NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|767988542|ref|XP_011544147|]
View 

integrin alpha-D isoform X12 [Homo sapiens]

Protein Classification

VWA domain-containing protein( domain architecture ID 10106982)

VWA (von Willebrand factor type A) domain-containing protein similar to mammalian alpha subunits of integrins

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_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 149-324 3.65e-94

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: 291.95  E-value: 3.65e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988542 149 MDIVFLIDGSGSIDQNDFNQMKGFVQAVMGQFEG--TDTLFALMQYSNLLKIHFTFTQFRTSPSQQSLVDPIVQLKGLTF 226
Cdd:cd01469    1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIgpTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988542 227 TATGILTVVTQLFHHKNGARKSAKKILIVITDGQKYKDPLEySDVIPQAEKAGIIRYAIGVGHAFQGPTARQELNTISSA 306
Cdd:cd01469   81 TATAIQYVVTELFSESNGARKDATKVLVVITDGESHDDPLL-KDVIPQAEREGIIRYAIGVGGHFQRENSREELKTIASK 159

                        170
                 ....*....|....*...
gi 767988542 307 PPQDHVFKVDNFAALGSI 324
Cdd:cd01469  160 PPEEHFFNVTDFAALKDI 177
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 464-506 2.45e-09

Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate cell-extracellular matrix and cell-cell interactions. They contain both alpha and beta subunits. Alpha integrins are proposed to contain a domain containing a 7-fold repeat that adopts a beta-propellor fold. Some of these domains contain an inserted von Willebrand factor type-A domain. Some repeats contain putative calcium-binding sites. The 7-fold repeat domain is homologous to a similar domain in phosphatidylinositol-glycan-specific phospholipase D.


:

Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 53.92  E-value: 2.45e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 767988542   464 IGSYFGASLCSV-DVDSDGSTDLiLIGAPHYYEQTRGGQVSVCP 506
Cdd:smart00191   1 PGSYFGYSVAGVgDVNGDGYPDL-LVGAPRANDAGETGAVYVYF 43
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 528-583 1.09e-08

Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate cell-extracellular matrix and cell-cell interactions. They contain both alpha and beta subunits. Alpha integrins are proposed to contain a domain containing a 7-fold repeat that adopts a beta-propellor fold. Some of these domains contain an inserted von Willebrand factor type-A domain. Some repeats contain putative calcium-binding sites. The 7-fold repeat domain is homologous to a similar domain in phosphatidylinositol-glycan-specific phospholipase D.


:

Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 51.99  E-value: 1.09e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 767988542   528 PWGRFGAALTVLGDVNEDKLIDVAIGAPGEQENR--GAVYLFHGaSESGISPSHSQRI 583
Cdd:smart00191   1 PGSYFGYSVAGVGDVNGDGYPDLLVGAPRANDAGetGAVYVYFG-SSGGGNSIPLQNL 57
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 593-625 1.26e-03

Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate cell-extracellular matrix and cell-cell interactions. They contain both alpha and beta subunits. Alpha integrins are proposed to contain a domain containing a 7-fold repeat that adopts a beta-propellor fold. Some of these domains contain an inserted von Willebrand factor type-A domain. Some repeats contain putative calcium-binding sites. The 7-fold repeat domain is homologous to a similar domain in phosphatidylinositol-glycan-specific phospholipase D.


:

Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 37.74  E-value: 1.26e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 767988542   593 QYFGQALSGGQDLTQDGLMDLAVGA--------RGQVLLLR 625
Cdd:smart00191   3 SYFGYSVAGVGDVNGDGYPDLLVGAprandageTGAVYVYF 43
 
Name Accession Description Interval E-value
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 149-324 3.65e-94

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: 291.95  E-value: 3.65e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988542 149 MDIVFLIDGSGSIDQNDFNQMKGFVQAVMGQFEG--TDTLFALMQYSNLLKIHFTFTQFRTSPSQQSLVDPIVQLKGLTF 226
Cdd:cd01469    1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIgpTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988542 227 TATGILTVVTQLFHHKNGARKSAKKILIVITDGQKYKDPLEySDVIPQAEKAGIIRYAIGVGHAFQGPTARQELNTISSA 306
Cdd:cd01469   81 TATAIQYVVTELFSESNGARKDATKVLVVITDGESHDDPLL-KDVIPQAEREGIIRYAIGVGGHFQRENSREELKTIASK 159

                        170
                 ....*....|....*...
gi 767988542 307 PPQDHVFKVDNFAALGSI 324
Cdd:cd01469  160 PPEEHFFNVTDFAALKDI 177
VWA pfam00092
von Willebrand factor type A domain;
150-327 1.19e-48

