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Conserved domains on  [gi|116126|sp|P04186|]
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RecName: Full=Complement factor B; AltName: Full=C3/C5 convertase; Contains: RecName: Full=Complement factor B Ba fragment; Contains: RecName: Full=Complement factor B Bb fragment; Flags: Precursor

Protein Classification

vWA_complement_factors and Tryp_SPc domain-containing protein( domain architecture ID 10636848)

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 ...
 266-463 4.49e-112

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: 338.11  E-value: 4.49e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116126   266 MNIYLVLDGSDSIGSSNFTGAKRCLTNLIEKVASYGVRPRYGLLTYATVPKVLVRVSDERSSDADWVTEKLNQISYEDHK 345
Cdd:cd01470   1 LNIYIALDASDSIGEEDFDEAKNAIKTLIEKISSYEVSPRYEIISYASDPKEIVSIRDFNSNDADDVIKRLEDFNYDDHG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116126   346 LKSGTNTKRALQAVYSMMSWAGDAPPEGWNRTRHVIIIMTDGLHNMGGNPVTVIQDIRALLDIGRDPKNPREDYLDVYVF 425
Cdd:cd01470  81 DKTGTNTAAALKKVYERMALEKVRNKEAFNETRHVIILFTDGKSNMGGSPLPTVDKIKNLVYKNNKSDNPREDYLDVYVF 160

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 116126   426 GVGPLVDSVNINALASKKDNEHHVFKVKDMEDLENVFY 463
Cdd:cd01470 161 GVGDDVNKEELNDLASKKDNERHFFKLKDYEDLQEVFD 198
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 486-752 2.33e-44

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: 159.36  E-value: 2.33e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116126   486 DYHKQPWQAKISVTRplkGHETCMGAVVSEYFVLTAAHCFmVDDQKHSIKVSVGGQRR--------DLEIEEVLFHPKYN 557
Cdd:cd00190   8 KIGSFPWQVSLQYTG---GRHFCGGSLISPRWVLTAAHCV-YSSAPSNYTVRLGSHDLssnegggqVIKVKKVIVHPNYN 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116126   558 ingkkaegiPEFYDYDVALVKLKNKLKYGQTLRPICLPCTEGTtralrLPQTATCkqhkeqllpvkdvkalFVS-----E 632
Cdd:cd00190  84 ---------PSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYN-----LPAGTTC----------------TVSgwgrtS 133

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116126   633 QGKSLTR--KEVYIKNGDKkASCERDAtkaqgyekvkDASEVVTPRFLCTGGVDpyADPNTCKGDSGGPLIVHKRSRFIQ 710
Cdd:cd00190 134 EGGPLPDvlQEVNVPIVSN-AECKRAY----------SYGGTITDNMLCAGGLE--GGKDACQGDSGGPLVCNDNGRGVL 200

                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 116126   711 VGVISWGVvdVCRdqrrqqlVPSYARDFHiNLFQVLPWLKDK 752
Cdd:cd00190 201 VGIVSWGS--GCA-------RPNYPGVYT-RVSSYLDWIQKT 232
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 100-155 2.16e-15

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


:

Pssm-ID: 153056 [Multi-domain]  Cd Length: 57  Bit Score: 70.95  E-value: 2.16e-15
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 116126   100 CPRPQDFENGEFWPRSPFYNLSDQISFQCYDGYVLRGSANRTCQENGRWDGQTAIC 155
Cdd:cd00033   1 CPPPPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTC 56
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 162-216 5.03e-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: 61.32  E-value: 5.03e-12
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 116126   162 CPNPGIPIGTRKVGSQ--YRLEDIVTYHCSRGLVLRGSQKRKCQEGGSWSGTEPSCQ 216
Cdd:cd00033   1 CPPPPVPENGTVTGSKgsYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 52-80 1.49e-03

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: 37.51  E-value: 1.49e-03
                           10        20
                   ....*....|....*....|....*....
gi 116126       52 GQALEYLCPSGFYPYPVQTRTCRSTGSWS 80
Cdd:smart00032  22 GDTVTYSCDPGYTLIGSSTITCLENGTWS 50
 
Name Accession Description Interval E-value
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
 266-463 4.49e-112

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: 338.11  E-value: 4.49e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116126   266 MNIYLVLDGSDSIGSSNFTGAKRCLTNLIEKVASYGVRPRYGLLTYATVPKVLVRVSDERSSDADWVTEKLNQISYEDHK 345
Cdd:cd01470   1 LNIYIALDASDSIGEEDFDEAKNAIKTLIEKISSYEVSPRYEIISYASDPKEIVSIRDFNSNDADDVIKRLEDFNYDDHG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116126   346 LKSGTNTKRALQAVYSMMSWAGDAPPEGWNRTRHVIIIMTDGLHNMGGNPVTVIQDIRALLDIGRDPKNPREDYLDVYVF 425
Cdd:cd01470  81 DKTGTNTAAALKKVYERMALEKVRNKEAFNETRHVIILFTDGKSNMGGSPLPTVDKIKNLVYKNNKSDNPREDYLDVYVF 160

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 116126   426 GVGPLVDSVNINALASKKDNEHHVFKVKDMEDLENVFY 463
Cdd:cd01470 161 GVGDDVNKEELNDLASKKDNERHFFKLKDYEDLQEVFD 198
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 486-752 2.33e-44

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: 159.36  E-value: 2.33e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116126   486 DYHKQPWQAKISVTRplkGHETCMGAVVSEYFVLTAAHCFmVDDQKHSIKVSVGGQRR--------DLEIEEVLFHPKYN 557
Cdd:cd00190   8 KIGSFPWQVSLQYTG---GRHFCGGSLISPRWVLTAAHCV-YSSAPSNYTVRLGSHDLssnegggqVIKVKKVIVHPNYN 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116126   558 ingkkaegiPEFYDYDVALVKLKNKLKYGQTLRPICLPCTEGTtralrLPQTATCkqhkeqllpvkdvkalFVS-----E 632
Cdd:cd00190  84 ---------PSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYN-----LPAGTTC----------------TVSgwgrtS 133

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116126   633 QGKSLTR--KEVYIKNGDKkASCERDAtkaqgyekvkDASEVVTPRFLCTGGVDpyADPNTCKGDSGGPLIVHKRSRFIQ 710
Cdd:cd00190 134 EGGPLPDvlQEVNVPIVSN-AECKRAY----------SYGGTITDNMLCAGGLE--GGKDACQGDSGGPLVCNDNGRGVL 200

                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 116126   711 VGVISWGVvdVCRdqrrqqlVPSYARDFHiNLFQVLPWLKDK 752
Cdd:cd00190 201 VGIVSWGS--GCA-------RPNYPGVYT-RVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 486-718 3.76e-41

