NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|71051532|gb|AAH36192|]
View 

COL14A1 protein [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 157-320 2.44e-88

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: 268.77  E-value: 2.44e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71051532 157 ADIVILVDGSWSIGRFNFRLVRHFLENLVTAFDVGSEKTRIGLAQYSGDPRIEWHLNAFSTKDEVIEAVRNLPYKGGNTL 236
Cdd:cd01482   1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71051532 237 TGLALNYIFENSFKPEAGSRTGVSKIGILITDGKSQDDIIPPSRNLRESGVELFAIGVKNADVNELQEIASEPDSTHVYN 316
Cdd:cd01482  81 TGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETHVFN 160


                ....
gi 71051532 317 VAEF 320
Cdd:cd01482 161 VADF 164
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 32-112 4.60e-13

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 64.83  E-value: 4.60e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71051532  32 PPTRLRYNVISHDSIQISWKAPRGKFG---GYKLLVTPTSGGKTNQLNLQN-TATKAIIQGLMPDQNYTVQIIAYNKDKE 107
Cdd:cd00063   3 PPTNLRVTDVTSTSVTLSWTPPEDDGGpitGYVVEYREKGSGDWKEVEVTPgSETSYTLTGLKPGTEYEFRVRAVNGGGE 82


                ....*
gi 71051532 108 SKPAQ 112
Cdd:cd00063  83 SPPSE 87
fn3 pfam00041
Fibronectin type III domain;
354-432 2.71e-11

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 59.74  E-value: 2.71e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71051532   354 GPPTELITSEVTARSFMVNWTHAP---GNVEKYRVVYYPTRGGKPD-EVVVDGTVSSTVLKNLMSLTEYQIAVFAIYAHT 429
Cdd:pfam00041   1 SAPSNLTVTDVTSTSLTVSWTPPPdgnGPITGYEVEYRPKNSGEPWnEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                  ...
gi 71051532   430 ASE 432
Cdd:pfam00041  81 EGP 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 447-516 1.06e-09

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


:

Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 55.31  E-value: 1.06e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71051532    447 SDLLLYDVTENSMRVKWDAV--PGASGYLILYAPLTEGLAGDEKEMKIGETHTDIELSGLLPNTEYTVTVYA 516
Cdd:smart00060   5 SNLRVTDVTSTSVTLSWEPPpdDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRA 76
 
Name Accession Description Interval E-value
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 157-320 2.44e-88

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: 268.77  E-value: 2.44e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71051532 157 ADIVILVDGSWSIGRFNFRLVRHFLENLVTAFDVGSEKTRIGLAQYSGDPRIEWHLNAFSTKDEVIEAVRNLPYKGGNTL 236
Cdd:cd01482   1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71051532 237 TGLALNYIFENSFKPEAGSRTGVSKIGILITDGKSQDDIIPPSRNLRESGVELFAIGVKNADVNELQEIASEPDSTHVYN 316
Cdd:cd01482  81 TGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETHVFN 160


                ....
gi 71051532 317 VAEF 320
Cdd:cd01482 161 VADF 164
VWA pfam00092
von Willebrand factor type A domain;
158-328 1.02e-69

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 220.99  E-value: 1.02e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71051532   158 DIVILVDGSWSIGRFNFRLVRHFLENLVTAFDVGSEKTRIGLAQYSGDPRIEWHLNAFSTKDEVIEAVRNLPYKGGNTL- 236
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTn 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71051532   237 TGLALNYIFENSFKPEAGSRTGVSKIGILITDGKSQD-DIIPPSRNLRESGVELFAIGVKNADVNELQEIASEPDSTHVY 315
Cdd:pfam00092  81 TGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEGHVF 160

                         170
                  ....*....|...
gi 71051532   316 NVAEFDLMHTVVE 328
Cdd:pfam00092 161 TVSDFEALEDLQD 173
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 158-323 3.85e-52

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: 175.34  E-value: 3.85e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71051532    158 DIVILVDGSWSIGRFNFRLVRHFLENLVTAFDVGSEKTRIGLAQYSGDPRIEWHLNAFSTKDEVIEAVRNLPYK-GGNTL 236
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKlGGGTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71051532    237 TGLALNYIFENSFKPEAGSRTGVSKIGILITDGKSQD---DIIPPSRNLRESGVELFAIGVKNA-DVNELQEIASEPDST 312
Cdd:smart00327  81 LGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVGNDvDEEELKKLASAPGGV 160

                          170
                   ....*....|.
gi 71051532    313 HVYNVAEFDLM 323
Cdd:smart00327 161 YVFLPELLDLL 171
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 32-112 4.60e-13

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 64.83  E-value: 4.60e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71051532  32 PPTRLRYNVISHDSIQISWKAPRGKFG---GYKLLVTPTSGGKTNQLNLQN-TATKAIIQGLMPDQNYTVQIIAYNKDKE 107
Cdd:cd00063   3 PPTNLRVTDVTSTSVTLSWTPPEDDGGpitGYVVEYREKGSGDWKEVEVTPgSETSYTLTGLKPGTEYEFRVRAVNGGGE 82