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 169.76  E-value: 1.19e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988542  150 DIVFLIDGSGSIDQNDFNQMKGFVQAVMGQFE--GTDTLFALMQYSNLLKIHFTFTQFRTSPSQQSLVDPI-VQLKGLTF 226
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDigPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLrYLGGGTTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988542  227 TATGILTVVTQLFHHKNGARKSAKKILIVITDGQKYKDplEYSDVIPQAEKAGIIRYAIGVGHAFqgptaRQELNTISSA 306
Cdd:pfam00092  81 TGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDG--DPEEVARELKSAGVTVFAVGVGNAD-----DEELRKIASE 153

                         170       180
                  ....*....|....*....|.
gi 767988542  307 PPQDHVFKVDNFAALGSIQKQ 327
Cdd:pfam00092 154 PGEGHVFTVSDFEALEDLQDQ 174
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 150-325 8.81e-38

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: 139.13  E-value: 8.81e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988542   150 DIVFLIDGSGSIDQNDFNQMKGFVQAVMGQFE--GTDTLFALMQYSNLLKIHFTFTQFRTSPSQQSLVDPI-VQLKGLTF 226
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDigPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLsYKLGGGTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988542   227 TATGILTVVTQLFHHKNGARKSAKKILIVITDGQKYKDPLEYSDVIPQAEKAGIIRYAIGVGHAFqgptARQELNTISSA 306
Cdd:smart00327  81 LGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDGPKDLLKAAKELKRSGVKVFVVGVGNDV----DEEELKKLASA 156

                          170
                   ....*....|....*....
gi 767988542   307 PPQDHVFKVDNFAALGSIQ 325
Cdd:smart00327 157 PGGVYVFLPELLDLLIDLL 175
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 464-506 2.45e-09

Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate cell-extracellular matrix and cell-cell interactions. They contain both alpha and beta subunits. Alpha integrins are proposed to contain a domain containing a 7-fold repeat that adopts a beta-propellor fold. Some of these domains contain an inserted von Willebrand factor type-A domain. Some repeats contain putative calcium-binding sites. The 7-fold repeat domain is homologous to a similar domain in phosphatidylinositol-glycan-specific phospholipase D.


Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 53.92  E-value: 2.45e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 767988542   464 IGSYFGASLCSV-DVDSDGSTDLiLIGAPHYYEQTRGGQVSVCP 506
Cdd:smart00191   1 PGSYFGYSVAGVgDVNGDGYPDL-LVGAPRANDAGETGAVYVYF 43
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 528-583 1.09e-08

Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate cell-extracellular matrix and cell-cell interactions. They contain both alpha and beta subunits. Alpha integrins are proposed to contain a domain containing a 7-fold repeat that adopts a beta-propellor fold. Some of these domains contain an inserted von Willebrand factor type-A domain. Some repeats contain putative calcium-binding sites. The 7-fold repeat domain is homologous to a similar domain in phosphatidylinositol-glycan-specific phospholipase D.


Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 51.99  E-value: 1.09e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 767988542   528 PWGRFGAALTVLGDVNEDKLIDVAIGAPGEQENR--GAVYLFHGaSESGISPSHSQRI 583
Cdd:smart00191   1 PGSYFGYSVAGVGDVNGDGYPDLLVGAPRANDAGetGAVYVYFG-SSGGGNSIPLQNL 57
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 125-328 1.45e-08

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: 56.49  E-value: 1.45e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988542 125 LLLGSRWEIIQTVPDATPECPHQEMDIVFLIDGSGSIDQND-FNQMKGFVQAVMGQFEGTDTLfALMQYSnllkiHFTFT 203
Cdd:COG1240   69 LLAVLLLLLALALAPLALARPQRGRDVVLVVDASGSMAAENrLEAAKGALLDFLDDYRPRDRV-GLVAFG-----GEAEV 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988542 204 QFRTSPSQQSLVDPIVQLK--GLTFTATGILTVVTQLfhhkNGARKSAKKILIVITDGQKYKDPLEYSDVIPQAEKAGII 281
Cdd:COG1240  143 LLPLTRDREALKRALDELPpgGGTPLGDALALALELL----KRADPARRKVIVLLTDGRDNAGRIDPLEAAELAAAAGIR 218

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 767988542 282 RYAIGVGHAFQGPTARQELNTISSAppqdHVFKVDNFAALGSIQKQL 328
Cdd:COG1240  219 IYTIGVGTEAVDEGLLREIAEATGG----RYFRADDLSELAAIYREI 261
acidobact_VWFA TIGR03436
VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include ...
 151-286 3.62e-05

VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include a region related to the von Willebrand factor type A (VWFA) domain (pfam00092). These domains are restricted to, and have undergone a large paralogous family expansion in, the Acidobacteria, including Solibacter usitatus and Acidobacterium capsulatum ATCC 51196.


