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Conserved domains on  [gi|11990428|dbj|BAB19788|]
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complement factor B/C2-B [Oncorhynchus mykiss]

Protein Classification

vWA_complement_factors and Tryp_SPc domain-containing protein( domain architecture ID 13332275)

protein containing domains CCP, vWA_complement_factors, and Tryp_SPc

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
 272-474 4.53e-101

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: 309.99  E-value: 4.53e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11990428 272 MNVFILMDTSGSISKTHFNLARGAIADLIRKLDSYEIELNFQVISYASQAKDIVDIVSSNDehvrSNVRSVLKRLAAFDH 351
Cdd:cd01470   1 LNIYIALDASDSIGEEDFDEAKNAIKTLIEKISSYEVSPRYEIISYASDPKEIVSIRDFNS----NDADDVIKRLEDFNY 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11990428 352 RSHGNKTGTNLYAALYRVYERMAILRERNETRFSETQNVILIETDGYSNTGGSPLAVLAKIRSLLGYSTSAlDHTEDKLL 431
Cdd:cd01470  77 DDHGDKTGTNTAAALKKVYERMALEKVRNKEAFNETRHVIILFTDGKSNMGGSPLPTVDKIKNLVYKNNKS-DNPREDYL 155

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 11990428 432 DVYVFGVGDNVNKNELNLIASRKRHEKHLFILKDYKQLGEVFN 474
Cdd:cd01470 156 DVYVFGVGDDVNKEELNDLASKKDNERHFFKLKDYEDLQEVFD 198
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 508-775 2.93e-36

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: 136.64  E-value: 2.93e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11990428 508 RPWHVnVITTGVKSETCQGSIVTQNWILTAAHCFSairfEGKVDQEKVTV-----KHGYGGNKAAKVLLVISHPQYNVNg 582
Cdd:cd00190  12 FPWQV-SLQYTGGRHFCGGSLISPRWVLTAAHCVY----SSAPSNYTVRLgshdlSSNEGGGQVIKVKKVIVHPNYNPS- 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11990428 583 lshkkvkeFYDYDIALVKVET-IKLSWTARPICLPCTKpanraMKMSPNSTCerhekallpmeetrayfinkgaTVkdak 661
Cdd:cd00190  86 --------TYDNDIALLKLKRpVTLSDNVRPICLPSSG-----YNLPAGTTC----------------------TV---- 126

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11990428 662 rkqT---HIHTGSKRPDCIKQAENTLLTPHD----ATLNEYVPDRFLCSGGSADHIDAvtCKGDSGGALFLLNRLRYFQV 734
Cdd:cd00190 127 ---SgwgRTSEGGPLPDVLQEVNVPIVSNAEckraYSYGGTITDNMLCAGGLEGGKDA--CQGDSGGPLVCNDNGRGVLV 201

                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 11990428 735 GVVSWGTknVCEpqdSSDRPppdarDFHISVFHLLPWLKQH 775
Cdd:cd00190 202 GIVSWGS--GCA---RPNYP-----GVYTRVSSYLDWIQKT 232
PHA02927 super family cl33700
secreted complement-binding protein; Provisional
 58-221 4.43e-11

secreted complement-binding protein; Provisional


The actual alignment was detected with superfamily member PHA02927:

Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 64.29  E-value: 4.43e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11990428   58 GSVLTYHCKAGHYPYPVSQRVCSAdGEWSSMRLADGRRVsrasCKEIMCPGQLQLDHGEFWPREQWLKPGESQSFSCHSG 137
Cdd:PHA02927 105 GSSITYSCNSGYQLIGESKSYCEL-GSTGSMVWNPEAPI----CESVKCQSPPSISNGRHNGYEDFYTDGSVVTYSCNSG 179

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11990428  138 FSLSGSAQRNCTSlGDWTGTiPVCdsQADDCKNPGVPPGALRS--EGRFRKGEKVQYRCQMGLDLLGSAERVCLESREWS 215
Cdd:PHA02927 180 YSLIGNSGVLCSG-GEWSDP-PTC--QIVKCPHPTISNGYLSSgfKRSYSYNDNVDFKCKYGYKLSGSSSSTCSPGNTWQ 255


                 ....*.
gi 11990428  216 GSETRC 221
Cdd:PHA02927 256 PELPKC 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 ...
 272-474 4.53e-101

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: 309.99  E-value: 4.53e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11990428 272 MNVFILMDTSGSISKTHFNLARGAIADLIRKLDSYEIELNFQVISYASQAKDIVDIVSSNDehvrSNVRSVLKRLAAFDH 351
Cdd:cd01470   1 LNIYIALDASDSIGEEDFDEAKNAIKTLIEKISSYEVSPRYEIISYASDPKEIVSIRDFNS----NDADDVIKRLEDFNY 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11990428 352 RSHGNKTGTNLYAALYRVYERMAILRERNETRFSETQNVILIETDGYSNTGGSPLAVLAKIRSLLGYSTSAlDHTEDKLL 431
Cdd:cd01470  77 DDHGDKTGTNTAAALKKVYERMALEKVRNKEAFNETRHVIILFTDGKSNMGGSPLPTVDKIKNLVYKNNKS-DNPREDYL 155

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 11990428 432 DVYVFGVGDNVNKNELNLIASRKRHEKHLFILKDYKQLGEVFN 474
Cdd:cd01470 156 DVYVFGVGDDVNKEELNDLASKKDNERHFFKLKDYEDLQEVFD 198
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 508-775 2.93e-36

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: 136.64  E-value: 2.93e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11990428 508 RPWHVnVITTGVKSETCQGSIVTQNWILTAAHCFSairfEGKVDQEKVTV-----KHGYGGNKAAKVLLVISHPQYNVNg 582
Cdd:cd00190  12 FPWQV-SLQYTGGRHFCGGSLISPRWVLTAAHCVY----SSAPSNYTVRLgshdlSSNEGGGQVIKVKKVIVHPNYNPS- 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11990428 583 lshkkvkeFYDYDIALVKVET-IKLSWTARPICLPCTKpanraMKMSPNSTCerhekallpmeetrayfinkgaTVkdak 661
Cdd:cd00190  86 --------TYDNDIALLKLKRpVTLSDNVRPICLPSSG-----YNLPAGTTC----------------------TV---- 126

