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Conserved domains on  [gi|225543438|ref|NP_001139375|]
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complement C2 isoform 2 precursor [Homo sapiens]

Protein Classification

vWA_complement_factors and Tryp_SPc domain-containing protein( domain architecture ID 10034133)

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 ...
 121-318 2.81e-97

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: 295.74  E-value: 2.81e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543438 121 LNLYLLLDCSQSVSENDFLIFKESASLMVDRIFSFEINVSVAIITFASEPKVLMSVLNDNSRDMTEVISSLENANYKDHE 200
Cdd:cd01470    1 LNIYIALDASDSIGEEDFDEAKNAIKTLIEKISSYEVSPRYEIISYASDPKEIVSIRDFNSNDADDVIKRLEDFNYDDHG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543438 201 NGTGTNTYAALNSVYLMmnnqMRLLGME-TMAWQEIRHAIILLTDGKSNMGGSPKTAVDHIREILNINQK----RNDYLD 275
Cdd:cd01470   81 DKTGTNTAAALKKVYER----MALEKVRnKEAFNETRHVIILFTDGKSNMGGSPLPTVDKIKNLVYKNNKsdnpREDYLD 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 225543438 276 IYAIGVGKlDVDWRELNELGSKKDGERHAFILQDTKALHQVFE 318
Cdd:cd01470  157 VYVFGVGD-DVNKEELNDLASKKDNERHFFKLKDYEDLQEVFD 198
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 341-610 2.22e-40

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: 147.04  E-value: 2.22e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543438 341 SDQERTPWHVTIKPKS-QETCRGALISDQWVLTAAHCFRdGNDHSLWRVNVGD----PKSQWGKEFLIEKAVISPGFDVF 415
Cdd:cd00190    7 AKIGSFPWQVSLQYTGgRHFCGGSLISPRWVLTAAHCVY-SSAPSNYTVRLGShdlsSNEGGGQVIKVKKVIVHPNYNPS 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543438 416 akknqgileFYGDDIALLKLAQKVKMSTHARPICLPCTMEANlalrrPQGSTCR-----DHENEllnkqsvpahfVALNG 490
Cdd:cd00190   86 ---------TYDNDIALLKLKRPVTLSDNVRPICLPSSGYNL-----PAGTTCTvsgwgRTSEG-----------GPLPD 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543438 491 SKLNINLKMgVEWTSCAEVVSQektmfpnltdvREVVTDQFLCSGTQE-DESPCKGESGGAVFLERRFRFFQVGLVSWGl 569
Cdd:cd00190  141 VLQEVNVPI-VSNAECKRAYSY-----------GGTITDNMLCAGGLEgGKDACQGDSGGPLVCNDNGRGVLVGIVSWG- 207

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 225543438 570 ynpcLGSADKNSrkraprskvppPRDFHiNLFRMQPWLRQH 610
Cdd:cd00190  208 ----SGCARPNY-----------PGVYT-RVSSYLDWIQKT 232
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 19-73 6.70e-13

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: 63.64  E-value: 6.70e-13
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 225543438  19 CPNPGISLGAVRTGF--RFGHGDKVRYRCSSNLVLTGSSERECQGNGVWSGTEPICR 73
Cdd:cd00033    1 CPPPPVPENGTVTGSkgSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57
 
Name Accession Description Interval E-value
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
 121-318 2.81e-97

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: 295.74  E-value: 2.81e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543438 121 LNLYLLLDCSQSVSENDFLIFKESASLMVDRIFSFEINVSVAIITFASEPKVLMSVLNDNSRDMTEVISSLENANYKDHE 200
Cdd:cd01470    1 LNIYIALDASDSIGEEDFDEAKNAIKTLIEKISSYEVSPRYEIISYASDPKEIVSIRDFNSNDADDVIKRLEDFNYDDHG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543438 201 NGTGTNTYAALNSVYLMmnnqMRLLGME-TMAWQEIRHAIILLTDGKSNMGGSPKTAVDHIREILNINQK----RNDYLD 275
Cdd:cd01470   81 DKTGTNTAAALKKVYER----MALEKVRnKEAFNETRHVIILFTDGKSNMGGSPLPTVDKIKNLVYKNNKsdnpREDYLD 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 225543438 276 IYAIGVGKlDVDWRELNELGSKKDGERHAFILQDTKALHQVFE 318
Cdd:cd01470  157 VYVFGVGD-DVNKEELNDLASKKDNERHFFKLKDYEDLQEVFD 198
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 341-610 2.22e-40

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: 147.04  E-value: 2.22e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543438 341 SDQERTPWHVTIKPKS-QETCRGALISDQWVLTAAHCFRdGNDHSLWRVNVGD----PKSQWGKEFLIEKAVISPGFDVF 415
Cdd:cd00190    7 AKIGSFPWQVSLQYTGgRHFCGGSLISPRWVLTAAHCVY-SSAPSNYTVRLGShdlsSNEGGGQVIKVKKVIVHPNYNPS 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543438 416 akknqgileFYGDDIALLKLAQKVKMSTHARPICLPCTMEANlalrrPQGSTCR-----DHENEllnkqsvpahfVALNG 490
Cdd:cd00190   86 ---------TYDNDIALLKLKRPVTLSDNVRPICLPSSGYNL-----PAGTTCTvsgwgRTSEG-----------GPLPD 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543438 491 SKLNINLKMgVEWTSCAEVVSQektmfpnltdvREVVTDQFLCSGTQE-DESPCKGESGGAVFLERRFRFFQVGLVSWGl 569
Cdd:cd00190  141 VLQEVNVPI-VSNAECKRAYSY-----------GGTITDNMLCAGGLEgGKDACQGDSGGPLVCNDNGRGVLVGIVSWG- 207