Pssm-ID: 274577 [Multi-domain]  Cd Length: 296  Bit Score: 46.53  E-value: 3.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988542  151 IVFLIDGSGSI--DQNDF-NQMKGFVQAVMGqfegTDTLFALMQYSNLLKIHFTFT-----------QFRT-SPSQQSLV 215
Cdd:TIGR03436  56 VGLVIDTSGSMrnDLDRArAAAIRFLKTVLR----PNDRVFVVTFNTRLRLLQDFTsdprlleaalnRLKPpLRTDYNSS 131

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767988542  216 DPIVQLKGLTFTATGILTVVTQLFHHKNGArKSAKKILIVITDGQKYKDPLEYSDVIPQAEKAGIIRYAIG 286
Cdd:TIGR03436 132 GAFVRDGGGTALYDAITLAALEQLANALAG-IPGRKALIVISDGGDNRSRDTLERAIDAAQRADVAIYSID 201
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
 468-504 4.82e-05

FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven copies in alpha integrins. This repeat has been predicted to fold into a beta propeller structure. The repeat is called the FG-GAP repeat after two conserved motifs in the repeat. The FG-GAP repeats are found in the N terminus of integrin alpha chains, a region that has been shown to be important for ligand binding. A putative Ca2+ binding motif is found in some of the repeats.


Pssm-ID: 460357  Cd Length: 36  Bit Score: 40.96  E-value: 4.82e-05
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 767988542  468 FGASLCSVDVDSDGSTDLIlIGAPHYYEQtRGGQVSV 504
Cdd:pfam01839   1 FGYSVAVGDLNGDGYADLA-VGAPGEGGA-GAGAVYV 35
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
 532-567 2.46e-04

FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven copies in alpha integrins. This repeat has been predicted to fold into a beta propeller structure. The repeat is called the FG-GAP repeat after two conserved motifs in the repeat. The FG-GAP repeats are found in the N terminus of integrin alpha chains, a region that has been shown to be important for ligand binding. A putative Ca2+ binding motif is found in some of the repeats.


Pssm-ID: 460357  Cd Length: 36  Bit Score: 39.03  E-value: 2.46e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 767988542  532 FGAALTVlGDVNEDKLIDVAIGAPGE-QENRGAVYLF 567
Cdd:pfam01839   1 FGYSVAV-GDLNGDGYADLAVGAPGEgGAGAGAVYVL 36
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 593-625 1.26e-03

Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate cell-extracellular matrix and cell-cell interactions. They contain both alpha and beta subunits. Alpha integrins are proposed to contain a domain containing a 7-fold repeat that adopts a beta-propellor fold. Some of these domains contain an inserted von Willebrand factor type-A domain. Some repeats contain putative calcium-binding sites. The 7-fold repeat domain is homologous to a similar domain in phosphatidylinositol-glycan-specific phospholipase D.


Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 37.74  E-value: 1.26e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 767988542   593 QYFGQALSGGQDLTQDGLMDLAVGA--------RGQVLLLR 625
Cdd:smart00191   3 SYFGYSVAGVGDVNGDGYPDLLVGAprandageTGAVYVYF 43
 
Name Accession Description Interval E-value
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 149-324 3.65e-94

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: 291.95  E-value: 3.65e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988542 149 MDIVFLIDGSGSIDQNDFNQMKGFVQAVMGQFEG--TDTLFALMQYSNLLKIHFTFTQFRTSPSQQSLVDPIVQLKGLTF 226
Cdd:cd01469    1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIgpTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988542 227 TATGILTVVTQLFHHKNGARKSAKKILIVITDGQKYKDPLEySDVIPQAEKAGIIRYAIGVGHAFQGPTARQELNTISSA 306
Cdd:cd01469   81 TATAIQYVVTELFSESNGARKDATKVLVVITDGESHDDPLL-KDVIPQAEREGIIRYAIGVGGHFQRENSREELKTIASK 159

                        170
                 ....*....|....*...
gi 767988542 307 PPQDHVFKVDNFAALGSI 324
Cdd:cd01469  160 PPEEHFFNVTDFAALKDI 177
VWA pfam00092
von Willebrand factor type A domain;
150-327 1.19e-48

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 169.76  E-value: 1.19e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988542  150 DIVFLIDGSGSIDQNDFNQMKGFVQAVMGQFE--GTDTLFALMQYSNLLKIHFTFTQFRTSPSQQSLVDPI-VQLKGLTF 226
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDigPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLrYLGGGTTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988542  227 TATGILTVVTQLFHHKNGARKSAKKILIVITDGQKYKDplEYSDVIPQAEKAGIIRYAIGVGHAFqgptaRQELNTISSA 306
Cdd:pfam00092  81 TGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDG--DPEEVARELKSAGVTVFAVGVGNAD-----DEELRKIASE 153

