNDNSRDmtEVISSLENANYKDhenGTGTNTYAALNSVYLMMNNqmrllgmETMA 117
Cdd:cd01450   32 LDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKD--DLLKAVKNLKYLG---GGGTNTGKALQYALEQLFS-------ESNA 99

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 540344553 118 WQEIRHAIILLTDGKSNMGGSPKTAVDHIREIlninqkrndYLDIYAIGVGklDVDWRELNELGSKKdGERHAF 191
Cdd:cd01450  100 RENVPKVIIVLTDGRSDDGGDPKEAAAKLKDE---------GIKVFVVGVG--PADEEELREIASCP-SERHVF 161
VWA pfam00092
von Willebrand factor type A domain;
44-205 1.25e-21

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 91.95  E-value: 1.25e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344553   44 NVSVAIITFASEPKVLMSvLNDNsRDMTEVISSLENANYKDH-ENGTGTNTYAALNSVYLMMNNQMRllgmetmawqEIR 122
Cdd:pfam00092  37 GTRVGLVQYSSDVRTEFP-LNDY-SSKEELLSAVDNLRYLGGgTTNTGKALKYALENLFSSAAGARP----------GAP 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344553  123 HAIILLTDGKSNMgGSPKTAVDHIREiLNINqkrndyldIYAIGVGklDVDWRELNELGSKKDgERHAFILQDTKALHQV 202
Cdd:pfam00092 105 KVVVLLTDGRSQD-GDPEEVARELKS-AGVT--------VFAVGVG--NADDEELRKIASEPG-EGHVFTVSDFEALEDL 171


                  ...
gi 540344553  203 FEH 205
Cdd:pfam00092 172 QDQ 174
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 225-463 6.82e-21

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 92.02  E-value: 6.82e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344553 225 NASDQERtPWHVTIKPKS---QETCRGALISDQWVLTAAHCFRDGNDHSLwRVNVG--DPKSQWGKEFLIEKAVISPGFD 299
Cdd:COG5640   36 PATVGEY-PWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDGPSDL-RVVIGstDLSTSGGTVVKVARIVVHPDYD 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344553 300 VFAkknqgilefYGDDIALLKLAQKVkmsTHARPICLPctmEANLALRRPQ-------GSTCRDHEN--ELLNKQSVPAh 370
Cdd:COG5640  114 PAT---------PGNDIALLKLATPV---PGVAPAPLA---TSADAAAPGTpatvagwGRTSEGPGSqsGTLRKADVPV- 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344553 371 fvalngsklninlkmgVEWTSCAevvsqektmfpnltDVREVVTDQFLCSGTQE-DESPCKGESGGAVFLERRFRFFQVG 449
Cdd:COG5640  178 ----------------VSDATCA--------------AYGGFDGGTMLCAGYPEgGKDACQGDSGGPLVVKDGGGWVLVG 227

                        250
                 ....*....|....
gi 540344553 450 LVSWGlYNPCLGSA 463
Cdd:COG5640  228 VVSWG-GGPCAAGY 240
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 37-201 1.28e-16

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: 77.49  E-value: 1.28e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344553    37 AIFSFEINVSVAIITFASEPKVLMSVlnDNSRDMTEVISSLENANYKDhenGTGTNTYAALNSVYLMMNNQMRllgmetm 116
Cdd:smart00327  30 QLDIGPDGDRVGLVTFSDDARVLFPL--NDSRSKDALLEALASLSYKL---GGGTNLGAALQYALENLFSKSA------- 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344553   117 AWQE-IRHAIILLTDGKSNMGGSpktavdhiREILNINQKRNDYLDIYAIGVGKlDVDWRELNELgSKKDGERHAFILQD 195
Cdd:smart00327  98 GSRRgAPKVVILITDGESNDGPK--------DLLKAAKELKRSGVKVFVVGVGN-DVDEEELKKL-ASAPGGVYVFLPEL 167


                   ....*.
gi 540344553   196 TKALHQ 201
Cdd:smart00327 168 LDLLID 173
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 44-188 2.92e-10