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 225543438 570 ynpcLGSADKNSrkraprskvppPRDFHiNLFRMQPWLRQH 610
Cdd:cd00190  208 ----SGCARPNY-----------PGVYT-RVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 341-573 1.06e-38

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: 1.06e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543438   341 SDQERTPWHVTIKPKS-QETCRGALISDQWVLTAAHCFRdGNDHSLWRVNVGDPKSQWGKE---FLIEKAVISPGFDvfa 416
Cdd:smart00020   8 ANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVR-GSDPSNIRVRLGSHDLSSGEEgqvIKVSKVIIHPNYN--- 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543438   417 kknqgiLEFYGDDIALLKLAQKVKMSTHARPICLPCTmeanlALRRPQGSTCRD----HENEllnkqSVPAHFVALNGSK 492
Cdd:smart00020  84 ------PSTYDNDIALLKLKEPVTLSDNVRPICLPSS-----NYNVPAGTTCTVsgwgRTSE-----GAGSLPDTLQEVN 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543438   493 LNInlkmgVEWTSCAEVVSQektmfpnltdvREVVTDQFLCSGTQE-DESPCKGESGGAVFLERRfRFFQVGLVSWGlyN 571
Cdd:smart00020 148 VPI-----VSNATCRRAYSG-----------GGAITDNMLCAGGLEgGKDACQGDSGGPLVCNDG-RWVLVGIVSWG--S 208


                   ..
gi 225543438   572 PC 573
Cdd:smart00020 209 GC 210
VWA pfam00092
von Willebrand factor type A domain;
122-319 2.38e-31

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 120.07  E-value: 2.38e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543438  122 NLYLLLDCSQSVSENDFLIFKESASLMVDRIFSFEINVSVAIITFASEPKVLMSvLNDNsRDMTEVISSLENANYKDH-E 200
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFP-LNDY-SSKEELLSAVDNLRYLGGgT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543438  201 NGTGTNTYAALNSVYLMMNNQMRllgmetmawqEIRHAIILLTDGKSNMgGSPKTAVDHIREiLNINqkrndyldIYAIG 280
Cdd:pfam00092  79 TNTGKALKYALENLFSSAAGARP----------GAPKVVVLLTDGRSQD-GDPEEVARELKS-AGVT--------VFAVG 138

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 225543438  281 VGklDVDWRELNELGSKKDgERHAFILQDTKALHQVFEH 319
Cdd:pfam00092 139 VG--NADDEELRKIASEPG-EGHVFTVSDFEALEDLQDQ 174
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 122-315 5.05e-27

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


Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 107.93  E-value: 5.05e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543438   122 NLYLLLDCSQSVSENDFLIFKESASLMVDRIFSFEINVSVAIITFASEPKVLMSVlnDNSRDMTEVISSLENANYKDhen 201
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPL--NDSRSKDALLEALASLSYKL--- 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543438   202 GTGTNTYAALNSVYLMMNNQMRllgmetmAWQE-IRHAIILLTDGKSNMGGSpktavdhiREILNINQKRNDYLDIYAIG 280
Cdd:smart00327  76 GGGTNLGAALQYALENLFSKSA-------GSRRgAPKVVILITDGESNDGPK--------DLLKAAKELKRSGVKVFVVG 140

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 225543438   281 VGKlDVDWRELNELgSKKDGERHAFILQDTKALHQ 315
Cdd:smart00327 141 VGN-DVDEEELKKL-ASAPGGVYVFLPELLDLLID 173
Trypsin pfam00089
Trypsin;
347-568 1.56e-23

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 99.05  E-value: 1.56e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543438  347 PWHVTIK-PKSQETCRGALISDQWVLTAAHCFRDGNDhslWRVNVGDP----KSQWGKEFLIEKAVISPGFDVFAKKNqg 421
Cdd:pfam00089  13 PWQVSLQlSSGKHFCGGSLISENWVLTAAHCVSGASD---VKVVLGAHnivlREGGEQKFDVEKIIVHPNYNPDTLDN-- 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543438  422 ilefygdDIALLKLAQKVKMSTHARPICLPCTmeanlALRRPQGSTC------RDHEN---ELLNKQSVPahfvalngsk 492
Cdd:pfam00089  88 -------DIALLKLESPVTLGDTVRPICLPDA-----SSDLPVGTTCtvsgwgNTKTLgpsDTLQEVTVP---------- 145

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 225543438  493 lninlkmgvewtscaeVVSQEKtmfpNLTDVREVVTDQFLCSGTQeDESPCKGESGGAVFLERRfrfFQVGLVSWG 568
Cdd:pfam00089 146 ----------------VVSRET----CRSAYGGTVTDTMICAGAG-GKDACQGDSGGPLVCSDG---ELIGIVSWG 197
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 339-577 1.00e-20