                         170       180
                  ....*....|....*....|.
gi 767988542  307 PPQDHVFKVDNFAALGSIQKQ 327
Cdd:pfam00092 154 PGEGHVFTVSDFEALEDLQDQ 174
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 150-325 8.81e-38

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: 139.13  E-value: 8.81e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988542   150 DIVFLIDGSGSIDQNDFNQMKGFVQAVMGQFE--GTDTLFALMQYSNLLKIHFTFTQFRTSPSQQSLVDPI-VQLKGLTF 226
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDigPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLsYKLGGGTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988542   227 TATGILTVVTQLFHHKNGARKSAKKILIVITDGQKYKDPLEYSDVIPQAEKAGIIRYAIGVGHAFqgptARQELNTISSA 306
Cdd:smart00327  81 LGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDGPKDLLKAAKELKRSGVKVFVVGVGNDV----DEEELKKLASA 156

                          170
                   ....*....|....*....
gi 767988542   307 PPQDHVFKVDNFAALGSIQ 325
Cdd:smart00327 157 PGGVYVFLPELLDLLIDLL 175
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 149-313 1.06e-31

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: 121.24  E-value: 1.06e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988542 149 MDIVFLIDGSGSIDQNDFNQMKGFVQAVMGQFE--GTDTLFALMQYSNLLKIHFTFTQFRTSPSQQSLVDPIVQLKGL-T 225
Cdd:cd01450    1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDigPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGgT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988542 226 FTATGILTVVTQLFHHKNgARKSAKKILIVITDGQKYKDPLEySDVIPQAEKAGIIRYAIGVGHAFQgptarQELNTISS 305
Cdd:cd01450   81 NTGKALQYALEQLFSESN-ARENVPKVIIVLTDGRSDDGGDP-KEAAAKLKDEGIKVFVVGVGPADE-----EELREIAS 153


                 ....*...
gi 767988542 306 APPQDHVF 313
Cdd:cd01450  154 CPSERHVF 161
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 150-318 6.91e-29

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: 113.15  E-value: 6.91e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988542 150 DIVFLIDGSGSIDQNDFNQMKGFVQAVMGQFE-GTD-TLFALMQYSNLLKIHFTFTQFrtsPSQQSLVDPIVQLK---GL 224
Cdd:cd01482    2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEiGPDgVQVGLVQYSDDPRTEFDLNAY---TSKEDVLAAIKNLPykgGN 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988542 225 TFTATGILTVVTQLFHHKNGARKSAKKILIVITDGQKYKDPLEYSDVipqAEKAGIIRYAIGVGHAfqgptARQELNTIS 304
Cdd:cd01482   79 TRTGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARV---LRNLGVNVFAVGVKDA-----DESELKMIA 150

                        170
                 ....*....|....
gi 767988542 305 SAPPQDHVFKVDNF 318
Cdd:cd01482  151 SKPSETHVFNVADF 164
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 150-318 9.90e-28

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: 110.01  E-value: 9.90e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988542 150 DIVFLIDGSGSIDQNDFNQMKGFVQAVMGQFE-GTD-TLFALMQYSNLLKIHFTFTQFRTspsQQSLVDPIVQLK---GL 224
Cdd:cd01472    2 DIVFLVDGSESIGLSNFNLVKDFVKRVVERLDiGPDgVRVGVVQYSDDPRTEFYLNTYRS---KDDVLEAVKNLRyigGG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988542 225 TFTATGILTVVTQLFHHKNGARKSAKKILIVITDGQKYKDPLEYSDVIPQaekAGIIRYAIGVGHAfqgptARQELNTIS 304
Cdd:cd01472   79 TNTGKALKYVRENLFTEASGSREGVPKVLVVITDGKSQDDVEEPAVELKQ---AGIEVFAVGVKNA-----DEEELKQIA 150

                        170
                 ....*....|....
gi 767988542 305 SAPPQDHVFKVDNF 318
Cdd:cd01472  151 SDPKELYVFNVADF 164
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 150-313 2.06e-26

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: 106.11  E-value: 2.06e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988542 150 DIVFLIDGSGSIDQNDFNQMKGFVQAVMGQF--EGTDTLFALMQYSNLLKIHFTFTQFRTSPSQQSLVDPIV-QLKGLTF 226
Cdd:cd00198    2 DIVFLLDVSGSMGGEKLDKAKEALKALVSSLsaSPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKkGLGGGTN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988542 227 TATGILTVVTQLfhhKNGARKSAKKILIVITDGQKYKDPLEYSDVIPQAEKAGIIRYAIGVGhafqGPTARQELNTISSA 306
Cdd:cd00198   82 IGAALRLALELL---KSAKRPNARRVIILLTDGEPNDGPELLAEAARELRKLGITVYTIGIG----DDANEDELKEIADK 154