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: 150.14  E-value: 3.76e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116126      486 DYHKQPWQAKISVTRplkGHETCMGAVVSEYFVLTAAHCFMvDDQKHSIKVSVGGQRR-------DLEIEEVLFHPKYNi 558
Cdd:smart00020   9 NIGSFPWQVSLQYGG---GRHFCGGSLISPRWVLTAAHCVR-GSDPSNIRVRLGSHDLssgeegqVIKVSKVIIHPNYN- 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116126      559 ngkkaegiPEFYDYDVALVKLKNKLKYGQTLRPICLPCTegttrALRLPQTATCkqhkeqllpvkdvkalFVSEQGK--- 635
Cdd:smart00020  84 --------PSTYDNDIALLKLKEPVTLSDNVRPICLPSS-----NYNVPAGTTC----------------TVSGWGRtse 134

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116126      636 -----SLTRKEVYIKNGDKKAsCERDatkaqgYEKvkdaSEVVTPRFLCTGGvdPYADPNTCKGDSGGPLiVHKRSRFIQ 710
Cdd:smart00020 135 gagslPDTLQEVNVPIVSNAT-CRRA------YSG----GGAITDNMLCAGG--LEGGKDACQGDSGGPL-VCNDGRWVL 200


                   ....*...
gi 116126      711 VGVISWGV 718
Cdd:smart00020 201 VGIVSWGS 208
Trypsin pfam00089
Trypsin;
488-749 7.76e-34

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 129.10  E-value: 7.76e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116126     488 HKQPWQAKISVTRplkGHETCMGAVVSEYFVLTAAHCF------MVDDQKHSIKVSVGGQRRdLEIEEVLFHPKYNingk 561
Cdd:pfam00089  10 GSFPWQVSLQLSS---GKHFCGGSLISENWVLTAAHCVsgasdvKVVLGAHNIVLREGGEQK-FDVEKIIVHPNYN---- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116126     562 kaegiPEFYDYDVALVKLKNKLKYGQTLRPICLPCTEGTtralrLPQTATCkqhkeqllpvkdvkalFVS------EQGK 635
Cdd:pfam00089  82 -----PDTLDNDIALLKLESPVTLGDTVRPICLPDASSD-----LPVGTTC----------------TVSgwgntkTLGP 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116126     636 SLTRKEVYIKNGDKkASCERDAtkaqgyekvkdaSEVVTPRFLCTGGVDPYAdpntCKGDSGGPLIVHKRsrfIQVGVIS 715
Cdd:pfam00089 136 SDTLQEVTVPVVSR-ETCRSAY------------GGTVTDTMICAGAGGKDA----CQGDSGGPLVCSDG---ELIGIVS 195

                         250       260       270
                  ....*....|....*....|....*....|....
gi 116126     716 WGvvDVCRDQRRqqlvpsyaRDFHINLFQVLPWL 749
Cdd:pfam00089 196 WG--YGCASGNY--------PGVYTPVSSYLDWI 219
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 267-450 9.76e-29

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: 112.93  E-value: 9.76e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116126      267 NIYLVLDGSDSIGSSNFTGAKRCLTNLIEKVASYGVRPRYGLLTYATVPKVLVRVSDERSSDAdwVTEKLNQISYedhKL 346
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDA--LLEALASLSY---KL 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116126      347 KSGTNTKRALQAVYSMMSwagdAPPEGWNR-TRHVIIIMTDGLHNMGGNpvtviqdirallDIGRDPKNPREDYLDVYVF 425
Cdd:smart00327  76 GGGTNLGAALQYALENLF----SKSAGSRRgAPKVVILITDGESNDGPK------------DLLKAAKELKRSGVKVFVV 139

                          170       180
                   ....*....|....*....|....*
gi 116126      426 GVGPLVDSVNINALASKKDNEHHVF 450
Cdd:smart00327 140 GVGNDVDEEELKKLASAPGGVYVFL 164
VWA pfam00092
von Willebrand factor type A domain;
267-464 2.20e-28

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 111.98  E-value: 2.20e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116126     267 NIYLVLDGSDSIGSSNFTGAKRCLTNLIEKVASYGVRPRYGLLTYATVPKVLVRVSDERSSDAdwVTEKLNQISYEDHKL 346
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEE--LLSAVDNLRYLGGGT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116126     347 KS-GTNTKRALQAVYSMMSWAGDappegwnRTRHVIIIMTDGlHNMGGNPVTVIQDIralldigrdpknpREDYLDVYVF 425
Cdd:pfam00092  79 TNtGKALKYALENLFSSAAGARP-------GAPKVVVLLTDG-RSQDGDPEEVAREL-------------KSAGVTVFAV 137

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 116126     426 GVGPlVDSVNINALASKKDNEhHVFKVKDMEDLENVFYQ 464
Cdd:pfam00092 138 GVGN-ADDEELRKIASEPGEG-HVFTVSDFEALEDLQDQ 174
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 491-717 2.62e-23

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 100.11  E-value: 2.62e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116126   491 PWQAKISVTRPLKGHeTCMGAVVSEYFVLTAAHCfMVDDQKHSIKVSVG--------GQRRdlEIEEVLFHPKYNingkk 562
Cdd:COG5640  43 PWMVALQSSNGPSGQ-FCGGTLIAPRWVLTAAHC-VDGDGPSDLRVVIGstdlstsgGTVV--KVARIVVHPDYD----- 113

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116126   563 aegiPEFYDYDVALVKLKnklkygqtlRPIclpcteGTTRALRLPQTATckqhkeqlLPVKDVKALFV------SEQGKS 636
Cdd:COG5640 114 ----PATPGNDIALLKLA---------TPV------PGVAPAPLATSAD--------AAAPGTPATVAgwgrtsEGPGSQ 166

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116126   637 LTRKevyikngdKKAScerdaTKAQGYEKVKDASEVVTPRFLCTGGVDPYADpnTCKGDSGGPLIVHKRSRFIQVGVISW 716
Cdd:COG5640 167 SGTL--------RKAD-----VPVVSDATCAAYGGFDGGTMLCAGYPEGGKD--ACQGDSGGPLVVKDGGGWVLVGVVSW 231


                .
gi 116126   717 G 717
Cdd:COG5640 232 G 232
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 100-155 2.16e-15

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


Pssm-ID: 153056 [Multi-domain]  Cd Length: 57  Bit Score: 70.95  E-value: 2.16e-15
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 116126   100 CPRPQDFENGEFWPRSPFYNLSDQISFQCYDGYVLRGSANRTCQENGRWDGQTAIC 155
Cdd:cd00033   1 CPPPPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTC 56
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 100-155 1.90e-14