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11990428 662 rkqT---HIHTGSKRPDCIKQAENTLLTPHD----ATLNEYVPDRFLCSGGSADHIDAvtCKGDSGGALFLLNRLRYFQV 734
Cdd:cd00190 127 ---SgwgRTSEGGPLPDVLQEVNVPIVSNAEckraYSYGGTITDNMLCAGGLEGGKDA--CQGDSGGPLVCNDNGRGVLV 201

                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 11990428 735 GVVSWGTknVCEpqdSSDRPppdarDFHISVFHLLPWLKQH 775
Cdd:cd00190 202 GIVSWGS--GCA---RPNYP-----GVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 508-771 7.74e-34

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: 129.72  E-value: 7.74e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11990428    508 RPWHVnVITTGVKSETCQGSIVTQNWILTAAHCFsairfeGKVDQEKVTVKHG------YGGNKAAKVLLVISHPQYNvn 581
Cdd:smart00020  13 FPWQV-SLQYGGGRHFCGGSLISPRWVLTAAHCV------RGSDPSNIRVRLGshdlssGEEGQVIKVSKVIIHPNYN-- 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11990428    582 glshkkvKEFYDYDIALVKVET-IKLSWTARPICLPCTkpanramkmspnstcerhekALLPMEETRAYFINKGATVKDA 660
Cdd:smart00020  84 -------PSTYDNDIALLKLKEpVTLSDNVRPICLPSS--------------------NYNVPAGTTCTVSGWGRTSEGA 136

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11990428    661 KR-----KQTHIHTGSKRpDCIKQAENtlltphdatlNEYVPDRFLCSGGSADHIDAvtCKGDSGGALFLLNRlRYFQVG 735
Cdd:smart00020 137 GSlpdtlQEVNVPIVSNA-TCRRAYSG----------GGAITDNMLCAGGLEGGKDA--CQGDSGGPLVCNDG-RWVLVG 202

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 11990428    736 VVSWGTknVCEpqdssdrpPPDARDFHISVFHLLPW 771
Cdd:smart00020 203 IVSWGS--GCA--------RPGKPGVYTRVSSYLDW 228
Trypsin pfam00089
Trypsin;
498-772 1.95e-27

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 110.99  E-value: 1.95e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11990428   498 VFGPTKKAYTRPWHVNVITTGvKSETCQGSIVTQNWILTAAHCFSAiRFEGKVDQEKVTVKHGYGGNKAAKVLLVISHPQ 577
Cdd:pfam00089   2 VGGDEAQPGSFPWQVSLQLSS-GKHFCGGSLISENWVLTAAHCVSG-ASDVKVVLGAHNIVLREGGEQKFDVEKIIVHPN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11990428   578 YNVNGLshkkvkefyDYDIALVKVET-IKLSWTARPICLPCTKPanramKMSPNSTCerhekallpmeeTRAYFINKGAT 656
Cdd:pfam00089  80 YNPDTL---------DNDIALLKLESpVTLGDTVRPICLPDASS-----DLPVGTTC------------TVSGWGNTKTL 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11990428   657 VKDAKRKQTHIHTGSkRPDCIKQaentlltphdatLNEYVPDRFLCSGGSadhiDAVTCKGDSGGALFLLNRlryFQVGV 736
Cdd:pfam00089 134 GPSDTLQEVTVPVVS-RETCRSA------------YGGTVTDTMICAGAG----GKDACQGDSGGPLVCSDG---ELIGI 193

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 11990428   737 VSWGtkNVCepqdSSDRPPpdarDFHISVFHLLPWL 772
Cdd:pfam00089 194 VSWG--YGC----ASGNYP----GVYTPVSSYLDWI 219
VWA pfam00092
von Willebrand factor type A domain;
273-474 4.29e-25

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 102.74  E-value: 4.29e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11990428   273 NVFILMDTSGSISKTHFNLARGAIADLIRKLDSYEIELNFQVISYASQAKDIVDIVSSndehvrSNVRSVLKRLAAFDHR 352
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDY------SSKEELLSAVDNLRYL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11990428   353 SHGNktgTNLYAALYRVYERmaILRERNETRFSETQNVILIeTDGYSNtGGSPLAVLAKIRSlLGYStsaldhtedklld 432
Cdd:pfam00092  75 GGGT---TNTGKALKYALEN--LFSSAAGARPGAPKVVVLL-TDGRSQ-DGDPEEVARELKS-AGVT------------- 133

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 11990428   433 VYVFGVGDNVNKnELNLIASRKRhEKHLFILKDYKQLGEVFN 474
Cdd:pfam00092 134 VFAVGVGNADDE-ELRKIASEPG-EGHVFTVSDFEALEDLQD 173
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 509-778 1.26e-23

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 100.88  E-value: 1.26e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11990428 509 PWHVNVITT-GVKSETCQGSIVTQNWILTAAHCFSAIRFEGkvdqekVTVKHG-----YGGNKAAKVLLVISHPQYNVNG 582
Cdd:COG5640  43 PWMVALQSSnGPSGQFCGGTLIAPRWVLTAAHCVDGDGPSD------LRVVIGstdlsTSGGTVVKVARIVVHPDYDPAT 116

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11990428 583 lshkkvkefYDYDIALVKVetiklswtARPIclPCTKP---ANRAMKMSPNSTcerhekallpmeeTRAY-FinkGATVK 658
Cdd:COG5640 117 ---------PGNDIALLKL--------ATPV--PGVAPaplATSADAAAPGTP-------------ATVAgW---GRTSE 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11990428 659 DakrkqthihtGSKRPDCIKQAENTLLTPHD-ATLNEYVPDRFLCSGGSADHIDAvtCKGDSGGALFLLNRLRYFQVGVV 737
Cdd:COG5640 162 G----------PGSQSGTLRKADVPVVSDATcAAYGGFDGGTMLCAGYPEGGKDA--CQGDSGGPLVVKDGGGWVLVGVV 229