                 ....*..
gi 767988542 307 PPQDHVF 313
Cdd:cd00198  155 TTGGAVF 161
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 150-336 5.56e-24

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: 100.92  E-value: 5.56e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988542 150 DIVFLIDGSGSIDQNDFNQMKGFVQAVMGQFE-GTD-TLFALMQYSNLLKIHFTFTQFRTSPSQQSLVDPIVQLKGLTFT 227
Cdd:cd01475    4 DLVFLIDSSRSVRPENFELVKQFLNQIIDSLDvGPDaTRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETGTMT 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988542 228 ATGILTVVTQLFHHKNGARKSAK---KILIVITDGQKyKDPLeySDVIPQAEKAGIIRYAIGVGHAFQGptarqELNTIS 304
Cdd:cd01475   84 GLAIQYAMNNAFSEAEGARPGSErvpRVGIVVTDGRP-QDDV--SEVAAKARALGIEMFAVGVGRADEE-----ELREIA 155

                        170       180       190
                 ....*....|....*....|....*....|..
gi 767988542 305 SAPPQDHVFKVDNFAALGSIQKQLQEKIYAVE 336
Cdd:cd01475  156 SEPLADHVFYVEDFSTIEELTKKFQGKICVVP 187
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 150-313 1.98e-17

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: 80.14  E-value: 1.98e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988542 150 DIVFLIDGSGSIDQNdFNQMKGFVQAVMGQFE--GTDTLFALMQYSNLLK--IHFTFTQFRTSPSQQSLVDPIVQLKGLT 225
Cdd:cd01476    2 DLLFVLDSSGSVRGK-FEKYKKYIERIVEGLEigPTATRVALITYSGRGRqrVRFNLPKHNDGEELLEKVDNLRFIGGTT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988542 226 FTATGIlTVVTQLFHHKNGARKSAKKILIVITDGQKYKDPLEYSDVIpqAEKAGIIRYAIGVGhaFQGPTARQELNTISS 305
Cdd:cd01476   81 ATGAAI-EVALQQLDPSEGRREGIPKVVVVLTDGRSHDDPEKQARIL--RAVPNIETFAVGTG--DPGTVDTEELHSITG 155


                 ....*...
gi 767988542 306 APpqDHVF 313
Cdd:cd01476  156 NE--DHIF 161
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 150-318 2.33e-13

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: 68.50  E-value: 2.33e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988542 150 DIVFLIDGSGSIDQNDFNQMKGFVQAVMGQFE-GTDTL-FALMQYSNLLKIHFTftqFRTSPSQQSLVDPI--VQLKGLT 225
Cdd:cd01481    2 DIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDvGPDKIrVAVVQFSDTPRPEFY---LNTHSTKADVLGAVrrLRLRGGS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988542 226 FTATG--ILTVVTQLFHHKNGAR--KSAKKILIVITDGQKYKDPLEYSDVIPQaekAGIIRYAIGVGHAfqgptARQELN 301
Cdd:cd01481   79 QLNTGsaLDYVVKNLFTKSAGSRieEGVPQFLVLITGGKSQDDVERPAVALKR---AGIVPFAIGARNA-----DLAELQ 150

                        170
                 ....*....|....*..
gi 767988542 302 TISSAPpqDHVFKVDNF 318
Cdd:cd01481  151 QIAFDP--SFVFQVSDF 165
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 150-324 3.39e-13

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: 68.69  E-value: 3.39e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988542 150 DIVFLIDGSGSIDQNdFNQMKGFVQAVMGQFEGTDTLFALMQYSNLLKIHFTFTQFRTSPSQQSLVDPIVQLKGLTFTAT 229
Cdd:cd01474    6 DLYFVLDKSGSVAAN-WIEIYDFVEQLVDRFNSPGLRFSFITFSTRATKILPLTDDSSAIIKGLEVLKKVTPSGQTYIHE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988542 230 GILTVVTQLFHHKNGARKSAkKILIVITDGQKYKDPLEYSD-VIPQAEKAGIIRYAIGVGHAFQgptarQELNTISSAPp 308
Cdd:cd01474   85 GLENANEQIFNRNGGGRETV-SVIIALTDGQLLLNGHKYPEhEAKLSRKLGAIVYCVGVTDFLK-----SQLINIADSK- 157

                        170
                 ....*....|....*..
gi 767988542 309 qDHVFKVDN-FAALGSI 324
Cdd:cd01474  158 -EYVFPVTSgFQALSGI 173
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 144-321 8.75e-11

