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Conserved domains on  [gi|295849303|ref|NP_001171534|]
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complement C2 isoform 3 [Homo sapiens]

Protein Classification

CCP and Tryp_SPc domain-containing protein( domain architecture ID 10034163)

protein containing domains CCP, vWFA, and Tryp_SPc

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
vWFA super family cl00057
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 115-236 4.17e-57

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


The actual alignment was detected with superfamily member cd01470:

Pssm-ID: 469594 [Multi-domain]  Cd Length: 198  Bit Score: 189.42  E-value: 4.17e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295849303 115 KDHENGTGTNTYAALNSVYLMMnnqmRLLGME-TMAWQEIRHAIILLTDGKSNMGGSPKTAVDHIREILNINQK----RN 189
Cdd:cd01470   77 DDHGDKTGTNTAAALKKVYERM----ALEKVRnKEAFNETRHVIILFTDGKSNMGGSPLPTVDKIKNLVYKNNKsdnpRE 152

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 295849303 190 DYLDIYAIGVGKlDVDWRELNELGSKKDGERHAFILQDTKALHQVFE 236
Cdd:cd01470  153 DYLDVYVFGVGD-DVNKEELNDLASKKDNERHFFKLKDYEDLQEVFD 198
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 259-528 4.23e-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: 145.11  E-value: 4.23e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295849303 259 SDQERTPWHVTIKPKS-QETCRGALISDQWVLTAAHCFRdGNDHSLWRVNVGD----PKSQWGKEFLIEKAVISPGFDVF 333
Cdd:cd00190    7 AKIGSFPWQVSLQYTGgRHFCGGSLISPRWVLTAAHCVY-SSAPSNYTVRLGShdlsSNEGGGQVIKVKKVIVHPNYNPS 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295849303 334 akknqgileFYGDDIALLKLAQKVKMSTHARPICLPCTMEANlalrrPQGSTCR-----DHENEllnkqsvpahfVALNG 408
Cdd:cd00190   86 ---------TYDNDIALLKLKRPVTLSDNVRPICLPSSGYNL-----PAGTTCTvsgwgRTSEG-----------GPLPD 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295849303 409 SKLNINLKMgVEWTSCAEVVSQektmfpnltdvREVVTDQFLCSGTQE-DESPCKGESGGAVFLERRFRFFQVGLVSWGl 487
Cdd:cd00190  141 VLQEVNVPI-VSNAECKRAYSY-----------GGTITDNMLCAGGLEgGKDACQGDSGGPLVCNDNGRGVLVGIVSWG- 207

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 295849303 488 ynpcLGSADKNSrkraprskvppPRDFHiNLFRMQPWLRQH 528
Cdd:cd00190  208 ----SGCARPNY-----------PGVYT-RVSSYLDWIQKT 232
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 28-82 1.45e-12

Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) have been identified in several proteins of the complement system; SUSHI repeats (short complement-like repeat, SCR) are abundant in complement control proteins. The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. Typically, 2 to 4 modules contribute to a binding site, implying that the orientation of the modules to each other is critical for function.


:

Pssm-ID: 153056 [Multi-domain]  Cd Length: 57  Bit Score: 62.48  E-value: 1.45e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 295849303  28 CPNPGISLGAVRTGF--RFGHGDKVRYRCSSNLVLTGSSERECQGNGVWSGTEPICR 82
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 ...
 115-236 4.17e-57

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: 189.42  E-value: 4.17e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295849303 115 KDHENGTGTNTYAALNSVYLMMnnqmRLLGME-TMAWQEIRHAIILLTDGKSNMGGSPKTAVDHIREILNINQK----RN 189
Cdd:cd01470   77 DDHGDKTGTNTAAALKKVYERM----ALEKVRnKEAFNETRHVIILFTDGKSNMGGSPLPTVDKIKNLVYKNNKsdnpRE 152