                ....*
gi 71051532 108 SKPAQ 112
Cdd:cd00063  83 SPPSE 87
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 157-308 2.26e-12

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


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 67.27  E-value: 2.26e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71051532 157 ADIVILVDGSWSIGRFN-FRLVRHFLENLVTAFDvgsEKTRIGLAQYSGdpRIEWHLNAFSTKDEVIEAVRNLPYKGGnT 235
Cdd:COG1240  93 RDVVLVVDASGSMAAENrLEAAKGALLDFLDDYR---PRDRVGLVAFGG--EAEVLLPLTRDREALKRALDELPPGGG-T 166

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71051532 236 LTGLALNYIFEnSFKPEAGSRtgvSKIGILITDGKSQDDIIPP---SRNLRESGVELFAIGVKNADVNE--LQEIASE 308
Cdd:COG1240 167 PLGDALALALE-LLKRADPAR---RKVIVLLTDGRDNAGRIDPleaAELAAAAGIRIYTIGVGTEAVDEglLREIAEA 240
fn3 pfam00041
Fibronectin type III domain;
32-110 1.32e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 60.51  E-value: 1.32e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71051532    32 PPTRLRYNVISHDSIQISWKAPR---GKFGGYKLLVTPT-SGGKTNQLNLQNTATKAIIQGLMPDQNYTVQIIAYNKDKE 107
Cdd:pfam00041   2 APSNLTVTDVTSTSLTVSWTPPPdgnGPITGYEVEYRPKnSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGE 81


                  ...
gi 71051532   108 SKP 110
Cdd:pfam00041  82 GPP 84
fn3 pfam00041
Fibronectin type III domain;
354-432 2.71e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 59.74  E-value: 2.71e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71051532   354 GPPTELITSEVTARSFMVNWTHAP---GNVEKYRVVYYPTRGGKPD-EVVVDGTVSSTVLKNLMSLTEYQIAVFAIYAHT 429
Cdd:pfam00041   1 SAPSNLTVTDVTSTSLTVSWTPPPdgnGPITGYEVEYRPKNSGEPWnEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                  ...
gi 71051532   430 ASE 432
Cdd:pfam00041  81 EGP 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 354-432 4.35e-10

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 56.35  E-value: 4.35e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71051532 354 GPPTELITSEVTARSFMVNWTHAP---GNVEKYRVVYYPTRGGKPDEV-VVDGTVSSTVLKNLMSLTEYQIAVFAIYAHT 429
Cdd:cd00063   2 SPPTNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYREKGSGDWKEVeVTPGSETSYTLTGLKPGTEYEFRVRAVNGGG 81


                ...
gi 71051532 430 ASE 432
Cdd:cd00063  82 ESP 84
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 447-516 1.06e-09

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 55.31  E-value: 1.06e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71051532    447 SDLLLYDVTENSMRVKWDAV--PGASGYLILYAPLTEGLAGDEKEMKIGETHTDIELSGLLPNTEYTVTVYA 516
Cdd:smart00060   5 SNLRVTDVTSTSVTLSWEPPpdDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRA 76
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 32-108 2.52e-09

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 54.16  E-value: 2.52e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71051532     32 PPTRLRYNVISHDSIQISWKAP-RGKFGGYKL---LVTPTSGGKTNQLNLQNTATKAIIQGLMPDQNYTVQIIAYNKDKE 107
Cdd:smart00060   3 PPSNLRVTDVTSTSVTLSWEPPpDDGITGYIVgyrVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAGE 82


                   .
gi 71051532    108 S 108
Cdd:smart00060  83 G 83
fn3 pfam00041
Fibronectin type III domain;
447-516 4.55e-09

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 53.19  E-value: 4.55e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71051532   447 SDLLLYDVTENSMRVKWDAVPGASG----YLILYAPLTEGlaGDEKEMKIGETHTDIELSGLLPNTEYTVTVYA 516
Cdd:pfam00041   4 SNLTVTDVTSTSLTVSWTPPPDGNGpitgYEVEYRPKNSG--EPWNEITVPGTTTSVTLTGLKPGTEYEVRVQA 75
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 447-532 2.64e-08

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 51.34  E-value: 2.64e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71051532 447 SDLLLYDVTENSMRVKWDAVPGA----SGYLILYAPLTEGlaGDEKEMKIGETHTDIELSGLLPNTEYTVTVYAMFGEEA 522
Cdd:cd00063   5 TNLRVTDVTSTSVTLSWTPPEDDggpiTGYVVEYREKGSG--DWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGGE 82

                        90
                ....*....|
gi 71051532 523 SDPVTGQETT 532
Cdd:cd00063  83 SPPSESVTVT 92
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 354-431 4.21e-08