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: 61.63  E-value: 8.75e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988542 144 CPhqeMDIVFLIDGSGSIDQNDFNQMKGFVQAVMGQF--------EGTDTLFALMQYSNLLKIHFTFTQFRTSPSQ-QSL 214
Cdd:cd01480    1 GP---VDITFVLDSSESVGLQNFDITKNFVKRVAERFlkdyyrkdPAGSWRVGVVQYSDQQEVEAGFLRDIRNYTSlKEA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988542 215 VDPIVQLKGLTFTATGILTVVTQLFHHkngARKSAKKILIVITDGQKYKDP---LEysDVIPQAEKAGIIRYAIGVghaf 291
Cdd:cd01480   78 VDNLEYIGGGTFTDCALKYATEQLLEG---SHQKENKFLLVITDGHSDGSPdggIE--KAVNEADHLGIKIFFVAV---- 148

                        170       180       190
                 ....*....|....*....|....*....|
gi 767988542 292 qGPTARQELNTISSAPPQDHVfkVDNFAAL 321
Cdd:cd01480  149 -GSQNEEPLSRIACDGKSALY--RENFAEL 175
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 464-506 2.45e-09

Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate cell-extracellular matrix and cell-cell interactions. They contain both alpha and beta subunits. Alpha integrins are proposed to contain a domain containing a 7-fold repeat that adopts a beta-propellor fold. Some of these domains contain an inserted von Willebrand factor type-A domain. Some repeats contain putative calcium-binding sites. The 7-fold repeat domain is homologous to a similar domain in phosphatidylinositol-glycan-specific phospholipase D.


Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 53.92  E-value: 2.45e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 767988542   464 IGSYFGASLCSV-DVDSDGSTDLiLIGAPHYYEQTRGGQVSVCP 506
Cdd:smart00191   1 PGSYFGYSVAGVgDVNGDGYPDL-LVGAPRANDAGETGAVYVYF 43
VWA_2 pfam13519
von Willebrand factor type A domain;
151-256 5.59e-09

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 54.22  E-value: 5.59e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988542  151 IVFLIDGSGSIDQND-----FNQMKGFVQAVMGQFEGtDTlFALMQYSNLLKIHFTFTQFRTSPsqQSLVDPIVQLKGLT 225
Cdd:pfam13519   1 LVFVLDTSGSMRNGDygptrLEAAKDAVLALLKSLPG-DR-VGLVTFGDGPEVLIPLTKDRAKI--LRALRRLEPKGGGT 76

                          90       100       110
                  ....*....|....*....|....*....|.
gi 767988542  226 FTATGILTVVTQLFHhkngARKSAKKILIVI 256
Cdd:pfam13519  77 NLAAALQLARAALKH----RRKNQPRRIVLI 103
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 528-583 1.09e-08

Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate cell-extracellular matrix and cell-cell interactions. They contain both alpha and beta subunits. Alpha integrins are proposed to contain a domain containing a 7-fold repeat that adopts a beta-propellor fold. Some of these domains contain an inserted von Willebrand factor type-A domain. Some repeats contain putative calcium-binding sites. The 7-fold repeat domain is homologous to a similar domain in phosphatidylinositol-glycan-specific phospholipase D.


Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 51.99  E-value: 1.09e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 767988542   528 PWGRFGAALTVLGDVNEDKLIDVAIGAPGEQENR--GAVYLFHGaSESGISPSHSQRI 583
Cdd:smart00191   1 PGSYFGYSVAGVGDVNGDGYPDLLVGAPRANDAGetGAVYVYFG-SSGGGNSIPLQNL 57
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 125-328 1.45e-08

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: 56.49  E-value: 1.45e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988542 125 LLLGSRWEIIQTVPDATPECPHQEMDIVFLIDGSGSIDQND-FNQMKGFVQAVMGQFEGTDTLfALMQYSnllkiHFTFT 203
Cdd:COG1240   69 LLAVLLLLLALALAPLALARPQRGRDVVLVVDASGSMAAENrLEAAKGALLDFLDDYRPRDRV-GLVAFG-----GEAEV 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988542 204 QFRTSPSQQSLVDPIVQLK--GLTFTATGILTVVTQLfhhkNGARKSAKKILIVITDGQKYKDPLEYSDVIPQAEKAGII 281
Cdd:COG1240  143 LLPLTRDREALKRALDELPpgGGTPLGDALALALELL----KRADPARRKVIVLLTDGRDNAGRIDPLEAAELAAAAGIR 218

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 767988542 282 RYAIGVGHAFQGPTARQELNTISSAppqdHVFKVDNFAALGSIQKQL 328
Cdd:COG1240  219 IYTIGVGTEAVDEGLLREIAEATGG----RYFRADDLSELAAIYREI 261
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 149-289 1.12e-06