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


Pssm-ID: 214478 [Multi-domain]  Cd Length: 56  Bit Score: 68.32  E-value: 1.90e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 116126      100 CPRPQDFENGEFWPRSPFYNLSDQISFQCYDGYVLRGSANRTCQENGRWDGQTAIC 155
Cdd:smart00032   1 CPPPPDIENGTVTSSSGTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 162-216 5.03e-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: 61.32  E-value: 5.03e-12
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 116126   162 CPNPGIPIGTRKVGSQ--YRLEDIVTYHCSRGLVLRGSQKRKCQEGGSWSGTEPSCQ 216
Cdd:cd00033   1 CPPPPVPENGTVTGSKgsYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57
PHA02927 PHA02927
secreted complement-binding protein; Provisional
 52-215 7.30e-12

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 66.60  E-value: 7.30e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116126     52 GQALEYLCPSGFYPYPVQTRTCR--STGS--WSDlqtrdqkivQKAECRAIRCPRPQDFENGEFWPRSPFYNLSDQISFQ 127
Cdd:PHA02927 105 GSSITYSCNSGYQLIGESKSYCElgSTGSmvWNP---------EAPICESVKCQSPPSISNGRHNGYEDFYTDGSVVTYS 175

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116126    128 CYDGYVLRGSANRTCQeNGRWDgQTAICDdgAGYCPNPGIPIGTRKVG--SQYRLEDIVTYHCSRGLVLRGSQKRKCQEG 205
Cdd:PHA02927 176 CNSGYSLIGNSGVLCS-GGEWS-DPPTCQ--IVKCPHPTISNGYLSSGfkRSYSYNDNVDFKCKYGYKLSGSSSSTCSPG 251

                        170
                 ....*....|
gi 116126    206 GSWSGTEPSC 215
Cdd:PHA02927 252 NTWQPELPKC 261
Sushi pfam00084
Sushi repeat (SCR repeat);
100-155 1.01e-11

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 60.59  E-value: 1.01e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 116126     100 CPRPQDFENGEFWPRSPFYNLSDQISFQCYDGYVLRGSANRTCQENGRWDGQTAIC 155
Cdd:pfam00084   1 CPPPPDIPNGKVSATKNEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 162-215 9.99e-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: 57.54  E-value: 9.99e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 116126      162 CPNPGIPIGTRKVGSQ--YRLEDIVTYHCSRGLVLRGSQKRKCQEGGSWSGTEPSC 215
Cdd:smart00032   1 CPPPPDIENGTVTSSSgtYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 222-462 4.49e-10

vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and metabolism];


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 61.11  E-value: 4.49e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116126   222 DSPQEVAEAFLSSLTETIEGADAEDGHSPGEQQKRKIVLDPSGSMNIYLVLDGSDSIGSSN-FTGAKRCLTNLIEkvaSY 300
Cdd:COG1240  49 LLLGLAGLGLLALLLAALLLLLAVLLLLLALALAPLALARPQRGRDVVLVVDASGSMAAENrLEAAKGALLDFLD---DY 125

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116126   301 GVRPRYGLLTYATVPKVLVRVSdersSDADWVTEKLNQIsyedhKLKSGTNTKRALQAVYSMMSWAGDAPpegwnrtRHV 380
Cdd:COG1240 126 RPRDRVGLVAFGGEAEVLLPLT----RDREALKRALDEL-----PPGGGTPLGDALALALELLKRADPAR-------RKV 189

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116126   381 IIIMTDGLHNMG-GNPVTVIQDIRAlLDIgrdpknpredylDVYVFGVG-PLVDSVNINALASKKDNEHhvFKVKDMEDL 458
Cdd:COG1240 190 IVLLTDGRDNAGrIDPLEAAELAAA-AGI------------RIYTIGVGtEAVDEGLLREIAEATGGRY--FRADDLSEL 254


                ....
gi 116126   459 ENVF 462
Cdd:COG1240 255 AAIY 258
Sushi pfam00084
Sushi repeat (SCR repeat);
162-215 1.05e-07

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 49.03  E-value: 1.05e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 116126     162 CPNP-----GIPIGTRkvgSQYRLEDIVTYHCSRGLVLRGSQKRKCQEGGSWSGTEPSC 215
Cdd:pfam00084   1 CPPPpdipnGKVSATK---NEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 52-80 1.49e-03

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: 37.51  E-value: 1.49e-03
                           10        20
                   ....*....|....*....|....*....
gi 116126       52 GQALEYLCPSGFYPYPVQTRTCRSTGSWS 80
Cdd:smart00032  22 GDTVTYSCDPGYTLIGSSTITCLENGTWS 50
PHA02817 PHA02817
EEV Host range protein; Provisional
 72-155 4.31e-03

EEV Host range protein; Provisional


Pssm-ID: 165167 [Multi-domain]  Cd Length: 225  Bit Score: 39.54  E-value: 4.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116126     72 TCRSTGSWSDLQTRdqkivqkaeCRAIRCPRP---QDFENGefWPRSPFYNLSDQISFQCYDGYVLRGSANRTCQENGRW 148
Cdd:PHA02817  70 ICEKDGKWNKEFPV---------CKIIRCRFPalqNGFVNG--IPDSKKFYYESEVSFSCKPGFVLIGTKYSVCGINSSW 138


                 ....*..
gi 116126    149 DGQTAIC 155
Cdd:PHA02817 139 IPKVPIC 145
 
Name Accession Description Interval E-value
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
 266-463 4.49e-112

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: 338.11  E-value: 4.49e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116126   266 MNIYLVLDGSDSIGSSNFTGAKRCLTNLIEKVASYGVRPRYGLLTYATVPKVLVRVSDERSSDADWVTEKLNQISYEDHK 345
Cdd:cd01470   1 LNIYIALDASDSIGEEDFDEAKNAIKTLIEKISSYEVSPRYEIISYASDPKEIVSIRDFNSNDADDVIKRLEDFNYDDHG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116126   346 LKSGTNTKRALQAVYSMMSWAGDAPPEGWNRTRHVIIIMTDGLHNMGGNPVTVIQDIRALLDIGRDPKNPREDYLDVYVF 425
Cdd:cd01470  81 DKTGTNTAAALKKVYERMALEKVRNKEAFNETRHVIILFTDGKSNMGGSPLPTVDKIKNLVYKNNKSDNPREDYLDVYVF 160

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 116126   426 GVGPLVDSVNINALASKKDNEHHVFKVKDMEDLENVFY 463
Cdd:cd01470 161 GVGDDVNKEELNDLASKKDNERHFFKLKDYEDLQEVFD 198
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 486-752 2.33e-44