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 92.02  E-value: 1.00e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543438 339 NASDQERtPWHVTIKPKS---QETCRGALISDQWVLTAAHCFRDGNDHSLwRVNVG--DPKSQWGKEFLIEKAVISPGFD 413
Cdd:COG5640   36 PATVGEY-PWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDGPSDL-RVVIGstDLSTSGGTVVKVARIVVHPDYD 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543438 414 VFAkknqgilefYGDDIALLKLAQKVkmsTHARPICLPctmEANLALRRPQ-------GSTCRDHEN--ELLNKQSVPAh 484
Cdd:COG5640  114 PAT---------PGNDIALLKLATPV---PGVAPAPLA---TSADAAAPGTpatvagwGRTSEGPGSqsGTLRKADVPV- 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543438 485 fvalngsklninlkmgVEWTSCAevvsqektmfpnltDVREVVTDQFLCSGTQE-DESPCKGESGGAVFLERRFRFFQVG 563
Cdd:COG5640  178 ----------------VSDATCA--------------AYGGFDGGTMLCAGYPEgGKDACQGDSGGPLVVKDGGGWVLVG 227

                        250
                 ....*....|....
gi 225543438 564 LVSWGlYNPCLGSA 577
Cdd:COG5640  228 VVSWG-GGPCAAGY 240
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 19-73 6.70e-13

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: 63.64  E-value: 6.70e-13
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 225543438  19 CPNPGISLGAVRTGF--RFGHGDKVRYRCSSNLVLTGSSERECQGNGVWSGTEPICR 73
Cdd:cd00033    1 CPPPPVPENGTVTGSkgSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 110-352 1.58e-12

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 68.59  E-value: 1.58e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543438 110 GRKIQIQRSGHLNLYLLLDCSQSVSENDFLIFKESASLMVDRIfsfEINVSVAIITFASEPKVLM-SVLNDNSRDMTEVI 188
Cdd:COG2304   81 PPKAAAEERPPLNLVFVIDVSGSMSGDKLELAKEAAKLLVDQL---RPGDRVSIVTFAGDARVLLpPTPATDRAKILAAI 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543438 189 SSLEnAnykdhenGTGTNTYAALNSVYlmmnNQMRllgmETMAWQEIRHaIILLTDGKSNMGgspKTAVDHIREILNINQ 268
Cdd:COG2304  158 DRLQ-A-------GGGTALGAGLELAY----ELAR----KHFIPGRVNR-VILLTDGDANVG---ITDPEELLKLAEEAR 217

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543438 269 KRNdyLDIYAIGVGkldVDWRE--LNELGSKKDGeRHAFIlQDTKALHQVFEhmldvsKLTDTIcGVGNMSANASDQERT 346
Cdd:COG2304  218 EEG--ITLTTLGVG---SDYNEdlLERLADAGGG-NYYYI-DDPEEAEKVFV------REFSRI-GYENRALATEDFPLP 283


                 ....*.
gi 225543438 347 PWHVTI 352
Cdd:COG2304  284 YGTLKL 289
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 19-72 5.21e-12

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: 61.00  E-value: 5.21e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 225543438    19 CPNPG-ISLGAVRTGF-RFGHGDKVRYRCSSNLVLTGSSERECQGNGVWSGTEPIC 72
Cdd:smart00032   1 CPPPPdIENGTVTSSSgTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
Sushi pfam00084
Sushi repeat (SCR repeat);
19-72 2.77e-08

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 50.58  E-value: 2.77e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 225543438   19 CPNPGISLGAVRTGFRFGH--GDKVRYRCSSNLVLTGSSERECQGNGVWSGTEPIC 72
Cdd:pfam00084   1 CPPPPDIPNGKVSATKNEYnyGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
PHA02927 PHA02927
secreted complement-binding protein; Provisional
 19-72 5.79e-05

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 45.03  E-value: 5.79e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 225543438  19 CPNPGISLGAVRTGFR--FGHGDKVRYRCSSNLVLTGSSERECQGNGVWSGTEPIC 72
Cdd:PHA02927 206 CPHPTISNGYLSSGFKrsYSYNDNVDFKCKYGYKLSGSSSSTCSPGNTWQPELPKC 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 ...
 121-318 2.81e-97

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: 295.74  E-value: 2.81e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543438 121 LNLYLLLDCSQSVSENDFLIFKESASLMVDRIFSFEINVSVAIITFASEPKVLMSVLNDNSRDMTEVISSLENANYKDHE 200
Cdd:cd01470    1 LNIYIALDASDSIGEEDFDEAKNAIKTLIEKISSYEVSPRYEIISYASDPKEIVSIRDFNSNDADDVIKRLEDFNYDDHG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543438 201 NGTGTNTYAALNSVYLMmnnqMRLLGME-TMAWQEIRHAIILLTDGKSNMGGSPKTAVDHIREILNINQK----RNDYLD 275
Cdd:cd01470   81 DKTGTNTAAALKKVYER----MALEKVRnKEAFNETRHVIILFTDGKSNMGGSPLPTVDKIKNLVYKNNKsdnpREDYLD 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 225543438 276 IYAIGVGKlDVDWRELNELGSKKDGERHAFILQDTKALHQVFE 318
Cdd:cd01470  157 VYVFGVGD-DVNKEELNDLASKKDNERHFFKLKDYEDLQEVFD 198
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 341-610 2.22e-40