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 50.69  E-value: 4.21e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71051532    354 GPPTELITSEVTARSFMVNWTH-APGNVEKYRVVYYPTRGGKPD---EVVVDGTVSSTVLKNLMSLTEYQIAVFAIYAHT 429
Cdd:smart00060   2 SPPSNLRVTDVTSTSVTLSWEPpPDDGITGYIVGYRVEYREEGSewkEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAG 81


                   ..
gi 71051532    430 AS 431
Cdd:smart00060  82 EG 83
PRK12279 PRK12279
50S ribosomal protein L22/unknown domain fusion protein; Provisional
 65-148 3.88e-04

50S ribosomal protein L22/unknown domain fusion protein; Provisional


Pssm-ID: 138835 [Multi-domain]  Cd Length: 311  Bit Score: 42.75  E-value: 3.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71051532   65 TPTSGGKTNQLNLQNTATKAIIQGLMPDQNYTVQIIAYNKDKESKPAQgqfRIKDLEKRKDPKPRVKVVDRGNGSRPSSP 144
Cdd:PRK12279  87 LPRAKGSADQLFKRTTHLEIVLSDDVNEREKELAAIKAKKSKKPLPVE---PKAKVETKKVAKPSKVEVKPVEKDENVDP 163


                 ....
gi 71051532  145 EEVK 148
Cdd:PRK12279 164 ELLK 167
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
31-112 4.22e-04

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 43.07  E-value: 4.22e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71051532  31 APPTRLRYNVISHDSIQISWKAPRGK-FGGYKLLVTPTSGGKTNQLNLQNTATKAIIQGLMPDQNYTVQIIAYNKD-KES 108
Cdd:COG3401 328 AAPSGLTATAVGSSSITLSWTASSDAdVTGYNVYRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAgNES 407


                ....
gi 71051532 109 KPAQ 112
Cdd:COG3401 408 APSE 411
 
Name Accession Description Interval E-value
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 157-320 2.44e-88

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: 268.77  E-value: 2.44e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71051532 157 ADIVILVDGSWSIGRFNFRLVRHFLENLVTAFDVGSEKTRIGLAQYSGDPRIEWHLNAFSTKDEVIEAVRNLPYKGGNTL 236
Cdd:cd01482   1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71051532 237 TGLALNYIFENSFKPEAGSRTGVSKIGILITDGKSQDDIIPPSRNLRESGVELFAIGVKNADVNELQEIASEPDSTHVYN 316
Cdd:cd01482  81 TGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETHVFN 160


                ....
gi 71051532 317 VAEF 320
Cdd:cd01482 161 VADF 164
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 157-320 1.93e-79

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: 245.99  E-value: 1.93e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71051532 157 ADIVILVDGSWSIGRFNFRLVRHFLENLVTAFDVGSEKTRIGLAQYSGDPRIEWHLNAFSTKDEVIEAVRNLPYKGGNTL 236
Cdd:cd01472   1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71051532 237 TGLALNYIFENSFKPEAGSRTGVSKIGILITDGKSQDDIIPPSRNLRESGVELFAIGVKNADVNELQEIASEPDSTHVYN 316
Cdd:cd01472  81 TGKALKYVRENLFTEASGSREGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDPKELYVFN 160


                ....
gi 71051532 317 VAEF 320
Cdd:cd01472 161 VADF 164
VWA pfam00092
von Willebrand factor type A domain;
158-328 1.02e-69

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 220.99  E-value: 1.02e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71051532   158 DIVILVDGSWSIGRFNFRLVRHFLENLVTAFDVGSEKTRIGLAQYSGDPRIEWHLNAFSTKDEVIEAVRNLPYKGGNTL- 236
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTn 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71051532   237 TGLALNYIFENSFKPEAGSRTGVSKIGILITDGKSQD-DIIPPSRNLRESGVELFAIGVKNADVNELQEIASEPDSTHVY 315
Cdd:pfam00092  81 TGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEGHVF 160

                         170
                  ....*....|...
gi 71051532   316 NVAEFDLMHTVVE 328
Cdd:pfam00092 161 TVSDFEALEDLQD 173
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 157-315 3.21e-55

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: 182.88  E-value: 3.21e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71051532 157 ADIVILVDGSWSIGRFNFRLVRHFLENLVTAFDVGSEKTRIGLAQYSGDPRIEWHLNAFSTKDEVIEAVRNLPYKGGN-T 235
Cdd:cd01450   1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGgT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71051532 236 LTGLALNYIFENSFKPeAGSRTGVSKIGILITDGKSQD--DIIPPSRNLRESGVELFAIGVKNADVNELQEIASEPDSTH 313
Cdd:cd01450  81 NTGKALQYALEQLFSE-SNARENVPKVIIVLTDGRSDDggDPKEAAAKLKDEGIKVFVVGVGPADEEELREIASCPSERH 159


                ..
gi 71051532 314 VY 315
Cdd:cd01450 160 VF 161
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 157-360 1.02e-54