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 295849303 190 DYLDIYAIGVGKlDVDWRELNELGSKKDGERHAFILQDTKALHQVFE 236
Cdd:cd01470  153 DYLDVYVFGVGD-DVNKEELNDLASKKDNERHFFKLKDYEDLQEVFD 198
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 259-528 4.23e-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: 145.11  E-value: 4.23e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295849303 259 SDQERTPWHVTIKPKS-QETCRGALISDQWVLTAAHCFRdGNDHSLWRVNVGD----PKSQWGKEFLIEKAVISPGFDVF 333
Cdd:cd00190    7 AKIGSFPWQVSLQYTGgRHFCGGSLISPRWVLTAAHCVY-SSAPSNYTVRLGShdlsSNEGGGQVIKVKKVIVHPNYNPS 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295849303 334 akknqgileFYGDDIALLKLAQKVKMSTHARPICLPCTMEANlalrrPQGSTCR-----DHENEllnkqsvpahfVALNG 408
Cdd:cd00190   86 ---------TYDNDIALLKLKRPVTLSDNVRPICLPSSGYNL-----PAGTTCTvsgwgRTSEG-----------GPLPD 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295849303 409 SKLNINLKMgVEWTSCAEVVSQektmfpnltdvREVVTDQFLCSGTQE-DESPCKGESGGAVFLERRFRFFQVGLVSWGl 487
Cdd:cd00190  141 VLQEVNVPI-VSNAECKRAYSY-----------GGTITDNMLCAGGLEgGKDACQGDSGGPLVCNDNGRGVLVGIVSWG- 207

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 295849303 488 ynpcLGSADKNSrkraprskvppPRDFHiNLFRMQPWLRQH 528
Cdd:cd00190  208 ----SGCARPNY-----------PGVYT-RVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 259-491 2.16e-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: 140.51  E-value: 2.16e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295849303   259 SDQERTPWHVTIKPKS-QETCRGALISDQWVLTAAHCFRdGNDHSLWRVNVGDPKSQWGKE---FLIEKAVISPGFDvfa 334
Cdd:smart00020   8 ANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVR-GSDPSNIRVRLGSHDLSSGEEgqvIKVSKVIIHPNYN--- 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295849303   335 kknqgiLEFYGDDIALLKLAQKVKMSTHARPICLPCTmeanlALRRPQGSTCRD----HENEllnkqSVPAHFVALNGSK 410
Cdd:smart00020  84 ------PSTYDNDIALLKLKEPVTLSDNVRPICLPSS-----NYNVPAGTTCTVsgwgRTSE-----GAGSLPDTLQEVN 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295849303   411 LNInlkmgVEWTSCAEVVSQektmfpnltdvREVVTDQFLCSGTQE-DESPCKGESGGAVFLERRfRFFQVGLVSWGlyN 489
Cdd:smart00020 148 VPI-----VSNATCRRAYSG-----------GGAITDNMLCAGGLEgGKDACQGDSGGPLVCNDG-RWVLVGIVSWG--S 208


                   ..
gi 295849303   490 PC 491
Cdd:smart00020 209 GC 210
Trypsin pfam00089
Trypsin;
265-486 3.07e-23

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 97.90  E-value: 3.07e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295849303  265 PWHVTIK-PKSQETCRGALISDQWVLTAAHCFRDGNDhslWRVNVGDP----KSQWGKEFLIEKAVISPGFDVFAKKNqg 339
Cdd:pfam00089  13 PWQVSLQlSSGKHFCGGSLISENWVLTAAHCVSGASD---VKVVLGAHnivlREGGEQKFDVEKIIVHPNYNPDTLDN-- 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295849303  340 ilefygdDIALLKLAQKVKMSTHARPICLPCTmeanlALRRPQGSTC------RDHEN---ELLNKQSVPahfvalngsk 410
Cdd:pfam00089  88 -------DIALLKLESPVTLGDTVRPICLPDA-----SSDLPVGTTCtvsgwgNTKTLgpsDTLQEVTVP---------- 145