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: 147.04  E-value: 2.22e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543438 341 SDQERTPWHVTIKPKS-QETCRGALISDQWVLTAAHCFRdGNDHSLWRVNVGD----PKSQWGKEFLIEKAVISPGFDVF 415
Cdd:cd00190    7 AKIGSFPWQVSLQYTGgRHFCGGSLISPRWVLTAAHCVY-SSAPSNYTVRLGShdlsSNEGGGQVIKVKKVIVHPNYNPS 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543438 416 akknqgileFYGDDIALLKLAQKVKMSTHARPICLPCTMEANlalrrPQGSTCR-----DHENEllnkqsvpahfVALNG 490
Cdd:cd00190   86 ---------TYDNDIALLKLKRPVTLSDNVRPICLPSSGYNL-----PAGTTCTvsgwgRTSEG-----------GPLPD 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543438 491 SKLNINLKMgVEWTSCAEVVSQektmfpnltdvREVVTDQFLCSGTQE-DESPCKGESGGAVFLERRFRFFQVGLVSWGl 569
Cdd:cd00190  141 VLQEVNVPI-VSNAECKRAYSY-----------GGTITDNMLCAGGLEgGKDACQGDSGGPLVCNDNGRGVLVGIVSWG- 207

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 225543438 570 ynpcLGSADKNSrkraprskvppPRDFHiNLFRMQPWLRQH 610
Cdd:cd00190  208 ----SGCARPNY-----------PGVYT-RVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 341-573 1.06e-38

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: 1.06e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543438   341 SDQERTPWHVTIKPKS-QETCRGALISDQWVLTAAHCFRdGNDHSLWRVNVGDPKSQWGKE---FLIEKAVISPGFDvfa 416
Cdd:smart00020   8 ANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVR-GSDPSNIRVRLGSHDLSSGEEgqvIKVSKVIIHPNYN--- 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543438   417 kknqgiLEFYGDDIALLKLAQKVKMSTHARPICLPCTmeanlALRRPQGSTCRD----HENEllnkqSVPAHFVALNGSK 492
Cdd:smart00020  84 ------PSTYDNDIALLKLKEPVTLSDNVRPICLPSS-----NYNVPAGTTCTVsgwgRTSE-----GAGSLPDTLQEVN 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543438   493 LNInlkmgVEWTSCAEVVSQektmfpnltdvREVVTDQFLCSGTQE-DESPCKGESGGAVFLERRfRFFQVGLVSWGlyN 571
Cdd:smart00020 148 VPI-----VSNATCRRAYSG-----------GGAITDNMLCAGGLEgGKDACQGDSGGPLVCNDG-RWVLVGIVSWG--S 208


                   ..
gi 225543438   572 PC 573
Cdd:smart00020 209 GC 210
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 121-305 5.65e-34

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: 127.02  E-value: 5.65e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543438 121 LNLYLLLDCSQSVSENDFLIFKESASLMVDRIFSFEINVSVAIITFASEPKVLMSVLNDNSRDmtEVISSLENANYKDhe 200
Cdd:cd01450    1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKD--DLLKAVKNLKYLG-- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543438 201 nGTGTNTYAALNSVYLMMNNqmrllgmETMAWQEIRHAIILLTDGKSNMGGSPKTAVDHIREIlninqkrndYLDIYAIG 280
Cdd:cd01450   77 -GGGTNTGKALQYALEQLFS-------ESNARENVPKVIIVLTDGRSDDGGDPKEAAAKLKDE---------GIKVFVVG 139

                        170       180
                 ....*....|....*....|....*
gi 225543438 281 VGklDVDWRELNELGSKKdGERHAF 305
Cdd:cd01450  140 VG--PADEEELREIASCP-SERHVF 161
VWA pfam00092
von Willebrand factor type A domain;
122-319 2.38e-31

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 120.07  E-value: 2.38e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543438  122 NLYLLLDCSQSVSENDFLIFKESASLMVDRIFSFEINVSVAIITFASEPKVLMSvLNDNsRDMTEVISSLENANYKDH-E 200
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFP-LNDY-SSKEELLSAVDNLRYLGGgT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543438  201 NGTGTNTYAALNSVYLMMNNQMRllgmetmawqEIRHAIILLTDGKSNMgGSPKTAVDHIREiLNINqkrndyldIYAIG 280
Cdd:pfam00092  79 TNTGKALKYALENLFSSAAGARP----------GAPKVVVLLTDGRSQD-GDPEEVARELKS-AGVT--------VFAVG 138

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 225543438  281 VGklDVDWRELNELGSKKDgERHAFILQDTKALHQVFEH 319
Cdd:pfam00092 139 VG--NADDEELRKIASEPG-EGHVFTVSDFEALEDLQDQ 174
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 122-315 5.05e-27