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: 159.36  E-value: 2.33e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116126   486 DYHKQPWQAKISVTRplkGHETCMGAVVSEYFVLTAAHCFmVDDQKHSIKVSVGGQRR--------DLEIEEVLFHPKYN 557
Cdd:cd00190   8 KIGSFPWQVSLQYTG---GRHFCGGSLISPRWVLTAAHCV-YSSAPSNYTVRLGSHDLssnegggqVIKVKKVIVHPNYN 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116126   558 ingkkaegiPEFYDYDVALVKLKNKLKYGQTLRPICLPCTEGTtralrLPQTATCkqhkeqllpvkdvkalFVS-----E 632
Cdd:cd00190  84 ---------PSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYN-----LPAGTTC----------------TVSgwgrtS 133

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116126   633 QGKSLTR--KEVYIKNGDKkASCERDAtkaqgyekvkDASEVVTPRFLCTGGVDpyADPNTCKGDSGGPLIVHKRSRFIQ 710
Cdd:cd00190 134 EGGPLPDvlQEVNVPIVSN-AECKRAY----------SYGGTITDNMLCAGGLE--GGKDACQGDSGGPLVCNDNGRGVL 200

                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 116126   711 VGVISWGVvdVCRdqrrqqlVPSYARDFHiNLFQVLPWLKDK 752
Cdd:cd00190 201 VGIVSWGS--GCA-------RPNYPGVYT-RVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 486-718 3.76e-41

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: 150.14  E-value: 3.76e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116126      486 DYHKQPWQAKISVTRplkGHETCMGAVVSEYFVLTAAHCFMvDDQKHSIKVSVGGQRR-------DLEIEEVLFHPKYNi 558
Cdd:smart00020   9 NIGSFPWQVSLQYGG---GRHFCGGSLISPRWVLTAAHCVR-GSDPSNIRVRLGSHDLssgeegqVIKVSKVIIHPNYN- 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116126      559 ngkkaegiPEFYDYDVALVKLKNKLKYGQTLRPICLPCTegttrALRLPQTATCkqhkeqllpvkdvkalFVSEQGK--- 635
Cdd:smart00020  84 --------PSTYDNDIALLKLKEPVTLSDNVRPICLPSS-----NYNVPAGTTC----------------TVSGWGRtse 134

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116126      636 -----SLTRKEVYIKNGDKKAsCERDatkaqgYEKvkdaSEVVTPRFLCTGGvdPYADPNTCKGDSGGPLiVHKRSRFIQ 710
Cdd:smart00020 135 gagslPDTLQEVNVPIVSNAT-CRRA------YSG----GGAITDNMLCAGG--LEGGKDACQGDSGGPL-VCNDGRWVL 200


                   ....*...
gi 116126      711 VGVISWGV 718
Cdd:smart00020 201 VGIVSWGS 208
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 266-450 1.78e-36

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: 134.73  E-value: 1.78e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116126   266 MNIYLVLDGSDSIGSSNFTGAKRCLTNLIEKVASYGVRPRYGLLTYATVPKVLVRVSDerSSDADWVTEKLNQISYEDHk 345
Cdd:cd01450   1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLND--YKSKDDLLKAVKNLKYLGG- 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116126   346 lkSGTNTKRALQAVYSMMSWagdaPPEGWNRTRHVIIIMTDGLHNMGGNPVTVIQDIRALldigrdpknpredYLDVYVF 425
Cdd:cd01450  78 --GGTNTGKALQYALEQLFS----ESNARENVPKVIIVLTDGRSDDGGDPKEAAAKLKDE-------------GIKVFVV 138

                       170       180
                ....*....|....*....|....*
gi 116126   426 GVGPlVDSVNINALASKKdNEHHVF 450
Cdd:cd01450 139 GVGP-ADEEELREIASCP-SERHVF 161
Trypsin pfam00089
Trypsin;
488-749 7.76e-34

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 129.10  E-value: 7.76e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116126     488 HKQPWQAKISVTRplkGHETCMGAVVSEYFVLTAAHCF------MVDDQKHSIKVSVGGQRRdLEIEEVLFHPKYNingk 561
Cdd:pfam00089  10 GSFPWQVSLQLSS---GKHFCGGSLISENWVLTAAHCVsgasdvKVVLGAHNIVLREGGEQK-FDVEKIIVHPNYN---- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116126     562 kaegiPEFYDYDVALVKLKNKLKYGQTLRPICLPCTEGTtralrLPQTATCkqhkeqllpvkdvkalFVS------EQGK 635
Cdd:pfam00089  82 -----PDTLDNDIALLKLESPVTLGDTVRPICLPDASSD-----LPVGTTC----------------TVSgwgntkTLGP 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116126     636 SLTRKEVYIKNGDKkASCERDAtkaqgyekvkdaSEVVTPRFLCTGGVDPYAdpntCKGDSGGPLIVHKRsrfIQVGVIS 715
Cdd:pfam00089 136 SDTLQEVTVPVVSR-ETCRSAY------------GGTVTDTMICAGAGGKDA----CQGDSGGPLVCSDG---ELIGIVS 195

                         250       260       270
                  ....*....|....*....|....*....|....
gi 116126     716 WGvvDVCRDQRRqqlvpsyaRDFHINLFQVLPWL 749
Cdd:pfam00089 196 WG--YGCASGNY--------PGVYTPVSSYLDWI 219
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 267-450 9.76e-29

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: 112.93  E-value: 9.76e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116126      267 NIYLVLDGSDSIGSSNFTGAKRCLTNLIEKVASYGVRPRYGLLTYATVPKVLVRVSDERSSDAdwVTEKLNQISYedhKL 346
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDA--LLEALASLSY---KL 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116126      347 KSGTNTKRALQAVYSMMSwagdAPPEGWNR-TRHVIIIMTDGLHNMGGNpvtviqdirallDIGRDPKNPREDYLDVYVF 425
Cdd:smart00327  76 GGGTNLGAALQYALENLF----SKSAGSRRgAPKVVILITDGESNDGPK------------DLLKAAKELKRSGVKVFVV 139

                          170       180
                   ....*....|....*....|....*
gi 116126      426 GVGPLVDSVNINALASKKDNEHHVF 450
Cdd:smart00327 140 GVGNDVDEEELKKLASAPGGVYVFL 164
VWA pfam00092
von Willebrand factor type A domain;
267-464 2.20e-28