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: 183.74  E-value: 1.02e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71051532 157 ADIVILVDGSWSIGRFNFRLVRHFLENLVTAFDVGSEKTRIGLAQYSGDPRIEWHLNAFSTKDEVIEAVRNLPYKGGNTL 236
Cdd:cd01475   3 TDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETGTM 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71051532 237 TGLALNYIFENSFKPEAGSRTG---VSKIGILITDGKSQDDIIPPSRNLRESGVELFAIGVKNADVNELQEIASEPDSTH 313
Cdd:cd01475  83 TGLAIQYAMNNAFSEAEGARPGserVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEPLADH 162

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 71051532 314 VYNVAEFDLMHTVVESLTRTLCSRVEEQDREIKASAHAITGPPTELI 360
Cdd:cd01475 163 VFYVEDFSTIEELTKKFQGKICVVPDLCATLSHVCQQVCISTPGSYL 209
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 157-320 2.34e-53

VWA_collagen alpha 3(VI) like: 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: 238758  Cd Length: 165  Bit Score: 178.29  E-value: 2.34e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71051532 157 ADIVILVDGSWSIGRFNFRLVRHFLENLVTAFDVGSEKTRIGLAQYSGDPRIEWHLNAFSTKDEVIEAVRNLPYKGGNTL 236
Cdd:cd01481   1 KDIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71051532 237 -TGLALNYIFENSFKPEAGSRT--GVSKIGILITDGKSQDDIIPPSRNLRESGVELFAIGVKNADVNELQEIASEPDstH 313
Cdd:cd01481  81 nTGSALDYVVKNLFTKSAGSRIeeGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDPS--F 158


                ....*..
gi 71051532 314 VYNVAEF 320
Cdd:cd01481 159 VFQVSDF 165
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 158-323 3.85e-52

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: 175.34  E-value: 3.85e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71051532    158 DIVILVDGSWSIGRFNFRLVRHFLENLVTAFDVGSEKTRIGLAQYSGDPRIEWHLNAFSTKDEVIEAVRNLPYK-GGNTL 236
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKlGGGTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71051532    237 TGLALNYIFENSFKPEAGSRTGVSKIGILITDGKSQD---DIIPPSRNLRESGVELFAIGVKNA-DVNELQEIASEPDST 312
Cdd:smart00327  81 LGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVGNDvDEEELKKLASAPGGV 160

                          170
                   ....*....|.
gi 71051532    313 HVYNVAEFDLM 323
Cdd:smart00327 161 YVFLPELLDLL 171
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 158-321 5.10e-40

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: 142.88  E-value: 5.10e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71051532 158 DIVILVDGSWSIGRFNFRLVRHFLENLVTAFDVGSEKTRIGLAQYSGDPRIEWHLNAFSTKDEVIEAVRNLPYKGGNTLT 237
Cdd:cd01469   2 DIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTNT 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71051532 238 GLALNYIFENSFKPEAGSRTGVSKIGILITDGKSQDD-----IIPPSrnlRESGVELFAIGV-----KNADVNELQEIAS 307
Cdd:cd01469  82 ATAIQYVVTELFSESNGARKDATKVLVVITDGESHDDpllkdVIPQA---EREGIIRYAIGVgghfqRENSREELKTIAS 158

                       170
                ....*....|....
gi 71051532 308 EPDSTHVYNVAEFD 321
Cdd:cd01469 159 KPPEEHFFNVTDFA 172
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 157-315 3.43e-34

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


Pssm-ID: 238119 [Multi-domain]  Cd Length: 161  Bit Score: 126.53  E-value: 3.43e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71051532 157 ADIVILVDGSWSIGRFNFRLVRHFLENLVTAFDVGSEKTRIGLAQYSGDPRIEWHLNAFSTKDEVIEAVRNLPYK-GGNT 235
Cdd:cd00198   1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGlGGGT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71051532 236 LTGLALNYIFENSFKPEagsRTGVSKIGILITDGKSQDDIIPP---SRNLRESGVELFAIGVKN-ADVNELQEIASEPDS 311
Cdd:cd00198  81 NIGAALRLALELLKSAK---RPNARRVIILLTDGEPNDGPELLaeaARELRKLGITVYTIGIGDdANEDELKEIADKTTG 157


                ....
gi 71051532 312 THVY 315
Cdd:cd00198 158 GAVF 161
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 157-312 1.72e-25