                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 11990428 738 SWGTkNVCEPQDSSdrpppdardFHISVFHLLPWLKQHLGT 778
Cdd:COG5640 230 SWGG-GPCAAGYPG---------VYTRVSAYRDWIKSTAGG 260
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 273-459 6.67e-22

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: 93.67  E-value: 6.67e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11990428    273 NVFILMDTSGSISKTHFNLARGAIADLIRKLDSYEIELNFQVISYASQAKDIVDIVSSNDehvrsnVRSVLKRLAAFDHR 352
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRS------KDALLEALASLSYK 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11990428    353 SHGnktGTNLYAALYRVYERmaILRERNETRFSETQNVILIeTDGYSNTGGSPLAVLAKIRSLLGystsaldhtedklLD 432
Cdd:smart00327  75 LGG---GTNLGAALQYALEN--LFSKSAGSRRGAPKVVILI-TDGESNDGPKDLLKAAKELKRSG-------------VK 135

                          170       180
                   ....*....|....*....|....*..
gi 11990428    433 VYVFGVGDNVNKNELNLIASRKRHEKH 459
Cdd:smart00327 136 VFVVGVGNDVDEEELKKLASAPGGVYV 162
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 263-453 6.51e-12

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: 66.50  E-value: 6.51e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11990428 263 RTLRVADGRMNVFILMDTSGSIS-KTHFNLARGAIADLIRKLDSYEielNFQVISYASQAKDIVDIVSSndehvRSNVRS 341
Cdd:COG1240  84 LALARPQRGRDVVLVVDASGSMAaENRLEAAKGALLDFLDDYRPRD---RVGLVAFGGEAEVLLPLTRD-----REALKR 155

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11990428 342 VLKRLAAFDhrshgnktGTNLYAALYRVYERmaiLRERNETRfsetQNVILIETDGYSNTG-GSPLAVLAKIRsllgyst 420
Cdd:COG1240 156 ALDELPPGG--------GTPLGDALALALEL---LKRADPAR----RKVIVLLTDGRDNAGrIDPLEAAELAA------- 213

                       170       180       190
                ....*....|....*....|....*....|....
gi 11990428 421 saldhteDKLLDVYVFGVG-DNVNKNELNLIASR 453
Cdd:COG1240 214 -------AAGIRIYTIGVGtEAVDEGLLREIAEA 240
PHA02927 PHA02927
secreted complement-binding protein; Provisional
 58-221 4.43e-11

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 64.29  E-value: 4.43e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11990428   58 GSVLTYHCKAGHYPYPVSQRVCSAdGEWSSMRLADGRRVsrasCKEIMCPGQLQLDHGEFWPREQWLKPGESQSFSCHSG 137
Cdd:PHA02927 105 GSSITYSCNSGYQLIGESKSYCEL-GSTGSMVWNPEAPI----CESVKCQSPPSISNGRHNGYEDFYTDGSVVTYSCNSG 179

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11990428  138 FSLSGSAQRNCTSlGDWTGTiPVCdsQADDCKNPGVPPGALRS--EGRFRKGEKVQYRCQMGLDLLGSAERVCLESREWS 215
Cdd:PHA02927 180 YSLIGNSGVLCSG-GEWSDP-PTC--QIVKCPHPTISNGYLSSgfKRSYSYNDNVDFKCKYGYKLSGSSSSTCSPGNTWQ 255


                 ....*.
gi 11990428  216 GSETRC 221
Cdd:PHA02927 256 PELPKC 261
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 168-222 1.71e-09

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: 54.01  E-value: 1.71e-09
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 11990428 168 CKNPGVPPGALR--SEGRFRKGEKVQYRCQMGLDLLGSAERVCLESREWSGSETRCQ 222
Cdd:cd00033   1 CPPPPVPENGTVtgSKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 168-221 6.11e-09

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


Pssm-ID: 214478 [Multi-domain]  Cd Length: 56  Bit Score: 52.53  E-value: 6.11e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 11990428    168 CKNPGVPPGAL--RSEGRFRKGEKVQYRCQMGLDLLGSAERVCLESREWSGSETRC 221
Cdd:smart00032   1 CPPPPDIENGTvtSSSGTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
Sushi pfam00084
Sushi repeat (SCR repeat);
106-161 8.07e-06

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 43.64  E-value: 8.07e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 11990428   106 CPGQLQLDHGEFWPREQWLKPGESQSFSCHSGFSLSGSAQRNCTSLGDWTGTIPVC 161
Cdd:pfam00084   1 CPPPPDIPNGKVSATKNEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
 
Name Accession Description Interval E-value
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
 272-474 4.53e-101

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: 309.99  E-value: 4.53e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11990428 272 MNVFILMDTSGSISKTHFNLARGAIADLIRKLDSYEIELNFQVISYASQAKDIVDIVSSNDehvrSNVRSVLKRLAAFDH 351
Cdd:cd01470   1 LNIYIALDASDSIGEEDFDEAKNAIKTLIEKISSYEVSPRYEIISYASDPKEIVSIRDFNS----NDADDVIKRLEDFNY 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11990428 352 RSHGNKTGTNLYAALYRVYERMAILRERNETRFSETQNVILIETDGYSNTGGSPLAVLAKIRSLLGYSTSAlDHTEDKLL 431
Cdd:cd01470  77 DDHGDKTGTNTAAALKKVYERMALEKVRNKEAFNETRHVIILFTDGKSNMGGSPLPTVDKIKNLVYKNNKS-DNPREDYL 155

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 11990428 432 DVYVFGVGDNVNKNELNLIASRKRHEKHLFILKDYKQLGEVFN 474
Cdd:cd01470 156 DVYVFGVGDDVNKEELNDLASKKDNERHFFKLKDYEDLQEVFD 198
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 508-775 2.93e-36