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 111.98  E-value: 2.20e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116126     267 NIYLVLDGSDSIGSSNFTGAKRCLTNLIEKVASYGVRPRYGLLTYATVPKVLVRVSDERSSDAdwVTEKLNQISYEDHKL 346
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEE--LLSAVDNLRYLGGGT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116126     347 KS-GTNTKRALQAVYSMMSWAGDappegwnRTRHVIIIMTDGlHNMGGNPVTVIQDIralldigrdpknpREDYLDVYVF 425
Cdd:pfam00092  79 TNtGKALKYALENLFSSAAGARP-------GAPKVVVLLTDG-RSQDGDPEEVAREL-------------KSAGVTVFAV 137

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 116126     426 GVGPlVDSVNINALASKKDNEhHVFKVKDMEDLENVFYQ 464
Cdd:pfam00092 138 GVGN-ADDEELRKIASEPGEG-HVFTVSDFEALEDLQDQ 174
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 491-717 2.62e-23

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 100.11  E-value: 2.62e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116126   491 PWQAKISVTRPLKGHeTCMGAVVSEYFVLTAAHCfMVDDQKHSIKVSVG--------GQRRdlEIEEVLFHPKYNingkk 562
Cdd:COG5640  43 PWMVALQSSNGPSGQ-FCGGTLIAPRWVLTAAHC-VDGDGPSDLRVVIGstdlstsgGTVV--KVARIVVHPDYD----- 113

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116126   563 aegiPEFYDYDVALVKLKnklkygqtlRPIclpcteGTTRALRLPQTATckqhkeqlLPVKDVKALFV------SEQGKS 636
Cdd:COG5640 114 ----PATPGNDIALLKLA---------TPV------PGVAPAPLATSAD--------AAAPGTPATVAgwgrtsEGPGSQ 166

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116126   637 LTRKevyikngdKKAScerdaTKAQGYEKVKDASEVVTPRFLCTGGVDPYADpnTCKGDSGGPLIVHKRSRFIQVGVISW 716
Cdd:COG5640 167 SGTL--------RKAD-----VPVVSDATCAAYGGFDGGTMLCAGYPEGGKD--ACQGDSGGPLVVKDGGGWVLVGVVSW 231


                .
gi 116126   717 G 717
Cdd:COG5640 232 G 232
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 267-450 1.18e-21

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: 92.24  E-value: 1.18e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116126   267 NIYLVLDGSDSIGSSNFTGAKRCLTNLIEKVASYGVRPRYGLLTYATVPKVLVRVSDerSSDADWVTEKLNQISYedhKL 346
Cdd:cd00198   2 DIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTT--DTDKADLLEAIDALKK---GL 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116126   347 KSGTNTKRALQAVYSMMSWAGDAPPegwnrtRHVIIIMTDGLHNMGGNPVTviQDIRALldigrdpknpREDYLDVYVFG 426
Cdd:cd00198  77 GGGTNIGAALRLALELLKSAKRPNA------RRVIILLTDGEPNDGPELLA--EAAREL----------RKLGITVYTIG 138

                       170       180
                ....*....|....*....|....
gi 116126   427 VGPLVDSVNINALASkKDNEHHVF 450
Cdd:cd00198 139 IGDDANEDELKEIAD-KTTGGAVF 161
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 100-155 2.16e-15

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


Pssm-ID: 153056 [Multi-domain]  Cd Length: 57  Bit Score: 70.95  E-value: 2.16e-15
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 116126   100 CPRPQDFENGEFWPRSPFYNLSDQISFQCYDGYVLRGSANRTCQENGRWDGQTAIC 155
Cdd:cd00033   1 CPPPPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTC 56
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 100-155 1.90e-14

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


Pssm-ID: 214478 [Multi-domain]  Cd Length: 56  Bit Score: 68.32  E-value: 1.90e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 116126      100 CPRPQDFENGEFWPRSPFYNLSDQISFQCYDGYVLRGSANRTCQENGRWDGQTAIC 155
Cdd:smart00032   1 CPPPPDIENGTVTSSSGTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 162-216 5.03e-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: 61.32  E-value: 5.03e-12
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 116126   162 CPNPGIPIGTRKVGSQ--YRLEDIVTYHCSRGLVLRGSQKRKCQEGGSWSGTEPSCQ 216
Cdd:cd00033   1 CPPPPVPENGTVTGSKgsYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57
PHA02927 PHA02927
secreted complement-binding protein; Provisional
 52-215 7.30e-12

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 66.60  E-value: 7.30e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116126     52 GQALEYLCPSGFYPYPVQTRTCR--STGS--WSDlqtrdqkivQKAECRAIRCPRPQDFENGEFWPRSPFYNLSDQISFQ 127
Cdd:PHA02927 105 GSSITYSCNSGYQLIGESKSYCElgSTGSmvWNP---------EAPICESVKCQSPPSISNGRHNGYEDFYTDGSVVTYS 175

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116126    128 CYDGYVLRGSANRTCQeNGRWDgQTAICDdgAGYCPNPGIPIGTRKVG--SQYRLEDIVTYHCSRGLVLRGSQKRKCQEG 205
Cdd:PHA02927 176 CNSGYSLIGNSGVLCS-GGEWS-DPPTCQ--IVKCPHPTISNGYLSSGfkRSYSYNDNVDFKCKYGYKLSGSSSSTCSPG 251

                        170
                 ....*....|
gi 116126    206 GSWSGTEPSC 215
Cdd:PHA02927 252 NTWQPELPKC 261
Sushi pfam00084
Sushi repeat (SCR repeat);
100-155 1.01e-11

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 60.59  E-value: 1.01e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 116126     100 CPRPQDFENGEFWPRSPFYNLSDQISFQCYDGYVLRGSANRTCQENGRWDGQTAIC 155
Cdd:pfam00084   1 CPPPPDIPNGKVSATKNEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
PHA02927 PHA02927
secreted complement-binding protein; Provisional
 52-216 9.58e-11

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 63.13  E-value: 9.58e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116126     52 GQALEYLCPSGFYPYPVQTRTCRSTGS-WSDLQtrdqkivqkaECRAIRCPRPQDFENGEFwpRSPFYNLSDQISFQCYD 130
Cdd:PHA02927  47 GDTIEYLCLPGYRKQKMGPIYAKCTGTgWTLFN----------QCIKRRCPSPRDIDNGQL--DIGGVDFGSSITYSCNS 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116126    131 GYVLRGSANRTCQENGR----WDGQTAICDdgAGYCPNPGIPIGTRKVGSQ--YRLEDIVTYHCSRGLVLRGSQKRKCQe 204
Cdd:PHA02927 115 GYQLIGESKSYCELGSTgsmvWNPEAPICE--SVKCQSPPSISNGRHNGYEdfYTDGSVVTYSCNSGYSLIGNSGVLCS- 191