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


Pssm-ID: 238753 [Multi-domain]  Cd Length: 163  Bit Score: 102.48  E-value: 1.72e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71051532 157 ADIVILVDGSWSIgRFNFRLVRHFLENLVTAFDVGSEKTRIGLAQYSGDPR--IEWHLNAFSTKDEVIEAVRNLPYKGGN 234
Cdd:cd01476   1 LDLLFVLDSSGSV-RGKFEKYKKYIERIVEGLEIGPTATRVALITYSGRGRqrVRFNLPKHNDGEELLEKVDNLRFIGGT 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71051532 235 TLTGLALNYIFeNSFKPEAGSRTGVSKIGILITDGKSQDDIIPPSRNLRES-GVELFAIGVKN---ADVNELQEIASEPD 310
Cdd:cd01476  80 TATGAAIEVAL-QQLDPSEGRREGIPKVVVVLTDGRSHDDPEKQARILRAVpNIETFAVGTGDpgtVDTEELHSITGNED 158


                ..
gi 71051532 311 ST 312
Cdd:cd01476 159 HI 160
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 158-294 8.39e-20

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: 87.06  E-value: 8.39e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71051532 158 DIVILVDGSWSIGRFN-FRLVRHFLENLVTAFDVGSEKTRIGLAQYSGDPRIEWHLNAFSTKDE-----VIEAVRNLPYK 231
Cdd:cd01471   2 DLYLLVDGSGSIGYSNwVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSPNSTNKdlalnAIRALLSLYYP 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71051532 232 GGNTLTGLALNYIFENSFKPeAGSRTGVSKIGILITDGKSQDD--IIPPSRNLRESGVELFAIGV 294
Cdd:cd01471  82 NGSTNTTSALLVVEKHLFDT-RGNRENAPQLVIIMTDGIPDSKfrTLKEARKLRERGVIIAVLGV 145
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 157-319 2.46e-16

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: 77.04  E-value: 2.46e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71051532 157 ADIVILVDGSWSIGRFNFRLVRHFLENLVTAF------DVGSEKTRIGLAQYSGDPRIEWHLNAF-STKDEVIEAVRNLP 229
Cdd:cd01480   3 VDITFVLDSSESVGLQNFDITKNFVKRVAERFlkdyyrKDPAGSWRVGVVQYSDQQEVEAGFLRDiRNYTSLKEAVDNLE 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71051532 230 YKGGNTLTGLALNYIFENSFKpeaGSRTGVSKIGILITDGKSQ---DDIIPPSRNLRES-GVELFAIGVkNADVNE-LQE 304
Cdd:cd01480  83 YIGGGTFTDCALKYATEQLLE---GSHQKENKFLLVITDGHSDgspDGGIEKAVNEADHlGIKIFFVAV-GSQNEEpLSR 158

                       170
                ....*....|....*.
gi 71051532 305 IASEPDSTHV-YNVAE 319
Cdd:cd01480 159 IACDGKSALYrENFAE 174
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 32-112 4.60e-13

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 64.83  E-value: 4.60e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71051532  32 PPTRLRYNVISHDSIQISWKAPRGKFG---GYKLLVTPTSGGKTNQLNLQN-TATKAIIQGLMPDQNYTVQIIAYNKDKE 107
Cdd:cd00063   3 PPTNLRVTDVTSTSVTLSWTPPEDDGGpitGYVVEYREKGSGDWKEVEVTPgSETSYTLTGLKPGTEYEFRVRAVNGGGE 82


                ....*
gi 71051532 108 SKPAQ 112
Cdd:cd00063  83 SPPSE 87
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 157-308 2.26e-12

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


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 67.27  E-value: 2.26e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71051532 157 ADIVILVDGSWSIGRFN-FRLVRHFLENLVTAFDvgsEKTRIGLAQYSGdpRIEWHLNAFSTKDEVIEAVRNLPYKGGnT 235
Cdd:COG1240  93 RDVVLVVDASGSMAAENrLEAAKGALLDFLDDYR---PRDRVGLVAFGG--EAEVLLPLTRDREALKRALDELPPGGG-T 166

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71051532 236 LTGLALNYIFEnSFKPEAGSRtgvSKIGILITDGKSQDDIIPP---SRNLRESGVELFAIGVKNADVNE--LQEIASE 308
Cdd:COG1240 167 PLGDALALALE-LLKRADPAR---RKVIVLLTDGRDNAGRIDPleaAELAAAAGIRIYTIGVGTEAVDEglLREIAEA 240
fn3 pfam00041
Fibronectin type III domain;
32-110 1.32e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 60.51  E-value: 1.32e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71051532    32 PPTRLRYNVISHDSIQISWKAPR---GKFGGYKLLVTPT-SGGKTNQLNLQNTATKAIIQGLMPDQNYTVQIIAYNKDKE 107
Cdd:pfam00041   2 APSNLTVTDVTSTSLTVSWTPPPdgnGPITGYEVEYRPKnSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGE 81


                  ...
gi 71051532   108 SKP 110
Cdd:pfam00041  82 GPP 84
fn3 pfam00041
Fibronectin type III domain;
354-432 2.71e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 59.74  E-value: 2.71e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71051532   354 GPPTELITSEVTARSFMVNWTHAP---GNVEKYRVVYYPTRGGKPD-EVVVDGTVSSTVLKNLMSLTEYQIAVFAIYAHT 429
Cdd:pfam00041   1 SAPSNLTVTDVTSTSLTVSWTPPPdgnGPITGYEVEYRPKNSGEPWnEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                  ...
gi 71051532   430 ASE 432
Cdd:pfam00041  81 EGP 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 354-432 4.35e-10