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: 136.64  E-value: 2.93e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11990428 508 RPWHVnVITTGVKSETCQGSIVTQNWILTAAHCFSairfEGKVDQEKVTV-----KHGYGGNKAAKVLLVISHPQYNVNg 582
Cdd:cd00190  12 FPWQV-SLQYTGGRHFCGGSLISPRWVLTAAHCVY----SSAPSNYTVRLgshdlSSNEGGGQVIKVKKVIVHPNYNPS- 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11990428 583 lshkkvkeFYDYDIALVKVET-IKLSWTARPICLPCTKpanraMKMSPNSTCerhekallpmeetrayfinkgaTVkdak 661
Cdd:cd00190  86 --------TYDNDIALLKLKRpVTLSDNVRPICLPSSG-----YNLPAGTTC----------------------TV---- 126

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11990428 662 rkqT---HIHTGSKRPDCIKQAENTLLTPHD----ATLNEYVPDRFLCSGGSADHIDAvtCKGDSGGALFLLNRLRYFQV 734
Cdd:cd00190 127 ---SgwgRTSEGGPLPDVLQEVNVPIVSNAEckraYSYGGTITDNMLCAGGLEGGKDA--CQGDSGGPLVCNDNGRGVLV 201

                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 11990428 735 GVVSWGTknVCEpqdSSDRPppdarDFHISVFHLLPWLKQH 775
Cdd:cd00190 202 GIVSWGS--GCA---RPNYP-----GVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 508-771 7.74e-34

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: 129.72  E-value: 7.74e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11990428    508 RPWHVnVITTGVKSETCQGSIVTQNWILTAAHCFsairfeGKVDQEKVTVKHG------YGGNKAAKVLLVISHPQYNvn 581
Cdd:smart00020  13 FPWQV-SLQYGGGRHFCGGSLISPRWVLTAAHCV------RGSDPSNIRVRLGshdlssGEEGQVIKVSKVIIHPNYN-- 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11990428    582 glshkkvKEFYDYDIALVKVET-IKLSWTARPICLPCTkpanramkmspnstcerhekALLPMEETRAYFINKGATVKDA 660
Cdd:smart00020  84 -------PSTYDNDIALLKLKEpVTLSDNVRPICLPSS--------------------NYNVPAGTTCTVSGWGRTSEGA 136

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11990428    661 KR-----KQTHIHTGSKRpDCIKQAENtlltphdatlNEYVPDRFLCSGGSADHIDAvtCKGDSGGALFLLNRlRYFQVG 735
Cdd:smart00020 137 GSlpdtlQEVNVPIVSNA-TCRRAYSG----------GGAITDNMLCAGGLEGGKDA--CQGDSGGPLVCNDG-RWVLVG 202

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 11990428    736 VVSWGTknVCEpqdssdrpPPDARDFHISVFHLLPW 771
Cdd:smart00020 203 IVSWGS--GCA--------RPGKPGVYTRVSSYLDW 228
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 272-461 4.41e-30

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: 116.62  E-value: 4.41e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11990428 272 MNVFILMDTSGSISKTHFNLARGAIADLIRKLDSYEIELNFQVISYASQAKDIVDIVSSNdehvrsNVRSVLKRLAAFDH 351
Cdd:cd01450   1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYK------SKDDLLKAVKNLKY 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11990428 352 RSHGnktGTNLYAALYRVYERMAILRERNEtrfsETQNVILIETDGYSNTGGSPLAVLAKIRsllgystsaldhteDKLL 431
Cdd:cd01450  75 LGGG---GTNTGKALQYALEQLFSESNARE----NVPKVIIVLTDGRSDDGGDPKEAAAKLK--------------DEGI 133

                       170       180       190
                ....*....|....*....|....*....|
gi 11990428 432 DVYVFGVGDnVNKNELNLIASrKRHEKHLF 461
Cdd:cd01450 134 KVFVVGVGP-ADEEELREIAS-CPSERHVF 161
Trypsin pfam00089
Trypsin;
498-772 1.95e-27

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 110.99  E-value: 1.95e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11990428   498 VFGPTKKAYTRPWHVNVITTGvKSETCQGSIVTQNWILTAAHCFSAiRFEGKVDQEKVTVKHGYGGNKAAKVLLVISHPQ 577
Cdd:pfam00089   2 VGGDEAQPGSFPWQVSLQLSS-GKHFCGGSLISENWVLTAAHCVSG-ASDVKVVLGAHNIVLREGGEQKFDVEKIIVHPN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11990428   578 YNVNGLshkkvkefyDYDIALVKVET-IKLSWTARPICLPCTKPanramKMSPNSTCerhekallpmeeTRAYFINKGAT 656
Cdd:pfam00089  80 YNPDTL---------DNDIALLKLESpVTLGDTVRPICLPDASS-----DLPVGTTC------------TVSGWGNTKTL 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11990428   657 VKDAKRKQTHIHTGSkRPDCIKQaentlltphdatLNEYVPDRFLCSGGSadhiDAVTCKGDSGGALFLLNRlryFQVGV 736
Cdd:pfam00089 134 GPSDTLQEVTVPVVS-RETCRSA------------YGGTVTDTMICAGAG----GKDACQGDSGGPLVCSDG---ELIGI 193

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 11990428   737 VSWGtkNVCepqdSSDRPPpdarDFHISVFHLLPWL 772
Cdd:pfam00089 194 VSWG--YGC----ASGNYP----GVYTPVSSYLDWI 219
VWA pfam00092
von Willebrand factor type A domain;
273-474 4.29e-25

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 102.74  E-value: 4.29e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11990428   273 NVFILMDTSGSISKTHFNLARGAIADLIRKLDSYEIELNFQVISYASQAKDIVDIVSSndehvrSNVRSVLKRLAAFDHR 352
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDY------SSKEELLSAVDNLRYL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11990428   353 SHGNktgTNLYAALYRVYERmaILRERNETRFSETQNVILIeTDGYSNtGGSPLAVLAKIRSlLGYStsaldhtedklld 432
Cdd:pfam00092  75 GGGT---TNTGKALKYALEN--LFSSAAGARPGAPKVVVLL-TDGRSQ-DGDPEEVARELKS-AGVT------------- 133