                        170
                 ....*....|..
gi 116126    205 GGSWSgTEPSCQ 216
Cdd:PHA02927 192 GGEWS-DPPTCQ 202
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 162-215 9.99e-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: 57.54  E-value: 9.99e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 116126      162 CPNPGIPIGTRKVGSQ--YRLEDIVTYHCSRGLVLRGSQKRKCQEGGSWSGTEPSC 215
Cdd:smart00032   1 CPPPPDIENGTVTSSSgtYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 222-462 4.49e-10

vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and metabolism];


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 61.11  E-value: 4.49e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116126   222 DSPQEVAEAFLSSLTETIEGADAEDGHSPGEQQKRKIVLDPSGSMNIYLVLDGSDSIGSSN-FTGAKRCLTNLIEkvaSY 300
Cdd:COG1240  49 LLLGLAGLGLLALLLAALLLLLAVLLLLLALALAPLALARPQRGRDVVLVVDASGSMAAENrLEAAKGALLDFLD---DY 125

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116126   301 GVRPRYGLLTYATVPKVLVRVSdersSDADWVTEKLNQIsyedhKLKSGTNTKRALQAVYSMMSWAGDAPpegwnrtRHV 380
Cdd:COG1240 126 RPRDRVGLVAFGGEAEVLLPLT----RDREALKRALDEL-----PPGGGTPLGDALALALELLKRADPAR-------RKV 189

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116126   381 IIIMTDGLHNMG-GNPVTVIQDIRAlLDIgrdpknpredylDVYVFGVG-PLVDSVNINALASKKDNEHhvFKVKDMEDL 458
Cdd:COG1240 190 IVLLTDGRDNAGrIDPLEAAELAAA-AGI------------RIYTIGVGtEAVDEGLLREIAEATGGRY--FRADDLSEL 254


                ....
gi 116126   459 ENVF 462
Cdd:COG1240 255 AAIY 258
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 266-458 1.29e-09

Integrins are a class of adhesion receptors that link the extracellular matrix to the cytoskeleton and cooperate with growth factor receptors to promote celll survival, cell cycle progression and cell migration. Integrins consist of an alpha and a beta sub-unit. Each sub-unit has a large extracellular portion, a single transmembrane segment and a short cytoplasmic domain. The N-terminal domains of the alpha and beta subunits associate to form the integrin headpiece, which contains the ligand binding site, whereas the C-terminal segments traverse the plasma membrane and mediate interaction with the cytoskeleton and with signalling proteins.The VWA domains present in the alpha subunits of integrins seem to be a chordate specific radiation of the gene family being found only in vertebrates. They mediate protein-protein interactions.


Pssm-ID: 238746 [Multi-domain]  Cd Length: 177  Bit Score: 58.14  E-value: 1.29e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116126   266 MNIYLVLDGSDSIGSSNFTGAKRCLTNLIEKVASYGVRPRYGLLTYATVPKVLVRVSDERSSDAdwVTEKLNQIsyedHK 345
Cdd:cd01469   1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEE--PLSLVKHI----SQ 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116126   346 LKSGTNTKRALQ-AVYSMMSWAGDAPPEgwnrTRHVIIIMTDGLHNMGGNPVTVIQDIRAlLDIGRdpknpredyldvYV 424
Cdd:cd01469  75 LLGLTNTATAIQyVVTELFSESNGARKD----ATKVLVVITDGESHDDPLLKDVIPQAER-EGIIR------------YA 137

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 116126   425 FGVGPLVDSVN----INALASKKDnEHHVFKVKDMEDL 458
Cdd:cd01469 138 IGVGGHFQRENsreeLKTIASKPP-EEHFFNVTDFAAL 174
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 266-433 3.21e-08

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


Pssm-ID: 238748 [Multi-domain]  Cd Length: 186  Bit Score: 54.31  E-value: 3.21e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116126   266 MNIYLVLDGSDSIGSSN-FTGAKRCLTNLIEKVASYGVRPRYGLLTYATVPKVLVRVSDERSSDAD---WVTEKLNQISY 341
Cdd:cd01471   1 LDLYLLVDGSGSIGYSNwVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSPNSTNKDlalNAIRALLSLYY 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116126   342 EdhklKSGTNTKRALQAVYSMM-SWAG---DAPpegwnrtrHVIIIMTDGLHNmggNPVTVIQDIRALldigrdpknpRE 417
Cdd:cd01471  81 P----NGSTNTTSALLVVEKHLfDTRGnreNAP--------QLVIIMTDGIPD---SKFRTLKEARKL----------RE 135

                       170
                ....*....|....*.
gi 116126   418 DYLDVYVFGVGPLVDS 433
Cdd:cd01471 136 RGVIIAVLGVGQGVNH 151
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 267-455 6.09e-08

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


Pssm-ID: 238749 [Multi-domain]  Cd Length: 164  Bit Score: 53.00  E-value: 6.09e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116126   267 NIYLVLDGSDSIGSSNFTGAKrcltNLIEKVA-SYGVRP---RYGLLTYATVPKVlVRVSDERSSDADwVTEKLNQISYe 342
Cdd:cd01472   2 DIVFLVDGSESIGLSNFNLVK----DFVKRVVeRLDIGPdgvRVGVVQYSDDPRT-EFYLNTYRSKDD-VLEAVKNLRY- 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116126   343 dhkLKSGTNTKRALQAVYSMMSWAGDAPPEGWNRtrhVIIIMTDglhnmGGNPVTVIQDIRALLDIGrdpknpredyldV 422
Cdd:cd01472  75 ---IGGGTNTGKALKYVRENLFTEASGSREGVPK---VLVVITD-----GKSQDDVEEPAVELKQAG------------I 131

                       170       180       190
                ....*....|....*....|....*....|....
gi 116126   423 YVFGVGPL-VDSVNINALASkKDNEHHVFKVKDM 455
Cdd:cd01472 132 EVFAVGVKnADEEELKQIAS-DPKELYVFNVADF 164
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 258-469 6.22e-08

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 54.72  E-value: 6.22e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116126   258 IVLDPSGSMNiylvldgSDSIgssnfTGAKRCLTNLIEKvasygVRP--RYGLLTYATVPKVLV---RVSDERSsdadwV 332
Cdd:COG2304  96 FVIDVSGSMS-------GDKL-----ELAKEAAKLLVDQ-----LRPgdRVSIVTFAGDARVLLpptPATDRAK-----I 153

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116126   333 TEKLNQIsyedhKLKSGTNTKRALQAVYSMmswAGDAPPEGWNRtrhVIIIMTDGLHNMGgnpVTVIQDIRALLDIGRDP 412
Cdd:COG2304 154 LAAIDRL-----QAGGGTALGAGLELAYEL---ARKHFIPGRVN---RVILLTDGDANVG---ITDPEELLKLAEEAREE 219