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: 58.73  E-value: 2.92e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344553  44 NVSVAIITFASEPKVLMSVLNDNSRDmtEVISSLENANYKdheNGTGTNTYAALNSVYLMMNNQMRLLGmetmawqeiRH 123
Cdd:cd00198   38 GDRVGLVTFGSNARVVLPLTTDTDKA--DLLEAIDALKKG---LGGGTNIGAALRLALELLKSAKRPNA---------RR 103

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 540344553 124 AIILLTDGKSNMGGSPKTAVdhIREIlninqkRNDYLDIYAIGVGkLDVDWRELNELGSKKDGER 188
Cdd:cd00198  104 VIILLTDGEPNDGPELLAEA--AREL------RKLGITVYTIGIG-DDANEDELKEIADKTTGGA 159
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 47-204 4.77e-10

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: 60.34  E-value: 4.77e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344553  47 VAIITFASEPKVLMSVlndnSRDMTEVISSLENANYkdhenGTGTNTYAALNSVYLMMNNQMrllgmetmawQEIRHAII 126
Cdd:COG1240  131 VGLVAFGGEAEVLLPL----TRDREALKRALDELPP-----GGGTPLGDALALALELLKRAD----------PARRKVIV 191

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 540344553 127 LLTDGKSNMG-GSPKTAVDHIREiLNInqkrndylDIYAIGVGKLDVDWRELNELGSKKDGErhAFILQDTKALHQVFE 204
Cdd:COG1240  192 LLTDGRDNAGrIDPLEAAELAAA-AGI--------RIYTIGVGTEAVDEGLLREIAEATGGR--YFRADDLSELAAIYR 259
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 47-238 9.09e-08

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 53.57  E-value: 9.09e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344553  47 VAIITFASEPKVLM-SVLNDNSRDMTEVISSLEnAnykdhenGTGTNTYAALNSVYlmmnNQMRllgmETMAWQEIRHaI 125
Cdd:COG2304  129 VSIVTFAGDARVLLpPTPATDRAKILAAIDRLQ-A-------GGGTALGAGLELAY----ELAR----KHFIPGRVNR-V 191

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344553 126 ILLTDGKSNMGgspKTAVDHIREILNINQKRNdyLDIYAIGVGkldVDWRE--LNELGSKKDGeRHAFIlQDTKALHQVF 203
Cdd:COG2304  192 ILLTDGDANVG---ITDPEELLKLAEEAREEG--ITLTTLGVG---SDYNEdlLERLADAGGG-NYYYI-DDPEEAEKVF 261

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 540344553 204 EhmldvsKLTDTIcGVGNMSANASDQERTPWHVTI 238
Cdd:COG2304  262 V------REFSRI-GYENRALATEDFPLPYGTLKL 289
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
 246-325 5.77e-06

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 46.98  E-value: 5.77e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344553 246 CRGALISDQWVLTAAHCF---RDGNDHSLWRVNVGDPKSQWGkEFLIEKAVISPGFDVFAKknqgilefYGDDIALLKLA 322
Cdd:COG3591   14 CTGTLIGPNLVLTAGHCVydgAGGGWATNIVFVPGYNGGPYG-TATATRFRVPPGWVASGD--------AGYDYALLRLD 84


                 ...
gi 540344553 323 QKV 325
Cdd:COG3591   85 EPL 87
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 35-195 7.98e-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: 46.13  E-value: 7.98e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344553  35 SAAIFSFEI---NVSVAIITFASEPKVLMSVLNDNSRDmtEVISSLENANYKdhenGTGTNTYAALNsvYLMMNNQMRLL 111
Cdd:cd01482   26 SSVVEAFEIgpdGVQVGLVQYSDDPRTEFDLNAYTSKE--DVLAAIKNLPYK----GGNTRTGKALT--HVREKNFTPDA 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344553 112 GMEtmawQEIRHAIILLTDGKSNmggspktavDHIREilnINQK-RNDYLDIYAIGVGklDVDWRELNELGSKKDgERHA 190
Cdd:cd01482   98 GAR----PGVPKVVILITDGKSQ---------DDVEL---PARVlRNLGVNVFAVGVK--DADESELKMIASKPS-ETHV 158


                 ....*
gi 540344553 191 FILQD 195
Cdd:cd01482  159 FNVAD 163
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
44-182 3.28e-04

Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 41.83  E-value: 3.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344553  44 NVSVAIITFASEPKVLMsvlndnsrDMTEViSSLENANYkdhENGTGTNTYAALNSV-YLMMNNQMRLLGMETMAWQEIr 122
Cdd:COG4245   46 TVEVSVITFDGEAKVLL--------PLTDL-EDFQPPDL---SASGGTPLGAALELLlDLIERRVQKYTAEGKGDWRPV- 112

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344553 123 haIILLTDGKSNmGGSPKTAvdhIREILNINQKRNDYldIYAIGVGKlDVDWRELNELGS 182
Cdd:COG4245  113 --VFLITDGEPT-DSDWEAA---LQRLKDGEAAKKAN--IFAIGVGP-DADTEVLKQLTD 163
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 40-195 3.53e-04

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: 41.06  E-value: 3.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344553  40 SFEI---NVSVAIITFASEPKVlMSVLNdNSRDMTEVISSLENANYKdhenGTGTNTYAALNsvYLMMNNQMRLLGMEtm 116
Cdd:cd01472   31 RLDIgpdGVRVGVVQYSDDPRT-EFYLN-TYRSKDDVLEAVKNLRYI----GGGTNTGKALK--YVRENLFTEASGSR-- 100

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 540344553 117 awQEIRHAIILLTDGKSNMGGspktavdhireILNINQKRNDYLDIYAIGVGKLDVDwrELNELGSkKDGERHAFILQD 195
Cdd:cd01472  101 --EGVPKVLVVITDGKSQDDV-----------EEPAVELKQAGIEVFAVGVKNADEE--ELKQIAS-DPKELYVFNVAD 163
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 3-168 5.24e-04

Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain [Function unknown];


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 41.97  E-value: 5.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344553   3 TRSAIAAPRILCsrgL-RSGSARatGSGVERSPSAAIFSFEI---NVSVAIITFASEPKVLMSVLNDNS-RDMTEVISSL 77
Cdd:COG2425  113 AVPLLEGPVVLC---VdTSGSMA--GSKEAAAKAAALALLRAlrpNRRFGVILFDTEVVEDLPLTADDGlEDAIEFLSGL 187

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344553  78 ENanykdhenGTGTNTYAALNSvylmmnnqmrllGMETMAWQEIRHA-IILLTDGKSnmGGSPKTAVDHIReilninQKR 156
Cdd:COG2425  188 FA--------GGGTDIAPALRA------------ALELLEEPDYRNAdIVLITDGEA--GVSPEELLREVR------AKE 239

                        170
                 ....*....|..
gi 540344553 157 NDYlDIYAIGVG 168
Cdd:COG2425  240 SGV-RLFTVAIG 250
VWA_2 pfam13519
von Willebrand factor type A domain;
19-109 2.12e-03

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 37.66  E-value: 2.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344553   19 RSGSARATGSGVERSPSA-----AIFSFEINVSVAIITFASEPKVLMSvLNDNSRDMTEVISSLEnanykdhENGTGTNT 93
Cdd:pfam13519   7 TSGSMRNGDYGPTRLEAAkdavlALLKSLPGDRVGLVTFGDGPEVLIP-LTKDRAKILRALRRLE-------PKGGGTNL 78

                          90
                  ....*....|....*.
gi 540344553   94 YAALNSVYLMMNNQMR 109
Cdd:pfam13519  79 AAALQLARAALKHRRK 94
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 119-227 6.22e-03

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


Pssm-ID: 238752 [Multi-domain]  Cd Length: 224  Bit Score: 38.13  E-value: 6.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540344553 119 QEIRHAIILLTDGKSNmggspktavDHIREIlnINQKRNDYLDIYAIGVGKLDVDwrELNELGSKKDGErHAFILQDTKA 198
Cdd:cd01475  106 ERVPRVGIVVTDGRPQ---------DDVSEV--AAKARALGIEMFAVGVGRADEE--ELREIASEPLAD-HVFYVEDFST 171

                         90       100
                 ....*....|....*....|....*....
gi 540344553 199 LHQVfehmldVSKLTDTICGVGNMSANAS 227
Cdd:cd01475  172 IEEL------TKKFQGKICVVPDLCATLS 194
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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