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 11990428   433 VYVFGVGDNVNKnELNLIASRKRhEKHLFILKDYKQLGEVFN 474
Cdd:pfam00092 134 VFAVGVGNADDE-ELRKIASEPG-EGHVFTVSDFEALEDLQD 173
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 509-778 1.26e-23

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 100.88  E-value: 1.26e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11990428 509 PWHVNVITT-GVKSETCQGSIVTQNWILTAAHCFSAIRFEGkvdqekVTVKHG-----YGGNKAAKVLLVISHPQYNVNG 582
Cdd:COG5640  43 PWMVALQSSnGPSGQFCGGTLIAPRWVLTAAHCVDGDGPSD------LRVVIGstdlsTSGGTVVKVARIVVHPDYDPAT 116

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11990428 583 lshkkvkefYDYDIALVKVetiklswtARPIclPCTKP---ANRAMKMSPNSTcerhekallpmeeTRAY-FinkGATVK 658
Cdd:COG5640 117 ---------PGNDIALLKL--------ATPV--PGVAPaplATSADAAAPGTP-------------ATVAgW---GRTSE 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11990428 659 DakrkqthihtGSKRPDCIKQAENTLLTPHD-ATLNEYVPDRFLCSGGSADHIDAvtCKGDSGGALFLLNRLRYFQVGVV 737
Cdd:COG5640 162 G----------PGSQSGTLRKADVPVVSDATcAAYGGFDGGTMLCAGYPEGGKDA--CQGDSGGPLVVKDGGGWVLVGVV 229

                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 11990428 738 SWGTkNVCEPQDSSdrpppdardFHISVFHLLPWLKQHLGT 778
Cdd:COG5640 230 SWGG-GPCAAGYPG---------VYTRVSAYRDWIKSTAGG 260
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 273-459 6.67e-22

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: 93.67  E-value: 6.67e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11990428    273 NVFILMDTSGSISKTHFNLARGAIADLIRKLDSYEIELNFQVISYASQAKDIVDIVSSNDehvrsnVRSVLKRLAAFDHR 352
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRS------KDALLEALASLSYK 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11990428    353 SHGnktGTNLYAALYRVYERmaILRERNETRFSETQNVILIeTDGYSNTGGSPLAVLAKIRSLLGystsaldhtedklLD 432
Cdd:smart00327  75 LGG---GTNLGAALQYALEN--LFSKSAGSRRGAPKVVILI-TDGESNDGPKDLLKAAKELKRSG-------------VK 135

                          170       180
                   ....*....|....*....|....*..
gi 11990428    433 VYVFGVGDNVNKNELNLIASRKRHEKH 459
Cdd:smart00327 136 VFVVGVGNDVDEEELKKLASAPGGVYV 162
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 273-453 9.18e-16

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: 75.29  E-value: 9.18e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11990428 273 NVFILMDTSGSISKTHFNLARGAIADLIRKLDSYEIELNFQVISYASQAKDIVDIvssndehvrSNVRSVLKRLAAFDHR 352
Cdd:cd00198   2 DIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPL---------TTDTDKADLLEAIDAL 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11990428 353 SHGNKTGTNLYAALyrvyeRMAILRERNETRFSETQNVILIeTDGYSNTGGSPLAVLAKIrsllgystsaldhTEDKLLD 432
Cdd:cd00198  73 KKGLGGGTNIGAAL-----RLALELLKSAKRPNARRVIILL-TDGEPNDGPELLAEAARE-------------LRKLGIT 133

                       170       180
                ....*....|....*....|.
gi 11990428 433 VYVFGVGDNVNKNELNLIASR 453
Cdd:cd00198 134 VYTIGIGDDANEDELKEIADK 154
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 263-453 6.51e-12

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: 66.50  E-value: 6.51e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11990428 263 RTLRVADGRMNVFILMDTSGSIS-KTHFNLARGAIADLIRKLDSYEielNFQVISYASQAKDIVDIVSSndehvRSNVRS 341
Cdd:COG1240  84 LALARPQRGRDVVLVVDASGSMAaENRLEAAKGALLDFLDDYRPRD---RVGLVAFGGEAEVLLPLTRD-----REALKR 155

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11990428 342 VLKRLAAFDhrshgnktGTNLYAALYRVYERmaiLRERNETRfsetQNVILIETDGYSNTG-GSPLAVLAKIRsllgyst 420
Cdd:COG1240 156 ALDELPPGG--------GTPLGDALALALEL---LKRADPAR----RKVIVLLTDGRDNAGrIDPLEAAELAA------- 213

                       170       180       190
                ....*....|....*....|....*....|....
gi 11990428 421 saldhteDKLLDVYVFGVG-DNVNKNELNLIASR 453
Cdd:COG1240 214 -------AAGIRIYTIGVGtEAVDEGLLREIAEA 240
PHA02927 PHA02927
secreted complement-binding protein; Provisional
 58-221 4.43e-11

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 64.29  E-value: 4.43e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11990428   58 GSVLTYHCKAGHYPYPVSQRVCSAdGEWSSMRLADGRRVsrasCKEIMCPGQLQLDHGEFWPREQWLKPGESQSFSCHSG 137
Cdd:PHA02927 105 GSSITYSCNSGYQLIGESKSYCEL-GSTGSMVWNPEAPI----CESVKCQSPPSISNGRHNGYEDFYTDGSVVTYSCNSG 179

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11990428  138 FSLSGSAQRNCTSlGDWTGTiPVCdsQADDCKNPGVPPGALRS--EGRFRKGEKVQYRCQMGLDLLGSAERVCLESREWS 215
Cdd:PHA02927 180 YSLIGNSGVLCSG-GEWSDP-PTC--QIVKCPHPTISNGYLSSgfKRSYSYNDNVDFKCKYGYKLSGSSSSTCSPGNTWQ 255