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 116126   413 KNPredyldVYVFGVGPLVDSVNINALASKKDNEHHVfkVKDMEDLENVFYQMIDET 469
Cdd:COG2304 220 GIT------LTTLGVGSDYNEDLLERLADAGGGNYYY--IDDPEEAEKVFVREFSRI 268
PHA02817 PHA02817
EEV Host range protein; Provisional
 95-215 6.41e-08

EEV Host range protein; Provisional


Pssm-ID: 165167 [Multi-domain]  Cd Length: 225  Bit Score: 54.18  E-value: 6.41e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116126     95 CRAIRCPRPQDFENGEFWPRSPFYNLSDQISFQCYDG-----YVLRGSANRTCQENGRWDGQTAICDdgAGYCPNP---- 165
Cdd:PHA02817  19 CDLNKCCYPPSIKNGYIYNKKTEYNIGSNVTFFCGNNtrgvrYTLVGEKNIICEKDGKWNKEFPVCK--IIRCRFPalqn 96

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 116126    166 ----GIPigtrkVGSQYRLEDIVTYHCSRGLVLRGSQKRKCQEGGSWSGTEPSC 215
Cdd:PHA02817  97 gfvnGIP-----DSKKFYYESEVSFSCKPGFVLIGTKYSVCGINSSWIPKVPIC 145
Sushi pfam00084
Sushi repeat (SCR repeat);
162-215 1.05e-07

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 49.03  E-value: 1.05e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 116126     162 CPNP-----GIPIGTRkvgSQYRLEDIVTYHCSRGLVLRGSQKRKCQEGGSWSGTEPSC 215
Cdd:pfam00084   1 CPPPpdipnGKVSATK---NEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 264-387 1.15e-07

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


Pssm-ID: 238757 [Multi-domain]  Cd Length: 186  Bit Score: 52.39  E-value: 1.15e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116126   264 GSMNIYLVLDGSDSIGSSNFTGAKRCLTNLIEKVASYGVRP------RYGLLTYATVPKVlVRVSDERSSDADWVTEKLN 337
Cdd:cd01480   1 GPVDITFVLDSSESVGLQNFDITKNFVKRVAERFLKDYYRKdpagswRVGVVQYSDQQEV-EAGFLRDIRNYTSLKEAVD 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 116126   338 QISYedhkLKSGTNTKRALQAVYSMMSwagDAPPEGWNRtrhVIIIMTDG 387
Cdd:cd01480  80 NLEY----IGGGTFTDCALKYATEQLL---EGSHQKENK---FLLVITDG 119
PHA02639 PHA02639
EEV host range protein; Provisional
 52-215 1.20e-05

EEV host range protein; Provisional


Pssm-ID: 165022 [Multi-domain]  Cd Length: 295  Bit Score: 47.74  E-value: 1.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116126     52 GQALEYLCPSGFYPYPVQTRTC---RSTGSWSDlqtrdqkivQKAECRAIRCPRPQDFENGEFWPRSPFYNLSDQISFQC 128
Cdd:PHA02639  43 GKLIEYTCNTDYALIGDRFRTCikdKNNAIWSN---------KAPFCMLKECNDPPSIINGKIYNKREMYKVGDEIYYVC 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116126    129 YD----GYVLRGSANRTCQENGRWDGQTAICDdgAGYCPNPGIP---IGTRKVGSQYRLEDIVTYHCSRGLVLRGSQKRK 201
Cdd:PHA02639 114 NEhkgvQYSLVGNEKITCIQDKSWKPDPPICK--MINCRFPALQngyINGIPSNKKFYYKTRVGFSCKSGFDLVGEKYST 191

                        170
                 ....*....|....
gi 116126    202 CQEGGSWSGTEPSC 215
Cdd:PHA02639 192 CNINATWFPSIPTC 205
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 264-476 2.15e-05

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


Pssm-ID: 238752 [Multi-domain]  Cd Length: 224  Bit Score: 46.22  E-value: 2.15e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116126   264 GSMNIYLVLDGSDSIGSSNFTGAKRCLTNLIEKVAsygVRP---RYGLLTYATvpKVLVRVSDERSSDADWVTEKLNQIS 340
Cdd:cd01475   1 GPTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLD---VGPdatRVGLVQYSS--TVKQEFPLGRFKSKADLKRAVRRME 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116126   341 YedhkLKSGTNTKRALQ-AVYSMMSWAGDAPPEGWNRTRhVIIIMTDGlhnmggnpvtviqdiRALLDIGRDPKNPREDY 419
Cdd:cd01475  76 Y----LETGTMTGLAIQyAMNNAFSEAEGARPGSERVPR-VGIVVTDG---------------RPQDDVSEVAAKARALG 135

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 116126   420 LDVYVFGVGPlVDSVNINALASKKDNEhHVFKVKD---MEDLENVFYQMIDETKSLSLCG 476
Cdd:cd01475 136 IEMFAVGVGR-ADEEELREIASEPLAD-HVFYVEDfstIEELTKKFQGKICVVPDLCATL 193
PHA02831 PHA02831
EEV host range protein; Provisional
 53-215 2.66e-05

EEV host range protein; Provisional


Pssm-ID: 165176 [Multi-domain]  Cd Length: 268  Bit Score: 46.52  E-value: 2.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116126     53 QALEYLCPSGFYPYPVqtrTCrSTGSWSdlqTRDQKIVQKaecraiRCPRPQDFENGEFWPRSPFYNLSDQISFQC---- 128
Cdd:PHA02831  44 ENLEYKCNNNFDKVFV---TC-NNGSWS---TKNMCIGKR------NCKDPVTILNGYIKNKKDQYSFGDSVTYACkvnk 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116126    129 YDGYVLRGSANRTCQeNGRWDGQTAICDdgAGYCPNPGIPIGTRKV-GSQYRLEDIVTYHCSRGLVLRGSQKRKCQEGGS 207
Cdd:PHA02831 111 LEKYSIVGNETVKCI-NKQWVPKYPVCK--LIRCKYPALQNGFLNVfEKKFYYGDIVNFKCKKGFILLGSSVSTCDINSI 187


                 ....*...
gi 116126    208 WSGTEPSC 215
Cdd:PHA02831 188 WYPGIPKC 195
VWA_2 pfam13519
von Willebrand factor type A domain;
258-383 3.13e-05

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 43.43  E-value: 3.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116126     258 IVLDPSGSMniylvldGSDSIGSSNFTGAKRCLTNLIEKvasygvRP--RYGLLTYATVPKVLVRVSDerssDADWVTEK 335
Cdd:pfam13519   3 FVLDTSGSM-------RNGDYGPTRLEAAKDAVLALLKS------LPgdRVGLVTFGDGPEVLIPLTK----DRAKILRA 65