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 56.35  E-value: 4.35e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71051532 354 GPPTELITSEVTARSFMVNWTHAP---GNVEKYRVVYYPTRGGKPDEV-VVDGTVSSTVLKNLMSLTEYQIAVFAIYAHT 429
Cdd:cd00063   2 SPPTNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYREKGSGDWKEVeVTPGSETSYTLTGLKPGTEYEFRVRAVNGGG 81


                ...
gi 71051532 430 ASE 432
Cdd:cd00063  82 ESP 84
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 447-516 1.06e-09

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 55.31  E-value: 1.06e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71051532    447 SDLLLYDVTENSMRVKWDAV--PGASGYLILYAPLTEGLAGDEKEMKIGETHTDIELSGLLPNTEYTVTVYA 516
Cdd:smart00060   5 SNLRVTDVTSTSVTLSWEPPpdDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRA 76
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 32-108 2.52e-09

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 54.16  E-value: 2.52e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71051532     32 PPTRLRYNVISHDSIQISWKAP-RGKFGGYKL---LVTPTSGGKTNQLNLQNTATKAIIQGLMPDQNYTVQIIAYNKDKE 107
Cdd:smart00060   3 PPSNLRVTDVTSTSVTLSWEPPpDDGITGYIVgyrVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAGE 82


                   .
gi 71051532    108 S 108
Cdd:smart00060  83 G 83
vWA_CTRP cd01473
CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an ...
 158-335 2.73e-09

CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an important phenomenon in parasite invasion and in malaria associated pathology.CTRP encodes a protein containing a putative signal sequence followed by a long extracellular region of 1990 amino acids, a transmembrane domain, and a short cytoplasmic segment. The extracellular region of CTRP contains two separated adhesive domains. The first domain contains six 210-amino acid-long homologous VWA domain repeats. The second domain contains seven repeats of 87-60 amino acids in length, which share similarities with the thrombospondin type 1 domain found in a variety of adhesive molecules. Finally, CTRP also contains consensus motifs found in the superfamily of haematopoietin receptors. The VWA domains in these proteins likely mediate protein-protein interactions.


Pssm-ID: 238750 [Multi-domain]  Cd Length: 192  Bit Score: 56.94  E-value: 2.73e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71051532 158 DIVILVDGSWSIGRFNFRL-VRHFLENLVTAFDVGSEKTRIGLAQYSGDPRIewhLNAFS-----TKDEVIEAVRNLP-- 229
Cdd:cd01473   2 DLTLILDESASIGYSNWRKdVIPFTEKIINNLNISKDKVHVGILLFAEKNRD---VVPFSdeeryDKNELLKKINDLKns 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71051532 230 YK-GGNTLTGLALNYIFENSFKPEaGSRTGVSKIGILITDG----KSQDDIIPPSRNLRESGVELFAIGVKNADVNELQE 304
Cdd:cd01473  79 YRsGGETYIVEALKYGLKNYTKHG-NRRKDAPKVTMLFTDGndtsASKKELQDISLLYKEENVKLLVVGVGAASENKLKL 157

                       170       180       190
                ....*....|....*....|....*....|....
gi 71051532 305 IA--SEPDSTHVYNV-AEFDLMHTVVESLTRTLC 335
Cdd:cd01473 158 LAgcDINNDNCPNVIkTEWNNLNGISKFLTDKIC 191
fn3 pfam00041
Fibronectin type III domain;
447-516 4.55e-09

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 53.19  E-value: 4.55e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71051532   447 SDLLLYDVTENSMRVKWDAVPGASG----YLILYAPLTEGlaGDEKEMKIGETHTDIELSGLLPNTEYTVTVYA 516
Cdd:pfam00041   4 SNLTVTDVTSTSLTVSWTPPPDGNGpitgYEVEYRPKNSG--EPWNEITVPGTTTSVTLTGLKPGTEYEVRVQA 75
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
 158-328 6.78e-09

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: 55.76  E-value: 6.78e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71051532 158 DIVILVDGSWSIGRFNFRLVRHFLENLVTAFDVGSEKTRIGLAQYSGDPRIEWHLNAFST--KDEVIEAVRNLPYK---- 231
Cdd:cd01470   2 NIYIALDASDSIGEEDFDEAKNAIKTLIEKISSYEVSPRYEIISYASDPKEIVSIRDFNSndADDVIKRLEDFNYDdhgd 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71051532 232 GGNTLTGLALNYIFENSFKPEAGSRTGVSKIG---ILITDGKSQ---------DDII------PPSRNLRESGVELFAIG 293
Cdd:cd01470  82 KTGTNTAAALKKVYERMALEKVRNKEAFNETRhviILFTDGKSNmggsplptvDKIKnlvyknNKSDNPREDYLDVYVFG 161