                 ....*.
gi 11990428  216 GSETRC 221
Cdd:PHA02927 256 PELPKC 261
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 259-451 8.43e-10

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


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 60.46  E-value: 8.43e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11990428 259 VTFGRTLRVADGRMNVFILMDTSGSISKTHFNLARGAIADLIRKLDSyeiELNFQVISYASQAKDIVDIVSSNdehvrsN 338
Cdd:COG2425 106 LAAPASAAVPLLEGPVVLCVDTSGSMAGSKEAAAKAAALALLRALRP---NRRFGVILFDTEVVEDLPLTADD------G 176

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11990428 339 VRSVLKRLAAFDHRShgnktGTNLYAALYRVYERMailrernETRFSETQNVILIeTDGYSntGGSPLAVLAKIRsllgy 418
Cdd:COG2425 177 LEDAIEFLSGLFAGG-----GTDIAPALRAALELL-------EEPDYRNADIVLI-TDGEA--GVSPEELLREVR----- 236

                       170       180       190
                ....*....|....*....|....*....|...
gi 11990428 419 sTSALDHTedklldVYVFGVGDNVNKNELNLIA 451
Cdd:COG2425 237 -AKESGVR------LFTVAIGDAGNPGLLEALA 262
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 168-222 1.71e-09

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: 54.01  E-value: 1.71e-09
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 11990428 168 CKNPGVPPGALR--SEGRFRKGEKVQYRCQMGLDLLGSAERVCLESREWSGSETRCQ 222
Cdd:cd00033   1 CPPPPVPENGTVtgSKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 106-161 5.89e-09

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: 52.85  E-value: 5.89e-09
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 11990428 106 CPGQLQLDHGEFWPREQWLKPGESQSFSCHSGFSLSGSAQRNCTSLGDWTGTIPVC 161
Cdd:cd00033   1 CPPPPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTC 56
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 168-221 6.11e-09

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


Pssm-ID: 214478 [Multi-domain]  Cd Length: 56  Bit Score: 52.53  E-value: 6.11e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 11990428    168 CKNPGVPPGAL--RSEGRFRKGEKVQYRCQMGLDLLGSAERVCLESREWSGSETRC 221
Cdd:smart00032   1 CPPPPDIENGTvtSSSGTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 106-161 6.74e-09

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


Pssm-ID: 214478 [Multi-domain]  Cd Length: 56  Bit Score: 52.53  E-value: 6.74e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 11990428    106 CPGQLQLDHGEFWPREQWLKPGESQSFSCHSGFSLSGSAQRNCTSLGDWTGTIPVC 161
Cdd:smart00032   1 CPPPPDIENGTVTSSSGTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 272-451 1.45e-08

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


Pssm-ID: 238748 [Multi-domain]  Cd Length: 186  Bit Score: 55.08  E-value: 1.45e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11990428 272 MNVFILMDTSGSISKTH-FNLARGAIADLIRKLDSYEIELNFQVISYASQAKDIVD---IVSSNDEHVRSNVRSVLKRla 347
Cdd:cd01471   1 LDLYLLVDGSGSIGYSNwVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRlssPNSTNKDLALNAIRALLSL-- 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11990428 348 afdHRSHGNktgTNLYAALYRVYErmaILRERNETRFSETQNVILIeTDGYSNTGGSPLAVLAKIRsllgystsaldhte 427
Cdd:cd01471  79 ---YYPNGS---TNTTSALLVVEK---HLFDTRGNRENAPQLVIIM-TDGIPDSKFRTLKEARKLR-------------- 134

                       170       180
                ....*....|....*....|....
gi 11990428 428 DKLLDVYVFGVGDNVNKNELNLIA 451
Cdd:cd01471 135 ERGVIIAVLGVGQGVNHEENRSLV 158
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 272-472 8.44e-08

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: 52.74  E-value: 8.44e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11990428 272 MNVFILMDTSGSISKTHFNLARGAIADLIRKLDSYEIELNFQVISYASqakDIVDIVSSNDEHVRSNVRSVLKRLAafdH 351
Cdd:cd01469   1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSE---SFRTEFTLNEYRTKEEPLSLVKHIS---Q 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11990428 352 RSHGNKTGTNLYAALYRVYermailRERNETRFSETQNVILIeTDGYSNtgGSPLavlakirsllgySTSALDHTEDKLL 431
Cdd:cd01469  75 LLGLTNTATAIQYVVTELF------SESNGARKDATKVLVVI-TDGESH--DDPL------------LKDVIPQAEREGI 133

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 11990428 432 DVYVFGVGDNVNKN----ELNLIASrKRHEKHLFILKDYKQLGEV 472
Cdd:cd01469 134 IRYAIGVGGHFQREnsreELKTIAS-KPPEEHFFNVTDFAALKDI 177
PHA02927 PHA02927
secreted complement-binding protein; Provisional
 46-161 7.76e-07

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 51.19  E-value: 7.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11990428   46 GGNVSYSQAGTEGSVLTYHCKAGHYPYPVSQRVCSAdGEWSSmrladgrrvsRASCKEIMCPgQLQLDHGefwpreqWLK 125
Cdd:PHA02927 157 GRHNGYEDFYTDGSVVTYSCNSGYSLIGNSGVLCSG-GEWSD----------PPTCQIVKCP-HPTISNG-------YLS 217

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 11990428  126 PGESQSFS--------CHSGFSLSGSAQRNCTSLGDWTGTIPVC 161
Cdd:PHA02927 218 SGFKRSYSyndnvdfkCKYGYKLSGSSSSTCSPGNTWQPELPKC 261
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 273-465 1.54e-06

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: 48.76  E-value: 1.54e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11990428 273 NVFILMDTSGSISKTHFNLARGAIADLIRKLDSYEIELNFQVISYASQAKDIVDIvssnDEHvrSNVRSVLKRLAAFDHR 352
Cdd:cd01472   2 DIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYL----NTY--RSKDDVLEAVKNLRYI 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11990428 353 SHGNKTGtnlyAALYRVYERmaiLRERNETRFSETQNVILIETDGYSNTGGSPLAVlakirsllgystsaldhtEDKLLD 432
Cdd:cd01472  76 GGGTNTG----KALKYVREN---LFTEASGSREGVPKVLVVITDGKSQDDVEEPAV------------------ELKQAG 130