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: 49.69  E-value: 1.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988542 149 MDIVFLIDGSGSI-DQNDFNQMKGFVQAVMGQFE-GTDTL-FALMQYSNLLKIHFTFTQFRtSPSQQSLVDPIVQLK--- 222
Cdd:cd01471    1 LDLYLLVDGSGSIgYSNWVTHVVPFLHTFVQNLNiSPDEInLYLVTFSTNAKELIRLSSPN-STNKDLALNAIRALLsly 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767988542 223 ---GLTFTATGILTVVTQLFHHKnGARKSAKKILIVITDGQkykdpleySDVIPQAEKA-------GIIRYAIGVGH 289
Cdd:cd01471   80 ypnGSTNTTSALLVVEKHLFDTR-GNRENAPQLVIIMTDGI--------PDSKFRTLKEarklrerGVIIAVLGVGQ 147
acidobact_VWFA TIGR03436
VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include ...
 151-286 3.62e-05

VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include a region related to the von Willebrand factor type A (VWFA) domain (pfam00092). These domains are restricted to, and have undergone a large paralogous family expansion in, the Acidobacteria, including Solibacter usitatus and Acidobacterium capsulatum ATCC 51196.


Pssm-ID: 274577 [Multi-domain]  Cd Length: 296  Bit Score: 46.53  E-value: 3.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988542  151 IVFLIDGSGSI--DQNDF-NQMKGFVQAVMGqfegTDTLFALMQYSNLLKIHFTFT-----------QFRT-SPSQQSLV 215
Cdd:TIGR03436  56 VGLVIDTSGSMrnDLDRArAAAIRFLKTVLR----PNDRVFVVTFNTRLRLLQDFTsdprlleaalnRLKPpLRTDYNSS 131

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767988542  216 DPIVQLKGLTFTATGILTVVTQLFHHKNGArKSAKKILIVITDGQKYKDPLEYSDVIPQAEKAGIIRYAIG 286
Cdd:TIGR03436 132 GAFVRDGGGTALYDAITLAALEQLANALAG-IPGRKALIVISDGGDNRSRDTLERAIDAAQRADVAIYSID 201
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
 468-504 4.82e-05

FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven copies in alpha integrins. This repeat has been predicted to fold into a beta propeller structure. The repeat is called the FG-GAP repeat after two conserved motifs in the repeat. The FG-GAP repeats are found in the N terminus of integrin alpha chains, a region that has been shown to be important for ligand binding. A putative Ca2+ binding motif is found in some of the repeats.


Pssm-ID: 460357  Cd Length: 36  Bit Score: 40.96  E-value: 4.82e-05
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 767988542  468 FGASLCSVDVDSDGSTDLIlIGAPHYYEQtRGGQVSV 504
Cdd:pfam01839   1 FGYSVAVGDLNGDGYADLA-VGAPGEGGA-GAGAVYV 35
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
 532-567 2.46e-04

FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven copies in alpha integrins. This repeat has been predicted to fold into a beta propeller structure. The repeat is called the FG-GAP repeat after two conserved motifs in the repeat. The FG-GAP repeats are found in the N terminus of integrin alpha chains, a region that has been shown to be important for ligand binding. A putative Ca2+ binding motif is found in some of the repeats.


Pssm-ID: 460357  Cd Length: 36  Bit Score: 39.03  E-value: 2.46e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 767988542  532 FGAALTVlGDVNEDKLIDVAIGAPGE-QENRGAVYLF 567
Cdd:pfam01839   1 FGYSVAV-GDLNGDGYADLAVGAPGEgGAGAGAVYVL 36
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 137-306 9.79e-04

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 42.01  E-value: 9.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988542 137 VPDATPECPHQEMDIVFLIDGSGSIDQNDFNQMKGFVQAVMGQFEGTDTlFALMQYSNLLKIHFTFTQFRtspSQQSLVD 216
Cdd:COG2304   80 QPPKAAAEERPPLNLVFVIDVSGSMSGDKLELAKEAAKLLVDQLRPGDR-VSIVTFAGDARVLLPPTPAT---DRAKILA 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988542 217 PIVQLKGLTFTA--TGILTVVTQLfhhKNGARKSAKKILIVITDGQ---KYKDPLEYSDVIPQAEKAGIIRYAIGVGHAF 291
Cdd:COG2304  156 AIDRLQAGGGTAlgAGLELAYELA---RKHFIPGRVNRVILLTDGDanvGITDPEELLKLAEEAREEGITLTTLGVGSDY 232

                        170
                 ....*....|....*
gi 767988542 292 QgptaRQELNTISSA 306
Cdd:COG2304  233 N----EDLLERLADA 243
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 593-625 1.26e-03

Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate cell-extracellular matrix and cell-cell interactions. They contain both alpha and beta subunits. Alpha integrins are proposed to contain a domain containing a 7-fold repeat that adopts a beta-propellor fold. Some of these domains contain an inserted von Willebrand factor type-A domain. Some repeats contain putative calcium-binding sites. The 7-fold repeat domain is homologous to a similar domain in phosphatidylinositol-glycan-specific phospholipase D.


Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 37.74  E-value: 1.26e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 767988542   593 QYFGQALSGGQDLTQDGLMDLAVGA--------RGQVLLLR 625
Cdd:smart00191   3 SYFGYSVAGVGDVNGDGYPDLLVGAprandageTGAVYVYF 43
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 148-290 1.41e-03

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


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 41.20  E-value: 1.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988542 148 EMDIVFLIDGSGSIDQNDFNQMKGFVQAVMGQFEGTDTlFALMQYSNLLKIHFTFTQfrtSPSQQSLVDPI--VQLKGLT 225
Cdd:COG2425  118 EGPVVLCVDTSGSMAGSKEAAAKAAALALLRALRPNRR-FGVILFDTEVVEDLPLTA---DDGLEDAIEFLsgLFAGGGT 193

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767988542 226 FTATGILTVVTQLfhhknGARKSAKKILIVITDGQkykDPLEYSDVIPQA-EKAGIIR-YAIGVGHA 290
Cdd:COG2425  194 DIAPALRAALELL-----EEPDYRNADIVLITDGE---AGVSPEELLREVrAKESGVRlFTVAIGDA 252
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 152-291 3.03e-03

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


Pssm-ID: 238742 [Multi-domain]  Cd Length: 170  Bit Score: 39.18  E-value: 3.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988542 152 VFLIDGSGSIDQNDFNQMKGFVQAVMGQFEGTDTLfALMQYSNLLKIHFTFTQFRtspSQQSLVDPIVQLK--GLTFTAT 229
Cdd:cd01465    4 VFVIDRSGSMDGPKLPLVKSALKLLVDQLRPDDRL-AIVTYDGAAETVLPATPVR---DKAAILAAIDRLTagGSTAGGA 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767988542 230 GILTVVTQLFHHKNgarKSAKKILIVITDGQKY---KDPLEYSDVIPQAEKAGIIRYAIGVGHAF 291
Cdd:cd01465   80 GIQLGYQEAQKHFV---PGGVNRILLATDGDFNvgeTDPDELARLVAQKRESGITLSTLGFGDNY 141
vWA_norD_type cd01454
norD type: Denitrifying bacteria contain both membrane bound and periplasmic nitrate ...
 240-290 3.31e-03

norD type: Denitrifying bacteria contain both membrane bound and periplasmic nitrate reductases. Denitrification plays a major role in completing the nitrogen cycle by converting nitrate or nitrite to nitrogen gas. The pathway for microbial denitrification has been established as NO3- ------> NO2- ------> NO -------> N2O ---------> N2. This reaction generally occurs under oxygen limiting conditions. Genetic and biochemical studies have shown that the first srep of the biochemical pathway is catalyzed by periplasmic nitrate reductases. This family is widely present in proteobacteria and firmicutes. This version of the domain is also present in some archaeal members. The function of the vWA domain in this sub-group is not known. Members of this subgroup have a conserved MIDAS motif.


Pssm-ID: 238731 [Multi-domain]  Cd Length: 174  Bit Score: 39.23  E-value: 3.31e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767988542 240 HHKNGARKSAKKILIVITDGQKYKDPleYSDVIPQ-----------AEKAGIIRYAIGVGHA 290
Cdd:cd01454   94 AERLLARPEKRKILLVISDGEPNDLD--YYEGNVFatedalravieARKLGIEVFGITIDRD 153
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
150-347 6.26e-03

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 38.75  E-value: 6.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988542 150 DIVFLIDGSGSIDQNDFNQMK----GFVQAVMGQFEGTDTL-FALMQYSNLLKIHFTFTqfrtspSQQSLVDPIVQLKGL 224
Cdd:COG4245    7 PVYLLLDTSGSMSGEPIEALNeglqALIDELRQDPYALETVeVSVITFDGEAKVLLPLT------DLEDFQPPDLSASGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988542 225 TFTATGILTVVTQL----FHHKNGARKSAKKILIVITDGQ----KYKDPLEYSDVIPQAEKAGIIryAIGVGHAfqgptA 296
Cdd:COG4245   81 TPLGAALELLLDLIerrvQKYTAEGKGDWRPVVFLITDGEptdsDWEAALQRLKDGEAAKKANIF--AIGVGPD-----A 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 767988542 297 RQE-LNTISsapPQDHVFKVDNFAalgsiqkQLQEKIYAVEGTQSRASSSFQ 347
Cdd:COG4245  154 DTEvLKQLT---DPVRALDALDGL-------DFREFFKWLSASVSSVSRSVG 195
 
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