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 71051532 294 V-KNADVNELQEIASE-PDSTHVYNVAEFDLMHTVVE 328
Cdd:cd01470 162 VgDDVNKEELNDLASKkDNERHFFKLKDYEDLQEVFD 198
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 447-532 2.64e-08

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 51.34  E-value: 2.64e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71051532 447 SDLLLYDVTENSMRVKWDAVPGA----SGYLILYAPLTEGlaGDEKEMKIGETHTDIELSGLLPNTEYTVTVYAMFGEEA 522
Cdd:cd00063   5 TNLRVTDVTSTSVTLSWTPPEDDggpiTGYVVEYREKGSG--DWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGGE 82

                        90
                ....*....|
gi 71051532 523 SDPVTGQETT 532
Cdd:cd00063  83 SPPSESVTVT 92
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 156-335 3.45e-08

ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, the causative agent of anthrax. ATR is the cellular receptor for the anthrax protective antigen and facilitates entry of the toxin into cells. The VWA domain in ATR contains the toxin binding site and mediates interaction with protective antigen. The binding is mediated by divalent cations that binds to the MIDAS motif. These proteins are a family of vertebrate ECM receptors expressed by endothelial cells.


Pssm-ID: 238751 [Multi-domain]  Cd Length: 185  Bit Score: 53.67  E-value: 3.45e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71051532 156 IADIVILVDGSWSIGRfNFRLVRHFLENLVTAFDvgSEKTRIGLAQYSGDPRIEWHLNAFSTKD----EVIEAVrnLPyk 231
Cdd:cd01474   4 HFDLYFVLDKSGSVAA-NWIEIYDFVEQLVDRFN--SPGLRFSFITFSTRATKILPLTDDSSAIikglEVLKKV--TP-- 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71051532 232 GGNTLTGLALNYIFENSFKPEAGSRTgVSKIGILITDGKSQDDiiPPSRNLRES------GVELFAIGVKNADVNELQEI 305
Cdd:cd01474  77 SGQTYIHEGLENANEQIFNRNGGGRE-TVSVIIALTDGQLLLN--GHKYPEHEAklsrklGAIVYCVGVTDFLKSQLINI 153

                       170       180       190
                ....*....|....*....|....*....|.
gi 71051532 306 ASEPDstHVYNVAE-FDLMHTVVESLTRTLC 335
Cdd:cd01474 154 ADSKE--YVFPVTSgFQALSGIIESVVKKAC 182
VWA_2 pfam13519
von Willebrand factor type A domain;
159-266 3.70e-08

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 51.14  E-value: 3.70e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71051532   159 IVILVDGSWSI-----GRFNFRLVRHFLENLVTAFDvgseKTRIGLAQYSGDPRIEWHLNafSTKDEVIEAVRNLPYKGG 233
Cdd:pfam13519   1 LVFVLDTSGSMrngdyGPTRLEAAKDAVLALLKSLP----GDRVGLVTFGDGPEVLIPLT--KDRAKILRALRRLEPKGG 74

                          90       100       110
                  ....*....|....*....|....*....|...
gi 71051532   234 NTLTGLALNYIFENSFKPeagsRTGVSKIGILI 266
Cdd:pfam13519  75 GTNLAAALQLARAALKHR----RKNQPRRIVLI 103
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 354-431 4.21e-08

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 50.69  E-value: 4.21e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71051532    354 GPPTELITSEVTARSFMVNWTH-APGNVEKYRVVYYPTRGGKPD---EVVVDGTVSSTVLKNLMSLTEYQIAVFAIYAHT 429
Cdd:smart00060   2 SPPSNLRVTDVTSTSVTLSWEPpPDDGITGYIVGYRVEYREEGSewkEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAG 81


                   ..
gi 71051532    430 AS 431
Cdd:smart00060  82 EG 83
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
355-534 1.10e-07

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 54.62  E-value: 1.10e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71051532 355 PPTELITSEVTARSFMVNWT-HAPGNVEKYRVvYYPTRGGKPDEVVVDGTVSSTVLKNLMSLTEYQIAVFAIYAH----T 429
Cdd:COG3401 235 APTGLTATADTPGSVTLSWDpVTESDATGYRV-YRSNSGDGPFTKVATVTTTSYTDTGLTNGTTYYYRVTAVDAAgnesA 313

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71051532 430 ASEGLRGTETTLALPMASDLLLYDVTENSMRVKWDAVPG--ASGYLILYAPLTEGLAGdekemKIGETHTDIEL--SGLL 505
Cdd:COG3401 314 PSNVVSVTTDLTPPAAPSGLTATAVGSSSITLSWTASSDadVTGYNVYRSTSGGGTYT-----KIAETVTTTSYtdTGLT 388