                       170       180       190
                ....*....|....*....|....*....|....
gi 11990428 433 VYVFGVGD-NVNKNELNLIASrKRHEKHLFILKD 465
Cdd:cd01472 131 IEVFAVGVkNADEEELKQIAS-DPKELYVFNVAD 163
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 38-87 5.15e-06

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: 44.38  E-value: 5.15e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 11990428  38 CSIAEKIRGGNVSYSQAGTE-GSVLTYHCKAGHYPYPVSQRVCSADGEWSS 87
Cdd:cd00033   1 CPPPPVPENGTVTGSKGSYSyGSTVTYSCNEGYTLVGSSTITCTENGGWSP 51
Sushi pfam00084
Sushi repeat (SCR repeat);
106-161 8.07e-06

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 43.64  E-value: 8.07e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 11990428   106 CPGQLQLDHGEFWPREQWLKPGESQSFSCHSGFSLSGSAQRNCTSLGDWTGTIPVC 161
Cdd:pfam00084   1 CPPPPDIPNGKVSATKNEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
Sushi pfam00084
Sushi repeat (SCR repeat);
38-87 1.13e-05

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 43.26  E-value: 1.13e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 11990428    38 CSIAEKIRGGNVSYSQAGTE-GSVLTYHCKAGHYPYPVSQRVCSADGEWSS 87
Cdd:pfam00084   1 CPPPPDIPNGKVSATKNEYNyGASVSYECDPGYRLVGSPTITCQEDGTWSP 51
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 270-473 1.40e-05

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: 46.99  E-value: 1.40e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11990428 270 GRMNVFILMDTSGSISKTHFNLARGAIADLIRKLDSYEIELNFQVISYASQAKDIVDIVSsndeHVRSnvRSVLKRLAAF 349
Cdd:cd01475   1 GPTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGR----FKSK--ADLKRAVRRM 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11990428 350 DHRSHGNKTGTNLYAALYRVYERMAILRERNEtrfsETQNVILIETDGYSNTGGSPLAVLAKIRSLLgystsaldhtedk 429
Cdd:cd01475  75 EYLETGTMTGLAIQYAMNNAFSEAEGARPGSE----RVPRVGIVVTDGRPQDDVSEVAAKARALGIE------------- 137

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 11990428 430 lldVYVFGVGdNVNKNELNLIASRKrHEKHLFILKDYK---QLGEVF 473
Cdd:cd01475 138 ---MFAVGVG-RADEEELREIASEP-LADHVFYVEDFStieELTKKF 179
PHA02954 PHA02954
EEV membrane glycoprotein; Provisional
 104-212 1.49e-05

EEV membrane glycoprotein; Provisional


Pssm-ID: 165263 [Multi-domain]  Cd Length: 317  Bit Score: 47.77  E-value: 1.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11990428  104 IMCPG----QLQLDHGEFWPREQWLKPGESQSFSCHSGFSLSGSAQRNCTSlGDWTgTIPVCDSQaddCKNPGVPPGaLR 179
Cdd:PHA02954 123 VTCPNaecqPLQLEHGSCQPVKEKYSFGEHITINCDVGYEVIGASYISCTA-NSWN-VIPSCQQK---CDIPSLSNG-LI 196

                         90       100       110
                 ....*....|....*....|....*....|...
gi 11990428  180 SEGRFRKGEKVQYRCQMGLDLLGSAERVCLESR 212
Cdd:PHA02954 197 SGSTFSIGGVIHLSCKSGFTLTGSPSSTCIDGK 229
PHA02831 PHA02831
EEV host range protein; Provisional
 57-228 2.09e-05

EEV host range protein; Provisional


Pssm-ID: 165176 [Multi-domain]  Cd Length: 268  Bit Score: 46.91  E-value: 2.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11990428   57 EGSVLTYHCKAGHYPYPVsqrVCSaDGEWSSMRLADGRRvsraSCKEimcpgQLQLDHGEFWPREQWLKPGESQSFSCH- 135
Cdd:PHA02831  42 ENENLEYKCNNNFDKVFV---TCN-NGSWSTKNMCIGKR----NCKD-----PVTILNGYIKNKKDQYSFGDSVTYACKv 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11990428  136 ---SGFSLSGSAQRNCTSlGDWTGTIPVCdsQADDCKNPGVPPGALRS-EGRFRKGEKVQYRCQMGLDLLGSAERVCLES 211
Cdd:PHA02831 109 nklEKYSIVGNETVKCIN-KQWVPKYPVC--KLIRCKYPALQNGFLNVfEKKFYYGDIVNFKCKKGFILLGSSVSTCDIN 185

                        170       180
                 ....*....|....*....|....*.
gi 11990428  212 REWSGSETRC---------QTQYAFD 228
Cdd:PHA02831 186 SIWYPGIPKCvkdkvhneiQPNYLFD 211
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 38-87 3.26e-05

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: 42.13  E-value: 3.26e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 11990428     38 CSIAEKIRGGNVSYSQAG-TEGSVLTYHCKAGHYPYPVSQRVCSADGEWSS 87
Cdd:smart00032   1 CPPPPDIENGTVTSSSGTySYGDTVTYSCDPGYTLIGSSTITCLENGTWSP 51
Sushi pfam00084
Sushi repeat (SCR repeat);
168-221 5.07e-05

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 41.33  E-value: 5.07e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 11990428   168 CKNPGVPPGALRS--EGRFRKGEKVQYRCQMGLDLLGSAERVCLESREWSGSETRC 221
Cdd:pfam00084   1 CPPPPDIPNGKVSatKNEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 274-466 1.42e-04