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 295849303  411 lninlkmgvewtscaeVVSQEKtmfpNLTDVREVVTDQFLCSGTQeDESPCKGESGGAVFLERRfrfFQVGLVSWG 486
Cdd:pfam00089 146 ----------------VVSRET----CRSAYGGTVTDTMICAGAG-GKDACQGDSGGPLVCSDG---ELIGIVSWG 197
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 257-495 7.82e-21

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 92.02  E-value: 7.82e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295849303 257 NASDQERtPWHVTIKPKS---QETCRGALISDQWVLTAAHCFRDGNDHSLwRVNVG--DPKSQWGKEFLIEKAVISPGFD 331
Cdd:COG5640   36 PATVGEY-PWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDGPSDL-RVVIGstDLSTSGGTVVKVARIVVHPDYD 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295849303 332 VFAkknqgilefYGDDIALLKLAQKVkmsTHARPICLPctmEANLALRRPQ-------GSTCRDHEN--ELLNKQSVPAh 402
Cdd:COG5640  114 PAT---------PGNDIALLKLATPV---PGVAPAPLA---TSADAAAPGTpatvagwGRTSEGPGSqsGTLRKADVPV- 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295849303 403 fvalngsklninlkmgVEWTSCAevvsqektmfpnltDVREVVTDQFLCSGTQE-DESPCKGESGGAVFLERRFRFFQVG 481
Cdd:COG5640  178 ----------------VSDATCA--------------AYGGFDGGTMLCAGYPEgGKDACQGDSGGPLVVKDGGGWVLVG 227

                        250
                 ....*....|....
gi 295849303 482 LVSWGlYNPCLGSA 495
Cdd:COG5640  228 VVSWG-GGPCAAGY 240
VWA pfam00092
von Willebrand factor type A domain;
120-237 6.68e-13

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 66.91  E-value: 6.68e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295849303  120 GTGTNTYAALNSVYLMMNNQMRllGMETmawqEIRHAIILLTDGKSNMgGSPKTAVDHIREiLNINqkrndyldIYAIGV 199
Cdd:pfam00092  76 GGTTNTGKALKYALENLFSSAA--GARP----GAPKVVVLLTDGRSQD-GDPEEVARELKS-AGVT--------VFAVGV 139

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 295849303  200 GklDVDWRELNELGSKKDgERHAFILQDTKALHQVFEH 237
Cdd:pfam00092 140 G--NADDEELRKIASEPG-EGHVFTVSDFEALEDLQDQ 174
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 28-82 1.45e-12

Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) have been identified in several proteins of the complement system; SUSHI repeats (short complement-like repeat, SCR) are abundant in complement control proteins. The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. Typically, 2 to 4 modules contribute to a binding site, implying that the orientation of the modules to each other is critical for function.


Pssm-ID: 153056 [Multi-domain]  Cd Length: 57  Bit Score: 62.48  E-value: 1.45e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 295849303  28 CPNPGISLGAVRTGF--RFGHGDKVRYRCSSNLVLTGSSERECQGNGVWSGTEPICR 82
Cdd:cd00033    1 CPPPPVPENGTVTGSkgSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 28-81 1.20e-11

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


Pssm-ID: 214478 [Multi-domain]  Cd Length: 56  Bit Score: 59.85  E-value: 1.20e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 295849303    28 CPNPG-ISLGAVRTGF-RFGHGDKVRYRCSSNLVLTGSSERECQGNGVWSGTEPIC 81
Cdd:smart00032   1 CPPPPdIENGTVTSSSgTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 85-233 5.03e-09

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: 55.92  E-value: 5.03e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295849303    85 YSYDFPEDVAPALGTSFSHMLGATNPTQKTkdheNGTGTNTYAALNSVYLMMNNQMRllgmetmAWQE-IRHAIILLTDG 163
Cdd:smart00327  45 FSDDARVLFPLNDSRSKDALLEALASLSYK----LGGGTNLGAALQYALENLFSKSA-------GSRRgAPKVVILITDG 113