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 116126     336 LNQISYEDhklkSGTNTKRALQAVYSMMswagdapPEGWNRTRHVIII 383
Cdd:pfam13519  66 LRRLEPKG----GGTNLAAALQLARAAL-------KHRRKNQPRRIVL 102
PHA02639 PHA02639
EEV host range protein; Provisional
 96-216 2.16e-04

EEV host range protein; Provisional


Pssm-ID: 165022 [Multi-domain]  Cd Length: 295  Bit Score: 43.88  E-value: 2.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116126     96 RAIRCPRPQDFENGEFWPRSPFYNLSDQISFQCYDGYVLRGSANRTC---QENGRWDGQTAICddGAGYCPNPGIPIGTR 172
Cdd:PHA02639  18 KSIYCDKPDDISNGFITELMEKYEIGKLIEYTCNTDYALIGDRFRTCikdKNNAIWSNKAPFC--MLKECNDPPSIINGK 95

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 116126    173 KVGSQ--YRLEDIVTYHCS--RGL--VLRGSQKRKCQEGGSWSGTEPSCQ 216
Cdd:PHA02639  96 IYNKRemYKVGDEIYYVCNehKGVqySLVGNEKITCIQDKSWKPDPPICK 145
vWA_BatA_type cd01467
VWA BatA type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 258-400 2.82e-04

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


Pssm-ID: 238744 [Multi-domain]  Cd Length: 180  Bit Score: 42.32  E-value: 2.82e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116126   258 IVLDPSGSMNIylvldgSDSIGSSNFTGAKRCLTNLIEKvasygvRP--RYGLLTYATVPKVLVRVSDERSSdadwVTEK 335
Cdd:cd01467   7 IALDVSGSMLA------QDFVKPSRLEAAKEVLSDFIDR------REndRIGLVVFAGAAFTQAPLTLDRES----LKEL 70

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 116126   336 LNQISYEDhkLKSGTntkrALqavysmmswaGDAPPEGWNRTRH------VIIIMTDGLHNMGG-NPVTVIQ 400
Cdd:cd01467  71 LEDIKIGL--AGQGT----AI----------GDAIGLAIKRLKNseakerVIVLLTDGENNAGEiDPATAAE 126
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
 508-721 4.69e-04

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 41.97  E-value: 4.69e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116126   508 CMGAVVSEYFVLTAAHCFMVDDQKH---SIKVSVGGQRRD---LEIEEVLFHPKYNINGKkaegipefYDYDVALVKLKN 581
Cdd:COG3591  14 CTGTLIGPNLVLTAGHCVYDGAGGGwatNIVFVPGYNGGPygtATATRFRVPPGWVASGD--------AGYDYALLRLDE 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116126   582 KLkygqtlrpiclpctEGTTRALRLPQTAtckqhkeqlLPVKDVKALFVSeqgksltrkevYIKNGDKKASCERDATkaq 661
Cdd:COG3591  86 PL--------------GDTTGWLGLAFND---------APLAGEPVTIIG-----------YPGDRPKDLSLDCSGR--- 128

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 116126   662 gyekVKDasevVTPRFLctggvdpYADPNTCKGDSGGPLIVHKRSRFIQVGVISWGVVDV 721
Cdd:COG3591 129 ----VTG----VQGNRL-------SYDCDTTGGSSGSPVLDDSDGGGRVVGVHSAGGADR 173
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 268-454 5.94e-04

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


Pssm-ID: 238759 [Multi-domain]  Cd Length: 164  Bit Score: 41.12  E-value: 5.94e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116126   268 IYLVLDGSDSIGSSNFTGAKRCLTNLIEKVASYGVRPRYGLLTYATVPKVLVRVSdeRSSDADWVTEKLNQISYedhklK 347
Cdd:cd01482   3 IVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLN--AYTSKEDVLAAIKNLPY-----K 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116126   348 SG-TNTKRALQAVY-SMMSWAGDAPPEgwnrTRHVIIIMTDGLHnmggnpvtviQDirallDIGRDPKNPREDYLDVYVF 425
Cdd:cd01482  76 GGnTRTGKALTHVReKNFTPDAGARPG----VPKVVILITDGKS----------QD-----DVELPARVLRNLGVNVFAV 136

                       170       180
                ....*....|....*....|....*....
gi 116126   426 GVGPlVDSVNINALASKKDnEHHVFKVKD 454
Cdd:cd01482 137 GVKD-ADESELKMIASKPS-ETHVFNVAD 163
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 52-80 1.49e-03

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: 37.51  E-value: 1.49e-03
                           10        20
                   ....*....|....*....|....*....
gi 116126       52 GQALEYLCPSGFYPYPVQTRTCRSTGSWS 80
Cdd:smart00032  22 GDTVTYSCDPGYTLIGSSTITCLENGTWS 50
PHA02954 PHA02954
EEV membrane glycoprotein; Provisional
 78-215 3.49e-03

EEV membrane glycoprotein; Provisional


Pssm-ID: 165263 [Multi-domain]  Cd Length: 317  Bit Score: 40.45  E-value: 3.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116126     78 SWSDLQTrdqkiVQKAECRaircprPQDFENGEFWPRSPFYNLSDQISFQCYDGYVLRGSANRTCQENGrWDgqtaICDD 157
Cdd:PHA02954 118 SWNDTVT-----CPNAECQ------PLQLEHGSCQPVKEKYSFGEHITINCDVGYEVIGASYISCTANS-WN----VIPS 181

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 116126    158 GAGYCPNPGIPIGTRKvGSQYRLEDIVTYHCSRGLVLRGSQKRKCQEgGSWSGTEPSC 215
Cdd:PHA02954 182 CQQKCDIPSLSNGLIS-GSTFSIGGVIHLSCKSGFTLTGSPSSTCID-GKWNPVLPIC 237
PHA02817 PHA02817
EEV Host range protein; Provisional
 72-155 4.31e-03

EEV Host range protein; Provisional


Pssm-ID: 165167 [Multi-domain]  Cd Length: 225  Bit Score: 39.54  E-value: 4.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116126     72 TCRSTGSWSDLQTRdqkivqkaeCRAIRCPRP---QDFENGefWPRSPFYNLSDQISFQCYDGYVLRGSANRTCQENGRW 148
Cdd:PHA02817  70 ICEKDGKWNKEFPV---------CKIIRCRFPalqNGFVNG--IPDSKKFYYESEVSFSCKPGFVLIGTKYSVCGINSSW 138


                 ....*..
gi 116126    149 DGQTAIC 155
Cdd:PHA02817 139 IPKVPIC 145
 
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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