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


Pssm-ID: 238759 [Multi-domain]  Cd Length: 164  Bit Score: 43.04  E-value: 1.42e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11990428 274 VFiLMDTSGSISKTHFNLARGAIADLIRKLDSYEIELNFQVISYASQAKDIVDIVSSNDehvrsnVRSVLKRLAAFDHRS 353
Cdd:cd01482   4 VF-LVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTS------KEDVLAAIKNLPYKG 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11990428 354 HGNKTGtnlyAALYRVYERmaILRERNETRfSETQNVILIETDGYSntggSPLAVLAKIRSllgystsaldhtedKLLDV 433
Cdd:cd01482  77 GNTRTG----KALTHVREK--NFTPDAGAR-PGVPKVVILITDGKS----QDDVELPARVL--------------RNLGV 131

                       170       180       190
                ....*....|....*....|....*....|....
gi 11990428 434 YVFGVG-DNVNKNELNLIASRKRhEKHLFILKDY 466
Cdd:cd01482 132 NVFAVGvKDADESELKMIASKPS-ETHVFNVADF 164
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
 515-741 1.50e-04

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 43.51  E-value: 1.50e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11990428 515 ITTGVKSETCQGSIVTQNWILTAAHCFSaiRFEGKVDQEKVTVKHGY--GGNKAAKVLLVISHPQYNVNGLShkkvkefy 592
Cdd:COG3591   5 LETDGGGGVCTGTLIGPNLVLTAGHCVY--DGAGGGWATNIVFVPGYngGPYGTATATRFRVPPGWVASGDA-------- 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11990428 593 DYDIALVKVETiklswtarpiclpctkpanramkmspnstcerhekallPMEETRAYFINKGATVKDAKRKQTHIHTGSK 672
Cdd:COG3591  75 GYDYALLRLDE--------------------------------------PLGDTTGWLGLAFNDAPLAGEPVTIIGYPGD 116

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 11990428 673 RPDCIKQAENTLLTphdatlneYVPDRFLcsggsadHIDAVTCKGDSGGALFLLNRLRYFQVGVVSWGT 741
Cdd:COG3591 117 RPKDLSLDCSGRVT--------GVQGNRL-------SYDCDTTGGSSGSPVLDDSDGGGRVVGVHSAGG 170
PHA02639 PHA02639
EEV host range protein; Provisional
 114-221 2.58e-04

EEV host range protein; Provisional


Pssm-ID: 165022 [Multi-domain]  Cd Length: 295  Bit Score: 43.88  E-value: 2.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11990428  114 HGEFWPREQWLKPGESQSFSC--HSG--FSLSGSAQRNCTSLGDWTGTIPVCdsQADDCKNPGVPPG---ALRSEGRFRK 186
Cdd:PHA02639  93 NGKIYNKREMYKVGDEIYYVCneHKGvqYSLVGNEKITCIQDKSWKPDPPIC--KMINCRFPALQNGyinGIPSNKKFYY 170

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 11990428  187 GEKVQYRCQMGLDLLGSAERVCLESREWSGSETRC 221
Cdd:PHA02639 171 KTRVGFSCKSGFDLVGEKYSTCNINATWFPSIPTC 205
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 273-451 6.22e-04

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


Pssm-ID: 238742 [Multi-domain]  Cd Length: 170  Bit Score: 41.10  E-value: 6.22e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11990428 273 NVFILMDTSGSISKTHFNLARGAIADLIRKLDSYEIelnFQVISYASQAKDIVDIVSSNDehvRSNVRSVLKRLAAFDhr 352
Cdd:cd01465   2 NLVFVIDRSGSMDGPKLPLVKSALKLLVDQLRPDDR---LAIVTYDGAAETVLPATPVRD---KAAILAAIDRLTAGG-- 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11990428 353 shgnktGTNLYAALYRVYErmailrERNETRFSETQNVILIETDGYSNTGGSplavlaKIRSLLGYSTSALDHTedklLD 432
Cdd:cd01465  74 ------STAGGAGIQLGYQ------EAQKHFVPGGVNRILLATDGDFNVGET------DPDELARLVAQKRESG----IT 131

                       170
                ....*....|....*....
gi 11990428 433 VYVFGVGDNVNKNELNLIA 451
Cdd:cd01465 132 LSTLGFGDNYNEDLMEAIA 150
VWA_2 pfam13519
von Willebrand factor type A domain;
274-393 8.13e-04

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 39.58  E-value: 8.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11990428   274 VFILMDTSGSIS-----KTHFNLARGAIADLIRKLDsyeiELNFQVISYASQAKDIVDIVSSNDEhvrsnVRSVLKRLAA 348
Cdd:pfam13519   1 LVFVLDTSGSMRngdygPTRLEAAKDAVLALLKSLP----GDRVGLVTFGDGPEVLIPLTKDRAK-----ILRALRRLEP 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 11990428   349 FDhrshgnkTGTNLYAALyrvyeRMAiLRERNETRFSETQNVILI 393
Cdd:pfam13519  72 KG-------GGTNLAAAL-----QLA-RAALKHRRKNQPRRIVLI 103
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 273-443 1.22e-03

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


Pssm-ID: 238738 [Multi-domain]  Cd Length: 171  Bit Score: 40.28  E-value: 1.22e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11990428 273 NVFILMDTSGSISKTHFNLARGAIADLIRKLDSyeiELNFQVISYASQAKDIVD-IVSSNDEHVRSnVRSVLKRLAAFDh 351
Cdd:cd01461   4 EVVFVIDTSGSMSGTKIEQTKEALLTALKDLPP---GDYFNIIGFSDTVEEFSPsSVSATAENVAA-AIEYVNRLQALG- 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11990428 352 rshgnktGTNLYAALYRVYERMAILRERnetrfseTQNVILIeTDGYSntgGSPLAVLAKIRSLLGYSTSaldhtedkll 431
Cdd:cd01461  79 -------GTNMNDALEAALELLNSSPGS-------VPQIILL-TDGEV---TNESQILKNVREALSGRIR---------- 130

                       170
                ....*....|..
gi 11990428 432 dVYVFGVGDNVN 443
Cdd:cd01461 131 -LFTFGIGSDVN 141
 
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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