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295849303   164 KSNMGGSpktavdhiREILNINQKRNDYLDIYAIGVGKlDVDWRELNELgSKKDGERHAFILQDTKALHQ 233
Cdd:smart00327 114 ESNDGPK--------DLLKAAKELKRSGVKVFVVGVGN-DVDEEELKKL-ASAPGGVYVFLPELLDLLID 173
Sushi pfam00084
Sushi repeat (SCR repeat);
28-81 3.72e-08

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 49.81  E-value: 3.72e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 295849303   28 CPNPGISLGAVRTGFRFGH--GDKVRYRCSSNLVLTGSSERECQGNGVWSGTEPIC 81
Cdd:pfam00084   1 CPPPPDIPNGKVSATKNEYnyGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 120-236 6.00e-06

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: 48.01  E-value: 6.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295849303 120 GTGTNTYAALNSVYLMMNNQMrllgmetmawQEIRHAIILLTDGKSNMG-GSPKTAVDHIREiLNInqkrndylDIYAIG 198
Cdd:COG1240  163 GGGTPLGDALALALELLKRAD----------PARRKVIVLLTDGRDNAGrIDPLEAAELAAA-AGI--------RIYTIG 223

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 295849303 199 VGKLDVDWRELNELGSKKDGErhAFILQDTKALHQVFE 236
Cdd:COG1240  224 VGTEAVDEGLLREIAEATGGR--YFRADDLSELAAIYR 259
PHA02927 PHA02927
secreted complement-binding protein; Provisional
 28-81 4.80e-05

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 45.03  E-value: 4.80e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 295849303  28 CPNPGISLGAVRTGFR--FGHGDKVRYRCSSNLVLTGSSERECQGNGVWSGTEPIC 81
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 ...
 115-236 4.17e-57

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: 189.42  E-value: 4.17e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295849303 115 KDHENGTGTNTYAALNSVYLMMnnqmRLLGME-TMAWQEIRHAIILLTDGKSNMGGSPKTAVDHIREILNINQK----RN 189
Cdd:cd01470   77 DDHGDKTGTNTAAALKKVYERM----ALEKVRnKEAFNETRHVIILFTDGKSNMGGSPLPTVDKIKNLVYKNNKsdnpRE 152

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 295849303 190 DYLDIYAIGVGKlDVDWRELNELGSKKDGERHAFILQDTKALHQVFE 236
Cdd:cd01470  153 DYLDVYVFGVGD-DVNKEELNDLASKKDNERHFFKLKDYEDLQEVFD 198
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 259-528 4.23e-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: 145.11  E-value: 4.23e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295849303 259 SDQERTPWHVTIKPKS-QETCRGALISDQWVLTAAHCFRdGNDHSLWRVNVGD----PKSQWGKEFLIEKAVISPGFDVF 333
Cdd:cd00190    7 AKIGSFPWQVSLQYTGgRHFCGGSLISPRWVLTAAHCVY-SSAPSNYTVRLGShdlsSNEGGGQVIKVKKVIVHPNYNPS 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295849303 334 akknqgileFYGDDIALLKLAQKVKMSTHARPICLPCTMEANlalrrPQGSTCR-----DHENEllnkqsvpahfVALNG 408
Cdd:cd00190   86 ---------TYDNDIALLKLKRPVTLSDNVRPICLPSSGYNL-----PAGTTCTvsgwgRTSEG-----------GPLPD 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295849303 409 SKLNINLKMgVEWTSCAEVVSQektmfpnltdvREVVTDQFLCSGTQE-DESPCKGESGGAVFLERRFRFFQVGLVSWGl 487
Cdd:cd00190  141 VLQEVNVPI-VSNAECKRAYSY-----------GGTITDNMLCAGGLEgGKDACQGDSGGPLVCNDNGRGVLVGIVSWG- 207

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 295849303 488 ynpcLGSADKNSrkraprskvppPRDFHiNLFRMQPWLRQH 528
Cdd:cd00190  208 ----SGCARPNY-----------PGVYT-RVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 259-491 2.16e-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: 140.51  E-value: 2.16e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295849303   259 SDQERTPWHVTIKPKS-QETCRGALISDQWVLTAAHCFRdGNDHSLWRVNVGDPKSQWGKE---FLIEKAVISPGFDvfa 334
Cdd:smart00020   8 ANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVR-GSDPSNIRVRLGSHDLSSGEEgqvIKVSKVIIHPNYN--- 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295849303   335 kknqgiLEFYGDDIALLKLAQKVKMSTHARPICLPCTmeanlALRRPQGSTCRD----HENEllnkqSVPAHFVALNGSK 410
Cdd:smart00020  84 ------PSTYDNDIALLKLKEPVTLSDNVRPICLPSS-----NYNVPAGTTCTVsgwgRTSE-----GAGSLPDTLQEVN 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295849303   411 LNInlkmgVEWTSCAEVVSQektmfpnltdvREVVTDQFLCSGTQE-DESPCKGESGGAVFLERRfRFFQVGLVSWGlyN 489
Cdd:smart00020 148 VPI-----VSNATCRRAYSG-----------GGAITDNMLCAGGLEgGKDACQGDSGGPLVCNDG-RWVLVGIVSWG--S 208


                   ..
gi 295849303   490 PC 491
Cdd:smart00020 209 GC 210
Trypsin pfam00089
Trypsin;
265-486 3.07e-23

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 97.90  E-value: 3.07e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295849303  265 PWHVTIK-PKSQETCRGALISDQWVLTAAHCFRDGNDhslWRVNVGDP----KSQWGKEFLIEKAVISPGFDVFAKKNqg 339
Cdd:pfam00089  13 PWQVSLQlSSGKHFCGGSLISENWVLTAAHCVSGASD---VKVVLGAHnivlREGGEQKFDVEKIIVHPNYNPDTLDN-- 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295849303  340 ilefygdDIALLKLAQKVKMSTHARPICLPCTmeanlALRRPQGSTC------RDHEN---ELLNKQSVPahfvalngsk 410
Cdd:pfam00089  88 -------DIALLKLESPVTLGDTVRPICLPDA-----SSDLPVGTTCtvsgwgNTKTLgpsDTLQEVTVP---------- 145

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 295849303  411 lninlkmgvewtscaeVVSQEKtmfpNLTDVREVVTDQFLCSGTQeDESPCKGESGGAVFLERRfrfFQVGLVSWG 486
Cdd:pfam00089 146 ----------------VVSRET----CRSAYGGTVTDTMICAGAG-GKDACQGDSGGPLVCSDG---ELIGIVSWG 197
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 257-495 7.82e-21

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 92.02  E-value: 7.82e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295849303 257 NASDQERtPWHVTIKPKS---QETCRGALISDQWVLTAAHCFRDGNDHSLwRVNVG--DPKSQWGKEFLIEKAVISPGFD 331
Cdd:COG5640   36 PATVGEY-PWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDGPSDL-RVVIGstDLSTSGGTVVKVARIVVHPDYD 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295849303 332 VFAkknqgilefYGDDIALLKLAQKVkmsTHARPICLPctmEANLALRRPQ-------GSTCRDHEN--ELLNKQSVPAh 402
Cdd:COG5640  114 PAT---------PGNDIALLKLATPV---PGVAPAPLA---TSADAAAPGTpatvagwGRTSEGPGSqsGTLRKADVPV- 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295849303 403 fvalngsklninlkmgVEWTSCAevvsqektmfpnltDVREVVTDQFLCSGTQE-DESPCKGESGGAVFLERRFRFFQVG 481
Cdd:COG5640  178 ----------------VSDATCA--------------AYGGFDGGTMLCAGYPEgGKDACQGDSGGPLVVKDGGGWVLVG 227

                        250
                 ....*....|....
gi 295849303 482 LVSWGlYNPCLGSA 495
Cdd:COG5640  228 VVSWG-GGPCAAGY 240
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 117-223 1.72e-14

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: 71.17  E-value: 1.72e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295849303 117 HENGTGTNTYAALNSVYLMMNNqmrllgmETMAWQEIRHAIILLTDGKSNMGGSPKTAVDHIREIlninqkrndYLDIYA 196
Cdd:cd01450   74 YLGGGGTNTGKALQYALEQLFS-------ESNARENVPKVIIVLTDGRSDDGGDPKEAAAKLKDE---------GIKVFV 137

                         90       100
                 ....*....|....*....|....*..
gi 295849303 197 IGVGklDVDWRELNELGSKKdGERHAF 223
Cdd:cd01450  138 VGVG--PADEEELREIASCP-SERHVF 161
VWA pfam00092
von Willebrand factor type A domain;
120-237 6.68e-13

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 66.91  E-value: 6.68e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295849303  120 GTGTNTYAALNSVYLMMNNQMRllGMETmawqEIRHAIILLTDGKSNMgGSPKTAVDHIREiLNINqkrndyldIYAIGV 199
Cdd:pfam00092  76 GGTTNTGKALKYALENLFSSAA--GARP----GAPKVVVLLTDGRSQD-GDPEEVARELKS-AGVT--------VFAVGV 139

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 295849303  200 GklDVDWRELNELGSKKDgERHAFILQDTKALHQVFEH 237
Cdd:pfam00092 140 G--NADDEELRKIASEPG-EGHVFTVSDFEALEDLQDQ 174
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 28-82 1.45e-12

Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) have been identified in several proteins of the complement system; SUSHI repeats (short complement-like repeat, SCR) are abundant in complement control proteins. The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. Typically, 2 to 4 modules contribute to a binding site, implying that the orientation of the modules to each other is critical for function.


Pssm-ID: 153056 [Multi-domain]  Cd Length: 57  Bit Score: 62.48  E-value: 1.45e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 295849303  28 CPNPGISLGAVRTGF--RFGHGDKVRYRCSSNLVLTGSSERECQGNGVWSGTEPICR 82
Cdd:cd00033    1 CPPPPVPENGTVTGSkgSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 28-81 1.20e-11

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


Pssm-ID: 214478 [Multi-domain]  Cd Length: 56  Bit Score: 59.85  E-value: 1.20e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 295849303    28 CPNPG-ISLGAVRTGF-RFGHGDKVRYRCSSNLVLTGSSERECQGNGVWSGTEPIC 81
Cdd:smart00032   1 CPPPPdIENGTVTSSSgTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 85-233 5.03e-09

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: 55.92  E-value: 5.03e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295849303    85 YSYDFPEDVAPALGTSFSHMLGATNPTQKTkdheNGTGTNTYAALNSVYLMMNNQMRllgmetmAWQE-IRHAIILLTDG 163
Cdd:smart00327  45 FSDDARVLFPLNDSRSKDALLEALASLSYK----LGGGTNLGAALQYALENLFSKSA-------GSRRgAPKVVILITDG 113

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295849303   164 KSNMGGSpktavdhiREILNINQKRNDYLDIYAIGVGKlDVDWRELNELgSKKDGERHAFILQDTKALHQ 233
Cdd:smart00327 114 ESNDGPK--------DLLKAAKELKRSGVKVFVVGVGN-DVDEEELKKL-ASAPGGVYVFLPELLDLLID 173
Sushi pfam00084
Sushi repeat (SCR repeat);
28-81 3.72e-08

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 49.81  E-value: 3.72e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 295849303   28 CPNPGISLGAVRTGFRFGH--GDKVRYRCSSNLVLTGSSERECQGNGVWSGTEPIC 81
Cdd:pfam00084   1 CPPPPDIPNGKVSATKNEYnyGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 120-236 6.00e-06

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: 48.01  E-value: 6.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295849303 120 GTGTNTYAALNSVYLMMNNQMrllgmetmawQEIRHAIILLTDGKSNMG-GSPKTAVDHIREiLNInqkrndylDIYAIG 198
Cdd:COG1240  163 GGGTPLGDALALALELLKRAD----------PARRKVIVLLTDGRDNAGrIDPLEAAELAAA-AGI--------RIYTIG 223

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 295849303 199 VGKLDVDWRELNELGSKKDGErhAFILQDTKALHQVFE 236
Cdd:COG1240  224 VGTEAVDEGLLREIAEATGGR--YFRADDLSELAAIYR 259
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
 278-357 6.53e-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: 6.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295849303 278 CRGALISDQWVLTAAHCF---RDGNDHSLWRVNVGDPKSQWGkEFLIEKAVISPGFDVFAKknqgilefYGDDIALLKLA 354
Cdd:COG3591   14 CTGTLIGPNLVLTAGHCVydgAGGGWATNIVFVPGYNGGPYG-TATATRFRVPPGWVASGD--------AGYDYALLRLD 84


                 ...
gi 295849303 355 QKV 357
Cdd:COG3591   85 EPL 87
PHA02927 PHA02927
secreted complement-binding protein; Provisional
 28-81 4.80e-05

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 45.03  E-value: 4.80e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 295849303  28 CPNPGISLGAVRTGFR--FGHGDKVRYRCSSNLVLTGSSERECQGNGVWSGTEPIC 81
Cdd:PHA02927 206 CPHPTISNGYLSSGFKrsYSYNDNVDFKCKYGYKLSGSSSSTCSPGNTWQPELPKC 261
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 116-220 6.65e-05

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: 43.32  E-value: 6.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295849303 116 DHENGTGTNTYAALNSVYLMMNNQMRLLGmetmawqeiRHAIILLTDGKSNMGGSPKTAVdhIREIlninqkRNDYLDIY 195
Cdd:cd00198   73 KKGLGGGTNIGAALRLALELLKSAKRPNA---------RRVIILLTDGEPNDGPELLAEA--AREL------RKLGITVY 135

                         90       100
                 ....*....|....*....|....*
gi 295849303 196 AIGVGkLDVDWRELNELGSKKDGER 220
Cdd:cd00198  136 TIGIG-DDANEDELKEIADKTTGGA 159
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 120-270 1.14e-03

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 41.24  E-value: 1.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295849303 120 GTGTNTYAALNSVYlmmnNQMRllgmETMAWQEIRHaIILLTDGKSNMGgspKTAVDHIREILNINQKRNdyLDIYAIGV 199
Cdd:COG2304  163 GGGTALGAGLELAY----ELAR----KHFIPGRVNR-VILLTDGDANVG---ITDPEELLKLAEEAREEG--ITLTTLGV 228

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 295849303 200 GkldVDWRE--LNELGSKKDGeRHAFIlQDTKALHQVFEhmldvsKLTDTIcGVGNMSANASDQERTPWHVTI 270
Cdd:COG2304  229 G---SDYNEdlLERLADAGGG-NYYYI-DDPEEAEKVFV------REFSRI-GYENRALATEDFPLPYGTLKL 289
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 120-227 3.21e-03

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: 38.42  E-value: 3.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295849303 120 GTGTNTYAALNsvYLMMNNQMRLLGMEtmawQEIRHAIILLTDGKSNmggspktavDHIREilnINQK-RNDYLDIYAIG 198
Cdd:cd01482   76 GGNTRTGKALT--HVREKNFTPDAGAR----PGVPKVVILITDGKSQ---------DDVEL---PARVlRNLGVNVFAVG 137

                         90       100
                 ....*....|....*....|....*....
gi 295849303 199 VGklDVDWRELNELGSKKDgERHAFILQD 227
Cdd:cd01482  138 VK--DADESELKMIASKPS-ETHVFNVAD 163
 
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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