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


Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 107.93  E-value: 5.05e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543438   122 NLYLLLDCSQSVSENDFLIFKESASLMVDRIFSFEINVSVAIITFASEPKVLMSVlnDNSRDMTEVISSLENANYKDhen 201
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPL--NDSRSKDALLEALASLSYKL--- 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543438   202 GTGTNTYAALNSVYLMMNNQMRllgmetmAWQE-IRHAIILLTDGKSNMGGSpktavdhiREILNINQKRNDYLDIYAIG 280
Cdd:smart00327  76 GGGTNLGAALQYALENLFSKSA-------GSRRgAPKVVILITDGESNDGPK--------DLLKAAKELKRSGVKVFVVG 140

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 225543438   281 VGKlDVDWRELNELgSKKDGERHAFILQDTKALHQ 315
Cdd:smart00327 141 VGN-DVDEEELKKL-ASAPGGVYVFLPELLDLLID 173
Trypsin pfam00089
Trypsin;
347-568 1.56e-23

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 99.05  E-value: 1.56e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543438  347 PWHVTIK-PKSQETCRGALISDQWVLTAAHCFRDGNDhslWRVNVGDP----KSQWGKEFLIEKAVISPGFDVFAKKNqg 421
Cdd:pfam00089  13 PWQVSLQlSSGKHFCGGSLISENWVLTAAHCVSGASD---VKVVLGAHnivlREGGEQKFDVEKIIVHPNYNPDTLDN-- 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543438  422 ilefygdDIALLKLAQKVKMSTHARPICLPCTmeanlALRRPQGSTC------RDHEN---ELLNKQSVPahfvalngsk 492
Cdd:pfam00089  88 -------DIALLKLESPVTLGDTVRPICLPDA-----SSDLPVGTTCtvsgwgNTKTLgpsDTLQEVTVP---------- 145

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 225543438  493 lninlkmgvewtscaeVVSQEKtmfpNLTDVREVVTDQFLCSGTQeDESPCKGESGGAVFLERRfrfFQVGLVSWG 568
Cdd:pfam00089 146 ----------------VVSRET----CRSAYGGTVTDTMICAGAG-GKDACQGDSGGPLVCSDG---ELIGIVSWG 197
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 339-577 1.00e-20

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 92.02  E-value: 1.00e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543438 339 NASDQERtPWHVTIKPKS---QETCRGALISDQWVLTAAHCFRDGNDHSLwRVNVG--DPKSQWGKEFLIEKAVISPGFD 413
Cdd:COG5640   36 PATVGEY-PWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDGPSDL-RVVIGstDLSTSGGTVVKVARIVVHPDYD 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543438 414 VFAkknqgilefYGDDIALLKLAQKVkmsTHARPICLPctmEANLALRRPQ-------GSTCRDHEN--ELLNKQSVPAh 484
Cdd:COG5640  114 PAT---------PGNDIALLKLATPV---PGVAPAPLA---TSADAAAPGTpatvagwGRTSEGPGSqsGTLRKADVPV- 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543438 485 fvalngsklninlkmgVEWTSCAevvsqektmfpnltDVREVVTDQFLCSGTQE-DESPCKGESGGAVFLERRFRFFQVG 563
Cdd:COG5640  178 ----------------VSDATCA--------------AYGGFDGGTMLCAGYPEgGKDACQGDSGGPLVVKDGGGWVLVG 227

                        250
                 ....*....|....
gi 225543438 564 LVSWGlYNPCLGSA 577
Cdd:COG5640  228 VVSWG-GGPCAAGY 240
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 121-302 1.32e-19

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


Pssm-ID: 238119 [Multi-domain]  Cd Length: 161  Bit Score: 86.08  E-value: 1.32e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543438 121 LNLYLLLDCSQSVSENDFLIFKESASLMVDRIFSFEINVSVAIITFASEPKVLMSVLNDNSRDmtEVISSLENANYKdhe 200
Cdd:cd00198    1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKA--DLLEAIDALKKG--- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543438 201 NGTGTNTYAALNSVYLMMNNQMRLLGmetmawqeiRHAIILLTDGKSNMGGSPKTAVdhIREIlninqkRNDYLDIYAIG 280
Cdd:cd00198   76 LGGGTNIGAALRLALELLKSAKRPNA---------RRVIILLTDGEPNDGPELLAEA--AREL------RKLGITVYTIG 138

                        170       180
                 ....*....|....*....|..
gi 225543438 281 VGkLDVDWRELNELGSKKDGER 302
Cdd:cd00198  139 IG-DDANEDELKEIADKTTGGA 159
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 19-73 6.70e-13

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: 63.64  E-value: 6.70e-13
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 225543438  19 CPNPGISLGAVRTGF--RFGHGDKVRYRCSSNLVLTGSSERECQGNGVWSGTEPICR 73
Cdd:cd00033    1 CPPPPVPENGTVTGSkgSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 110-352 1.58e-12

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 68.59  E-value: 1.58e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543438 110 GRKIQIQRSGHLNLYLLLDCSQSVSENDFLIFKESASLMVDRIfsfEINVSVAIITFASEPKVLM-SVLNDNSRDMTEVI 188
Cdd:COG2304   81 PPKAAAEERPPLNLVFVIDVSGSMSGDKLELAKEAAKLLVDQL---RPGDRVSIVTFAGDARVLLpPTPATDRAKILAAI 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543438 189 SSLEnAnykdhenGTGTNTYAALNSVYlmmnNQMRllgmETMAWQEIRHaIILLTDGKSNMGgspKTAVDHIREILNINQ 268
Cdd:COG2304  158 DRLQ-A-------GGGTALGAGLELAY----ELAR----KHFIPGRVNR-VILLTDGDANVG---ITDPEELLKLAEEAR 217

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543438 269 KRNdyLDIYAIGVGkldVDWRE--LNELGSKKDGeRHAFIlQDTKALHQVFEhmldvsKLTDTIcGVGNMSANASDQERT 346
Cdd:COG2304  218 EEG--ITLTTLGVG---SDYNEdlLERLADAGGG-NYYYI-DDPEEAEKVFV------REFSRI-GYENRALATEDFPLP 283


                 ....*.
gi 225543438 347 PWHVTI 352
Cdd:COG2304  284 YGTLKL 289
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 109-318 4.20e-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: 66.89  E-value: 4.20e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543438 109 LGRKIQIQRSGHLNLYLLLDCSQSVSENDFL-IFKESASLMVDRIFSfeiNVSVAIITFASEPKVLMSVlndnSRDMTEV 187
Cdd:COG1240   81 LAPLALARPQRGRDVVLVVDASGSMAAENRLeAAKGALLDFLDDYRP---RDRVGLVAFGGEAEVLLPL----TRDREAL 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543438 188 ISSLENANYkdhenGTGTNTYAALNSVYLMMNNQMrllgmetmawQEIRHAIILLTDGKSNMG-GSPKTAVDHIREiLNI 266
Cdd:COG1240  154 KRALDELPP-----GGGTPLGDALALALELLKRAD----------PARRKVIVLLTDGRDNAGrIDPLEAAELAAA-AGI 217

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 225543438 267 nqkrndylDIYAIGVGKLDVDWRELNELGSKKDGErhAFILQDTKALHQVFE 318
Cdd:COG1240  218 --------RIYTIGVGTEAVDEGLLREIAEATGGR--YFRADDLSELAAIYR 259
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 19-72 5.21e-12

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: 61.00  E-value: 5.21e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 225543438    19 CPNPG-ISLGAVRTGF-RFGHGDKVRYRCSSNLVLTGSSERECQGNGVWSGTEPIC 72
Cdd:smart00032   1 CPPPPdIENGTVTSSSgTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
Sushi pfam00084
Sushi repeat (SCR repeat);
19-72 2.77e-08

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 50.58  E-value: 2.77e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 225543438   19 CPNPGISLGAVRTGFRFGH--GDKVRYRCSSNLVLTGSSERECQGNGVWSGTEPIC 72
Cdd:pfam00084   1 CPPPPDIPNGKVSATKNEYnyGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 122-309 5.23e-08

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


Pssm-ID: 238749 [Multi-domain]  Cd Length: 164  Bit Score: 52.62  E-value: 5.23e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543438 122 NLYLLLDCSQSVSENDFLIFKESASLMVDRifsFEI---NVSVAIITFASEPKVlMSVLNdNSRDMTEVISSLENANYKd 198
Cdd:cd01472    2 DIVFLVDGSESIGLSNFNLVKDFVKRVVER---LDIgpdGVRVGVVQYSDDPRT-EFYLN-TYRSKDDVLEAVKNLRYI- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543438 199 henGTGTNTYAALNsvYLMMNNQMRLLGMEtmawQEIRHAIILLTDGKSNMGGspktavdhireILNINQKRNDYLDIYA 278
Cdd:cd01472   76 ---GGGTNTGKALK--YVRENLFTEASGSR----EGVPKVLVVITDGKSQDDV-----------EEPAVELKQAGIEVFA 135

                        170       180       190
                 ....*....|....*....|....*....|.
gi 225543438 279 IGVGKLDVDwrELNELGSkKDGERHAFILQD 309
Cdd:cd01472  136 VGVKNADEE--ELKQIAS-DPKELYVFNVAD 163
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 119-341 5.26e-08

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: 53.93  E-value: 5.26e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543438 119 GHLNLYLLLDCSQSVSENDFLIFKESASLMVDRIFSFEINVSVAIITFASEPKVLMSVLNDNSR-DMTEVISSLENAnyk 197
Cdd:cd01475    1 GPTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKaDLKRAVRRMEYL--- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543438 198 dhenGTGTNTYAALNsvYLMMNNQMRLLGMETMAwQEIRHAIILLTDGKSNmggspktavDHIREIlnINQKRNDYLDIY 277
Cdd:cd01475   78 ----ETGTMTGLAIQ--YAMNNAFSEAEGARPGS-ERVPRVGIVVTDGRPQ---------DDVSEV--AAKARALGIEMF 139

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 225543438 278 AIGVGKLDVDwrELNELGSKKDGErHAFILQDTKALHQVfehmldVSKLTDTICGVGNMSANAS 341
Cdd:cd01475  140 AVGVGRADEE--ELREIASEPLAD-HVFYVEDFSTIEEL------TKKFQGKICVVPDLCATLS 194
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 121-306 1.48e-07

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: 51.50  E-value: 1.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543438 121 LNLYLLLDCSQSVSENDFLIFKESASLMVDRIfsfEINVSVAIITFASEPK-VLMSVLNDNSRDMTEVISSLenanykdh 199
Cdd:cd01465    1 LNLVFVIDRSGSMDGPKLPLVKSALKLLVDQL---RPDDRLAIVTYDGAAEtVLPATPVRDKAAILAAIDRL-------- 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543438 200 ENGTGTNTYAalnsvylmmnnqmrllGMEtMAWQEIRHA--------IILLTDGKSNMGgspktaVDHIREIL-NINQKR 270
Cdd:cd01465   70 TAGGSTAGGA----------------GIQ-LGYQEAQKHfvpggvnrILLATDGDFNVG------ETDPDELArLVAQKR 126

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 225543438 271 NDYLDIYAIGVGKldvDWRE--LNELGSKKDGeRHAFI 306
Cdd:cd01465  127 ESGITLSTLGFGD---NYNEdlMEAIADAGNG-NTAYI 160
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 125-309 2.12e-07

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: 51.13  E-value: 2.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543438 125 LLLDCSQSVSENDFlifKESASLMVDRIFSFEI---NVSVAIITFASEPKVLMSVLNDNSRDmtEVISSLENANYKdhen 201
Cdd:cd01482    5 FLVDGSWSIGRSNF---NLVRSFLSSVVEAFEIgpdGVQVGLVQYSDDPRTEFDLNAYTSKE--DVLAAIKNLPYK---- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543438 202 GTGTNTYAALNsvYLMMNNQMRLLGMEtmawQEIRHAIILLTDGKSNmggspktavDHIREilnINQK-RNDYLDIYAIG 280
Cdd:cd01482   76 GGNTRTGKALT--HVREKNFTPDAGAR----PGVPKVVILITDGKSQ---------DDVEL---PARVlRNLGVNVFAVG 137

                        170       180
                 ....*....|....*....|....*....
gi 225543438 281 VGklDVDWRELNELGSKKDgERHAFILQD 309
Cdd:cd01482  138 VK--DADESELKMIASKPS-ETHVFNVAD 163
VWA_2 pfam13519
von Willebrand factor type A domain;
123-223 2.13e-07

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 49.21  E-value: 2.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543438  123 LYLLLDCSQSVSENDFLIFK-ESASLMVDRIFSFEINVSVAIITFASEPKVLMSvLNDNSRDMTEVISSLEnanykdhEN 201
Cdd:pfam13519   1 LVFVLDTSGSMRNGDYGPTRlEAAKDAVLALLKSLPGDRVGLVTFGDGPEVLIP-LTKDRAKILRALRRLE-------PK 72

                          90       100
                  ....*....|....*....|..
gi 225543438  202 GTGTNTYAALNSVYLMMNNQMR 223
Cdd:pfam13519  73 GGGTNLAAALQLARAALKHRRK 94
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
120-296 3.99e-07

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 50.69  E-value: 3.99e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543438 120 HLNLYLLLDCSQSVSENDFLIFKESASLMVDRIFSFEI---NVSVAIITFASEPKVLMsvlndnsrDMTEViSSLENANY 196
Cdd:COG4245    5 RLPVYLLLDTSGSMSGEPIEALNEGLQALIDELRQDPYaleTVEVSVITFDGEAKVLL--------PLTDL-EDFQPPDL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543438 197 kdhENGTGTNTYAALNSV-YLMMNNQMRLLGMETMAWQEIrhaIILLTDGKSNmGGSPKTAvdhIREILNINQKRNDYld 275
Cdd:COG4245   76 ---SASGGTPLGAALELLlDLIERRVQKYTAEGKGDWRPV---VFLITDGEPT-DSDWEAA---LQRLKDGEAAKKAN-- 143

                        170       180
                 ....*....|....*....|.
gi 225543438 276 IYAIGVGKlDVDWRELNELGS 296
Cdd:COG4245  144 IFAIGVGP-DADTEVLKQLTD 163
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 121-306 3.98e-06

VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have diverse functions in cell-cell and cell-extracellular matrix interactions. Because of their involvement in many biologically important adhesion processes, integrins are conserved across a wide range of multicellular animals. Integrins from invertebrates have been identified from six phyla. There are no data to date to suggest any immunological functions for the invertebrate integrins. The members of this sub-group have the conserved MIDAS motif that is charateristic of this domain suggesting the involvement of the integrins in the recognition and binding of multi-ligands.


Pssm-ID: 238753 [Multi-domain]  Cd Length: 163  Bit Score: 47.39  E-value: 3.98e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543438 121 LNLYLLLDCSQSVSEndflIFKESASLMVDRIFSFEIN---VSVAIITFASEPKVLMSVLNDNSRDMTEVISSLENANyk 197
Cdd:cd01476    1 LDLLFVLDSSGSVRG----KFEKYKKYIERIVEGLEIGptaTRVALITYSGRGRQRVRFNLPKHNDGEELLEKVDNLR-- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543438 198 dHENGTgTNTYAALN-SVYLMMNNQMRLLGMETMAwqeirhaiILLTDGKSNmgGSPKTAVDHIREILNInqkrndylDI 276
Cdd:cd01476   75 -FIGGT-TATGAAIEvALQQLDPSEGRREGIPKVV--------VVLTDGRSH--DDPEKQARILRAVPNI--------ET 134

                        170       180       190
                 ....*....|....*....|....*....|.
gi 225543438 277 YAIGVG-KLDVDWRELNELGSKkdgERHAFI 306
Cdd:cd01476  135 FAVGTGdPGTVDTEELHSITGN---EDHIFT 162
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
 360-439 7.43e-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: 7.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543438 360 CRGALISDQWVLTAAHCF---RDGNDHSLWRVNVGDPKSQWGkEFLIEKAVISPGFDVFAKknqgilefYGDDIALLKLA 436
Cdd:COG3591   14 CTGTLIGPNLVLTAGHCVydgAGGGWATNIVFVPGYNGGPYG-TATATRFRVPPGWVASGD--------AGYDYALLRLD 84


                 ...
gi 225543438 437 QKV 439
Cdd:COG3591   85 EPL 87
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 126-313 1.07e-05

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: 46.19  E-value: 1.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543438 126 LLDCSQSVSENDFLIFKESASLMVDRIFSFEINVSVAIITFASEPKVLMSvLNDnSRDMTEVISSLENAnykdHENGTGT 205
Cdd:cd01469    6 VLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFT-LNE-YRTKEEPLSLVKHI----SQLLGLT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543438 206 NTYAALNSVylmmnnQMRLLGMETMAWQEIRHAIILLTDGKSNmGGSPKTAVdhireilnINQKRNDYLDIYAIGVGKL- 284
Cdd:cd01469   80 NTATAIQYV------VTELFSESNGARKDATKVLVVITDGESH-DDPLLKDV--------IPQAEREGIIRYAIGVGGHf 144

                        170       180       190
                 ....*....|....*....|....*....|.
gi 225543438 285 --DVDWRELNELGSKKDgERHAFILQDTKAL 313
Cdd:cd01469  145 qrENSREELKTIASKPP-EEHFFNVTDFAAL 174
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 121-282 1.37e-05

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: 46.22  E-value: 1.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543438 121 LNLYLLLDCSQSVSENDFliFKESASLMVDRIFSFEIN---VSVAIITFASEPKVLMSVLNDNSRD---MTEVISSLENA 194
Cdd:cd01471    1 LDLYLLVDGSGSIGYSNW--VTHVVPFLHTFVQNLNISpdeINLYLVTFSTNAKELIRLSSPNSTNkdlALNAIRALLSL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543438 195 NYKdheNGTgTNTYAALNSVyLMMNNQMRllgmetMAWQEIRHAIILLTDGKSNmggSPKTAVDHIREILNINQKrndyl 274
Cdd:cd01471   79 YYP---NGS-TNTTSALLVV-EKHLFDTR------GNRENAPQLVIIMTDGIPD---SKFRTLKEARKLRERGVI----- 139


                 ....*...
gi 225543438 275 dIYAIGVG 282
Cdd:cd01471  140 -IAVLGVG 146
PHA02927 PHA02927
secreted complement-binding protein; Provisional
 19-72 5.79e-05

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 45.03  E-value: 5.79e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 225543438  19 CPNPGISLGAVRTGFR--FGHGDKVRYRCSSNLVLTGSSERECQGNGVWSGTEPIC 72
Cdd:PHA02927 206 CPHPTISNGYLSSGFKrsYSYNDNVDFKCKYGYKLSGSSSSTCSPGNTWQPELPKC 261
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 123-282 8.75e-05

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


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 44.67  E-value: 8.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543438 123 LYLLLDCSQSVSENDFLIFKESASLMVDRIFSfeiNVSVAIITFASEPKVLMSVLNDNS-RDMTEVISSLENanykdhen 201
Cdd:COG2425  121 VVLCVDTSGSMAGSKEAAAKAAALALLRALRP---NRRFGVILFDTEVVEDLPLTADDGlEDAIEFLSGLFA-------- 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543438 202 GTGTNTYAALNSvylmmnnqmrllGMETMAWQEIRHA-IILLTDGKSnmGGSPKTAVDHIReilninQKRNDYlDIYAIG 280
Cdd:COG2425  190 GGGTDIAPALRA------------ALELLEEPDYRNAdIVLITDGEA--GVSPEELLREVR------AKESGV-RLFTVA 248


                 ..
gi 225543438 281 VG 282
Cdd:COG2425  249 IG 250
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 119-247 4.93e-04

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


Pssm-ID: 238757 [Multi-domain]  Cd Length: 186  Bit Score: 41.60  E-value: 4.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543438 119 GHLNLYLLLDCSQSVSENDFLIFKESASLMVDRIFSFE------INVSVAIITFASEPKVlMSVLNDNSRDMTEVISSLE 192
Cdd:cd01480    1 GPVDITFVLDSSESVGLQNFDITKNFVKRVAERFLKDYyrkdpaGSWRVGVVQYSDQQEV-EAGFLRDIRNYTSLKEAVD 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 225543438 193 NANYKdhenGTGTNTYAALNSVYlmmnNQMRllgmETMAWQEIRHAiILLTDGKS 247
Cdd:cd01480   80 NLEYI----GGGTFTDCALKYAT----EQLL----EGSHQKENKFL-LVITDGHS 121
 
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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