                       170       180       190
                ....*....|....*....|....*....|...
gi 71051532 506 PNTEYTVTVYAM----FGEEASDPVTGQETTSP 534
Cdd:COG3401 389 PGTTYYYKVTAVdaagNESAPSEEVSATTASAA 421
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 152-308 4.74e-06

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


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 48.14  E-value: 4.74e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71051532 152 QTPAIADIVILVDGSWSIGRFNFRLVRHFLENLVTAFdvgSEKTRIGLAQYSGDPRIEWHLNAFSTKDEVIEAVRNLPYK 231
Cdd:COG2425 114 VPLLEGPVVLCVDTSGSMAGSKEAAAKAAALALLRAL---RPNRRFGVILFDTEVVEDLPLTADDGLEDAIEFLSGLFAG 190

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71051532 232 GGnTLTGLALNYIFEnSFKPEAGSRTGVskigILITDGKSQDDIIPPSRNLR--ESGVELFAIGVKNADVNELQEIASE 308
Cdd:COG2425 191 GG-TDIAPALRAALE-LLEEPDYRNADI----VLITDGEAGVSPEELLREVRakESGVRLFTVAIGDAGNPGLLEALAD 263
PRK12279 PRK12279
50S ribosomal protein L22/unknown domain fusion protein; Provisional
 65-148 3.88e-04

50S ribosomal protein L22/unknown domain fusion protein; Provisional


Pssm-ID: 138835 [Multi-domain]  Cd Length: 311  Bit Score: 42.75  E-value: 3.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71051532   65 TPTSGGKTNQLNLQNTATKAIIQGLMPDQNYTVQIIAYNKDKESKPAQgqfRIKDLEKRKDPKPRVKVVDRGNGSRPSSP 144
Cdd:PRK12279  87 LPRAKGSADQLFKRTTHLEIVLSDDVNEREKELAAIKAKKSKKPLPVE---PKAKVETKKVAKPSKVEVKPVEKDENVDP 163


                 ....
gi 71051532  145 EEVK 148
Cdd:PRK12279 164 ELLK 167
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
31-112 4.22e-04

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 43.07  E-value: 4.22e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71051532  31 APPTRLRYNVISHDSIQISWKAPRGK-FGGYKLLVTPTSGGKTNQLNLQNTATKAIIQGLMPDQNYTVQIIAYNKD-KES 108
Cdd:COG3401 328 AAPSGLTATAVGSSSITLSWTASSDAdVTGYNVYRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAgNES 407


                ....
gi 71051532 109 KPAQ 112
Cdd:COG3401 408 APSE 411
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
31-112 5.32e-03

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 39.60  E-value: 5.32e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71051532  31 APPTRLRYNVISHDSIQISWKAPRGK-FGGYKLLVTPTSGGKTNQLNlQNTATKAIIQGLMPDQNYTVQIIAYNKD-KES 108
Cdd:COG3401 234 SAPTGLTATADTPGSVTLSWDPVTESdATGYRVYRSNSGDGPFTKVA-TVTTTSYTDTGLTNGTTYYYRVTAVDAAgNES 312


                ....
gi 71051532 109 KPAQ 112
Cdd:COG3401 313 APSN 316
vWA_VGCC_like cd01463
VWA Voltage gated Calcium channel like: Voltage-gated calcium channels are a complex of five ...
 158-308 7.47e-03

VWA Voltage gated Calcium channel like: Voltage-gated calcium channels are a complex of five proteins: alpha 1, beta 1, gamma, alpha 2 and delta. The alpha 2 and delta subunits result from proteolytic processing of a single gene product and carries at its N-terminus the VWA and cache domains, The alpha 2 delta gene family has orthologues in D. melanogaster and C. elegans but none have been detected in aither A. thaliana or yeast. The exact biochemical function of the VWA domain is not known but the alpha 2 delta complex has been shown to regulate various functional properties of the channel complex.


Pssm-ID: 238740 [Multi-domain]  Cd Length: 190  Bit Score: 37.76  E-value: 7.47e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71051532 158 DIVILVDGSWSIGRFNFRLVRHFLENLVTAFdvgSEKTRIGLAQYSGD-----PRIEWHL--NAFSTKDEVIEAVRNLPY 230
Cdd:cd01463  15 DIVILLDVSGSMTGQRLHLAKQTVSSILDTL---SDNDFFNIITFSNEvnpvvPCFNDTLvqATTSNKKVLKEALDMLEA 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71051532 231 KGGNTLTgLALNYIFE----NSFKPEAGSRTGVSKIGILITDGKSQ--DDII-------PPSRNLResgVELFAIGVKNA 297
Cdd:cd01463  92 KGIANYT-KALEFAFSlllkNLQSNHSGSRSQCNQAIMLITDGVPEnyKEIFdkynwdkNSEIPVR---VFTYLIGREVT 167

                       170
                ....*....|.
gi 71051532 298 DVNELQEIASE 308
Cdd:cd01463 168 DRREIQWMACE 178
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH